|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
1-1354 |
0e+00 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 1953.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1 MNNLLNHSGEyPISNEIMNISKYWLIEEKEAVTKLVDKAHMSSVQKAQVRERAYGLVEKVRKNRlKKSGIDAFMIEYDLS 80
Cdd:PRK11905 1 MFQMFAPPFR-PQSALRQAITAAYRRDEAEAVQALLEAATLSDEARAAIRERARKLVEALRAKR-KGTGVEALLQEYSLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 81 SEEGIVLMCLAEALLRVPDKYTIDLLIKDKLTSAAWKNHVGREKHLFVNAATWSLMLTGKILKNP-HGAYRKVFQNLLKK 159
Cdd:PRK11905 79 SQEGVALMCLAEALLRIPDTATRDALIRDKIAPGDWKSHLGGSKSLFVNAATWGLMLTGKLLSTVnDRGLSAALTRLIAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 160 SSEPVIRQAMKQAMKIVGKQYVLGETIEEALKVSETKVARGYSYSYDMLGEAAMTMADADYYYGQYLHAINELAKYATNK 239
Cdd:PRK11905 159 LGEPVIRKAVDMAMRMMGEQFVTGETIEEALKRARELEARGYRYSYDMLGEAARTAADAERYYRDYERAIHAIGKAATGR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 240 EIKKNPGISIKLSALHPRYEVAKHQRVHEELYPKLLKLTQLAKEYNVGMNIDAEETERLQISLELVERLAHEPSLDGFDG 319
Cdd:PRK11905 239 GVYDGPGISVKLSALHPRYERAQRERVMAELLPRLKALALLAKAYDIGLNIDAEEADRLELSLDLLEALCSDPDLAGWNG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 320 IGIVVQAYQKRAPYVLDYLANLAKKTNRRFMIRLVKGAYWDAEIKHAQEQGLADYPVFTRKYHTDVSYQACVKQLFEHHQ 399
Cdd:PRK11905 319 IGFVVQAYQKRCPFVIDYLIDLARRSGRRLMVRLVKGAYWDAEIKRAQVDGLEGFPVFTRKVHTDVSYIACARKLLAARD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 400 YIYPQFATHNAQTVAVVMELANGNKDFEFQCLHGMGDPLYDNIVGKEgYEDIPCRIYAPVGGHKHLLAYLVRRLLENGAN 479
Cdd:PRK11905 399 VIYPQFATHNAQTLAAIYELAGGKGDFEFQCLHGMGEPLYDQVVGKE-KLGRPCRIYAPVGTHETLLAYLVRRLLENGAN 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 480 SSFVNRIVDENLPIEELIEDPVKKAVDYGCGQHPNIPYPKDIVAP-RLNSQGHNTNDFAVLAEMYKNIEKYTLKnTYKAK 558
Cdd:PRK11905 478 SSFVNRIVDENVPVEELIADPVEKVAAMGVAPHPQIPLPRDLYGPeRRNSKGLDLSDEATLAALDEALNAFAAK-TWHAA 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 559 PIVSNVDIDKSTaEAVINP-NTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAI 637
Cdd:PRK11905 557 PLLAGGDVDGGT-RPVLNPaDHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFAL 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 638 AMIEAGKTLSNAIDEVREAVDFCRYYAAQARREFNGPIELPalsdhlkqieftgRGAMVCISPWNFPLAIFLGQITAVLA 717
Cdd:PRK11905 636 AVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGPGHKP-------------LGPVVCISPWNFPLAIFTGQIAAALV 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 718 AGNTVVAKPAEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKSSEI 797
Cdd:PRK11905 703 AGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPP 782
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 798 VPFIAETGGQNAMIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVG 877
Cdd:PRK11905 783 VPLIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVG 862
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 878 PVIDKEAADNLNAYIEEKKKQFKLVYQAQPNEDTQKGTFVMPTAFEIEKLSDLGREQFGPILHILRFKANELSKLIKDIN 957
Cdd:PRK11905 863 PVIDAEAQANIEAHIEAMRAAGRLVHQLPLPAETEKGTFVAPTLIEIDSISDLEREVFGPVLHVVRFKADELDRVIDDIN 942
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 958 STGYGLTAGVHSRINEVMNYVKNNIKAGNVYVNRNIVGAVVGVQPFGGQGKSGTGPKAGGPYYMHRLANEklsgvgavee 1037
Cdd:PRK11905 943 ATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVRE---------- 1012
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1038 iynpekiandelatnklikdkysitnivagekakkdkfvdlksadgknigkkyvasvstvdkaievayAEADAWNHINAE 1117
Cdd:PRK11905 1013 --------------------------------------------------------------------APTPIPPAHESV 1024
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1118 DRALIVEKFLDLLEKERHLIASCLVTESNvsvedahiqidktiqqvayyclqAKKEFAHPELLPGPTGEIDELSLKGRGV 1197
Cdd:PRK11905 1025 DTDAAARDFLAWLDKEGKAALAAAARDAR-----------------------ARSALGLEQELPGPTGESNLLSLHPRGR 1081
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1198 VVSMSSSCDLLIRfvgQTTAALLAGNTVVaKPAYTGSLTAYNIVKLMLKAGVdpKVINLILSDDEeitsallfnskVALV 1277
Cdd:PRK11905 1082 VLCVADTEEALLR---QLAAALATGNVAV-VAADSGLAAALADLPGLVAARI--DWTQDWEADDP-----------FAGA 1144
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754263081 1278 TFSGSISAVKQVHQALALRRGAIIPFVaesvakdgkctslAIETASPLYLRRFVVEKTVSVDTTASGGNASLMSLEE 1354
Cdd:PRK11905 1145 LLEGDAERARAVRQALAARPGAIVPLI-------------AAEPTDAYDLARLVEERSVSINTTAAGGNASLMALGE 1208
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
20-1028 |
0e+00 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 1663.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 20 ISKYWLIEEKEAVTKLVDKAHMSSVQKAQVRERAYGLVEKVRKNRLKKSGIDAFMIEYDLSSEEGIVLMCLAEALLRVPD 99
Cdd:PRK11904 17 ISALYRVDEAAYLRELLELAPLSPEEKARVTARATQLVEAVRAKKKKLGGIDAFLQEYSLSTEEGIALMCLAEALLRIPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 100 KYTIDLLIKDKLTSAAWKNHVGREKHLFVNAATWSLMLTGKILKNPHGAYRK---VFQNLLKKSSEPVIRQAMKQAMKIV 176
Cdd:PRK11904 97 AATADALIRDKLSGADWKKHLGRSDSLFVNASTWGLMLTGKVVKLDKKADGTpsgVLKRLVNRLGEPVIRKAMRQAMKIM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 177 GKQYVLGETIEEALKVSETKVARGYSYSYDMLGEAAMTMADADYYYGQYLHAINELAKYATNKEIKKNPGISIKLSALHP 256
Cdd:PRK11904 177 GKQFVLGRTIEEALKRARSARNKGYRYSFDMLGEAALTAADAERYFKAYARAIEAIGRAAGGADLPARPGISIKLSALHP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 257 RYEVAKHQRVHEELYPKLLKLTQLAKEYNVGMNIDAEETERLQISLELVERLAHEPSLDGFDGIGIVVQAYQKRAPYVLD 336
Cdd:PRK11904 257 RYEAAQRERVLAELVPRVLELARLAKEANIGLTIDAEEADRLELSLDLFEALFRDPSLKGWGGFGLAVQAYQKRALPVLD 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 337 YLANLAKKTNRRFMIRLVKGAYWDAEIKHAQEQGLADYPVFTRKYHTDVSYQACVKQLFEHHQYIYPQFATHNAQTVAVV 416
Cdd:PRK11904 337 WLADLARRQGRRIPVRLVKGAYWDSEIKRAQELGLPGYPVFTRKAATDVSYLACARKLLSARGAIYPQFATHNAHTVAAI 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 417 MELANGnKDFEFQCLHGMGDPLYDNIVGkegYEDIPCRIYAPVGGHKHLLAYLVRRLLENGANSSFVNRIVDENLPIEEL 496
Cdd:PRK11904 417 LEMAGH-RGFEFQRLHGMGEALYDALLD---APGIPCRIYAPVGSHKDLLPYLVRRLLENGANSSFVHRLVDPDVPIEEL 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 497 IEDPVKKAVDYGCGQHPNIPYPKDIVAP-RLNSQGHNTNDFAVLAEMYKNIEKYTlKNTYKAKPIVSNvdidKSTAEAVI 575
Cdd:PRK11904 493 VADPVEKLRSFETLPNPKIPLPRDIFGPeRKNSKGLNLNDRSELEPLAAAIAAFL-EKQWQAGPIING----EGEARPVV 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 576 NP-NTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEVR 654
Cdd:PRK11904 568 SPaDRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAEVR 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 655 EAVDFCRYYAAQARREFNGPIELPALSDHLKQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPIIA 734
Cdd:PRK11904 648 EAVDFCRYYAAQARRLFGAPEKLPGPTGESNELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIA 727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 735 YKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKSSEIVPFIAETGGQNAMIVDS 814
Cdd:PRK11904 728 AEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRTLAARDGPIVPLIAETGGQNAMIVDS 807
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 815 SSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNLNAYIEE 894
Cdd:PRK11904 808 TALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIER 887
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 895 KKKQFKLVYQAQPNEDTQKGTFVMPTAFEIEKLSDLGREQFGPILHILRFKANELSKLIKDINSTGYGLTAGVHSRINEV 974
Cdd:PRK11904 888 MKREARLLAQLPLPAGTENGHFVAPTAFEIDSISQLEREVFGPILHVIRYKASDLDKVIDAINATGYGLTLGIHSRIEET 967
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....
gi 754263081 975 MNYVKNNIKAGNVYVNRNIVGAVVGVQPFGGQGKSGTGPKAGGPYYMHRLANEK 1028
Cdd:PRK11904 968 ADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEK 1021
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
19-1352 |
0e+00 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 1381.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 19 NISKYWLIEEKEAVTKLVDKAHMSSVQKAQVRERAYGLVEKVRKNrlKKSGIDAFMI-----EYDLSSEEGIVLMCLAEA 93
Cdd:PRK11809 94 AITAAYRRPETEAVPMLLEQARLPAPLAEAAHKLAYQLAEKLRNQ--KSAGGRAGMVqgllqEFSLSSQEGVALMCLAEA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 94 LLRVPDKYTIDLLIKDKLTSAAWKNHVGREKHLFVNAATWSLMLTGKILK-NPHGAYRKVFQNLLKKSSEPVIRQAMKQA 172
Cdd:PRK11809 172 LLRIPDKATRDALIRDKISNGNWQSHLGRSPSLFVNAATWGLLFTGKLVStHNEASLSSSLNRIIGKSGEPLIRKGVDMA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 173 MKIVGKQYVLGETIEEALKVSETKVARGYSYSYDMLGEAAMTMADADYYYGQYLHAINELAKYATNKEIKKNPGISIKLS 252
Cdd:PRK11809 252 MRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTEADAQAYLASYEQAIHAIGKASNGRGIYEGPGISIKLS 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 253 ALHPRYEVAKHQRVHEELYPKLLKLTQLAKEYNVGMNIDAEETERLQISLELVERLAHEPSLDGFDGIGIVVQAYQKRAP 332
Cdd:PRK11809 332 ALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIGFVIQAYQKRCP 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 333 YVLDYLANLAKKTNRRFMIRLVKGAYWDAEIKHAQEQGLADYPVFTRKYHTDVSYQACVKQLFEHHQYIYPQFATHNAQT 412
Cdd:PRK11809 412 FVIDYLIDLARRSRRRLMIRLVKGAYWDSEIKRAQVDGLEGYPVYTRKVYTDVSYLACARKLLAVPNLIYPQFATHNAHT 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 413 VAVVMELANGN---KDFEFQCLHGMGDPLYDNIVGK--EGYEDIPCRIYAPVGGHKHLLAYLVRRLLENGANSSFVNRIV 487
Cdd:PRK11809 492 LAAIYHLAGQNyypGQYEFQCLHGMGEPLYEQVVGKvaDGKLNRPCRIYAPVGTHETLLAYLVRRLLENGANTSFVNRIA 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 488 DENLPIEELIEDPVK--KAVDYGCGQ----HPNIPYPKDIVAP-RLNSQGHNTNDFAVLAEMYKNIEKYTLkNTYKAKPI 560
Cdd:PRK11809 572 DTSLPLDELVADPVEavEKLAQQEGQlglpHPKIPLPRDLYGKgRANSAGLDLANEHRLASLSSALLASAH-QKWQAAPM 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 561 VSNvDIDKSTAEAVINP-NTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAM 639
Cdd:PRK11809 651 LED-PVAAGEMSPVINPaDPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLV 729
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 640 IEAGKTLSNAIDEVREAVDFCRYYAAQARREFNGPIELPAlsdhlkqieftgrGAMVCISPWNFPLAIFLGQITAVLAAG 719
Cdd:PRK11809 730 REAGKTFSNAIAEVREAVDFLRYYAGQVRDDFDNDTHRPL-------------GPVVCISPWNFPLAIFTGQVAAALAAG 796
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 720 NTVVAKPAEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKSS---E 796
Cdd:PRK11809 797 NSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDpqgR 876
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 797 IVPFIAETGGQNAMIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDV 876
Cdd:PRK11809 877 PIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDI 956
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 877 GPVIDKEAADNLNAYIEEKKKQFKLVYQA-QPN-EDTQKGTFVMPTAFEIEKLSDLGREQFGPILHILRFKANELSKLIK 954
Cdd:PRK11809 957 GPVIDAEAKANIERHIQAMRAKGRPVFQAaRENsEDWQSGTFVPPTLIELDSFDELKREVFGPVLHVVRYNRNQLDELIE 1036
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 955 DINSTGYGLTAGVHSRINEVMNYVKNNIKAGNVYVNRNIVGAVVGVQPFGGQGKSGTGPKAGGPYYMHRLaneklsgvga 1034
Cdd:PRK11809 1037 QINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRL---------- 1106
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1035 veeiynpekiandeLATNKlikdkysitnivagekakkdkfvdlksadgknigkkyvasvstvDKAIEVAYAEADAWNHI 1114
Cdd:PRK11809 1107 --------------LATRP--------------------------------------------EDALAVTLARQDAEYPV 1128
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1115 NAEDRALIVEKFLDLlekerhliasclvtesnvsVEDAHIQIDKTIQQVAYYCLQAKKEFAHpeLLPGPTGEIDELSLKG 1194
Cdd:PRK11809 1129 DAQLRAALLAPLTAL-------------------REWAAEREPELAALCDQYAELAQAGTTR--LLPGPTGERNTYTLLP 1187
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1195 RGVVVSMSSS-CDLLIrfvgQTTAALLAGNTVVAkPAYTGSLTAYNIvklmLKAGVDPKVInlILSDDEEITSALlfnsk 1273
Cdd:PRK11809 1188 RERVLCLADTeQDALT----QLAAVLAVGSQALW-PDDALHRALVAA----LPAAVQARIQ--LAKDWQLADQPF----- 1251
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 754263081 1274 vALVTFSGSISAVKQVHQALALRRGAIIPfvAESVAKDGKCtslaietaspLYLRRFVVEKTVSVDTTASGGNASLMSL 1352
Cdd:PRK11809 1252 -DAVLFHGDSDQLRALCEQVAQRDGPIVS--VQGFARGETN----------ILLERLLIERSLSVNTAAAGGNASLMTI 1317
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
12-1350 |
0e+00 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 1339.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 12 PISNEIMNISKYWLIEEKEAVTKLVDKAHMSSVQKAQVRERAYGLVEKVRKNRLKKSGIDAFMiEYDLSSEEGIVLMCLA 91
Cdd:COG4230 12 PALPLRAAIAAAERAEELLAAAALLAAAALAAAAAAAAAAAALAARERVRARRGGGGGLLLLL-ELSSLSSEALALLLLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 92 EALLRVPDKYTIDLLIKDKLTSAAWKNHVGREKHLFVNAATWSLMLTGKILKN-PHGAYRKVFQNLLKKSSEPVIRQAMK 170
Cdd:COG4230 91 LLLLALAATRDAAARDDDDKGDGASHLGSSSSSSSSAAAATLLLLGLLLLTALeSSLSLASGLLRLLGRLGRPGIRRAMR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 171 QAMKIVGKQYVLGETIEEALKVSETKVARGYSYSYDMLGEAAMTMADADYYYGQYLHAINELAKYATNKEIKKNPGISIK 250
Cdd:COG4230 171 AAMMMMMGLFGVGFVTEEAAEAARKAARKREYYYYDMLGEAAAAAADAAAYAYAYAAAAAAAIAAAGGGSGGPGPSISSS 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 251 LSALH----PRYEVAKHQRVHEELYPKLLKLTQLAKEYNVGMNIDAEETERLQISLELVERLAHEPSLDGFDGIGIVVQA 326
Cdd:COG4230 251 LSVLLsarhPRYRRRREERLLLLLLPLLALLALAAININIDEEEDAEELLLLLLLLDLLAALLLDGGLGGGGGVGQAVQA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 327 YQKRAPYVLDYLANLAKKTNRRFMIRLVKGAYWDAEIKHAQEQGLADYPVFTRKYHTDVSYQACVKQLFEHHQYIYPQFA 406
Cdd:COG4230 331 YAKALLLVLDLLARRRRRRRRRLVVRLVKGAEWDREIQRAQVLGYVVYPVTTRKVLYDAAALALALLLLAAQPAFAPQFA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 407 THNAQTVAVVMELAnGNKDFEFQCLHGMGDPLYDniVGKEGYEDIPCRIYAPVGGHKHLLAYLVRRLLENGANSSFVNRI 486
Cdd:COG4230 411 THAAATAAAAAAAG-GGGEFEFQCLHGMGEYLYD--QVGRGKLGRPCRIYAPVGSHEDLLAYLVRRLLENGANSSFVNRI 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 487 VDENLPIEELIEDPVKKAVDYGCGQHPNIPYPKDIVAP-RLNSQGHNTNDFAVLAEMYKNIEKYtLKNTYKAKPIVSNVD 565
Cdd:COG4230 488 ADEDVPVEELIADPVEKARALGGAPHPRIPLPRDLYGPeRRNSAGLDLSDEAVLAALSAALAAA-AEKQWQAAPLIAGEA 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 566 IDkSTAEAVINP-NTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGK 644
Cdd:COG4230 567 AS-GEARPVRNPaDHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGK 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 645 TLSNAIDEVREAVDFCRYYAAQARREFNGPIELPalsdhlkqieftGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVA 724
Cdd:COG4230 646 TLPDAIAEVREAVDFCRYYAAQARRLFAAPTVLR------------GRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLA 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 725 KPAEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKSSEIVPFIAET 804
Cdd:COG4230 714 KPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAARDGPIVPLIAET 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 805 GGQNAMIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEA 884
Cdd:COG4230 794 GGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEA 873
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 885 ADNLNAYIEEKKKQFKLVYQAQPNEDTQKGTFVMPTAFEIEKLSDLGREQFGPILHILRFKANELSKLIKDINSTGYGLT 964
Cdd:COG4230 874 RANLEAHIERMRAEGRLVHQLPLPEECANGTFVAPTLIEIDSISDLEREVFGPVLHVVRYKADELDKVIDAINATGYGLT 953
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 965 AGVHSRINEVMNYVKNNIKAGNVYVNRNIVGAVVGVQPFGGQGKSGTGPKAGGPYYMHRLANEKLSGVgaveeiynpeki 1044
Cdd:COG4230 954 LGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATERTVTV------------ 1021
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1045 andelatnklikdkysitNIVAgekakkdkfvdlksADGknigkkyvasvstvdkaievayaeadawnhiNAEDRALive 1124
Cdd:COG4230 1022 ------------------NTTA--------------AGG-------------------------------NASLLAL--- 1035
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1125 kfldllekerhliasclvtesnvsvEDAHIQIDKTIqqvayyclqakkefahpeLLPGPTGEIDELSLKGRGVVVSMSSS 1204
Cdd:COG4230 1036 -------------------------GDWLASLLGAL------------------TLPGPTGERNTLTLRPRGRVLCLADS 1072
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1205 CDLLIRfvgQTTAALLAGNTVV--AKPAYTGsltaynivklmLKAGVDPkvinlilsddeeitsallfnsKVALVTFSGS 1282
Cdd:COG4230 1073 LEALLA---QLAAALATGNRAVvaADLALAG-----------LPAVLLP---------------------PFDAVLFEGR 1117
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 754263081 1283 ISAVKqvhQALALRRGAIIPFVaesvakdgkctslaietASPLYLRRFVVEktvsvdttaSGGNASLM 1350
Cdd:COG4230 1118 LRALR---QALAARDGAIVPVI-----------------DAGYDLERLLEE---------AGGNASLM 1156
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
478-1044 |
0e+00 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 794.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 478 ANSSFVNRIVDENLPIEELIEDpvkkavdygcgqhpnipypkdivaprlnsqghntndfavlaemyknIEKYTLKnTYKA 557
Cdd:cd07125 1 ANSSFVNRIFDLEVPLEALADA----------------------------------------------LKAFDEK-EWEA 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 558 KPIVSNVDIDKSTAEAVINPNTGD-TIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIA 636
Cdd:cd07125 34 IPIINGEETETGEGAPVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 637 IAMIEAGKTLSNAIDEVREAVDFCRYYAAQARREFNGPiELPALSDHLKQIEFTGRGAMVCISPWNFPLAIFLGQITAVL 716
Cdd:cd07125 114 LAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDP-ELPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAAL 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 717 AAGNTVVAKPAEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKSSE 796
Cdd:cd07125 193 AAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAERDGP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 797 IVPFIAETGGQNAMIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDV 876
Cdd:cd07125 273 ILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 877 GPVIDKEAADNLNAYIEEKKKQFKLVYQAQPNEDtqKGTFVMPTAFEIEKLSDLGREQFGPILHILRFKANELSKLIKDI 956
Cdd:cd07125 353 GPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDG--NGYFVAPGIIEIVGIFDLTTEVFGPILHVIRFKAEDLDEAIEDI 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 957 NSTGYGLTAGVHSRINEVMNYVKNNIKAGNVYVNRNIVGAVVGVQPFGGQGKSGTGPKAGGPYYMHRLANEKLSGVGAVE 1036
Cdd:cd07125 431 NATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGPKAGGPNYLLRFGNEKTVSLNTTA 510
|
....*...
gi 754263081 1037 EIYNPEKI 1044
Cdd:cd07125 511 AGGNPSLL 518
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
39-1027 |
0e+00 |
|
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440272 [Multi-domain] Cd Length: 975 Bit Score: 711.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 39 AHMSSVQKAQVRERAYGLVEKVRKNRLkkSGIDAFMIEYDLSSEEGIVLMCLAEALLRVPDKYTIDLLIKDKLtsaawkn 118
Cdd:COG0506 3 AALDEALRARAVALARRLVEAIRAAPE--GGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKL------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 119 hvGREKHLFVNAATWSLMLTgkilknphgayrkvfqnLLKKSSEPVIRQAMKQAMKIVGKQYVLGETIEEALKVSETKVA 198
Cdd:COG0506 74 --AKSPSFLVNASTWGLMLT-----------------LVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAARKLRA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 199 RGYSYSYDMLGEAAMTMADADYYYGQYLHAINELAKYATnkeikKNPGISIKLSALHPRYEVAKHQRVHEELYPKLLKLT 278
Cdd:COG0506 135 KGYRVSLDLLGEAVLTEAEAERYLDAYLEALEAIGAAGV-----DRPGVSVKLSALGPRYSPAQRERVVEELLERLRPLA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 279 QLAKEYNVGMNIDAEETERLQISLELVERLAHEPSLDGFDGIGIVVQAYQKRAPYVLDYLANLAKKTNRRFMIRLVKGAY 358
Cdd:COG0506 210 RAAREAGIFVTIDMEEYDRLDLTLDVFERLLADPELAGWPGVGIVLQAYLKRAEADLDRLAALARRGGRRIRVRLVKGAY 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 359 WDAEIKHAQEQGLaDYPVFTRKYHTDVSYQACVKQLFEHHQYIYPQFATHNAQTVAVVMELAN----GNKDFEFQCLHGM 434
Cdd:COG0506 290 WDPEIVRAQVHGW-PYPVFTRKADTDANYLRCARKLLEAGDAIYPQFATHNARTIAAALALAGergrPPDRFEFQMLYGM 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 435 GDPLYDNIVGKEGYEDIPCRIYAPVGGHKHLLAYLVRRLLENGANSSF-VNRIVDENLPIEELIEDPVKKAVDYGCGQHP 513
Cdd:COG0506 369 GEDLQRALAAVDGGRLLLYCPVVAPVGGDAALAYLLRRLLENNSFLNFfVADFDDDEDLLEFPREPPRFLAALAAPTPPP 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 514 NIPYPKDIVAPRLNSQGHNTNDFAVLAEMYKNIEKYTLKNTYKAKPIVSNVDiDKSTAEAVINPNTGDTIGTVINADAKM 593
Cdd:COG0506 449 PPPLRRQRRRRRRARGGALAAALAAAAAAAALAAAAAAAAALAAAAAGAAAA-AAAAAVAVVPAAAAAVVAAAAAAAAAA 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 594 AKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEVREAVDFCRYYAAQARREFNG 673
Cdd:COG0506 528 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAARAAA 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 674 PIELPALSDHLKQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPIIAYKAIKLLFKAGLPKGVLQF 753
Cdd:COG0506 608 PPPPPPGGLVALLPLGPLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAGGGVLVL 687
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 754 TPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKSSEIVPFIAETGGQNAMIVDSSSLPEQVTGDVIRSAFDSA 833
Cdd:COG0506 688 GAGGGAGGAAALTLAAAAAAATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVAASAAASASAS 767
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 834 GQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNLNAYIEEKKKQFKLVYQAQPNEDTQK 913
Cdd:COG0506 768 ASLLSLLALLLLDADLVILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLPGGGPLVPGLL 847
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 914 GTFVMPTAFEIEKLSDLGREQFGPILHILRFKANELSKLIKDINSTGYGLTAGVHSRINEVMNYVKNNIKAGNVYVNRNI 993
Cdd:COG0506 848 TAPLLVALILGLIVLVLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGGGGGG 927
|
970 980 990
....*....|....*....|....*....|....
gi 754263081 994 VGAVVGVQPFGGQGKSGTGPKAGGPYYMHRLANE 1027
Cdd:COG0506 928 GGGGGGGGGGGGGGGGGGGGGGGGAGTLALAAAA 961
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
525-1024 |
0e+00 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 621.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 525 RLNSQGHNTNDFAVLAEMYKNIEKYTLKnTYKAKPIVSNVDIDKSTAEAVINP-NTGDTIGTVINADAKMAKRALKNAQS 603
Cdd:TIGR01238 7 RKNSLGIDLDNESELKPLEAQIHAWADK-TWQAAPIIGHSYKADGEAQPVTNPaDRRDIVGQVFHANLAHVQAAIDSAQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 604 AFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEVREAVDFCRYYAAQARrefngpielpalsDH 683
Cdd:TIGR01238 86 AFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVR-------------DV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 684 LKQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGS 763
Cdd:TIGR01238 153 LGEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 764 ALVQSPVCKGVIFTGSTEVAGIINQTLASKSSEIVPFIAETGGQNAMIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRIL 843
Cdd:TIGR01238 233 ALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 844 CLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNLNAYIEEKKKQFKLVYQA--QPNEDTQKGTFVMPTA 921
Cdd:TIGR01238 313 CVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLtlDDSRACQHGTFVAPTL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 922 FEIEKLSDLGREQFGPILHILRFKANELSKLIKDINSTGYGLTAGVHSRINEVMNYVKNNIKAGNVYVNRNIVGAVVGVQ 1001
Cdd:TIGR01238 393 FELDDIAELSEEVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQ 472
|
490 500
....*....|....*....|...
gi 754263081 1002 PFGGQGKSGTGPKAGGPYYMHRL 1024
Cdd:TIGR01238 473 PFGGQGLSGTGPKAGGPHYLYRL 495
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
566-1028 |
1.86e-157 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 483.23 E-value: 1.86e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 566 IDKSTAEAVINP-NTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGK 644
Cdd:cd07083 28 VDTKERMVSVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 645 TLSNAIDEVREAVDFCRYYAAQARREFNGPIELPALSDHLKQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVA 724
Cdd:cd07083 108 NWVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 725 KPAEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKSSE---IVPFI 801
Cdd:cd07083 188 KPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLAPGqtwFKRLY 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 802 AETGGQNAMIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVID 881
Cdd:cd07083 268 VETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVID 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 882 KEAADNLNAYIEEKKKQFKLVyqAQPNEDTQKGTFVMPTAFEIE--KLSDLGREQFGPILHILRFKANELSKLIKDINST 959
Cdd:cd07083 348 AEQEAKVLSYIEHGKNEGQLV--LGGKRLEGEGYFVAPTVVEEVppKARIAQEEIFGPVLSVIRYKDDDFAEALEVANST 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 754263081 960 GYGLTAGVHSRINEVMNYVKNNIKAGNVYVNRNIVGAVVGVQPFGGQGKSGTGPKAGGPYYMHRLANEK 1028
Cdd:cd07083 426 PYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHYLRRFLEMK 494
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
189-485 |
1.06e-147 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 449.25 E-value: 1.06e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 189 ALKVSETKVARGYSYSYDMLGEAAMTMADADYYYGQYLHAINELAKYATNKEIKKNPGISIKLSALHPRYEVAKHQRVHE 268
Cdd:pfam01619 1 ALKTIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDALGKAAGPWPLGPRPGISVKLSALHPRYEPLERERVMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 269 ELYPKLLKLTQLAKEYNVGMNIDAEETERLQISLELVERLAHEPSLDGFDGIGIVVQAYQKRAPYVLDYLANLAKKTNRR 348
Cdd:pfam01619 81 ELLERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNGVGITLQAYLKDALAVLDWLLELARRRGRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 349 FMIRLVKGAYWDAEIKHAQeQGLADYPVFTRKYHTDVSYQACVKQLFEHHQYIYPQFATHNAQTVAVVMELANGN----K 424
Cdd:pfam01619 161 LGVRLVKGAYWDSEIKRAQ-QGGWPYPVFTRKEATDANYEACARFLLENHDRIYPQFATHNARSVAAALALAEELgippR 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754263081 425 DFEFQCLHGMGDPLYDNIVgKEGYediPCRIYAPVGGHKHLLAYLVRRLLENGANSSFVNR 485
Cdd:pfam01619 240 RFEFQQLYGMGDNLSFALV-AAGY---RVRKYAPVGPHEELLAYLVRRLLENTANSSFVRR 296
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
574-1020 |
5.93e-137 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 429.34 E-value: 5.93e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINP-NTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDE 652
Cdd:cd07124 50 SRNPaDPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADAD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 653 VREAVDFCRYYAAQARRefNGPIELPALSDHLKQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPI 732
Cdd:cd07124 130 VAEAIDFLEYYAREMLR--LRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 733 IAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQtLASKSSE----IVPFIAETGGQN 808
Cdd:cd07124 208 IAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYE-RAAKVQPgqkwLKRVIAEMGGKN 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 809 AMIVDSSS-LPEQVTGdVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADN 887
Cdd:cd07124 287 AIIVDEDAdLDEAAEG-IVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDR 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 888 LNAYIEEKKKQFKLVYQAQPNEDTQKGTFVMPTAFE-IEKLSDLGREQ-FGPILHILrfKANELSKLIKDINSTGYGLTA 965
Cdd:cd07124 366 IRRYIEIGKSEGRLLLGGEVLELAAEGYFVQPTIFAdVPPDHRLAQEEiFGPVLAVI--KAKDFDEALEIANDTEYGLTG 443
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 754263081 966 GVHSRINEVMNYVKNNIKAGNVYVNRNIVGAVVGVQPFGGQGKSGTGPKAGGPYY 1020
Cdd:cd07124 444 GVFSRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGFKMSGTGSKAGGPDY 498
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
573-1028 |
1.47e-125 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 396.90 E-value: 1.47e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 573 AVINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDE 652
Cdd:pfam00171 10 EVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 653 VREAVDFCRYYAAQARReFNGPIeLPALSDHLKQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPI 732
Cdd:pfam00171 90 VDRAIDVLRYYAGLARR-LDGET-LPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 733 IAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKsseIVPFIAETGGQNAMIV 812
Cdd:pfam00171 168 TALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQN---LKRVTLELGGKNPLIV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 813 DSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNLNAYI 892
Cdd:pfam00171 245 LEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 893 EEKKKQ-FKLVYQAQPNEDtqKGTFVMPTAFE-IEKLSDLGREQ-FGPILHILRFKanELSKLIKDINSTGYGLTAGVHS 969
Cdd:pfam00171 325 EDAKEEgAKLLTGGEAGLD--NGYFVEPTVLAnVTPDMRIAQEEiFGPVLSVIRFK--DEEEAIEIANDTEYGLAAGVFT 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 754263081 970 RINEVMNYVKNNIKAGNVYVNRNIVGAVVGVqPFGGQGKSGTGpKAGGPYYMHRLANEK 1028
Cdd:pfam00171 401 SDLERALRVARRLEAGMVWINDYTTGDADGL-PFGGFKQSGFG-REGGPYGLEEYTEVK 457
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
573-1017 |
4.84e-124 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 393.72 E-value: 4.84e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 573 AVINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDE 652
Cdd:COG1012 24 DVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARGE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 653 VREAVDFCRYYAAQARReFNGPIELPALSDHLKQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPI 732
Cdd:COG1012 104 VDRAADFLRYYAGEARR-LYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 733 IAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKsseIVPFIAETGGQNAMIV 812
Cdd:COG1012 183 SALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAEN---LKRVTLELGGKNPAIV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 813 DSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNLNAYI 892
Cdd:COG1012 260 LDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYI 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 893 EE-KKKQFKLVYQAQPNEDtQKGTFVMPTAFE-IEKLSDLGR-EQFGPILHILRFKanELSKLIKDINSTGYGLTAGVHS 969
Cdd:COG1012 340 EDaVAEGAELLTGGRRPDG-EGGYFVEPTVLAdVTPDMRIAReEIFGPVLSVIPFD--DEEEAIALANDTEYGLAASVFT 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 754263081 970 R-INEVMnYVKNNIKAGNVYVNRNIVGAVVGvQPFGGQGKSGTGPKAGG 1017
Cdd:COG1012 417 RdLARAR-RVARRLEAGMVWINDGTTGAVPQ-APFGGVKQSGIGREGGR 463
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
596-1023 |
4.23e-118 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 375.78 E-value: 4.23e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 596 RALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEVREAVDFCRYYAAQARReFNGPI 675
Cdd:cd07078 2 AAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARR-LHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 676 ELPALSDHLKQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPIIAYKAIKLLFKAGLPKGVLQFTP 755
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 756 GDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLAsksSEIVPFIAETGGQNAMIVDSSSLPEQVTGDVIRSAFDSAGQ 835
Cdd:cd07078 161 GDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAA---ENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 836 RCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNLNAYIEE-KKKQFKLVYQAQPNeDTQKG 914
Cdd:cd07078 238 VCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDaKAEGAKLLCGGKRL-EGGKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 915 TFVMPTAFEIEKLSDL--GREQFGPILHILRFKANElsKLIKDINSTGYGLTAGVHSRINEVMNYVKNNIKAGNVYVNRN 992
Cdd:cd07078 317 YFVPPTVLTDVDPDMPiaQEEIFGPVLPVIPFKDEE--EAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDY 394
|
410 420 430
....*....|....*....|....*....|.
gi 754263081 993 IVGAVVGvQPFGGQGKSGTGpKAGGPYYMHR 1023
Cdd:cd07078 395 SVGAEPS-APFGGVKQSGIG-REGGPYGLEE 423
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
574-1021 |
2.97e-109 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 355.01 E-value: 2.97e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINP-NTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDE 652
Cdd:PRK03137 54 SINPaNKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADAD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 653 VREAVDFCRYYAAQARREFNGPIELPALSDHlKQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPI 732
Cdd:PRK03137 134 TAEAIDFLEYYARQMLKLADGKPVESRPGEH-NRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 733 IAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQtLASKSSE----IVPFIAETGGQN 808
Cdd:PRK03137 213 IAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYE-RAAKVQPgqiwLKRVIAEMGGKD 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 809 AMIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYiDTDVGPVIDKEAADNL 888
Cdd:PRK03137 292 AIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPED-NAYMGPVINQASFDKI 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 889 NAYIEEKKKQFKLVyqAQPNEDTQKGTFVMPTAF-EIEKLSDLGREQ-FGPILHILrfKANELSKLIKDINSTGYGLTAG 966
Cdd:PRK03137 371 MSYIEIGKEEGRLV--LGGEGDDSKGYFIQPTIFaDVDPKARIMQEEiFGPVVAFI--KAKDFDHALEIANNTEYGLTGA 446
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 754263081 967 VHSRINEVMNYVKNNIKAGNVYVNRNIVGAVVGVQPFGGQGKSGTGPKAGGPYYM 1021
Cdd:PRK03137 447 VISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYL 501
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
575-1021 |
7.04e-105 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 342.62 E-value: 7.04e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 575 INP-NTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEV 653
Cdd:TIGR01237 51 INPcDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 654 REAVDFCRYYAAQARrEFNGPIELPALSDHLKQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPII 733
Cdd:TIGR01237 131 AEAIDFMEYYARQMI-ELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 734 AYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLAS---KSSEIVPFIAETGGQNAM 810
Cdd:TIGR01237 210 AAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAKvqpGQKHLKRVIAEMGGKDTV 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 811 IVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNLNA 890
Cdd:TIGR01237 290 IVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIME 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 891 YIEEKKKQFKLVYQAQpnEDTQKGTFVMPTAF-EIEKLSDLGREQ-FGPILHILRfkANELSKLIKDINSTGYGLTAGVH 968
Cdd:TIGR01237 370 YIEIGKAEGRLVSGGC--GDDSKGYFIGPTIFaDVDRKARLAQEEiFGPVVAFIR--ASDFDEALEIANNTEYGLTGGVI 445
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 754263081 969 SRINEVMNYVKNNIKAGNVYVNRNIVGAVVGVQPFGGQGKSGTGPKAGGPYYM 1021
Cdd:TIGR01237 446 SNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPFGGFKMSGTDSKAGGPDYL 498
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
601-1028 |
9.53e-92 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 301.07 E-value: 9.53e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 601 AQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEVREAVDFCRYYAAQARREfNGPIELPAL 680
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKL-GGPELPSPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 681 SDHLKQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGAT 760
Cdd:cd06534 82 PGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 761 VGSALVQSPVCKGVIFTGSTEVAGIINQTLAsksSEIVPFIAETGGQNAMIVDSSSLPEQVTGDVIRSAFDSAGQRCSAL 840
Cdd:cd06534 162 VGAALLSHPRVDKISFTGSTAVGKAIMKAAA---ENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 841 RILCLQEDIADNYIKMIVGamkelkigdskyIDTDVGPviDKEAADNlnayieekkkqfklvyqaqpnedtqkgtfvmpt 920
Cdd:cd06534 239 SRLLVHESIYDEFVEKLVT------------VLVDVDP--DMPIAQE--------------------------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 921 afeieklsdlgrEQFGPILHILRFKANElsKLIKDINSTGYGLTAGVHSRINEVMNYVKNNIKAGNVYVNRNIVGAVVGv 1000
Cdd:cd06534 272 ------------EIFGPVLPVIRFKDEE--EAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPE- 336
|
410 420
....*....|....*....|....*...
gi 754263081 1001 QPFGGQGKSGTGpKAGGPYYMHRLANEK 1028
Cdd:cd06534 337 APFGGVKNSGIG-REGGPYGLEEYTRTK 363
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
570-1019 |
1.53e-90 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 301.86 E-value: 1.53e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 570 TAEAVINP-NTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSN 648
Cdd:cd07097 14 DGEENRNPsDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 649 AIDEVREAVDFCRYYAAQARReFNGPIeLPalSDHLKQIEFTGR---GAMVCISPWNFPLAIFLGQITAVLAAGNTVVAK 725
Cdd:cd07097 94 ARGEVTRAGQIFRYYAGEALR-LSGET-LP--STRPGVEVETTReplGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 726 PAEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKSSEIVpfiAETG 805
Cdd:cd07097 170 PAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQ---LEMG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 806 GQNAMIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAA 885
Cdd:cd07097 247 GKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 886 DNLNAYIEEKKKQ-FKLVYQAQPNEDTQKGTFVMPTAFE-IEKLSDLGREQ-FGPILHILRfkANELSKLIKDINSTGYG 962
Cdd:cd07097 327 EKDLRYIEIARSEgAKLVYGGERLKRPDEGYYLAPALFAgVTNDMRIAREEiFGPVAAVIR--VRDYDEALAIANDTEFG 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 754263081 963 LTAG-VHSRINEVMNYvKNNIKAGNVYVNRNIVGAVVGVqPFGGQGKSGTGPKAGGPY 1019
Cdd:cd07097 405 LSAGiVTTSLKHATHF-KRRVEAGVVMVNLPTAGVDYHV-PFGGRKGSSYGPREQGEA 460
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
574-1026 |
1.28e-87 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 293.70 E-value: 1.28e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEV 653
Cdd:cd07086 17 SRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLGEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 654 REAVDFCRYYAAQARReFNGPI---ELPalsDHlKQIEF-TGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQ 729
Cdd:cd07086 97 QEMIDICDYAVGLSRM-LYGLTipsERP---GH-RLMEQwNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSET 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 730 TPIIAYKAIKLLFKA----GLPKGVLQFTPGdGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKSSEIvpfIAETG 805
Cdd:cd07086 172 TPLTAIAVTKILAEVleknGLPPGVVNLVTG-GGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFGRV---LLELG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 806 GQNAMIV-DSSSLPEQVTGdVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEA 884
Cdd:cd07086 248 GNNAIIVmDDADLDLAVRA-VLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 885 ADNLNAYIEEKKKQ-FKLVYQAQPNEDTQKGTFVMPTAFEIEKLSD--LGREQFGPILHILRFKanELSKLIKDINSTGY 961
Cdd:cd07086 327 VEKYLNAIEIAKSQgGTVLTGGKRIDGGEPGNYVEPTIVTGVTDDAriVQEETFAPILYVIKFD--SLEEAIAINNDVPQ 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 962 GLTAGVHSR-INEVMNYVKNN-IKAGNVYVNRNIVGAVVGVqPFGGQGKSGTGPKAGG---PYYMHRLAN 1026
Cdd:cd07086 405 GLSSSIFTEdLREAFRWLGPKgSDCGIVNVNIPTSGAEIGG-AFGGEKETGGGRESGSdawKQYMRRSTC 473
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
574-1019 |
1.33e-87 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 292.80 E-value: 1.33e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEV 653
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 654 REAVDFCRYYAAQARREFNGPIELPALSdhlKQIEFTGR--GAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTP 731
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPG---KRILVIKQpvGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 732 IIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAgiinQTLASKSSE-IVPFIAETGGqNA- 809
Cdd:cd07103 158 LSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVG----KLLMAQAADtVKRVSLELGG-NAp 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 810 MIV-DSSSLPEQVTGdVIRSAFDSAGQRC-SALRILClQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADN 887
Cdd:cd07103 233 FIVfDDADLDKAVDG-AIASKFRNAGQTCvCANRIYV-HESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 888 LNAYIEE-KKKQFKLVYQAQPNEDtqKGTFVMPTAfeiekLSDLGR-------EQFGPILHILRFKanELSKLIKDINST 959
Cdd:cd07103 311 VEALVEDaVAKGAKVLTGGKRLGL--GGYFYEPTV-----LTDVTDdmlimneETFGPVAPIIPFD--TEDEVIARANDT 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 960 GYGLTAGVHSRINEVMNYVKNNIKAGNVYVNRNIVGAVvgVQPFGGQGKSGTGpKAGGPY 1019
Cdd:cd07103 382 PYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLISDA--EAPFGGVKESGLG-REGGKE 438
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
575-1018 |
1.58e-85 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 287.71 E-value: 1.58e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 575 INP-NTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEV 653
Cdd:cd07131 19 RNPaDLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGDV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 654 REAVDFCRYYAAQARREFNG--PIELPalsdhlKQIEFTGR---GAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAE 728
Cdd:cd07131 99 QEAIDMAQYAAGEGRRLFGEtvPSELP------NKDAMTRRqpiGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 729 QTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLAsKSSEIVPfiAETGGQN 808
Cdd:cd07131 173 DTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCA-RPNKRVA--LEMGGKN 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 809 AMIV-DSSSLPEQVTGdVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADN 887
Cdd:cd07131 250 PIIVmDDADLDLALEG-ALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 888 LNAYIEEKKKQFKLV----YQAQPNeDTQKGTFVMPTAFEIE--KLSDLGREQFGPILHILRFKANElsKLIKDINSTGY 961
Cdd:cd07131 329 VLNYNEIGKEEGATLllggERLTGG-GYEKGYFVEPTVFTDVtpDMRIAQEEIFGPVVALIEVSSLE--EAIEIANDTEY 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 754263081 962 GLTAGVHSR-INEVMNYVKnNIKAGNVYVNRNIVGAVVGVqPFGGQGKSGTGPKAGGP 1018
Cdd:cd07131 406 GLSSAIYTEdVNKAFRARR-DLEAGITYVNAPTIGAEVHL-PFGGVKKSGNGHREAGT 461
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
564-1022 |
2.51e-84 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 284.16 E-value: 2.51e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 564 VDIDKSTAEAVINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAG 643
Cdd:cd07088 7 VPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 644 KTLSNAIDEVREAVDFCRYYAAQARReFNGPIeLPALSDHLK-QIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTV 722
Cdd:cd07088 87 KTLSLARVEVEFTADYIDYMAEWARR-IEGEI-IPSDRPNENiFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 723 VAKPAEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEvAGIinQTLASKSSEIVPFIA 802
Cdd:cd07088 165 VIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTE-AGQ--KIMEAAAENITKVSL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 803 ETGGQNAMIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDK 882
Cdd:cd07088 242 ELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 883 EAADNLNAYIEEKKKQ-FKLVYQ-AQPNedTQKGTFVMPTAFE-IEKLSDLGREQ-FGPILHILRFkaNELSKLIKDINS 958
Cdd:cd07088 322 AALDKVEEMVERAVEAgATLLTGgKRPE--GEKGYFYEPTVLTnVRQDMEIVQEEiFGPVLPVVKF--SSLDEAIELAND 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754263081 959 TGYGLTAGVHSR-INEVMnYVKNNIKAGNVYVNRNIVGAVVGVQpfGGQGKSGTGpKAGGPYYMH 1022
Cdd:cd07088 398 SEYGLTSYIYTEnLNTAM-RATNELEFGETYINRENFEAMQGFH--AGWKKSGLG-GADGKHGLE 458
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
573-1029 |
1.17e-80 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 273.07 E-value: 1.17e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 573 AVINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDE 652
Cdd:cd07145 2 EVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 653 VREAVDFCRYYAAQARREFNGPIELPALSDHLKQIEFTGR---GAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQ 729
Cdd:cd07145 82 VERTIRLFKLAAEEAKVLRGETIPVDAYEYNERRIAFTVRepiGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 730 TPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIInqtlASKS-SEIVPFIAETGGQN 808
Cdd:cd07145 162 TPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLI----ASKAgGTGKKVALELGGSD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 809 AMIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNL 888
Cdd:cd07145 238 PMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 889 NAYIEE-KKKQFKLVYQAQpnedTQKGTFVMPTAFEIEKLSD--LGREQFGPILHILRFKANElsKLIKDINSTGYGLTA 965
Cdd:cd07145 318 ENLVNDaVEKGGKILYGGK----RDEGSFFPPTVLENDTPDMivMKEEVFGPVLPIAKVKDDE--EAVEIANSTEYGLQA 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 754263081 966 GVHSR-INEVMnYVKNNIKAGNVYVNR-------NIvgavvgvqPFGGQGKSGTGpKAGGPYYMHRLANEKL 1029
Cdd:cd07145 392 SVFTNdINRAL-KVARELEAGGVVINDstrfrwdNL--------PFGGFKKSGIG-REGVRYTMLEMTEEKT 453
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
574-1029 |
2.38e-79 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 269.47 E-value: 2.38e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEV 653
Cdd:cd07149 3 VISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 654 REAVDFCRYYAAQARREFNGPIELPALSDHLKQIEFTGR---GAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQT 730
Cdd:cd07149 83 DRAIETLRLSAEEAKRLAGETIPFDASPGGEGRIGFTIRepiGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 731 PIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKsseivPFIAETGGQNAM 810
Cdd:cd07149 163 PLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLK-----KVTLELGSNAAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 811 IVDSSSLPEQVTGDVIRSAFDSAGQRC-SALRILcLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNLN 889
Cdd:cd07149 238 IVDADADLEKAVERCVSGAFANAGQVCiSVQRIF-VHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 890 AYIEEKKKQ-FKLVYQAQPNedtqkGTFVMPTAfeiekLSDLGR-------EQFGPILHILRFKanELSKLIKDINSTGY 961
Cdd:cd07149 317 EWVEEAVEGgARLLTGGKRD-----GAILEPTV-----LTDVPPdmkvvceEVFAPVVSLNPFD--TLDEAIAMANDSPY 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 754263081 962 GLTAGVH-SRINEVMnYVKNNIKAGNVYVNrNIVGAVVGVQPFGGQGKSGTGpKAGGPYYMHRLANEKL 1029
Cdd:cd07149 385 GLQAGVFtNDLQKAL-KAARELEVGGVMIN-DSSTFRVDHMPYGGVKESGTG-REGPRYAIEEMTEIKL 450
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
574-1016 |
3.04e-77 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 264.07 E-value: 3.04e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINPNTGDTIGTVINADAKMAKRALKNAQSAFED--WNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAID 651
Cdd:cd07091 23 TINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEESAK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 652 -EVREAVDFCRYYAAQARReFNGpiELPALSDHlkQIEFTGRGAM-VC--ISPWNFPLAIFLGQITAVLAAGNTVVAKPA 727
Cdd:cd07091 103 gDVALSIKCLRYYAGWADK-IQG--KTIPIDGN--FLAYTRREPIgVCgqIIPWNFPLLMLAWKLAPALAAGNTVVLKPA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 728 EQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQtlASKSSEIVPFIAETGGQ 807
Cdd:cd07091 178 EQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIME--AAAKSNLKKVTLELGGK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 808 NAMIV-DSSSLPEQVTGDVIRSAFDSaGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAAD 886
Cdd:cd07091 256 SPNIVfDDADLDKAVEWAAFGIFFNQ-GQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 887 NLNAYIEEKKKQ-FKLVYQAQPNEDtqKGTFVMPTAF-EIEKLSDLGREQ-FGPILHILRFKANElsKLIKDINSTGYGL 963
Cdd:cd07091 335 KILSYIESGKKEgATLLTGGERHGS--KGYFIQPTVFtDVKDDMKIAKEEiFGPVVTILKFKTED--EVIERANDTEYGL 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 754263081 964 TAGVHSR-INEVMnYVKNNIKAGNVYVNR-NIVGAVVgvqPFGGQGKSGTGPKAG 1016
Cdd:cd07091 411 AAGVFTKdINKAL-RVSRALKAGTVWVNTyNVFDAAV---PFGGFKQSGFGRELG 461
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
574-1019 |
9.44e-76 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 259.03 E-value: 9.44e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNA--ID 651
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLArtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 652 EVREAVDFcRYYA---AQARREFngpieLPALSDHLKQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAE 728
Cdd:cd07093 81 IPRAAANF-RFFAdyiLQLDGES-----YPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 729 QTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKsseIVPFIAETGGQN 808
Cdd:cd07093 155 WTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPN---LKPVSLELGGKN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 809 AMIV-DSSSLPEQVTGdVIRSAFDSAGQRCSA-LRILcLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAAD 886
Cdd:cd07093 232 PNIVfADADLDRAVDA-AVRSSFSNNGEVCLAgSRIL-VQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 887 NLNAYIEEKKKQ-FKLVY--QAQPNEDTQKGTFVMPTAFEIEKLSD--LGREQFGPILHILRFKANElsKLIKDINSTGY 961
Cdd:cd07093 310 KVLGYVELARAEgATILTggGRPELPDLEGGYFVEPTVITGLDNDSrvAQEEIFGPVVTVIPFDDEE--EAIELANDTPY 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 754263081 962 GLTAGVHSR-INEVMNyVKNNIKAGNVYVNRNIVGAVvgVQPFGGQGKSGTGpKAGGPY 1019
Cdd:cd07093 388 GLAAYVWTRdLGRAHR-VARRLEAGTVWVNCWLVRDL--RTPFGGVKASGIG-REGGDY 442
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
574-1016 |
9.51e-76 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 259.41 E-value: 9.51e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINPNTGDTIGTVINADAKMAKRALKNAQSAFED--WNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAID 651
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 652 EVREAVDFCRYYAAQARREFNG--PIELPalsDHLKqieFTGR---GAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKP 726
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAviPVDKG---DYLN---FTRReplGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 727 AEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKsseIVPFIAETGG 806
Cdd:cd07114 155 SEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAEN---LAPVTLELGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 807 QNAMIV-DSSSLPEQVTGdVIRSAFDSAGQRCSA-LRILcLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEA 884
Cdd:cd07114 232 KSPNIVfDDADLDAAVNG-VVAGIFAAAGQTCVAgSRLL-VQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 885 ADNLNAYIEEKKKQ-FKLVYQAQP--NEDTQKGTFVMPTAFE-IEKLSDLGREQ-FGPILHILRFKANElsKLIKDINST 959
Cdd:cd07114 310 LEKVERYVARAREEgARVLTGGERpsGADLGAGYFFEPTILAdVTNDMRIAQEEvFGPVLSVIPFDDEE--EAIALANDS 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 960 GYGLTAGVHSR-INEVMnYVKNNIKAGNVYVN--RnivgAVVGVQPFGGQGKSGTGPKAG 1016
Cdd:cd07114 388 EYGLAAGIWTRdLARAH-RVARAIEAGTVWVNtyR----ALSPSSPFGGFKDSGIGRENG 442
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
560-1023 |
1.37e-75 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 260.98 E-value: 1.37e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 560 IVSNVDIDKSTAEAVINP-NTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLE-KNTDEFIAI 637
Cdd:cd07123 36 VIGGKEVRTGNTGKQVMPhDHAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSgKYRYELNAA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 638 AMIEAGKTLSNA-IDEVREAVDFCRYYAAQARREFNG-PIELPALSdhLKQIEFTG-RGAMVCISPWNFPlAIFLGQITA 714
Cdd:cd07123 116 TMLGQGKNVWQAeIDAACELIDFLRFNVKYAEELYAQqPLSSPAGV--WNRLEYRPlEGFVYAVSPFNFT-AIGGNLAGA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 715 VLAAGNTVVAKPAEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKS 794
Cdd:cd07123 193 PALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 795 SEIVPF---IAETGGQNAMIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKY 871
Cdd:cd07123 273 DRYRTYpriVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDD 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 872 IDTDVGPVIDKEAADNLNAYIEEKKKQFKLVYQAQPNEDTQKGTFVMPTAFEIE--KLSDLGREQFGPILHILRFKANEL 949
Cdd:cd07123 353 FSNFMGAVIDEKAFDRIKGYIDHAKSDPEAEIIAGGKCDDSVGYFVEPTVIETTdpKHKLMTEEIFGPVLTVYVYPDSDF 432
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 754263081 950 SKLIKDINSTG-YGLTAGVHSR----INEVMNYVKNniKAGNVYVNRNIVGAVVGVQPFGGQGKSGTGPKAGGPYYMHR 1023
Cdd:cd07123 433 EETLELVDTTSpYALTGAIFAQdrkaIREATDALRN--AAGNFYINDKPTGAVVGQQPFGGARASGTNDKAGSPLNLLR 509
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
573-1028 |
2.01e-75 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 258.13 E-value: 2.01e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 573 AVINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDE 652
Cdd:cd07094 2 DVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 653 VREAVDFCRYYAAQARREFNGPIELPALSDHLKQIEFTGR---GAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQ 729
Cdd:cd07094 82 VDRAIDTLRLAAEEAERIRGEEIPLDATQGSDNRLAWTIRepvGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 730 TPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKSSEIvpfiaETGGQNA 809
Cdd:cd07094 162 TPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKRIAL-----ELGGNAP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 810 MIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNLN 889
Cdd:cd07094 237 VIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 890 AYIEEK-KKQFKLVYQAQPnedtqKGTFVMPTAFEIEKLSDLGR--EQFGPILHILRFkaNELSKLIKDINSTGYGLTAG 966
Cdd:cd07094 317 RWVEEAvEAGARLLCGGER-----DGALFKPTVLEDVPRDTKLSteETFGPVVPIIRY--DDFEEAIRIANSTDYGLQAG 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 754263081 967 VHSRINEVMNYVKNNIKAGNVYVNRNIVgAVVGVQPFGGQGKSGTGpKAGGPYYMHRLANEK 1028
Cdd:cd07094 390 IFTRDLNVAFKAAEKLEVGGVMVNDSSA-FRTDWMPFGGVKESGVG-REGVPYAMEEMTEEK 449
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
573-1022 |
6.37e-75 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 258.47 E-value: 6.37e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 573 AVINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDE 652
Cdd:PLN02278 43 PVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 653 VREAVDFCRYYAAQARREFnGPIELPALSDH----LKQieftGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAE 728
Cdd:PLN02278 123 VAYGASFLEYFAEEAKRVY-GDIIPSPFPDRrllvLKQ----PVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 729 QTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAgiinQTLASKSSEIVPFIA-ETGGq 807
Cdd:PLN02278 198 LTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVG----KKLMAGAAATVKRVSlELGG- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 808 NA--MIVDSSSLPEQVTGDVIrSAFDSAGQRC-SALRILcLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEA 884
Cdd:PLN02278 273 NApfIVFDDADLDVAVKGALA-SKFRNSGQTCvCANRIL-VQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAA 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 885 ADNLNAYIEEK-KKQFKLVYQAQPNedTQKGTFVMPTAF-EIEKLSDLGREQ-FGPILHILRFKANElsKLIKDINSTGY 961
Cdd:PLN02278 351 VQKVESHVQDAvSKGAKVLLGGKRH--SLGGTFYEPTVLgDVTEDMLIFREEvFGPVAPLTRFKTEE--EAIAIANDTEA 426
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754263081 962 GLTAGVHSRINEVMNYVKNNIKAGNVYVNRNIVGAVVGvqPFGGQGKSGTGpKAGGPYYMH 1022
Cdd:PLN02278 427 GLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA--PFGGVKQSGLG-REGSKYGID 484
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
574-1028 |
1.04e-74 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 256.21 E-value: 1.04e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNA-IDE 652
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 653 VREAVDFCRYYAAQARReFNG---PIELPALSdhlkqieFTGR---GAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKP 726
Cdd:cd07115 81 VPRAADTFRYYAGWADK-IEGeviPVRGPFLN-------YTVRepvGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 727 AEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKSSEIVpfiAETGG 806
Cdd:cd07115 153 AELTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVS---LELGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 807 QNAMIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAAD 886
Cdd:cd07115 230 KSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 887 NLNAYIEEKKKQ-FKLVYQAQpnEDTQKGTFVMPTAFEIEKLSD-LGREQ-FGPILHILRFKANELSKLIKdiNSTGYGL 963
Cdd:cd07115 310 RVLDYVDVGREEgARLLTGGK--RPGARGFFVEPTIFAAVPPEMrIAQEEiFGPVVSVMRFRDEEEALRIA--NGTEYGL 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754263081 964 TAGVHSRINEVMNYVKNNIKAGNVYVnrNIVGAVVGVQPFGGQGKSGTGpKAGGPYYMHRLANEK 1028
Cdd:cd07115 386 AAGVWTRDLGRAHRVAAALKAGTVWI--NTYNRFDPGSPFGGYKQSGFG-REMGREALDEYTEVK 447
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
576-1028 |
3.95e-74 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 254.56 E-value: 3.95e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 576 NPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEVRE 655
Cdd:cd07150 5 NPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 656 AVDFCRYYAAQARReFNGPIeLPalSDHLKQIEFTGR---GAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPI 732
Cdd:cd07150 85 TPELLRAAAGECRR-VRGET-LP--SDSPGTVSMSVRrplGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 733 IAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAgiinQTLASKSSE-IVPFIAETGGQNAMI 811
Cdd:cd07150 161 IGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVG----REIAEKAGRhLKKITLELGGKNPLI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 812 VDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNLNAY 891
Cdd:cd07150 237 VLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 892 IEEK-KKQFKLVYQAqpnedTQKGTFVMPTAfeiekLSDLGR-------EQFGPILHILRFKANElsKLIKDINSTGYGL 963
Cdd:cd07150 317 VEDAvAKGAKLLTGG-----KYDGNFYQPTV-----LTDVTPdmrifreETFGPVTSVIPAKDAE--EALELANDTEYGL 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 754263081 964 TAGVHSR-INEVMNYVKnNIKAGNVYVNRNIV--GAVVgvqPFGGQGKSGTGpKAGGPYYMHRLANEK 1028
Cdd:cd07150 385 SAAILTNdLQRAFKLAE-RLESGMVHINDPTIldEAHV---PFGGVKASGFG-REGGEWSMEEFTELK 447
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
574-1012 |
8.83e-73 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 251.34 E-value: 8.83e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNT-PASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDE 652
Cdd:cd07082 20 VYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALKE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 653 VREAVDFCRYYAAQARREFNGPIELPALSDHLKQIEFTGR---GAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQ 729
Cdd:cd07082 100 VDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKGKIAQVRReplGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 730 TPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIInqtlaSKSSEIVPFIAETGGQNA 809
Cdd:cd07082 180 GVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRL-----KKQHPMKRLVLELGGKDP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 810 MIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNLN 889
Cdd:cd07082 255 AIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 890 AYIEE-KKKQFKLVYQAQPNEdtqkGTFVMPTAFEI--EKLSDLGREQFGPILHILRFkaNELSKLIKDINSTGYGLTAG 966
Cdd:cd07082 335 GLIDDaVAKGATVLNGGGREG----GNLIYPTLLDPvtPDMRLAWEEPFGPVLPIIRV--NDIEEAIELANKSNYGLQAS 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 754263081 967 VHSRINEVMNYVKNNIKAGNVYVN----RNIvgavvGVQPFGGQGKSGTG 1012
Cdd:cd07082 409 IFTKDINKARKLADALEVGTVNINskcqRGP-----DHFPFLGRKDSGIG 453
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
573-1012 |
3.86e-72 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 249.06 E-value: 3.86e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 573 AVINPNTGDTIGTVINADAKMAKRALKNAQSAFED--WNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAI 650
Cdd:cd07112 5 ATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 651 -DEVREAVDFCRYYAaQARREFNGPIElPALSDHLKQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQ 729
Cdd:cd07112 85 aVDVPSAANTFRWYA-EAIDKVYGEVA-PTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 730 TPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQtlASKSSEIVPFIAETGGQNA 809
Cdd:cd07112 163 SPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLE--YSGQSNLKRVWLECGGKSP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 810 MIV--DSSSLpEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADN 887
Cdd:cd07112 241 NIVfaDAPDL-DAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 888 LNAYIEE-KKKQFKLVYQAQPNEDTQKGTFVMPTAFE-IEKLSDLGREQ-FGPILHILRFKANElsKLIKDINSTGYGLT 964
Cdd:cd07112 320 VLGYIESgKAEGARLVAGGKRVLTETGGFFVEPTVFDgVTPDMRIAREEiFGPVLSVITFDSEE--EAVALANDSVYGLA 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 754263081 965 AGVHSR-INEVMNYVKnNIKAGNVYVnrNIVGAVVGVQPFGGQGKSGTG 1012
Cdd:cd07112 398 ASVWTSdLSRAHRVAR-RLRAGTVWV--NCFDEGDITTPFGGFKQSGNG 443
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
574-1029 |
7.36e-72 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 248.04 E-value: 7.36e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINPNTGDTIGTVINADAKMAKRALKNAQSAFEdwnNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEV 653
Cdd:cd07146 3 VRNPYTGEVVGTVPAGTEEALREALALAASYRS---TLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 654 REAVDFCRYYAAQARREFNGPIELPALSDHLKQIEFTGR---GAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQT 730
Cdd:cd07146 80 GRAADVLRFAAAEALRDDGESFSCDLTANGKARKIFTLReplGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 731 PIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKSSeivpfIAETGGQNAM 810
Cdd:cd07146 160 PLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYKRQ-----LLELGGNDPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 811 IV-DSSSLPEQVTGdVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNLN 889
Cdd:cd07146 235 IVmDDADLERAATL-AVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 890 AYIEEKKKQ-FKLVYQAQpnedtQKGTFVMPTAFE-IEKLSDLGREQ-FGPILHILRFKanELSKLIKDINSTGYGLTAG 966
Cdd:cd07146 314 NRVEEAIAQgARVLLGNQ-----RQGALYAPTVLDhVPPDAELVTEEtFGPVAPVIRVK--DLDEAIAISNSTAYGLSSG 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754263081 967 VHSRINEVMNYVKNNIKAGNVYVNrNIVGAVVGVQPFGGQGKSGTGPKAGGPYYMHRLANEKL 1029
Cdd:cd07146 387 VCTNDLDTIKRLVERLDVGTVNVN-EVPGFRSELSPFGGVKDSGLGGKEGVREAMKEMTNVKT 448
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
574-1015 |
2.62e-71 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 246.50 E-value: 2.62e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTL-SNAIDE 652
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 653 VREAVDFCRYYAAQArREFNGPIeLPALSDhlkQIEFTGR---GAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQ 729
Cdd:cd07108 81 AAVLADLFRYFGGLA-GELKGET-LPFGPD---VLTYTVReplGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 730 TPIIAYKAIKLLfKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKsseIVPFIAETGGQNA 809
Cdd:cd07108 156 APLAVLLLAEIL-AQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADR---LIPVSLELGGKSP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 810 MIVDSSSLPEQVTGDVIRSA-FDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNL 888
Cdd:cd07108 232 MIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 889 NAYIEEKKKQ--FKLVYQAQPNEDTQ--KGTFVMPTAFE-IEKLSDLGREQ-FGPILHILRFKanELSKLIKDINSTGYG 962
Cdd:cd07108 312 CGYIDLGLSTsgATVLRGGPLPGEGPlaDGFFVQPTIFSgVDNEWRLAREEiFGPVLCAIPWK--DEDEVIAMANDSHYG 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 754263081 963 LTAGVHSR-INEVMNYVkNNIKAGNVYVNRNiVGAVVGvQPFGGQGKSGTGPKA 1015
Cdd:cd07108 390 LAAYVWTRdLGRALRAA-HALEAGWVQVNQG-GGQQPG-QSYGGFKQSGLGREA 440
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
572-1016 |
1.09e-70 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 245.78 E-value: 1.09e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 572 EAVINPNTGDTIGTVINADAKMAKRALKNAQSAFED-WNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTL-SNA 649
Cdd:cd07144 25 IKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYhSNA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 650 IDEVREAVDFCRYYAAQARREFNGPIELpalsDHLKQiEFTGRGAM-VC--ISPWNFPLAIFLGQITAVLAAGNTVVAKP 726
Cdd:cd07144 105 LGDLDEIIAVIRYYAGWADKIQGKTIPT----SPNKL-AYTLHEPYgVCgqIIPWNYPLAMAAWKLAPALAAGNTVVIKP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 727 AEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKSSEIVpfiAETGG 806
Cdd:cd07144 180 AENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAVT---LECGG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 807 QNAMIVDSSSLPEQVTGDVIRSAFDSAGQRCSAL-RILcLQEDIADNYIKMIVGAMKE-LKIGDSKYIDTDVGPVIDKEA 884
Cdd:cd07144 257 KSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATsRIY-VQESIYDKFVEKFVEHVKQnYKVGSPFDDDTVVGPQVSKTQ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 885 ADNLNAYIEEKKKQF-KLVYQAQPN-EDTQKGTFVMPTAF-EIEKLSDLGREQ-FGPILHILRFKANElsKLIKDINSTG 960
Cdd:cd07144 336 YDRVLSYIEKGKKEGaKLVYGGEKApEGLGKGYFIPPTIFtDVPQDMRIVKEEiFGPVVVISKFKTYE--EAIKKANDTT 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 754263081 961 YGLTAGVHSRINEVMNYVKNNIKAGNVYVNRNIVGAvVGVqPFGGQGKSGTGPKAG 1016
Cdd:cd07144 414 YGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSD-VGV-PFGGFKMSGIGRELG 467
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
574-1012 |
4.01e-70 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 242.91 E-value: 4.01e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINPNTGDTIGTVINADAKMAKRALKNAQSAFE-DWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDE 652
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFEsGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 653 VREAVDFCRYYAAQARREFNGPIelPALSDHLkqiEFTGR---GAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQ 729
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETI--PLGPGYF---VYTVRephGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 730 TPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVaGIINQTLASKssEIVPFIAETGGQNA 809
Cdd:cd07109 156 APLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVET-GIAVMRAAAE--NVVPVTLELGGKSP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 810 MIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYiDTDVGPVIDKEAADNLN 889
Cdd:cd07109 233 QIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 890 AYIEEKKKQ-FKLVYQAQPNED-TQKGTFVMPTAF-EIEKLSDLGREQ-FGPILHILRFKanELSKLIKDINSTGYGLTA 965
Cdd:cd07109 312 GFVARARARgARIVAGGRIAEGaPAGGYFVAPTLLdDVPPDSRLAQEEiFGPVLAVMPFD--DEAEAIALANGTDYGLVA 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 754263081 966 GVHSRINEVMNYVKNNIKAGNVYVNRniVGAVVGVQ-PFGGQGKSGTG 1012
Cdd:cd07109 390 GVWTRDGDRALRVARRLRAGQVFVNN--YGAGGGIElPFGGVKKSGHG 435
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
574-1012 |
3.73e-69 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 240.12 E-value: 3.73e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEV 653
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 654 REAVDFCRYYAAQARrefngPIELPALSDHLK-QIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPI 732
Cdd:cd07106 81 GGAVAWLRYTASLDL-----PDEVIEDDDTRRvELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 733 IAYKAIKLLFKAgLPKGVLQFTPGDGAtVGSALVQSPVCKGVIFTGSTEVAGIInqtLASKSSEIVPFIAETGGQNAMIV 812
Cdd:cd07106 156 CTLKLGELAQEV-LPPGVLNVVSGGDE-LGPALTSHPDIRKISFTGSTATGKKV---MASAAKTLKRVTLELGGNDAAIV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 813 DSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNLNAYI 892
Cdd:cd07106 231 LPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 893 EE-KKKQFKLVYQAQPNEDtqKGTFVMPTAfeIEKLSDLGR----EQFGPILHILRFKanELSKLIKDINSTGYGLTAGV 967
Cdd:cd07106 311 EDaKAKGAKVLAGGEPLDG--PGYFIPPTI--VDDPPEGSRivdeEQFGPVLPVLKYS--DEDEVIARANDSEYGLGASV 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 754263081 968 HSRINEVMNYVKNNIKAGNVYVNRNivGAVVGVQPFGGQGKSGTG 1012
Cdd:cd07106 385 WSSDLERAEAVARRLEAGTVWINTH--GALDPDAPFGGHKQSGIG 427
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
564-1028 |
5.12e-69 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 240.89 E-value: 5.12e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 564 VDIDKSTAEAVINPNTGDTIGTVINADAKMAKRALKNAQSAFE-DWN-NTPASQRANILEKFANLLEKNTDEFIAIAMIE 641
Cdd:cd07143 16 VDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFEtDWGlKVSGSKRGRCLSKLADLMERNLDYLASIEALD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 642 AGKTLSNAID-EVREAVDFCRYYAAQARREFNGPIElpalsDHLKQIEFTGRGAM-VC--ISPWNFPLAIFLGQITAVLA 717
Cdd:cd07143 96 NGKTFGTAKRvDVQASADTFRYYGGWADKIHGQVIE-----TDIKKLTYTRHEPIgVCgqIIPWNFPLLMCAWKIAPALA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 718 AGNTVVAKPAEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQtlASKSSEI 797
Cdd:cd07143 171 AGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVME--AAAKSNL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 798 VPFIAETGGQNAMIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVG 877
Cdd:cd07143 249 KKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 878 PVIDKEAADNLNAYIEEKKKQFKLVYQAQpNEDTQKGTFVMPTAFE--IEKLSDLGREQFGPILHILRFKANElsKLIKD 955
Cdd:cd07143 329 PQVSQIQYERIMSYIESGKAEGATVETGG-KRHGNEGYFIEPTIFTdvTEDMKIVKEEIFGPVVAVIKFKTEE--EAIKR 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754263081 956 INSTGYGLTAGVHSR-INEVMNyVKNNIKAGNVYVN-RNIVGAVVgvqPFGGQGKSGTGpKAGGPYYMHRLANEK 1028
Cdd:cd07143 406 ANDSTYGLAAAVFTNnINNAIR-VANALKAGTVWVNcYNLLHHQV---PFGGYKQSGIG-RELGEYALENYTQIK 475
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
593-1020 |
6.61e-69 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 238.71 E-value: 6.61e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 593 MAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEVREA---VDFcryyAAQARR 669
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMagkIDI----SIKAYH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 670 EFNGPIELPaLSDHLKQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPIIAYKAIKLLFKAGLPKG 749
Cdd:cd07095 77 ERTGERATP-MAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 750 VLQFTPGdGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKSSEIVPFiaETGGQNAMIVDSSSLPEQVTGDVIRSA 829
Cdd:cd07095 156 VLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILAL--EMGGNNPLVVWDVADIDAAAYLIVQSA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 830 FDSAGQRCS-ALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNLnayieEKKKQFKLVYQAQP- 907
Cdd:cd07095 233 FLTAGQRCTcARRLIVPDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARY-----LLAQQDLLALGGEPl 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 908 ---NEDTQKGTFVMPTAFEIEKLSDLGREQ-FGPILHILRfkANELSKLIKDINSTGYGLTAGVHSRINEVMNYVKNNIK 983
Cdd:cd07095 308 lamERLVAGTAFLSPGIIDVTDAADVPDEEiFGPLLQVYR--YDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIR 385
|
410 420 430
....*....|....*....|....*....|....*...
gi 754263081 984 AGNVYVNRNIVGAvVGVQPFGGQGKSGTG-PKAggpYY 1020
Cdd:cd07095 386 AGIVNWNRPTTGA-SSTAPFGGVGLSGNHrPSA---YY 419
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
594-1022 |
7.49e-69 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 238.58 E-value: 7.49e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 594 AKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEVREAVDFCRYYAAQARReFNG 673
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRR-PEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 674 PIeLPAlsdhlkqiEFTGRGAMV---------CISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPIIAYKAIKLLFK- 743
Cdd:cd07104 81 EI-LPS--------DVPGKESMVrrvplgvvgVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIAEIFEe 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 744 AGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQtLASKSSEIVPFiaETGGQNAMIVDSSSLPEQVTG 823
Cdd:cd07104 152 AGLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGE-LAGRHLKKVAL--ELGGNNPLIVLDDADLDLAVS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 824 DVIRSAFDSAGQRC-SALRILcLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNLNAYIEEKKKQ-FKL 901
Cdd:cd07104 229 AAAFGAFLHQGQICmAAGRIL-VHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAgARL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 902 VyqaqpNEDTQKGTFVMPTAfeiekLSDLGR-------EQFGPILHILRFK----ANELSklikdiNSTGYGLTAGVHSR 970
Cdd:cd07104 308 L-----TGGTYEGLFYQPTV-----LSDVTPdmpifreEIFGPVAPVIPFDddeeAVELA------NDTEYGLSAAVFTR 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 754263081 971 -INEVMNYVKnNIKAGNVYVNRNIV--GAVVgvqPFGGQGKSGTGpKAGGPYYMH 1022
Cdd:cd07104 372 dLERAMAFAE-RLETGMVHINDQTVndEPHV---PFGGVKASGGG-RFGGPASLE 421
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
574-1026 |
2.42e-68 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 238.55 E-value: 2.42e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINPNTGDTIGTVINADAKMAKRALKNAQSAFED--WNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNA-I 650
Cdd:cd07142 23 TIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQArY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 651 DEVREAVDFCRYYAAQARREFNgpIELPALSDHLKQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQT 730
Cdd:cd07142 103 AEVPLAARLFRYYAGWADKIHG--MTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 731 PIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQtLASKSSeIVPFIAETGGQNAM 810
Cdd:cd07142 181 PLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQ-LAAKSN-LKPVTLELGGKSPF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 811 IVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNLNA 890
Cdd:cd07142 259 IVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILS 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 891 YIEEKKKQ-FKLVYQAQPNEDtqKGTFVMPTAF-EIEKLSDLGREQ-FGPILHILRFKanELSKLIKDINSTGYGLTAGV 967
Cdd:cd07142 339 YIEHGKEEgATLITGGDRIGS--KGYYIQPTIFsDVKDDMKIARDEiFGPVQSILKFK--TVDEVIKRANNSKYGLAAGV 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 968 HSRINEVMNYVKNNIKAGNVYVN-RNIVGAVVgvqPFGGQGKSGTGPKAGgpyyMHRLAN 1026
Cdd:cd07142 415 FSKNIDTANTLSRALKAGTVWVNcYDVFDASI---PFGGYKMSGIGREKG----IYALNN 467
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
575-1016 |
3.78e-68 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 237.21 E-value: 3.78e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 575 INPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEVR 654
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 655 EAVDFCRYYAAQARREFN-----GPIELPALSDHLKQieftGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQ 729
Cdd:cd07101 81 DVAIVARYYARRAERLLKprrrrGAIPVLTRTTVNRR----PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 730 TPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSpvCKGVIFTGSTEVAGIINQTLASKsseIVPFIAETGGQNA 809
Cdd:cd07101 157 TALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGRR---LIGCSLELGGKNP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 810 MIVDSSSLPEQVTGDVIRSAFDSAGQRC-SALRILcLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNL 888
Cdd:cd07101 232 MIVLEDADLDKAAAGAVRACFSNAGQLCvSIERIY-VHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 889 NAYIEEKKKQFKLVY---QAQPNedtqKGT-FVMPTAFE--IEKLSDLGREQFGPILHILRFKanELSKLIKDINSTGYG 962
Cdd:cd07101 311 TAHVDDAVAKGATVLaggRARPD----LGPyFYEPTVLTgvTEDMELFAEETFGPVVSIYRVA--DDDEAIELANDTDYG 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 754263081 963 LTAGVHSRINEVMNYVKNNIKAGNVYVNRNIVGAVVGVQ-PFGGQGKSGTGPKAG 1016
Cdd:cd07101 385 LNASVWTRDGARGRRIAARLRAGTVNVNEGYAAAWASIDaPMGGMKDSGLGRRHG 439
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
566-1012 |
1.40e-67 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 236.26 E-value: 1.40e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 566 IDKSTAEA--VINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAG 643
Cdd:cd07085 10 VESKTTEWldVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 644 KTLSNAIDEVR---EAVDFCryyaaqarrefngpIELPALS--DHLKQI-----EFTGR---GAMVCISPWNFPLAIFLG 710
Cdd:cd07085 90 KTLADARGDVLrglEVVEFA--------------CSIPHLLkgEYLENVargidTYSYRqplGVVAGITPFNFPAMIPLW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 711 QITAVLAAGNTVVAKPAEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVgSALVQSPVCKGVIFTGSTEVAGIINQTl 790
Cdd:cd07085 156 MFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAV-NALLDHPDIKAVSFVGSTPVGEYIYER- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 791 ASKSSEIVpfIAETGGQNAMIVdsssLP----EQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKI 866
Cdd:cd07085 234 AAANGKRV--QALGGAKNHAVV----MPdadlEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 867 GDSKYIDTDVGPVIDKEAADNLNAYIEEKKKQ-FKLV-----YQAQPNEDtqkGTFVMPTAFE-IEKLSDLGREQ-FGPI 938
Cdd:cd07085 308 GAGDDPGADMGPVISPAAKERIEGLIESGVEEgAKLVldgrgVKVPGYEN---GNFVGPTILDnVTPDMKIYKEEiFGPV 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754263081 939 LHILRfkANELSKLIKDINSTGYGLTAGVHSRINEVMNYVKNNIKAGNVYVNRNIvgAV-VGVQPFGGQGKSGTG 1012
Cdd:cd07085 385 LSIVR--VDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPI--PVpLAFFSFGGWKGSFFG 455
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
574-1012 |
6.29e-67 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 233.81 E-value: 6.29e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEV 653
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 654 REAVDFCRYYAAQArREFNGPiELPALSDHLkqiEFTGR---GAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQT 730
Cdd:cd07107 81 MVAAALLDYFAGLV-TELKGE-TIPVGGRNL---HYTLRepyGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 731 PIIAYKAIKlLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKsseIVPFIAETGGQNAM 810
Cdd:cd07107 156 PLSALRLAE-LAREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG---IKHVTLELGGKNAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 811 IVDSSSLPEQVTGDVIRSA-FDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNLN 889
Cdd:cd07107 232 IVFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVM 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 890 AYIEE-KKKQFKLVY--QAQPNEDTQKGTFVMPTAF-EIEKLSDLGREQ-FGPILHILRFKanELSKLIKDINSTGYGLT 964
Cdd:cd07107 312 HYIDSaKREGARLVTggGRPEGPALEGGFYVEPTVFaDVTPGMRIAREEiFGPVLSVLRWR--DEAEMVAQANGVEYGLT 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 754263081 965 AGVHSRINEVMNYVKNNIKAGNVYVN---RNIVGAvvgvqPFGGQGKSGTG 1012
Cdd:cd07107 390 AAIWTNDISQAHRTARRVEAGYVWINgssRHFLGA-----PFGGVKNSGIG 435
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
560-1012 |
7.35e-66 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 232.85 E-value: 7.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 560 IVSNVDIDKSTAEAVINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAM 639
Cdd:PRK09407 22 LTARVDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 640 IEAGKTLSNAIDEVREAVDFCRYYAAQARREFN-----GPIELPALSDHLKQieftGRGAMVCISPWNFPLAIFLGQITA 714
Cdd:PRK09407 102 LETGKARRHAFEEVLDVALTARYYARRAPKLLAprrraGALPVLTKTTELRQ----PKGVVGVISPWNYPLTLAVSDAIP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 715 VLAAGNTVVAKPAEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSpvCKGVIFTGSTEVAGIINQTLASKs 794
Cdd:PRK09407 178 ALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAGRR- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 795 seIVPFIAETGGQNAMIV-DSSSLPEQVTGdVIRSAFDSAGQRC-SALRILcLQEDIADNYIKMIVGAMKELKIGDSKYI 872
Cdd:PRK09407 255 --LIGFSLELGGKNPMIVlDDADLDKAAAG-AVRACFSNAGQLCiSIERIY-VHESIYDEFVRAFVAAVRAMRLGAGYDY 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 873 DTDVGPVIDKEAADNLNAYIEE-KKKQFKLVYQAQPNEDtqkgtfVMPTAFEIEKLSD------LGREQ-FGPILHILRF 944
Cdd:PRK09407 331 SADMGSLISEAQLETVSAHVDDaVAKGATVLAGGKARPD------LGPLFYEPTVLTGvtpdmeLAREEtFGPVVSVYPV 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 754263081 945 KanELSKLIKDINSTGYGLTAGVHSRINEVMNYVKNNIKAGNVYVNRNIVGAVVGVQ-PFGGQGKSGTG 1012
Cdd:PRK09407 405 A--DVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSVDaPMGGMKDSGLG 471
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
575-1016 |
7.74e-66 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 230.69 E-value: 7.74e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 575 INPNTGDTIGTVINADAKMAKRALKNAQSAFED--WNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDE 652
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 653 VREAVDFCRYYAAQARR----EFN--GPielpalsDHLKQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKP 726
Cdd:cd07118 82 IEGAADLWRYAASLARTlhgdSYNnlGD-------DMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 727 AEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAgiiNQTLASKSSEIVPFIAETGG 806
Cdd:cd07118 155 SEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVG---KAIAAAAARNLKKVSLELGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 807 QNAMIVDSSSLPEQVTGDVIRSAFDSAGQRC-SALRILcLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAA 885
Cdd:cd07118 232 KNPQIVFADADLDAAADAVVFGVYFNAGECCnSGSRLL-VHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 886 DNLNAYIEEKKKQFKLVYQAQPNEDTQKGTFVMPTAF-EIEKLSDLGREQ-FGPILHILRFKAneLSKLIKDINSTGYGL 963
Cdd:cd07118 311 AKITDYVDAGRAEGATLLLGGERLASAAGLFYQPTIFtDVTPDMAIAREEiFGPVLSVLTFDT--VDEAIALANDTVYGL 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 754263081 964 TAGVHSR-INEVMnYVKNNIKAGNVYVNRNIVGAVvgVQPFGGQGKSGTGPKAG 1016
Cdd:cd07118 389 SAGVWSKdIDTAL-TVARRIRAGTVWVNTFLDGSP--ELPFGGFKQSGIGRELG 439
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
574-1012 |
1.48e-65 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 229.88 E-value: 1.48e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEV 653
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 654 REAVDFCRYYAAQARREFNGPIELPALSdhlkqIEFTGR---GAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQT 730
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPLPGGS-----FAYTRReplGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 731 PIIAYKAIKLLFKAGLPKGVLQFTPGDGATvGSALVQSPVCKGVIFTGSTEVAGIInqtLASKSSEIVPFIAETGGQNAM 810
Cdd:cd07090 156 PLTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKV---MSAAAKGIKHVTLELGGKSPL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 811 IV-DSSSLPEQVTGDVIrSAFDSAGQRCS-ALRILcLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNL 888
Cdd:cd07090 232 IIfDDADLENAVNGAMM-ANFLSQGQVCSnGTRVF-VQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 889 NAYIEEKKKQ-FKLVY---QAQPNEDTQKGTFVMPTAF-------EIEKlsdlgREQFGPILHILRFKANElsKLIKDIN 957
Cdd:cd07090 310 LGYIESAKQEgAKVLCggeRVVPEDGLENGFYVSPCVLtdctddmTIVR-----EEIFGPVMSILPFDTEE--EVIRRAN 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 754263081 958 STGYGLTAGVHSRINEVMNYVKNNIKAGNVYVNR-NIVGAVVgvqPFGGQGKSGTG 1012
Cdd:cd07090 383 DTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINTyNISPVEV---PFGGYKQSGFG 435
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
573-1012 |
2.04e-65 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 230.28 E-value: 2.04e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 573 AVINPNTGDTIGTVINADAKMAKRALKNAQSAFE--DWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAI 650
Cdd:cd07119 16 DIINPANGEVIATVPEGTAEDAKRAIAAARRAFDsgEWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 651 DEVREAVDFCRYYAAQARREFNGPIELPALSDHLKQIEFTGrgamVC--ISPWNFPLAIFLGQITAVLAAGNTVVAKPAE 728
Cdd:cd07119 96 IDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVG----VCglITPWNYPLLQAAWKLAPALAAGNTVVIKPSE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 729 QTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKSSEIVpfiAETGGQN 808
Cdd:cd07119 172 VTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKVA---LELGGKN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 809 AMIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNL 888
Cdd:cd07119 249 PNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 889 NAYIEE-KKKQFKLVYQAQ-PNEDT-QKGTFVMPTAF-EIEKLSDLGREQ-FGPILHILRFKANElsKLIKDINSTGYGL 963
Cdd:cd07119 329 LSYIQLgKEEGARLVCGGKrPTGDElAKGYFVEPTIFdDVDRTMRIVQEEiFGPVLTVERFDTEE--EAIRLANDTPYGL 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 754263081 964 TAGVHSRINEVMNYVKNNIKAGNVYVNRniVGAVVGVQPFGGQGKSGTG 1012
Cdd:cd07119 407 AGAVWTKDIARANRVARRLRAGTVWIND--YHPYFAEAPWGGYKQSGIG 453
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
575-1012 |
3.43e-64 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 225.95 E-value: 3.43e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 575 INPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEVR 654
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 655 EAVDFCRYYAAQA-----RREFNGPielPALSDHLKQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQ 729
Cdd:cd07099 81 LALEAIDWAARNAprvlaPRKVPTG---LLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 730 TPIIAYKAIKLLFKAGLPKGVLQFTPGDGATvGSALVQSPVCKgVIFTGST----EVAGIINQTLasksseiVPFIAETG 805
Cdd:cd07099 158 TPLVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAALIDAGVDK-VAFTGSVatgrKVMAAAAERL-------IPVVLELG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 806 GQNAMIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAA 885
Cdd:cd07099 229 GKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 886 DNLNAYIEE-KKKQFKLVYQAQPNEDtqKGTFVMPTAF-EIEKLSDLGREQ-FGPILHILRFkaNELSKLIKDINSTGYG 962
Cdd:cd07099 309 DIVRRHVDDaVAKGAKALTGGARSNG--GGPFYEPTVLtDVPHDMDVMREEtFGPVLPVMPV--ADEDEAIALANDSRYG 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 754263081 963 LTAGVHSRINEVMNYVKNNIKAGNVYVNRNIVGAVVGVQPFGGQGKSGTG 1012
Cdd:cd07099 385 LSASVFSRDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGG 434
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
573-1016 |
4.35e-64 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 226.46 E-value: 4.35e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 573 AVINPNTGDTIGTVINADAKMAKRALKNAQSAFE---DWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNA 649
Cdd:cd07141 25 PTINPATGEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 650 -IDEVREAVDFCRYYAAQARREFNGPIelPALSDH--LKQIEFTGrgamVC--ISPWNFPLAIFLGQITAVLAAGNTVVA 724
Cdd:cd07141 105 yLVDLPGAIKVLRYYAGWADKIHGKTI--PMDGDFftYTRHEPVG----VCgqIIPWNFPLLMAAWKLAPALACGNTVVL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 725 KPAEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQtlASKSSEIVPFIAET 804
Cdd:cd07141 179 KPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQ--AAGKSNLKRVTLEL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 805 GGQNAMIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEA 884
Cdd:cd07141 257 GGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 885 ADNLNAYIEEKKKQ-FKLVYQAQPNEDtqKGTFVMPTAFeieklSD------LGREQ-FGPILHILRFKanELSKLIKDI 956
Cdd:cd07141 337 FKKILELIESGKKEgAKLECGGKRHGD--KGYFIQPTVF-----SDvtddmrIAKEEiFGPVQQIFKFK--TIDEVIERA 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 754263081 957 NSTGYGLTAGVHSR-INEVMnYVKNNIKAGNVYVNrniVGAVVGVQ-PFGGQGKSGTGPKAG 1016
Cdd:cd07141 408 NNTTYGLAAAVFTKdIDKAI-TFSNALRAGTVWVN---CYNVVSPQaPFGGYKMSGNGRELG 465
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
575-1016 |
6.49e-63 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 223.54 E-value: 6.49e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 575 INPNTGDTIGTVINADAKMAKRALKNAQSAFED--WNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGK--TLSNAI 650
Cdd:PLN02766 41 RDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHgpWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKlfALGKAV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 651 DeVREAVDFCRYYAAQARRefngpIELPALSDHLKQIEFTGR---GAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPA 727
Cdd:PLN02766 121 D-IPAAAGLLRYYAGAADK-----IHGETLKMSRQLQGYTLKepiGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 728 EQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQtlASKSSEIVPFIAETGGQ 807
Cdd:PLN02766 195 EQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQ--AAATSNLKQVSLELGGK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 808 NAMIV-DSSSLPEQVtgDVIRSA-FDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAA 885
Cdd:PLN02766 273 SPLLIfDDADVDMAV--DLALLGiFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQF 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 886 DNLNAYIEEKKKQ-FKLVYQAQPNEDtqKGTFVMPTAFE--IEKLSDLGREQFGPILHILRFKANElsKLIKDINSTGYG 962
Cdd:PLN02766 351 EKILSYIEHGKREgATLLTGGKPCGD--KGYYIEPTIFTdvTEDMKIAQDEIFGPVMSLMKFKTVE--EAIKKANNTKYG 426
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 754263081 963 LTAGVHSRINEVMNYVKNNIKAGNVYVNRNIvgAVVGVQPFGGQGKSGTGPKAG 1016
Cdd:PLN02766 427 LAAGIVTKDLDVANTVSRSIRAGTIWVNCYF--AFDPDCPFGGYKMSGFGRDQG 478
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
575-1010 |
2.91e-62 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 221.37 E-value: 2.91e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 575 INPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEVr 654
Cdd:PRK09457 20 RNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEV- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 655 EA----VDFcryyAAQARREFNGPIELPALsDHLKQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQT 730
Cdd:PRK09457 99 TAminkIAI----SIQAYHERTGEKRSEMA-DGAAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 731 PIIAYKAIKLLFKAGLPKGVLQFTPGDGATvGSALVQSPVCKGVIFTGSTEVAGIINQTLASKSSEIVPFiaETGGQNAM 810
Cdd:PRK09457 174 PWVAELTVKLWQQAGLPAGVLNLVQGGRET-GKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEKILAL--EMGGNNPL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 811 IVDSSSLPEQVTGDVIRSAFDSAGQRCS-ALRILCLQEDIADNYIKMIVGAMKELKIGDSkyiDTD----VGPVIDKEAA 885
Cdd:PRK09457 251 VIDEVADIDAAVHLIIQSAFISAGQRCTcARRLLVPQGAQGDAFLARLVAVAKRLTVGRW---DAEpqpfMGAVISEQAA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 886 DNL---NAYIEEKKKQfKLVYQAQPNEDTqkgTFVMPTAFEIEKLSDLGREQ-FGPILHILRFkaNELSKLIKDINSTGY 961
Cdd:PRK09457 328 QGLvaaQAQLLALGGK-SLLEMTQLQAGT---GLLTPGIIDVTGVAELPDEEyFGPLLQVVRY--DDFDEAIRLANNTRF 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 754263081 962 GLTAGVHSRINEVMNYVKNNIKAGNVYVNRNIVGAvVGVQPFGGQGKSG 1010
Cdd:PRK09457 402 GLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGA-SSAAPFGGVGASG 449
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
574-1012 |
1.26e-61 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 218.65 E-value: 1.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWN-NTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAID- 651
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 652 EVREAVDFCRYYAAQARReFNGPIELPALSDHLKQIEFTGR----GAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPA 727
Cdd:cd07089 81 QVDGPIGHLRYFADLADS-FPWEFDLPVPALRGGPGRRVVRrepvGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 728 EQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIInqtLASKSSEIVPFIAETGGQ 807
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRI---MAQAAATLKRVLLELGGK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 808 NAMIVDSSSLPEQVTGDVIRSAFDSAGQRCSAL-RILcLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAAD 886
Cdd:cd07089 237 SANIVLDDADLAAAAPAAVGVCMHNAGQGCALTtRLL-VPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 887 NLNAYIEEKKKQ-FKLVYQAQPNEDTQKGTFVMPTAFeieklSDLG-------REQFGPILHILRFKANElsKLIKDINS 958
Cdd:cd07089 316 RVEGYIARGRDEgARLVTGGGRPAGLDKGFYVEPTLF-----ADVDndmriaqEEIFGPVLVVIPYDDDD--EAVRIAND 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 754263081 959 TGYGLTAGVHSRINEVMNYVKNNIKAGNVYVNrnivGAVVGV--QPFGGQGKSGTG 1012
Cdd:cd07089 389 SDYGLSGGVWSADVDRAYRVARRIRTGSVGIN----GGGGYGpdAPFGGYKQSGLG 440
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
594-1012 |
1.44e-61 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 217.44 E-value: 1.44e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 594 AKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEVREAVDFCRYYAAQARREFNG 673
Cdd:cd07105 2 ADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 674 PIelPALSDhlkqieftGRGAMV---------CISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPIIAYKAIKLLFKA 744
Cdd:cd07105 82 SI--PSDKP--------GTLAMVvkepvgvvlGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 745 GLPKGVLQF---TPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLAsksSEIVPFIAETGGQNAMIV-DSSSLPEQ 820
Cdd:cd07105 152 GLPKGVLNVvthSPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAA---KHLKPVLLELGGKAPAIVlEDADLDAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 821 VTGdVIRSAFDSAGQRC-SALRILcLQEDIADNYIKMIVGAMKELKIGdskyiDTDVGPVIDKEAADNLNAYIEEK-KKQ 898
Cdd:cd07105 229 ANA-ALFGAFLNSGQICmSTERII-VHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDAlSKG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 899 FKLVYQAqPNEDTQKGTFVMPTAFE-IEKLSDLGREQ-FGPILHILRFKANElsKLIKDINSTGYGLTAGVHSR-INEVM 975
Cdd:cd07105 302 AKLVVGG-LADESPSGTSMPPTILDnVTPDMDIYSEEsFGPVVSIIRVKDEE--EAVRIANDSEYGLSAAVFTRdLARAL 378
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 754263081 976 NYVKnNIKAGNVYVNrnivGAVVGVQ---PFGGQGKSGTG 1012
Cdd:cd07105 379 AVAK-RIESGAVHIN----GMTVHDEptlPHGGVKSSGYG 413
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
574-1012 |
2.08e-61 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 217.58 E-value: 2.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAI-DE 652
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 653 VREAVDFCRYYAAqARREFNGPIELPALSDHLKQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPI 732
Cdd:cd07092 81 LPGAVDNFRFFAG-AARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 733 IAYKAIKLLfKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEvAGiiNQTLASKSSEIVPFIAETGGQNAMIV 812
Cdd:cd07092 160 TTLLLAELA-AEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVR-TG--KKVARAAADTLKRVHLELGGKAPVIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 813 -DSSSLPEQVTGdvIRSA-FDSAGQRC-SALRILcLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNLN 889
Cdd:cd07092 236 fDDADLDAAVAG--IATAgYYNAGQDCtAACRVY-VHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 890 AYIEEKKKQFKLVYQAQPNEDtqKGTFVMPT-------AFEIeklsdLGREQFGPILHILRFKanELSKLIKDINSTGYG 962
Cdd:cd07092 313 GFVERAPAHARVLTGGRRAEG--PGYFYEPTvvagvaqDDEI-----VQEEIFGPVVTVQPFD--DEDEAIELANDVEYG 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 754263081 963 LTAGVHSRINEVMNYVKNNIKAGNVYVNRNIVgaVVGVQPFGGQGKSGTG 1012
Cdd:cd07092 384 LASSVWTRDVGRAMRLSARLDFGTVWVNTHIP--LAAEMPHGGFKQSGYG 431
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
575-1012 |
3.75e-61 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 217.21 E-value: 3.75e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 575 INPNTGDTIGTVINADAKMAKRALKNAQSAFE--DWNNTPAsQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDE 652
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFDetDWAHDPR-LRARVLLELADAFEANAERLARLLALENGKILGEARFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 653 VREAVDFCRYYAAQARREFNGPIEL-P-ALSDHLKQieftGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQT 730
Cdd:cd07120 81 ISGAISELRYYAGLARTEAGRMIEPePgSFSLVLRE----PMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 731 PIIAYKAIKLLFKA-GLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIInqtLASKSSEIVPFIAETGGQNA 809
Cdd:cd07120 157 AQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAI---MAAAAPTLKRLGLELGGKTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 810 MIV-DSSSLpEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNL 888
Cdd:cd07120 234 CIVfDDADL-DAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 889 NAYIEEKKKQFK--LVYQAQPNEDTQKGTFVMPTAFEI-EKLSDLGREQ-FGPILHILRFkANElSKLIKDINSTGYGLT 964
Cdd:cd07120 313 DRMVERAIAAGAevVLRGGPVTEGLAKGAFLRPTLLEVdDPDADIVQEEiFGPVLTLETF-DDE-AEAVALANDTDYGLA 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 754263081 965 AGVHSR-INEVMNyVKNNIKAGNVYVN---RNIVGAvvgvqPFGGQGKSGTG 1012
Cdd:cd07120 391 ASVWTRdLARAMR-VARAIRAGTVWINdwnKLFAEA-----EEGGYRQSGLG 436
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
574-1022 |
4.93e-61 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 217.65 E-value: 4.93e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKtlsnAIDEV 653
Cdd:cd07111 41 TINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGK----PIRES 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 654 RE-----AVDFCRYYAAQArrefngpielpalsdHLKQIEFTGRGAM-VC--ISPWNFPLAIFLGQITAVLAAGNTVVAK 725
Cdd:cd07111 117 RDcdiplVARHFYHHAGWA---------------QLLDTELAGWKPVgVVgqIVPWNFPLLMLAWKICPALAMGNTVVLK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 726 PAEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATvGSALVQSPVCKGVIFTGSTEVAGIINQTLASKSSEIVpfiAETG 805
Cdd:cd07111 182 PAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKLS---LELG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 806 GQNAMIV-DSSSLPEQVTGdVIRSAFDSAGQRCSA-LRILcLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKE 883
Cdd:cd07111 258 GKSPFIVfDDADLDSAVEG-IVDAIWFNQGQVCCAgSRLL-VQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 884 AADNLNAYIEEKKKQFKLVYQAqPNEDTQKGTFVMPTAFE-IEKLSDLGREQ-FGPILHILRFKANELSKLIKdiNSTGY 961
Cdd:cd07111 336 QLKRIRELVEEGRAEGADVFQP-GADLPSKGPFYPPTLFTnVPPASRIAQEEiFGPVLVVLTFRTAKEAVALA--NNTPY 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754263081 962 GLTAGVHS-RINEVMNyVKNNIKAGNVYVN-RNIVGAVVgvqPFGGQGKSGTGpKAGGPYYMH 1022
Cdd:cd07111 413 GLAASVWSeNLSLALE-VALSLKAGVVWINgHNLFDAAA---GFGGYRESGFG-REGGKEGLY 470
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
573-1012 |
5.17e-61 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 217.31 E-value: 5.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 573 AVINPNTGDTIGTVINADAKMAKRALKNAQSAFED-WNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKT--LSNA 649
Cdd:cd07113 18 DITNPATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSihLSRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 650 IdEVREAVDFCRYYAAQARReFNGpiELPALSDHLKQIE----FTGR---GAMVCISPWNFPLAIFLGQITAVLAAGNTV 722
Cdd:cd07113 98 F-EVGQSANFLRYFAGWATK-ING--ETLAPSIPSMQGErytaFTRRepvGVVAGIVPWNFSVMIAVWKIGAALATGCTI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 723 VAKPAEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGAtVGSALVQSPVCKGVIFTGSTEVAGIINqtlASKSSEIVPFIA 802
Cdd:cd07113 174 VIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGKKIG---RQAASDLTRVTL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 803 ETGGQNAMIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDK 882
Cdd:cd07113 250 ELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 883 EAADNLNAYIE-EKKKQFKLVYQAqpNEDTQKGTFVMPTAFEIEKLSD--LGREQFGPILHILRFKANElsKLIKDINST 959
Cdd:cd07113 330 PHFDKVCSYLDdARAEGDEIVRGG--EALAGEGYFVQPTLVLARSADSrlMREETFGPVVSFVPYEDEE--ELIQLINDT 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 754263081 960 GYGLTAGVHSR-INEVMNYVKnNIKAGNVYVN-RNIVGAVVgvqPFGGQGKSGTG 1012
Cdd:cd07113 406 PFGLTASVWTNnLSKALRYIP-RIEAGTVWVNmHTFLDPAV---PFGGMKQSGIG 456
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
580-1018 |
1.07e-60 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 215.24 E-value: 1.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 580 GDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEVREAVDF 659
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 660 CRYYAAQARREfNGPIeLPALSDHLKQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPIIAYKAIK 739
Cdd:cd07152 81 LHEAAGLPTQP-QGEI-LPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 740 LLFK-AGLPKGVLQFTPGdGATVGSALVQSPVCKGVIFTGSTEVAGIINQtLASKSSEIVPFiaETGGQNAMIVDSSSLP 818
Cdd:cd07152 159 RLFEeAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGE-AAGRHLKKVSL--ELGGKNALIVLDDADL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 819 EQVTGDVIRSAFDSAGQRC-SALRILcLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNLNAYIEEKKK 897
Cdd:cd07152 235 DLAASNGAWGAFLHQGQICmAAGRHL-VHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 898 QFKLVYQAqpneDTQKGTFVMPT----------AFEieklsdlgREQFGPILHILRFKANElsKLIKDINSTGYGLTAGV 967
Cdd:cd07152 314 AGARLEAG----GTYDGLFYRPTvlsgvkpgmpAFD--------EEIFGPVAPVTVFDSDE--EAVALANDTEYGLSAGI 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 754263081 968 HSR-INEVMNyVKNNIKAGNVYVNRNIVGAVVgVQPFGGQGKSGTGPKAGGP 1018
Cdd:cd07152 380 ISRdVGRAMA-LADRLRTGMLHINDQTVNDEP-HNPFGGMGASGNGSRFGGP 429
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
574-1012 |
2.66e-60 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 215.06 E-value: 2.66e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKtlsnaidev 653
Cdd:cd07138 18 VINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGA--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 654 reAVDFCRyyAAQARRefnGPIELPALSDHLKQIEFTGR-----------GAMVCISPWNFPLaiflGQIT----AVLAA 718
Cdd:cd07138 89 --PITLAR--AAQVGL---GIGHLRAAADALKDFEFEERrgnslvvrepiGVCGLITPWNWPL----NQIVlkvaPALAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 719 GNTVVAKPAEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEvAGIINQTLASKSSEIV 798
Cdd:cd07138 158 GCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTR-AGKRVAEAAADTVKRV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 799 pfIAETGGQNAMIV-DSSSLPEQVTgDVIRSAFDSAGQRCSAL-RILcLQEDIADNYIKMIVGAMKELKIGDSKYIDTDV 876
Cdd:cd07138 237 --ALELGGKSANIIlDDADLEKAVP-RGVAACFANSGQSCNAPtRML-VPRSRYAEAEEIAAAAAEAYVVGDPRDPATTL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 877 GPVIDKEAADNLNAYIEEKKKQ-FKLVY-QAQPNEDTQKGTFVMPTAFeieklSD------LGREQ-FGPILHILRFKAN 947
Cdd:cd07138 313 GPLASAAQFDRVQGYIQKGIEEgARLVAgGPGRPEGLERGYFVKPTVF-----ADvtpdmtIAREEiFGPVLSIIPYDDE 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 754263081 948 ElsKLIKDINSTGYGLTAGVHSRINEVMNYVKNNIKAGNVYVNrnivGAVVGVQ-PFGGQGKSGTG 1012
Cdd:cd07138 388 D--EAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN----GAAFNPGaPFGGYKQSGNG 447
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
575-1016 |
5.08e-60 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 216.21 E-value: 5.08e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 575 INPNTGDTIGTVINADAKMAKRALKNAQSAFED--WNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAID- 651
Cdd:PLN02466 78 LDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKa 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 652 EVREAVDFCRYYAAQARREFNgpIELPALSDHLKQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTP 731
Cdd:PLN02466 158 ELPMFARLFRYYAGWADKIHG--LTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTP 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 732 IIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIInQTLASKSSeIVPFIAETGGQNAMI 811
Cdd:PLN02466 236 LSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIV-LELAAKSN-LKPVTLELGGKSPFI 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 812 VDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYI-KMIVGAMKELkIGDSKYIDTDVGPVIDKEAADNLNA 890
Cdd:PLN02466 314 VCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVeKAKARALKRV-VGDPFKKGVEQGPQIDSEQFEKILR 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 891 YIEEKKKQfKLVYQAQPNEDTQKGTFVMPTAF-EIEKLSDLGREQ-FGPILHILRFKanELSKLIKDINSTGYGLTAGVH 968
Cdd:PLN02466 393 YIKSGVES-GATLECGGDRFGSKGYYIQPTVFsNVQDDMLIAQDEiFGPVQSILKFK--DLDEVIRRANNTRYGLAAGVF 469
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 754263081 969 SRINEVMNYVKNNIKAGNVYVN-RNIVGAVVgvqPFGGQGKSGTGPKAG 1016
Cdd:PLN02466 470 TQNLDTANTLSRALRVGTVWVNcFDVFDAAI---PFGGYKMSGIGREKG 515
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
564-1016 |
8.27e-59 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 211.20 E-value: 8.27e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 564 VDIDKSTAEAVINPNTGDTIGTVINADAKMAKRALKNAQSAFED--WNNTPASQRANILEKFANLLEKNTDEFIAIAMIE 641
Cdd:cd07140 15 VDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELATIESLD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 642 AGKTLSNAID-EVREAVDFCRYYAAQARREFNGPIEL-PALSDHlkQIEFTGRGAM-VC--ISPWNFPLAIFLGQITAVL 716
Cdd:cd07140 95 SGAVYTLALKtHVGMSIQTFRYFAGWCDKIQGKTIPInQARPNR--NLTLTKREPIgVCgiVIPWNYPLMMLAWKMAACL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 717 AAGNTVVAKPAEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKSSE 796
Cdd:cd07140 173 AAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAVSNLK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 797 IVPFiaETGGQNAMIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDV 876
Cdd:cd07140 253 KVSL--ELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDH 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 877 GPVIDKEAADNLNAYIEEKKKQ-FKLVYQAQPNEdtQKGTFVMPTAF-EIEKLSDLGREQ-FGPILHILRFKANELSKLI 953
Cdd:cd07140 331 GPQNHKAHLDKLVEYCERGVKEgATLVYGGKQVD--RPGFFFEPTVFtDVEDHMFIAKEEsFGPIMIISKFDDGDVDGVL 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754263081 954 KDINSTGYGLTAGVHSR-INEVMnYVKNNIKAGNVYVN---RNIVGAvvgvqPFGGQGKSGTGPKAG 1016
Cdd:cd07140 409 QRANDTEYGLASGVFTKdINKAL-YVSDKLEAGTVFVNtynKTDVAA-----PFGGFKQSGFGKDLG 469
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
574-1026 |
1.17e-58 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 210.53 E-value: 1.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEV 653
Cdd:cd07130 16 SISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLGEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 654 REAVDFCRyYAAQARREFNGPI---ELPalsDHLKQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQT 730
Cdd:cd07130 96 QEMIDICD-FAVGLSRQLYGLTipsERP---GHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 731 PIIAYKAIKL----LFKAGLPKGVLQFTPGdGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKSSEIvpfIAETGG 806
Cdd:cd07130 172 PLTAIAVTKIvarvLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGRS---LLELGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 807 QNAMIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAAD 886
Cdd:cd07130 248 NNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAVD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 887 NLNAYIEEKKKQ-FKLVYqaQPNEDTQKGTFVMPTAFEIEKLSDL-GREQFGPILHILRFKanELSKLIKDINSTGYGLT 964
Cdd:cd07130 328 NYLAAIEEAKSQgGTVLF--GGKVIDGPGNYVEPTIVEGLSDAPIvKEETFAPILYVLKFD--TLEEAIAWNNEVPQGLS 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754263081 965 AGVHSR-INEVMNYV-KNNIKAGNVYVNRNIVGAVVGvQPFGGQGKSGTGPKAGG---PYYMHRLAN 1026
Cdd:cd07130 404 SSIFTTdLRNAFRWLgPKGSDCGIVNVNIGTSGAEIG-GAFGGEKETGGGRESGSdawKQYMRRSTC 469
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
564-1019 |
1.43e-58 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 210.53 E-value: 1.43e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 564 VDIDKSTAEAVINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAG 643
Cdd:PRK11241 20 LDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 644 KTLSNAIDEVREAVDFCRYYAAQARREFNGPIELPALSDHLKQIEfTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVV 723
Cdd:PRK11241 100 KPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIK-QPIGVTAAITPWNFPAAMITRKAGPALAAGCTMV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 724 AKPAEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAgiiNQTLASKSSEIVPFIAE 803
Cdd:PRK11241 179 LKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIG---RQLMEQCAKDIKKVSLE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 804 TGGQNAMIV-DSSSLPEQVTGDVIrSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDK 882
Cdd:PRK11241 256 LGGNAPFIVfDDADLDKAVEGALA-SKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 883 EAADNLNAYIEEK-KKQFKLVYQAQPNEdtQKGTFVMPTAF-EIEKLSDLGREQ-FGPILHILRFKanELSKLIKDINST 959
Cdd:PRK11241 335 KAVAKVEEHIADAlEKGARVVCGGKAHE--LGGNFFQPTILvDVPANAKVAKEEtFGPLAPLFRFK--DEADVIAQANDT 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 960 GYGLTAGVHSRINEVMNYVKNNIKAGNVYVNRNIVGAVVGvqPFGGQGKSGTGpKAGGPY 1019
Cdd:PRK11241 411 EFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGIKASGLG-REGSKY 467
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
596-1029 |
2.22e-58 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 208.08 E-value: 2.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 596 RALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEVREAVDFCRYYAAQA----RREf 671
Cdd:cd07100 3 AALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAeaflADE- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 672 ngPIELPALSDHlkqIEFTGRGAMVCISPWNFPL---AIFLGQItavLAAGNTVVAKPAEQTPIIAYKAIKLLFKAGLPK 748
Cdd:cd07100 82 --PIETDAGKAY---VRYEPLGVVLGIMPWNFPFwqvFRFAAPN---LMAGNTVLLKHASNVPGCALAIEELFREAGFPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 749 GVLQFTPGDGATVgSALVQSPVCKGVIFTGStEVAGIINQTLASKssEIVPFIAETGGQNAMIVDSSSLPEQVTGDVIRS 828
Cdd:cd07100 154 GVFQNLLIDSDQV-EAIIADPRVRGVTLTGS-ERAGRAVAAEAGK--NLKKSVLELGGSDPFIVLDDADLDKAVKTAVKG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 829 AFDSAGQRC-SALRILcLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNLNAYIEEKKKQ-FKLVYQAQ 906
Cdd:cd07100 230 RLQNAGQSCiAAKRFI-VHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAgATLLLGGK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 907 PNEdtQKGTFVMPTAFE-IEKLSDLGREQ-FGPILHILRFK----ANELSklikdiNSTGYGLTAGVHSRINEVMNYVKN 980
Cdd:cd07100 309 RPD--GPGAFYPPTVLTdVTPGMPAYDEElFGPVAAVIKVKdeeeAIALA------NDSPFGLGGSVFTTDLERAERVAR 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 754263081 981 NIKAGNVYVNRnIVGAVVGVqPFGGQGKSGTGpKAGGPYYMHRLANEKL 1029
Cdd:cd07100 381 RLEAGMVFING-MVKSDPRL-PFGGVKRSGYG-RELGRFGIREFVNIKT 426
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
574-1012 |
7.52e-58 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 207.93 E-value: 7.52e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEV 653
Cdd:cd07151 14 VLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANIEW 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 654 REAVDFCRYYAAQARREfNGPIeLPALSDHLKQIEFtgR---GAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQT 730
Cdd:cd07151 94 GAAMAITREAATFPLRM-EGRI-LPSDVPGKENRVY--ReplGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 731 PI-----IAykaiKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAgiinQTLASKSSEIVPFIA-ET 804
Cdd:cd07151 170 PItggllLA----KIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVG----RHIGELAGRHLKKVAlEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 805 GGQNAMIVDSSSLPEQVTGDVIRSAFDSAGQRCSAL-RILcLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKE 883
Cdd:cd07151 242 GGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAInRII-VHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINES 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 884 AADNLNAYIEEKKKQ-FKLVYQAQPNedtqkGTFVMPTAF-EIEKLSDLGREQ-FGPILHILRFKANElsKLIKDINSTG 960
Cdd:cd07151 321 QVDGLLDKIEQAVEEgATLLVGGEAE-----GNVLEPTVLsDVTNDMEIAREEiFGPVAPIIKADDEE--EALELANDTE 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 754263081 961 YGLTAGVHSRINEVMNYVKNNIKAGNVYVNRNIVGAVVGVqPFGGQGKSGTG 1012
Cdd:cd07151 394 YGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPHV-PFGGEKNSGLG 444
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
574-1012 |
7.14e-57 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 205.27 E-value: 7.14e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTL--SNAID 651
Cdd:cd07559 20 NYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIreTLAAD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 652 eVREAVDFCRYYAAQARREFNGPIELPA--LSDHLKQ-IEFTGRgamvcISPWNFPLAIFLGQITAVLAAGNTVVAKPAE 728
Cdd:cd07559 100 -IPLAIDHFRYFAGVIRAQEGSLSEIDEdtLSYHFHEpLGVVGQ-----IIPWNFPLLMAAWKLAPALAAGNTVVLKPAS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 729 QTPIIAYKAIKlLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKsseIVPFIAETGGQN 808
Cdd:cd07559 174 QTPLSILVLME-LIGDLLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAEN---LIPVTLELGGKS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 809 AMIVDSSSLPEQ------VTGDVIRSAFDSaGQRCSA-LRILcLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVID 881
Cdd:cd07559 250 PNIFFDDAMDADddfddkAEEGQLGFAFNQ-GEVCTCpSRAL-VQESIYDEFIERAVERFEAIKVGNPLDPETMMGAQVS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 882 KEAADNLNAYIEEKKKQ-FKLVYQAQPNE--DTQKGTFVMPTAFEI--EKLSDLGREQFGPILHILRFKANElsKLIKDI 956
Cdd:cd07559 328 KDQLEKILSYVDIGKEEgAEVLTGGERLTlgGLDKGYFYEPTLIKGgnNDMRIFQEEIFGPVLAVITFKDEE--EAIAIA 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 754263081 957 NSTGYGLTAGVHSR-INEVMNyVKNNIKAGNVYVN-RNIVGAVVgvqPFGGQGKSGTG 1012
Cdd:cd07559 406 NDTEYGLGGGVWTRdINRALR-VARGIQTGRVWVNcYHQYPAHA---PFGGYKKSGIG 459
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
571-1012 |
7.56e-57 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 205.14 E-value: 7.56e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 571 AEAVINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAI 650
Cdd:PRK13473 18 KQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 651 -DEVREAVDFCRYYAAQARReFNGPIELPALSDHLKQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQ 729
Cdd:PRK13473 98 nDEIPAIVDVFRFFAGAARC-LEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 730 TPIIAYKAIKLLFKAgLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLAS--KSSEIvpfiaETGGQ 807
Cdd:PRK13473 177 TPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADsvKRTHL-----ELGGK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 808 NAMIV-DSSSLPEQVTGdvIRS-AFDSAGQRCS-ALRILcLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEA 884
Cdd:PRK13473 251 APVIVfDDADLDAVVEG--IRTfGYYNAGQDCTaACRIY-AQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAAH 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 885 ADNLNAYIEEKKKQ--FKLVYQAQPNEDtqKGTFVMPTA-------FEIEKlsdlgREQFGPILHILRFKanELSKLIKD 955
Cdd:PRK13473 328 RDRVAGFVERAKALghIRVVTGGEAPDG--KGYYYEPTLlagarqdDEIVQ-----REVFGPVVSVTPFD--DEDQAVRW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 754263081 956 INSTGYGLTAGVHSR-INEVMNyVKNNIKAGNVYVNRNIVgaVVGVQPFGGQGKSGTG 1012
Cdd:PRK13473 399 ANDSDYGLASSVWTRdVGRAHR-VSARLQYGCTWVNTHFM--LVSEMPHGGQKQSGYG 453
|
|
| Pro_dh-DNA_bdg |
pfam14850 |
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of ... |
70-180 |
8.52e-57 |
|
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of bifunctional proline-dehydrogenases and is found to bind DNA.
Pssm-ID: 434266 [Multi-domain] Cd Length: 112 Bit Score: 191.56 E-value: 8.52e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 70 IDAFMIEYDLSSEEGIVLMCLAEALLRVPDKYTIDLLIKDKLTSAAWKNHVGREKHLFVNAATWSLMLTGKILK-NPHGA 148
Cdd:pfam14850 1 VEALLQEYSLSSEEGVALMCLAEALLRVPDAATADALIRDKLGRGDWKSHLGHSDSLLVNASTWGLMLTGRLLDdEPEGT 80
|
90 100 110
....*....|....*....|....*....|..
gi 754263081 149 YRKVFQNLLKKSSEPVIRQAMKQAMKIVGKQY 180
Cdd:pfam14850 81 LAGALKRLVGRLGEPVIRKAVRQAMRLMGRQF 112
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
574-1012 |
1.51e-56 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 203.74 E-value: 1.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEV 653
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 654 REAVDFCRYYAAQARR-EFNGPIELPalsdhLKQIEFTGR------GAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKP 726
Cdd:cd07110 81 DDVAGCFEYYADLAEQlDAKAERAVP-----LPSEDFKARvrrepvGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 727 AEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLAsksSEIVPFIAETGG 806
Cdd:cd07110 156 SELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAA---QDIKPVSLELGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 807 QNAMIV-DSSSLpEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAA 885
Cdd:cd07110 233 KSPIIVfDDADL-EKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 886 DNLNAYIEEKKKQ-FKLVYQAQPNEDTQKGTFVMPTAF-EIEKLSDLGREQ-FGPILHILRFKANElsKLIKDINSTGYG 962
Cdd:cd07110 312 EKVLSFIARGKEEgARLLCGGRRPAHLEKGYFIAPTVFaDVPTDSRIWREEiFGPVLCVRSFATED--EAIALANDSEYG 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 754263081 963 LTAGVHSRINEVMNYVKNNIKAGNVYVNrniVGAVVGVQ-PFGGQGKSGTG 1012
Cdd:cd07110 390 LAAAVISRDAERCDRVAEALEAGIVWIN---CSQPCFPQaPWGGYKRSGIG 437
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
574-1020 |
4.28e-56 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 202.09 E-value: 4.28e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEV 653
Cdd:cd07147 3 VTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 654 REAVDFCRYYAAQARReFNGpiELPALSDHLKQIEFTG------RGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPA 727
Cdd:cd07147 83 ARAIDTFRIAAEEATR-IYG--EVLPLDISARGEGRQGlvrrfpIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 728 EQTPIIAYKAIKLLFKAGLPKGVLQFTP--GDGAtvgSALVQSPVCKGVIFTGSTEVaGIINQTLASKSSEIVpfiaETG 805
Cdd:cd07147 160 SRTPLSALILGEVLAETGLPKGAFSVLPcsRDDA---DLLVTDERIKLLSFTGSPAV-GWDLKARAGKKKVVL----ELG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 806 GQNAMIVDSSSLPEQVTGDVIRSAFDSAGQRC-SALRILcLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEA 884
Cdd:cd07147 232 GNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCiSVQRVL-VHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 885 ADNLNAYIEEKKKQ-FKLVYQAqpnedTQKGTFVMPTAFEIEKLSDL--GREQFGPILHILRFkaNELSKLIKDINSTGY 961
Cdd:cd07147 311 AERVEGWVNEAVDAgAKLLTGG-----KRDGALLEPTILEDVPPDMEvnCEEVFGPVVTVEPY--DDFDEALAAVNDSKF 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 962 GLTAGVHSR-INEVMnYVKNNIKAGNVYVNrNIVGAVVGVQPFGGQGKSGTGPKagGPYY 1020
Cdd:cd07147 384 GLQAGVFTRdLEKAL-RAWDELEVGGVVIN-DVPTFRVDHMPYGGVKDSGIGRE--GVRY 439
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
575-991 |
4.70e-56 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 202.09 E-value: 4.70e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 575 INPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEfIAIAM-IEAGKTLSNAIDEV 653
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDE-IAEELtWQMGRPIAQAGGEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 654 REAVDFCRYYAAQARREFnGPIELPALSDHLKQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPII 733
Cdd:cd07102 80 RGMLERARYMISIAEEAL-ADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 734 AYKAIKLLFKAGLPKGVLQFTPGDGATvGSALVQSPVCKGVIFTGSTEVAGIINQTLASKsseivpFIA---ETGGQNAM 810
Cdd:cd07102 159 GERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAGR------FIKvglELGGKDPA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 811 IVDSSSLPEQVTGDVIRSAFDSAGQRCSAL-RILcLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNLN 889
Cdd:cd07102 232 YVRPDADLDAAAESLVDGAFFNSGQSCCSIeRIY-VHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 890 AYIEEKKKQ--FKLVYQAQPNEDTQKGTFVMPTAfeiekLSD-------LGREQFGPILHILRFKANElsKLIKDINSTG 960
Cdd:cd07102 311 AQIADAIAKgaRALIDGALFPEDKAGGAYLAPTV-----LTNvdhsmrvMREETFGPVVGIMKVKSDA--EAIALMNDSE 383
|
410 420 430
....*....|....*....|....*....|.
gi 754263081 961 YGLTAGVHSRINEVMNYVKNNIKAGNVYVNR 991
Cdd:cd07102 384 YGLTASVWTKDIARAEALGEQLETGTVFMNR 414
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
573-1012 |
5.09e-54 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 196.91 E-value: 5.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 573 AVINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTL--SNAI 650
Cdd:cd07117 19 DSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIreTRAV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 651 DeVREAVDFCRYYAAQARREFNGPIELPalSDHLKQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQT 730
Cdd:cd07117 99 D-IPLAADHFRYFAGVIRAEEGSANMID--EDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 731 PIIAYKAIKlLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKsseIVPFIAETGGQNAM 810
Cdd:cd07117 176 SLSLLELAK-IIQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKK---LIPATLELGGKSAN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 811 IV-DSSSLPEQVTGDVIRSAFDSaGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNLN 889
Cdd:cd07117 252 IIfDDANWDKALEGAQLGILFNQ-GQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKIL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 890 AYIEEKKKQFKLVY---QAQPNEDTQKGTFVMPTAFE-IEKLSDLGREQ-FGPILHILRFKANElsKLIKDINSTGYGLT 964
Cdd:cd07117 331 SYVDIAKEEGAKILtggHRLTENGLDKGFFIEPTLIVnVTNDMRVAQEEiFGPVATVIKFKTED--EVIDMANDSEYGLG 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 754263081 965 AGVHSR-INEVMNyVKNNIKAGNVYVNR-NIVGAVVgvqPFGGQGKSGTG 1012
Cdd:cd07117 409 GGVFTKdINRALR-VARAVETGRVWVNTyNQIPAGA---PFGGYKKSGIG 454
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
573-1012 |
4.37e-53 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 194.73 E-value: 4.37e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 573 AVINPNTGDTIGTVINADAKMAKRALKNAQSAFE--DWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAI 650
Cdd:PRK09847 38 ETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 651 -DEVREAVDFCRYYAaQARREFNGPIElPALSDHLKQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQ 729
Cdd:PRK09847 118 rDDIPGAARAIRWYA-EAIDKVYGEVA-TTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 730 TPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAgiiNQTLA-SKSSEIVPFIAETGGQN 808
Cdd:PRK09847 196 SPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTG---KQLLKdAGDSNMKRVWLEAGGKS 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 809 AMIV--DSSSLpEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAAD 886
Cdd:PRK09847 273 ANIVfaDCPDL-QQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHAD 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 887 NLNAYIEEKKKQFKLVYQAQpneDTQKGTFVMPTAF-EIEKLSDLGREQ-FGPILHILRFKANELSKLIKdiNSTGYGLT 964
Cdd:PRK09847 352 SVHSFIREGESKGQLLLDGR---NAGLAAAIGPTIFvDVDPNASLSREEiFGPVLVVTRFTSEEQALQLA--NDSQYGLG 426
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 754263081 965 AGVHSRINEVMNYVKNNIKAGNVYVNRNIVGAVvgVQPFGGQGKSGTG 1012
Cdd:PRK09847 427 AAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDM--TVPFGGYKQSGNG 472
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
574-1018 |
1.31e-52 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 192.40 E-value: 1.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINPNTGDTIGTVINADAKMAKRALKNAQSAFED--WNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAID 651
Cdd:cd07139 18 VVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISWSRR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 652 -EVREAVDFCRYYAAQARrEFNGPIELPALsdhlkqieFTGR--------GAMVCISPWNFPLAIFLGQITAVLAAGNTV 722
Cdd:cd07139 98 aQGPGPAALLRYYAALAR-DFPFEERRPGS--------GGGHvlvrrepvGVVAAIVPWNAPLFLAALKIAPALAAGCTV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 723 VAKPAEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDgATVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKsseIVPFIA 802
Cdd:cd07139 169 VLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPAD-REVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGER---LARVTL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 803 ETGGQNAMIVDSSSLPEQVTGDVIRSAFDSAGQRCSAL-RILCLQEdIADNYIKMIVGAMKELKIGDSKYIDTDVGPVID 881
Cdd:cd07139 245 ELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALtRILVPRS-RYDEVVEALAAAVAALKVGDPLDPATQIGPLAS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 882 KEAADNLNAYIEEKKKQ-FKLVYQAQPNEDTQKGTFVMPTAF-EIEKLSDLGREQ-FGPILHILRFKANElsKLIKDINS 958
Cdd:cd07139 324 ARQRERVEGYIAKGRAEgARLVTGGGRPAGLDRGWFVEPTLFaDVDNDMRIAQEEiFGPVLSVIPYDDED--DAVRIAND 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754263081 959 TGYGLTAGVHSRINEVMNYVKNNIKAGNVYVNrnivGAVVGVQ-PFGGQGKSGTGpKAGGP 1018
Cdd:cd07139 402 SDYGLSGSVWTADVERGLAVARRIRTGTVGVN----GFRLDFGaPFGGFKQSGIG-REGGP 457
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
1058-1306 |
3.34e-50 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 186.63 E-value: 3.34e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1058 KYSITNIVAGEKAKKDKFVDLKS--ADGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERH 1135
Cdd:cd07125 30 EWEAIPIINGEETETGEGAPVIDpaDHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1136 -LIASClVTESNVSVEDAHIQIDKTIQQVAYYCLQAKKEFAHPELlPGPTGEIDELSLKGRGVVVSMSS-SCDLLIrFVG 1213
Cdd:cd07125 110 eLIALA-AAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPEL-PGPTGELNGLELHGRGVFVCISPwNFPLAI-FTG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1214 QTTAALLAGNTVVAKPAYTGSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQAL 1293
Cdd:cd07125 187 QIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRAL 266
|
250
....*....|...
gi 754263081 1294 ALRRGAIIPFVAE 1306
Cdd:cd07125 267 AERDGPILPLIAE 279
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
1086-1306 |
1.07e-49 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 192.72 E-value: 1.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1086 IGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKER-HLIASClvtesnvsvedaHIQIDKTIQQ-V 1163
Cdd:PRK11904 576 VGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRaELIALC------------VREAGKTLQDaI 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1164 A----------YYCLQAKKEFAHPELLPGPTGEIDELSLKGRGVVVSMSS-SCDLLIrFVGQTTAALLAGNTVVAKPAYT 1232
Cdd:PRK11904 644 AevreavdfcrYYAAQARRLFGAPEKLPGPTGESNELRLHGRGVFVCISPwNFPLAI-FLGQVAAALAAGNTVIAKPAEQ 722
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 754263081 1233 GSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALALRRGAIIPFVAE 1306
Cdd:PRK11904 723 TPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRTLAARDGPIVPLIAE 796
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
574-1029 |
1.29e-47 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 177.61 E-value: 1.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNN-TPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDE 652
Cdd:cd07148 3 VVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNwLPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 653 VREAVDFCRYyAAQARREFNG---PIELPALSDHlkQIEFTGR---GAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKP 726
Cdd:cd07148 83 VTRAIDGVEL-AADELGQLGGreiPMGLTPASAG--RIAFTTRepiGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 727 AEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGAtVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKSSeivpfIA-ETG 805
Cdd:cd07148 160 ALATPLSCLAFVDLLHEAGLPEGWCQAVPCENA-VAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPGTR-----CAlEHG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 806 GQNAMIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAA 885
Cdd:cd07148 234 GAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 886 DNLNAYIEEK-KKQFKLVYQAQPNEDTQKGTFVMPTAFEIEKLSDlgREQFGPILHIlrFKANELSKLIKDINSTGYGLT 964
Cdd:cd07148 314 DRVEEWVNEAvAAGARLLCGGKRLSDTTYAPTVLLDPPRDAKVST--QEIFGPVVCV--YSYDDLDEAIAQANSLPVAFQ 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 754263081 965 AGVHSRINEVMNYVKNNIKAGNVYVNRNiVGAVVGVQPFGGQGKSGTGpkAGG-PYYMHRLANEKL 1029
Cdd:cd07148 390 AAVFTKDLDVALKAVRRLDATAVMVNDH-TAFRVDWMPFAGRRQSGYG--TGGiPYTMHDMTQEKM 452
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
575-1023 |
2.25e-47 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 178.10 E-value: 2.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 575 INPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEVR 654
Cdd:PLN02315 39 VNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 655 EAVDFCRyYAAQARREFNGPIELPALSDHLKQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPIIA 734
Cdd:PLN02315 119 EIIDMCD-FAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLIT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 735 YKAIKL----LFKAGLPKGVLQFTPGdGATVGSALVQSPVCKGVIFTGSTEVAGIINQTLASKSSEIvpfIAETGGQNAM 810
Cdd:PLN02315 198 IAMTKLvaevLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKC---LLELSGNNAI 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 811 IV-DSSSLPEQVTGdVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNLN 889
Cdd:PLN02315 274 IVmDDADIQLAVRS-VLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 890 AYIEEKKKQF-KLVYQAQPNEdtQKGTFVMPTAFEIEKLSDLGREQ-FGPILHILRFKAneLSKLIKDINSTGYGLTAGV 967
Cdd:PLN02315 353 KGIEIIKSQGgKILTGGSAIE--SEGNFVQPTIVEISPDADVVKEElFGPVLYVMKFKT--LEEAIEINNSVPQGLSSSI 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754263081 968 HSRINEVM-NYV-KNNIKAGNVYVNRNIVGAVVGvQPFGGQGKSGTGPKAGG---PYYMHR 1023
Cdd:PLN02315 429 FTRNPETIfKWIgPLGSDCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAGSdswKQYMRR 488
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
574-1012 |
2.10e-46 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 174.68 E-value: 2.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAI--D 651
Cdd:PRK13252 26 VINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQETSvvD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 652 EVREAvDFCRYYAAQArrefngpielPALSDhlKQIEFTG-------RGAM-VC--ISPWNFPLAIFLGQITAVLAAGNT 721
Cdd:PRK13252 106 IVTGA-DVLEYYAGLA----------PALEG--EQIPLRGgsfvytrREPLgVCagIGAWNYPIQIACWKSAPALAAGNA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 722 VVAKPAEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGAtVGSALVQSPVCKGVIFTGSTEVAgiiNQTLASKSSEIVPFI 801
Cdd:PRK13252 173 MIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTG---KKVMAAAAASLKEVT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 802 AETGGQNAMIV-DSSSLPEQVTGDVIrSAFDSAGQRCS-ALRILcLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPV 879
Cdd:PRK13252 249 MELGGKSPLIVfDDADLDRAADIAML-ANFYSSGQVCTnGTRVF-VQKSIKAAFEARLLERVERIRIGDPMDPATNFGPL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 880 IDKEAADNLNAYIEEKKKQ-FKLVY--QAQPNEDTQKGTFVMPTAFeiEKLSD---LGREQ-FGPILHILRFKANElsKL 952
Cdd:PRK13252 327 VSFAHRDKVLGYIEKGKAEgARLLCggERLTEGGFANGAFVAPTVF--TDCTDdmtIVREEiFGPVMSVLTFDDED--EV 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 953 IKDINSTGYGLTAGVHSRINEVMNYVKNNIKAGNVYVNRniVGAVVGVQPFGGQGKSGTG 1012
Cdd:PRK13252 403 IARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINT--WGESPAEMPVGGYKQSGIG 460
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
576-1016 |
5.93e-46 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 172.87 E-value: 5.93e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 576 NPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNA-IDEVR 654
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDAsLGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 655 EAVDFCRYYAAqarrefNGPIEL-------PALSDHLK-QIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKP 726
Cdd:cd07098 82 VTCEKIRWTLK------HGEKALrpesrpgGLLMFYKRaRVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 727 AEQT--PIIAYKAI--KLLFKAGLPKGVLQFTPGDGATvGSALVQSPVCKGVIFTGSTEVAGIInqtLASKSSEIVPFIA 802
Cdd:cd07098 156 SEQVawSSGFFLSIirECLAACGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKV---MAAAAESLTPVVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 803 ETGGQNAMIV-DSSSLpEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVID 881
Cdd:cd07098 232 ELGGKDPAIVlDDADL-DQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMIS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 882 KEAADNLNAYIEEKKKQ-FKLVYQAQPNEDTQ--KGTFVMPT-------AFEIEKlsdlgREQFGPILHILRFKANElsK 951
Cdd:cd07098 311 PARFDRLEELVADAVEKgARLLAGGKRYPHPEypQGHYFPPTllvdvtpDMKIAQ-----EEVFGPVMVVMKASDDE--E 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754263081 952 LIKDINSTGYGLTAGVHSRINEVMNYVKNNIKAGNVYVNRNIVGAVVGVQPFGGQGKSGTGPKAG 1016
Cdd:cd07098 384 AVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFGRFAG 448
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
574-1016 |
3.85e-45 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 171.45 E-value: 3.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 574 VINPNTGDTIGTVINADAKMAKRALKNAQSAF-----EDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSN 648
Cdd:PLN02467 27 VVNPATEETIGDIPAATAEDVDAAVEAARKAFkrnkgKDWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 649 A---IDEVREAVDfcrYYAAQAR---REFNGPIELPalsdhlkQIEFTGR------GAMVCISPWNFPLAIFLGQITAVL 716
Cdd:PLN02467 107 AawdMDDVAGCFE---YYADLAEaldAKQKAPVSLP-------METFKGYvlkeplGVVGLITPWNYPLLMATWKVAPAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 717 AAGNTVVAKPAEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIInqtLASKSSE 796
Cdd:PLN02467 177 AAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKI---MTAAAQM 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 797 IVPFIAETGGQNAMIV-DSSSLPEQVTGDVIrSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTD 875
Cdd:PLN02467 254 VKPVSLELGGKSPIIVfDDVDLDKAVEWAMF-GCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 876 VGPVIDKEAADNLNAYIEEKKKQ-FKLVYQAQPNEDTQKGTFVMPTAFEIEKLSD-LGREQ-FGPILHILRFKANElsKL 952
Cdd:PLN02467 333 LGPVVSEGQYEKVLKFISTAKSEgATILCGGKRPEHLKKGFFIEPTIITDVTTSMqIWREEvFGPVLCVKTFSTED--EA 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 953 IKDINSTGYGLTAGVHSRINEVMNYVKNNIKAGNVYVNRNivgavvgvQ------PFGGQGKSGTGPKAG 1016
Cdd:PLN02467 411 IELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCS--------QpcfcqaPWGGIKRSGFGRELG 472
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
620-1012 |
4.53e-45 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 168.76 E-value: 4.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 620 LEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEVREAVDFCRYYAAQARReFNGPIelpALSDHLKQIEFTGR---GAMV 696
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARR-YEGEI---IQSDRPGENILLFKralGVTT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 697 CISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIF 776
Cdd:PRK10090 77 GILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 777 TGSTEvAGIinQTLASKSSEIVPFIAETGGQNAMIV-DSSSLPEQVTGdVIRSAFDSAGQRCSALRILCLQEDIADNYIK 855
Cdd:PRK10090 157 TGSVS-AGE--KIMAAAAKNITKVCLELGGKAPAIVmDDADLDLAVKA-IVDSRVINSGQVCNCAERVYVQKGIYDQFVN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 856 MIVGAMKELKIGD-SKYIDTDVGPVIDKEAADNLNAYIEEKKKQ-FKLVYQAQPNEdtQKGTFVMPTAF-EIEKLSDLGR 932
Cdd:PRK10090 233 RLGEAMQAVQFGNpAERNDIAMGPLINAAALERVEQKVARAVEEgARVALGGKAVE--GKGYYYPPTLLlDVRQEMSIMH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 933 EQ-FGPILHILRFkaNELSKLIKDINSTGYGLTAGVHSRINEVMNYVKNNIKAGNVYVNRNIVGAVVGVQpfGGQGKSGT 1011
Cdd:PRK10090 311 EEtFGPVLPVVAF--DTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFH--AGWRKSGI 386
|
.
gi 754263081 1012 G 1012
Cdd:PRK10090 387 G 387
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
575-1012 |
3.66e-43 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 164.93 E-value: 3.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 575 INPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTdEFIAIA-MIEAGKTLSNAID-E 652
Cdd:cd07116 21 ITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANL-EMLAVAeTWDNGKPVRETLAaD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 653 VREAVDFCRYYAAQARREFNGPIELPA--LSDHLKQieftGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQT 730
Cdd:cd07116 100 IPLAIDHFRYFAGCIRAQEGSISEIDEntVAYHFHE----PLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 731 PIIAYKAIKLLFKAgLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEVAGIINQTlasKSSEIVPFIAETGGQ--- 807
Cdd:cd07116 176 PASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQY---ASENIIPVTLELGGKspn 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 808 ----NAMIVDSSSLPEQVTGDVIrSAFDSaGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKE 883
Cdd:cd07116 252 iffaDVMDADDAFFDKALEGFVM-FALNQ-GEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 884 AADNLNAYIEEKKKQFKLVY----QAQPNEDTQKGTFVMPTAFEIEKLSDLGREQFGPILHILRFKANElsKLIKDINST 959
Cdd:cd07116 330 QLEKILSYIDIGKEEGAEVLtggeRNELGGLLGGGYYVPTTFKGGNKMRIFQEEIFGPVLAVTTFKDEE--EALEIANDT 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 754263081 960 GYGLTAGVHSRINEVMNYVKNNIKAGNVYVnrNIVGAVVGVQPFGGQGKSGTG 1012
Cdd:cd07116 408 LYGLGAGVWTRDGNTAYRMGRGIQAGRVWT--NCYHLYPAHAAFGGYKQSGIG 458
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
573-1012 |
1.12e-39 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 154.13 E-value: 1.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 573 AVINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDE 652
Cdd:PRK09406 4 ATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 653 VREAVDFCRYYAAQARREF-NGPIELPALSDHLKQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTP 731
Cdd:PRK09406 84 ALKCAKGFRYYAEHAEALLaDEPADAAAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 732 IIAYKAIKLLFKAGLPKGVLQfTPGDGATVGSALVQSPVCKGVIFTGStEVAGiinQTLAS-KSSEIVPFIAETGGQNAM 810
Cdd:PRK09406 164 QTALYLADLFRRAGFPDGCFQ-TLLVGSGAVEAILRDPRVAAATLTGS-EPAG---RAVAAiAGDEIKKTVLELGGSDPF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 811 IVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNLNA 890
Cdd:PRK09406 239 IVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 891 YIEEKKKQFKLVYQAQPNEDtQKGTFVMPTAF-EIEKLSDLGREQ-FGPILHILRfkANELSKLIKDINSTGYGLTAGVH 968
Cdd:PRK09406 319 QVDDAVAAGATILCGGKRPD-GPGWFYPPTVItDITPDMRLYTEEvFGPVASLYR--VADIDEAIEIANATTFGLGSNAW 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 754263081 969 SR-INEVMNYVkNNIKAGNVYVNrnivGAVVGVQ--PFGGQGKSGTG 1012
Cdd:PRK09406 396 TRdEAEQERFI-DDLEAGQVFIN----GMTVSYPelPFGGVKRSGYG 437
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
573-990 |
1.91e-36 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 145.28 E-value: 1.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 573 AVINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEfIAIAMI-EAGKTLSNAID 651
Cdd:PLN00412 34 AITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAP-IAECLVkEIAKPAKDAVT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 652 EVREAVDFCRYYAAQARRefngpieLPALSDHLKQIEFTGR-------------GAMVCISPWNFPLAIFLGQITAVLAA 718
Cdd:PLN00412 113 EVVRSGDLISYTAEEGVR-------ILGEGKFLVSDSFPGNernkycltskiplGVVLAIPPFNYPVNLAVSKIAPALIA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 719 GNTVVAKPAEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFT-GSTEVAgiinqtlASKSSEI 797
Cdd:PLN00412 186 GNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTgGDTGIA-------ISKKAGM 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 798 VPFIAETGGQNAMIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYiDTDVG 877
Cdd:PLN00412 259 VPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPED-DCDIT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 878 PVIDKEAADNLNAYIEEKKKQFKLVYQaqpnEDTQKGTFVMPTAfeIEKLSDLGR----EQFGPILHILRFKANElsKLI 953
Cdd:PLN00412 338 PVVSESSANFIEGLVMDAKEKGATFCQ----EWKREGNLIWPLL--LDNVRPDMRiaweEPFGPVLPVIRINSVE--EGI 409
|
410 420 430
....*....|....*....|....*....|....*...
gi 754263081 954 KDINSTGYGLTAGVHSR-INEVMnYVKNNIKAGNVYVN 990
Cdd:PLN00412 410 HHCNASNFGLQGCVFTRdINKAI-LISDAMETGTVQIN 446
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
586-1012 |
2.20e-35 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 142.09 E-value: 2.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 586 VINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIA------------IAMIEAGKTLSNaIDEV 653
Cdd:PTZ00381 1 QEPDNPEIIPPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEavhkdlgrhpfeTKMTEVLLTVAE-IEHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 654 REAVDfcRYyaaqARREfngPIELPALSDHLKQ-IEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPI 732
Cdd:PTZ00381 80 LKHLD--EY----LKPE---KVDTVGVFGPGKSyIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 733 IAyKAIKLLFKAGLPKGVLQFTPGdGATVGSALVQSPVcKGVIFTGSTEVAGIINQTLASKsseIVPFIAETGGQNAMIV 812
Cdd:PTZ00381 151 TS-KLMAKLLTKYLDPSYVRVIEG-GVEVTTELLKEPF-DHIFFTGSPRVGKLVMQAAAEN---LTPCTLELGGKSPVIV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 813 DSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELkIGDSKYIDTDVGPVIDKEAADNLNAYI 892
Cdd:PTZ00381 225 DKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAELI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 893 EEKKKQFklVYQAQPNEDTQkgtFVMPTAFEIEKLSD--LGREQFGPILHILRFKanELSKLIKDINSTGYGLTAGVHSR 970
Cdd:PTZ00381 304 KDHGGKV--VYGGEVDIENK---YVAPTIIVNPDLDSplMQEEIFGPILPILTYE--NIDEVLEFINSRPKPLALYYFGE 376
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 754263081 971 INEVMNYVKNNIKAGNVYVNRNIVGAVVGVQPFGGQGKSGTG 1012
Cdd:PTZ00381 377 DKRHKELVLENTSSGAVVINDCVFHLLNPNLPFGGVGNSGMG 418
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
698-1012 |
2.90e-35 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 140.35 E-value: 2.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 698 ISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPIIAyKAIKLLFKAGLPKGVLQFTPGdGATVGSALVQSPVCKgVIFT 777
Cdd:cd07087 107 IGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATS-ALLAKLIPKYFDPEAVAVVEG-GVEVATALLAEPFDH-IFFT 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 778 GSTEVAGIINQtLASKSseIVPFIAETGGQNAMIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMI 857
Cdd:cd07087 184 GSPAVGKIVME-AAAKH--LTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIKDELIEEL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 858 VGAMKELkIGDSKYIDTDVGPVIDKEAADNLNAYIEekkkQFKLVYQAQPNEDTQkgtFVMPTAFEIEKLSD--LGREQF 935
Cdd:cd07087 261 KKAIKEF-YGEDPKESPDYGRIINERHFDRLASLLD----DGKVVIGGQVDKEER---YIAPTILDDVSPDSplMQEEIF 332
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754263081 936 GPILHILRFkaNELSKLIKDINSTGYGLTAGVHSRINEVMNYVKNNIKAGNVYVNRNIVGAVVGVQPFGGQGKSGTG 1012
Cdd:cd07087 333 GPILPILTY--DDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGGVGNSGMG 407
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
562-990 |
2.96e-35 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 143.73 E-value: 2.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 562 SNVDIDKSTAEAVINPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIE 641
Cdd:PLN02419 121 SFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 642 AGKTLSNAIDEVREAVDFCRYYAAQARREFNGpiELPALSDHLKQI---EFTGRGAMVCisPWNFPLAIFLGQITAVLAA 718
Cdd:PLN02419 201 QGKTLKDSHGDIFRGLEVVEHACGMATLQMGE--YLPNVSNGVDTYsirEPLGVCAGIC--PFNFPAMIPLWMFPVAVTC 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 719 GNTVVAKPAEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVgSALVQSPVCKGVIFTGSTEVAGIINQTLASKSSEIV 798
Cdd:PLN02419 277 GNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQ 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 799 pfiAETGGQNAMIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDiADNYIKMIVGAMKELKIGDSKYIDTDVGP 878
Cdd:PLN02419 356 ---SNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGD-AKSWEDKLVERAKALKVTCGSEPDADLGP 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 879 VIDKEAADNLNAYIEEK-KKQFKLVYQAQ----PNedTQKGTFVMPTAFE--IEKLSDLGREQFGPILHILrfKANELSK 951
Cdd:PLN02419 432 VISKQAKERICRLIQSGvDDGAKLLLDGRdivvPG--YEKGNFIGPTILSgvTPDMECYKEEIFGPVLVCM--QANSFDE 507
|
410 420 430
....*....|....*....|....*....|....*....
gi 754263081 952 LIKDINSTGYGLTAGVHSRINEVMNYVKNNIKAGNVYVN 990
Cdd:PLN02419 508 AISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
692-1012 |
3.17e-34 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 137.35 E-value: 3.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 692 RGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPIIAyKAIKLLFKAGLPKGVLQFTPGDGATVGsALVQSPVC 771
Cdd:cd07135 109 LGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTA-ALLAELVPKYLDPDAFQVVQGGVPETT-ALLEQKFD 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 772 KgVIFTGSTEVAGIINQTlASKSseIVPFIAETGGQNAMIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIAD 851
Cdd:cd07135 187 K-IFYTGSGRVGRIIAEA-AAKH--LTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYD 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 852 NYIKMIVGAMKELKIGDSKYiDTDVGPVIDKEAADNLNAYIEEKKKqfKLVYQAQPNEDTQkgtFVMPTAFEIEKLSD-- 929
Cdd:cd07135 263 EFVEELKKVLDEFYPGGANA-SPDYTRIVNPRHFNRLKSLLDTTKG--KVVIGGEMDEATR---FIPPTIVSDVSWDDsl 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 930 LGREQFGPILHILrfKANELSKLIKDINSTGYGLTAGVHSRINEVMNYVKNNIKAGNVYVNRNIVGAVVGVQPFGGQGKS 1009
Cdd:cd07135 337 MSEELFGPVLPII--KVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNAPFGGVGDS 414
|
...
gi 754263081 1010 GTG 1012
Cdd:cd07135 415 GYG 417
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
1081-1306 |
1.00e-33 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 136.51 E-value: 1.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1081 ADGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDKTI 1160
Cdd:pfam00171 15 ATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGEVDRAI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1161 QQVAYYCLQAKKEfaHPELLPGPTGEIDELSLKGRGVVVSMSSSCDLLIRFVGQTTAALLAGNTVVAKPAYTGSLTAYNI 1240
Cdd:pfam00171 95 DVLRYYAGLARRL--DGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 754263081 1241 VKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALALRrgaIIPFVAE 1306
Cdd:pfam00171 173 AELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQN---LKRVTLE 235
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
575-1012 |
1.79e-33 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 135.76 E-value: 1.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 575 INPNTGDTIGTVINADAKMAKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEVR 654
Cdd:PRK13968 12 VNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 655 EAVDFCRYYAAqarrefNGPIEL---PALSDHLKQ-IEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQT 730
Cdd:PRK13968 92 KSANLCDWYAE------HGPAMLkaePTLVENQQAvIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 731 PIIAYKAIKLLFKAGLPKGVLQFTPGDGATVgSALVQSPVCKGVIFTGSTEVAGIINqtlASKSSEIVPFIAETGGQNAM 810
Cdd:PRK13968 166 MGCAQLIAQVFKDAGIPQGVYGWLNADNDGV-SQMINDSRIAAVTVTGSVRAGAAIG---AQAGAALKKCVLELGGSDPF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 811 IV-DSSSLPEQVTGDVIrSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNLN 889
Cdd:PRK13968 242 IVlNDADLELAVKAAVA-GRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 890 AYIEEKKKQ-FKLVYQAQPNEDtqKGTFVMPTAFE--IEKLSDLGREQFGPILHILRFKANELSklIKDINSTGYGLTAG 966
Cdd:PRK13968 321 HQVEATLAEgARLLLGGEKIAG--AGNYYAPTVLAnvTPEMTAFREELFGPVAAITVAKDAEHA--LELANDSEFGLSAT 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 754263081 967 VHSRINEVMNYVKNNIKAGNVYVNRniVGAVVGVQPFGGQGKSGTG 1012
Cdd:PRK13968 397 IFTTDETQARQMAARLECGGVFING--YCASDARVAFGGVKKSGFG 440
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
1080-1351 |
2.77e-33 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 135.78 E-value: 2.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1080 SADGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEK-ERHLIASClVTESNVSVEDAHIQIDK 1158
Cdd:cd07083 40 FAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRrRRELIATL-TYEVGKNWVEAIDDVAE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1159 TIQQVAYYCLQAKKEFAHPELLPGPTGEIDELSLKGRGVVVSMSSSCDLLIRFVGQTTAALLAGNTVVAKPAYTGSLTAY 1238
Cdd:cd07083 119 AIDFIRYYARAALRLRYPAVEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGY 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1239 NIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALA---LRRGAIIPFVAESvakDGKCT 1315
Cdd:cd07083 199 KVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAArlaPGQTWFKRLYVET---GGKNA 275
|
250 260 270
....*....|....*....|....*....|....*.
gi 754263081 1316 SLAIETASPlylrRFVVEKTVSVDTTASGGNASLMS 1351
Cdd:cd07083 276 IIVDETADF----ELVVEGVVVSAFGFQGQKCSAAS 307
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
686-1028 |
3.40e-32 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 131.19 E-value: 3.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 686 QIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTP---IIAYKAIKLLFKaglPKGVLQFTpGDgATVG 762
Cdd:cd07134 95 KIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPhtsAVIAKIIREAFD---EDEVAVFE-GD-AEVA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 763 SALVQSPVcKGVIFTGSTEVAGIInQTLASKSSEIVPFiaETGGQNAMIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRI 842
Cdd:cd07134 170 QALLELPF-DHIFFTGSPAVGKIV-MAAAAKHLASVTL--ELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 843 LCLQEDIADNYIKMIVGAMKELKIGDSKYIDT-DVGPVIDKEAADNLNAYIEE-KKKQFKLVYQAQPNEDTQkgtFVMPT 920
Cdd:cd07134 246 VFVHESVKDAFVEHLKAEIEKFYGKDAARKASpDLARIVNDRHFDRLKGLLDDaVAKGAKVEFGGQFDAAQR---YIAPT 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 921 AfeiekLSDLGR-------EQFGPILHILRFKanELSKLIKDINSTGYGLTAGVHSRINEVMNYVKNNIKAGNVYVNRNI 993
Cdd:cd07134 323 V-----LTNVTPdmkimqeEIFGPVLPIITYE--DLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVV 395
|
330 340 350
....*....|....*....|....*....|....*
gi 754263081 994 VGAVVGVQPFGGQGKSGTGpKAGGPYYMHRLANEK 1028
Cdd:cd07134 396 LHFLNPNLPFGGVNNSGIG-SYHGVYGFKAFSHER 429
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
596-1023 |
6.20e-31 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 127.74 E-value: 6.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 596 RALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEVREAVDFcRYYA--AQARREFNG 673
Cdd:cd07084 3 RALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQL-RARAfvIYSYRIPHE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 674 PIE-LPALSDHLKQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPIIAYKAIKLLFKAG-LPKGVL 751
Cdd:cd07084 82 PGNhLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 752 QFTPGDGATvGSALVQSPVCKGVIFTGSTEVAgiinQTLASKSSEIvPFIAETGGQNAMIVDSSSlPEQ--VTGDVIRSA 829
Cdd:cd07084 162 TLINGDGKT-MQALLLHPNPKMVLFTGSSRVA----EKLALDAKQA-RIYLELAGFNWKVLGPDA-QAVdyVAWQCVQDM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 830 FDSAGQRCSALRILCLQEDIAdnyIKMIVGAMKELkIGDSKYIDTDVGPVIdkeaADNLNAYIEEKKKQFKLVYQAQPNE 909
Cdd:cd07084 235 TACSGQKCTAQSMLFVPENWS---KTPLVEKLKAL-LARRKLEDLLLGPVQ----TFTTLAMIAHMENLLGSVLLFSGKE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 910 ------DTQKGTFVMPTAF----EIEKLSDL-GREQFGPILHILRFKANELSKLIKDINSTGYGLTAGVHSRINEVMNYV 978
Cdd:cd07084 307 lknhsiPSIYGACVASALFvpidEILKTYELvTEEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYSNDPIFLQEL 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 754263081 979 KNNI-KAGNVY-VNRNIVGAVVGVQPFGGQGKSGTGPKAGGPYYMHR 1023
Cdd:cd07084 387 IGNLwVAGRTYaILRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIKL 433
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
1086-1307 |
1.31e-29 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 125.02 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1086 IGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDKTIQQVAY 1165
Cdd:TIGR01238 65 VGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRY 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1166 YCLQAKKEFahpellpgptgeiDELSLKGRGVVVSMSSSCDLLIRFVGQTTAALLAGNTVVAKPAYTGSLTAYNIVKLML 1245
Cdd:TIGR01238 145 YAKQVRDVL-------------GEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQ 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 754263081 1246 KAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALALRRGAIIPFVAES 1307
Cdd:TIGR01238 212 EAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLIAET 273
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
1081-1306 |
2.29e-28 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 120.62 E-value: 2.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1081 ADGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDKTI 1160
Cdd:COG1012 29 ATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARGEVDRAA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1161 QQVAYYCLQAKKefAHPELLPGPTGEIDELSLKG-RGVVVSMS---SSCDLLIRFVGqttAALLAGNTVVAKPAYTGSLT 1236
Cdd:COG1012 109 DFLRYYAGEARR--LYGETIPSDAPGTRAYVRREpLGVVGAITpwnFPLALAAWKLA---PALAAGNTVVLKPAEQTPLS 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1237 AYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALALRrgaIIPFVAE 1306
Cdd:COG1012 184 ALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAEN---LKRVTLE 250
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
1098-1306 |
1.39e-26 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 114.61 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1098 DKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDKTIQQVAYYCLQAKKEFAhP 1177
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHG-E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1178 ELLPGPTGEIDELSLKGRGVVVSMSSSCDLLIRFVGQTTAALLAGNTVVAKPAYTGSLTAYNIVKLMLKAGVDPKVINLI 1257
Cdd:cd07078 80 VIPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 754263081 1258 LSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALALRrgaIIPFVAE 1306
Cdd:cd07078 160 TGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAEN---LKRVTLE 205
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
1064-1282 |
2.50e-26 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 115.01 E-value: 2.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1064 IVAGEKAK-KDKFVDLKSAD-GKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCL 1141
Cdd:cd07124 36 VIGGKEVRtEEKIESRNPADpSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1142 VTESNVSVEDAHIQIDKTIQQVAYYCLQAKKefAHPELLPGPTGEIDELSLKGRGVVVSMSSSCDLLIRFVGQTTAALLA 1221
Cdd:cd07124 116 VLEVGKNWAEADADVAEAIDFLEYYAREMLR--LRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVT 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754263081 1222 GNTVVAKPAYTGSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGS 1282
Cdd:cd07124 194 GNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGS 254
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
594-1012 |
9.56e-25 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 109.04 E-value: 9.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 594 AKRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGK-TLSNAIDEVREAVDFCRYYAAQ-----A 667
Cdd:cd07137 1 APRLVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKpSAESFRDEVSVLVSSCKLAIKElkkwmA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 668 RREFNGPIE-LPALSdhlkQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPIIAyKAIKLLFKAGL 746
Cdd:cd07137 81 PEKVKTPLTtFPAKA----EIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATS-ALLAKLIPEYL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 747 PKGVLQFTPGdGATVGSALVQSPVCKgVIFTGSTEVAGIInqtLASKSSEIVPFIAETGGQNAMIVDSSSLPEQVTGDVI 826
Cdd:cd07137 156 DTKAIKVIEG-GVPETTALLEQKWDK-IFFTGSPRVGRII---MAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 827 RSAFDS-AGQRCSALRILCLQEDIADNYIKMIVGAMKELkIGDSKYIDTDVGPVIDKEAADNLNAYIEEKKKQFKLVYQA 905
Cdd:cd07137 231 GGKWGCnNGQACIAPDYVLVEESFAPTLIDALKNTLEKF-FGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 906 QPNEDTQK--GTFVMPTAFEIEKLSDlgrEQFGPILHILRFKANELSklIKDINSTGYGLTAGVHSRINEVMNYVKNNIK 983
Cdd:cd07137 310 ERDEKNLYiePTILLDPPLDSSIMTE---EIFGPLLPIITVKKIEES--IEIINSRPKPLAAYVFTKNKELKRRIVAETS 384
|
410 420
....*....|....*....|....*....
gi 754263081 984 AGNVYVNRNIVGAVVGVQPFGGQGKSGTG 1012
Cdd:cd07137 385 SGGVTFNDTVVQYAIDTLPFGGVGESGFG 413
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
596-837 |
7.03e-24 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 106.86 E-value: 7.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 596 RALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEVREAVDFCRYYAAQARR-EFNGP 674
Cdd:cd07129 3 AAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVREgSWLDA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 675 IELPALSD-------HLKQIeFTGRGAMVCISPWNFPLAiF--LGQITA-VLAAGNTVVAK--PA-----EQTPIIAYKA 737
Cdd:cd07129 83 RIDPADPDrqplprpDLRRM-LVPLGPVAVFGASNFPLA-FsvAGGDTAsALAAGCPVVVKahPAhpgtsELVARAIRAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 738 IKllfKAGLPKGVLQFTPGDGATVGSALVQSPVCKGVIFTGSTEvAGIINQTLASKSSEIVPFIAETGGQNAMIVdsssL 817
Cdd:cd07129 161 LR---ATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRR-GGRALFDAAAARPEPIPFYAELGSVNPVFI----L 232
|
250 260
....*....|....*....|....*..
gi 754263081 818 PEQVT--GDVIRSAFD-----SAGQRC 837
Cdd:cd07129 233 PGALAerGEAIAQGFVgsltlGAGQFC 259
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
1110-1306 |
2.67e-23 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 103.46 E-value: 2.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1110 AWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDKTIQQVAYYCLQAKKEFAHPELLPGPTGEIdE 1189
Cdd:cd06534 9 AWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPGGEA-Y 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1190 LSLKGRGVVVSMSSSCDLLIRFVGQTTAALLAGNTVVAKPAYTGSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALL 1269
Cdd:cd06534 88 VRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAALL 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 754263081 1270 FNSKVALVTFSGSISAVKQVHQALALRrgaIIPFVAE 1306
Cdd:cd06534 168 SHPRVDKISFTGSTAVGKAIMKAAAEN---LKPVTLE 201
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
1068-1294 |
5.58e-23 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 104.27 E-value: 5.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1068 EKAKKDKFVD-LKSADGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESN 1146
Cdd:cd07088 7 VPSSSGETIDvLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1147 VSVEDAHIQIDKTIQQVAYYCLQAKKefAHPELLPG-PTGEIDELSLKGRGVVVSMSS---SCDLLIRFVGqttAALLAG 1222
Cdd:cd07088 87 KTLSLARVEVEFTADYIDYMAEWARR--IEGEIIPSdRPNENIFIFKVPIGVVAGILPwnfPFFLIARKLA---PALVTG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 754263081 1223 NTVVAKPAYTGSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALA 1294
Cdd:cd07088 162 NTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAA 233
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
698-1012 |
6.86e-22 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 100.66 E-value: 6.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 698 ISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPIIAyKAIKLLFKAGLPKGVLQFTPGdGATVGSALVQSPVCKgVIFT 777
Cdd:cd07136 107 IAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTS-KVIAKIIEETFDEEYVAVVEG-GVEENQELLDQKFDY-IFFT 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 778 GSTEVAGIINQtLASKssEIVPFIAETGGQNAMIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMI 857
Cdd:cd07136 184 GSVRVGKIVME-AAAK--HLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVKEKFIKEL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 858 VGAMKELkIGDSKYIDTDVGPVIDKEAADNLNAYIEEKkkqfKLVYQAQPNEDTQKgtfVMPTAFEIEKLSD--LGREQF 935
Cdd:cd07136 261 KEEIKKF-YGEDPLESPDYGRIINEKHFDRLAGLLDNG----KIVFGGNTDRETLY---IEPTILDNVTWDDpvMQEEIF 332
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754263081 936 GPILHILRFKanELSKLIKDINSTGYGLTAGVHSRINEVMNYVKNNIKAGNVYVNRNIVGAVVGVQPFGGQGKSGTG 1012
Cdd:cd07136 333 GPILPVLTYD--TLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYLPFGGVGNSGMG 407
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
1082-1297 |
8.47e-22 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 100.36 E-value: 8.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1082 DGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDKTIQ 1161
Cdd:cd07149 8 DGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDRAIE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1162 QVAYYCLQAKKefAHPELLPG---PTGEidelslkGR---------GVVVSMS---SSCDLLIRFVGqttAALLAGNTVV 1226
Cdd:cd07149 88 TLRLSAEEAKR--LAGETIPFdasPGGE-------GRigftirepiGVVAAITpfnFPLNLVAHKVG---PAIAAGNAVV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754263081 1227 AKPAYTGSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALALRR 1297
Cdd:cd07149 156 LKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLKK 226
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
615-1025 |
6.22e-21 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 98.11 E-value: 6.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 615 QRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDeVREAVDFCRYYAAQARREFN-------GPIElpALSdhlKQI 687
Cdd:cd07128 60 ERAAMLKALAKYLMERKEDLYALSAATGATRRDSWID-IDGGIGTLFAYASLGRRELPnahflveGDVE--PLS---KDG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 688 EFTGR-------GAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPIIAYKAIKLLFKAG-LPKGVLQFTPGDGA 759
Cdd:cd07128 134 TFVGQhiltprrGVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGSVG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 760 TVGSALVQSPVckgVIFTGSTEVAGII--NQTLASKSseiVPFIAETGGQNAMIVDSSSLPEQVTGD-----VIRSAFDS 832
Cdd:cd07128 214 DLLDHLGEQDV---VAFTGSAATAAKLraHPNIVARS---IRFNAEADSLNAAILGPDATPGTPEFDlfvkeVAREMTVK 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 833 AGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNLNAYIEEKKKQFKLVYQAQPNE--- 909
Cdd:cd07128 288 AGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFevv 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 910 --DTQKGTFVMPTAFEIEKLSDLGR----EQFGPILHILRFK-ANELSKLIKdinsTGYG-LTAGVHSRINEVMNYVKNN 981
Cdd:cd07128 368 gaDAEKGAFFPPTLLLCDDPDAATAvhdvEAFGPVATLMPYDsLAEAIELAA----RGRGsLVASVVTNDPAFARELVLG 443
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 754263081 982 IKA--GNVYV-NRNIVGAVVG---VQP---FGGQGKSGTGPKAGG----PYYMHRLA 1025
Cdd:cd07128 444 AAPyhGRLLVlNRDSAKESTGhgsPLPqlvHGGPGRAGGGEELGGlrgvKHYMQRTA 500
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
693-1012 |
1.32e-20 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 97.10 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 693 GAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTP---------IIAY---KAIKllfkaglpkgVLQftpgDGAT 760
Cdd:PLN02203 110 GVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPatsaflaanIPKYldsKAVK----------VIE----GGPA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 761 VGSALVQSPVCKgVIFTGSTEVAGIInqtLASKSSEIVPFIAETGGQNAMIVDSSSLP---EQVTGDVIRSAFDS-AGQR 836
Cdd:PLN02203 176 VGEQLLQHKWDK-IFFTGSPRVGRII---MTAAAKHLTPVALELGGKCPCIVDSLSSSrdtKVAVNRIVGGKWGScAGQA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 837 CSALRILCLQEDIADNYIKMIVGAMKELkIGDSKYIDTDVGPVIDKEAADNLNAYIEEKKKQFKLVYQAQPNEDTqkgTF 916
Cdd:PLN02203 252 CIAIDYVLVEERFAPILIELLKSTIKKF-FGENPRESKSMARILNKKHFQRLSNLLKDPRVAASIVHGGSIDEKK---LF 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 917 VMPTAFEIEKL-SDLGREQ-FGPILHILRFKANELSklIKDINSTGYGLTAGVHSRINEVMNYVKNNIKAGNVYVNRNIV 994
Cdd:PLN02203 328 IEPTILLNPPLdSDIMTEEiFGPLLPIITVKKIEDS--IAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAII 405
|
330
....*....|....*...
gi 754263081 995 GAVVGVQPFGGQGKSGTG 1012
Cdd:PLN02203 406 QYACDSLPFGGVGESGFG 423
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
595-1012 |
6.78e-20 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 94.21 E-value: 6.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 595 KRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFI-AIAM------IEAGKT-LSNAIDEVREAVDFCRYYAAQ 666
Cdd:cd07132 1 AEAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVeALAKdlrkpkFEAVLSeILLVKNEIKYAISNLPEWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 667 ARrefnGPIELPALSDHLkQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPIIAyKAIKLLFKAGL 746
Cdd:cd07132 81 EP----VKKNLATLLDDV-YIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATA-KLLAELIPKYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 747 PKGVLQFTPGdGATVGSALVQSPVCKgVIFTGSTEVAGIINQTlASKssEIVPFIAETGGQNAMIVDSSSLPEQVTGDVI 826
Cdd:cd07132 155 DKECYPVVLG-GVEETTELLKQRFDY-IFYTGSTSVGKIVMQA-AAK--HLTPVTLELGGKSPCYVDKSCDIDVAARRIA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 827 RSAFDSAGQRCSALR-ILCLQEdIADNYIKMIVGAMKELKIGDSKYiDTDVGPVIDKEAADNLNAYIEEKkkqfKLVYQA 905
Cdd:cd07132 230 WGKFINAGQTCIAPDyVLCTPE-VQEKFVEALKKTLKEFYGEDPKE-SPDYGRIINDRHFQRLKKLLSGG----KVAIGG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 906 QPNEDTQkgtFVMPTAFEIEKLSD--LGREQFGPILHILrfKANELSKLIKDINSTGYGLTAGVHSRINEVMNYVKNNIK 983
Cdd:cd07132 304 QTDEKER---YIAPTVLTDVKPSDpvMQEEIFGPILPIV--TVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTS 378
|
410 420
....*....|....*....|....*....
gi 754263081 984 AGNVYVNRNIVGAVVGVQPFGGQGKSGTG 1012
Cdd:cd07132 379 SGGVCVNDTIMHYTLDSLPFGGVGNSGMG 407
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
1062-1311 |
6.93e-20 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 94.56 E-value: 6.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1062 TNIVAGE-KAKKDKFVDLKS-ADGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINA-EDRALIVEKFLDLLEKERHLIA 1138
Cdd:cd07082 3 KYLINGEwKESSGKTIEVYSpIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPlEERIDCLHKFADLLKENKEEVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1139 SCLVTESNVSVEDAHIQIDKTIQQVAYYCLQAKKEfaHPELLPGPtGEIDELSLKGR------GVVVSMSSSCDLLIRFV 1212
Cdd:cd07082 83 NLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRL--DGDSLPGD-WFPGTKGKIAQvrreplGVVLAIGPFNYPLNLTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1213 GQTTAALLAGNTVVAKPAYTGSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSisavkqVHQA 1292
Cdd:cd07082 160 SKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGS------TEVG 233
|
250 260
....*....|....*....|
gi 754263081 1293 LALRR-GAIIPFVAESVAKD 1311
Cdd:cd07082 234 NRLKKqHPMKRLVLELGGKD 253
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
1064-1282 |
1.01e-19 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 94.62 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1064 IVAGEKAK-KDKFVDLKSADGKN-IGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCL 1141
Cdd:PRK03137 40 IIGGERITtEDKIVSINPANKSEvVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1142 VTESNVSVEDAHIQIDKTIQQVAYYCLQAKKEFAHPELLPGPtGEIDELSLKGRGVVVSMSSSCDLLIRFVGQTTAALLA 1221
Cdd:PRK03137 120 VKEAGKPWAEADADTAEAIDFLEYYARQMLKLADGKPVESRP-GEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVA 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754263081 1222 GNTVVAKPAYTGSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGS 1282
Cdd:PRK03137 199 GNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGS 259
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
1082-1300 |
3.27e-19 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 92.50 E-value: 3.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1082 DGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDKTIQ 1161
Cdd:cd07094 8 DGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRAID 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1162 QVAYYCLQAKKEFAhpELLPGP--TGEIDELSLKGR---GVVVSMSSSCDLLIRFVGQTTAALLAGNTVVAKPAYTGSLT 1236
Cdd:cd07094 88 TLRLAAEEAERIRG--EEIPLDatQGSDNRLAWTIRepvGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 754263081 1237 AYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALALRRGAI 1300
Cdd:cd07094 166 ALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKRIAL 229
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
1081-1282 |
4.52e-19 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 91.72 E-value: 4.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1081 ADGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDKTI 1160
Cdd:cd07103 5 ATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVDYAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1161 QQVAYYCLQAKKefAHPELLPGPTGEIDELSLKGR-GVVV---------SMssscdlLIRFVGqttAALLAGNTVVAKPA 1230
Cdd:cd07103 85 SFLEWFAEEARR--IYGRTIPSPAPGKRILVIKQPvGVVAaitpwnfpaAM------ITRKIA---PALAAGCTVVLKPA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 754263081 1231 YTGSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGS 1282
Cdd:cd07103 154 EETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGS 205
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
595-1012 |
5.80e-19 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 91.39 E-value: 5.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 595 KRALKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFI-AIA------------MIEAGKTLsNAIDEVREAVDfcR 661
Cdd:cd07133 1 QALLERQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAeAISadfghrsrhetlLAEILPSI-AGIKHARKHLK--K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 662 YYAAQARRefNGPIELPALSdhlkQIEFTGRGAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPIIAyKAIKLL 741
Cdd:cd07133 78 WMKPSRRH--VGLLFLPAKA----EVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTS-ALLAEL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 742 FKAGLPKGVLQFTPGdGATVGSALVQSPVCKgVIFTGSTEVAGIInqtLASKSSEIVPFIAETGGQNAMIVDSSSLPEQV 821
Cdd:cd07133 151 LAEYFDEDEVAVVTG-GADVAAAFSSLPFDH-LLFTGSTAVGRHV---MRAAAENLTPVTLELGGKSPAIIAPDADLAKA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 822 TGDVIRSAFDSAGQRCSALRILCLQEDIADNYIKMIVGAMKEL--KIGDSKyidtDVGPVIDKEAADNLNAYIEE-KKKQ 898
Cdd:cd07133 226 AERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMypTLADNP----DYTSIINERHYARLQGLLEDaRAKG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 899 FKLVYQAQPNEDTQKGTFVMPTA-FEIEKLSDLGREQ-FGPILHILRFKanELSKLIKDINSTGYGLTAGVHSRINEVMN 976
Cdd:cd07133 302 ARVIELNPAGEDFAATRKLPPTLvLNVTDDMRVMQEEiFGPILPILTYD--SLDEAIDYINARPRPLALYYFGEDKAEQD 379
|
410 420 430
....*....|....*....|....*....|....*.
gi 754263081 977 YVKNNIKAGNVYVNRNIVGAVVGVQPFGGQGKSGTG 1012
Cdd:cd07133 380 RVLRRTHSGGVTINDTLLHVAQDDLPFGGVGASGMG 415
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
693-1016 |
2.14e-18 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 90.11 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 693 GAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPIIAYKAIKLLfKAGLPKGVLQFTPGdGATVGSALVQSPVCK 772
Cdd:PLN02174 114 GVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEG-AVTETTALLEQKWDK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 773 gVIFTGSTEVAGIInqtLASKSSEIVPFIAETGGQNAMIVDSSSLPEQVTGDVIRSAFD-SAGQRC-SALRILCLQEdia 850
Cdd:PLN02174 192 -IFYTGSSKIGRVI---MAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACiSPDYILTTKE--- 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 851 dnYIKMIVGAMK---ELKIGDSKYIDTDVGPVIDKEAADNLNAYIEEKKKQFKLVYQAQPNEDTQKgtfVMPTAFEIEKL 927
Cdd:PLN02174 265 --YAPKVIDAMKkelETFYGKNPMESKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGEKDRENLK---IAPTILLDVPL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 928 SDL--GREQFGPILHILrfKANELSKLIKDINSTGYGLTAGVHSRINEVMNYVKNNIKAGNVYVNRNIVGAVVGVQPFGG 1005
Cdd:PLN02174 340 DSLimSEEIFGPLLPIL--TLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGG 417
|
330
....*....|.
gi 754263081 1006 QGKSGTGPKAG 1016
Cdd:PLN02174 418 VGESGMGAYHG 428
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
1081-1286 |
1.91e-17 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 86.91 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1081 ADGKNIGKKYVASVSTVDKAIEVAYAEADAWN-HINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAH-IQIDK 1158
Cdd:cd07089 5 ATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARaMQVDG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1159 TIQQVAYYCLQAKKeFAHPELLPGPTgeiDELSLKGR-------GVVVSMSSSCDLLIRFVGQTTAALLAGNTVVAKPAY 1231
Cdd:cd07089 85 PIGHLRYFADLADS-FPWEFDLPVPA---LRGGPGRRvvrrepvGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 754263081 1232 TGSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSiSAV 1286
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGS-TAV 214
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
1081-1289 |
5.44e-17 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 85.48 E-value: 5.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1081 ADGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDKTI 1160
Cdd:cd07145 7 ANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVERTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1161 QQVAYYCLQAKKefahpelLPGPTGEIDELSLKGR----------GVVVSMSSSCDLLIRFVGQTTAALLAGNTVVAKPA 1230
Cdd:cd07145 87 RLFKLAAEEAKV-------LRGETIPVDAYEYNERriaftvrepiGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 754263081 1231 YTGSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQV 1289
Cdd:cd07145 160 SNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLI 218
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
615-945 |
9.32e-17 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 85.14 E-value: 9.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 615 QRANILEKFANLLEKNTDEFIAIAMIEAGKTLSNAIDEVREAVDFCRYYA--------AQARREfNGPIEL---PALSDh 683
Cdd:PRK11903 64 QRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAklgaalgdARLLRD-GEAVQLgkdPAFQG- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 684 lKQIEFTGRGAMVCISPWNFPlAIFLGQITAV-LAAGNTVVAKPAEQTPIIAYKAIKLLFKAG-LPKGVLQFTPGDGATV 761
Cdd:PRK11903 142 -QHVLVPTRGVALFINAFNFP-AWGLWEKAAPaLLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSSAGL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 762 GSALVQSPVckgVIFTGSTEVAGIInQTLASKSSEIVPFIAETGGQNAMIVdsssLPEQVTG---------DVIRSAFDS 832
Cdd:PRK11903 220 LDHLQPFDV---VSFTGSAETAAVL-RSHPAVVQRSVRVNVEADSLNSALL----GPDAAPGseafdlfvkEVVREMTVK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 833 AGQRCSALRILCLQEDIADNYIKMIVGAMKELKIGDSKYIDTDVGPVIDKEAADNLNAYIEEKKKQFKLVY----QAQPN 908
Cdd:PRK11903 292 SGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFdgggFALVD 371
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 754263081 909 EDTQKGTFVMPTAFEIEKLSDLGR----EQFGPILHILRFK 945
Cdd:PRK11903 372 ADPAVAACVGPTLLGASDPDAATAvhdvEVFGPVATLLPYR 412
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
1099-1286 |
9.99e-16 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 81.66 E-value: 9.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1099 KAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDKTIQQVAYYCLQAKKEFAhpE 1178
Cdd:PLN02278 66 DAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYG--D 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1179 LLPGPTGEIDELSLKGR-GVVVSMSS---SCDLLIRFVGqttAALLAGNTVVAKPAYTGSLTAYNIVKLMLKAGVDPKVI 1254
Cdd:PLN02278 144 IIPSPFPDRRLLVLKQPvGVVGAITPwnfPLAMITRKVG---PALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVL 220
|
170 180 190
....*....|....*....|....*....|..
gi 754263081 1255 NLILSDDEEITSALLFNSKVALVTFSGSiSAV 1286
Cdd:PLN02278 221 NVVMGDAPEIGDALLASPKVRKITFTGS-TAV 251
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
1081-1294 |
1.61e-15 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 81.20 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1081 ADGKNIGKKYVASVSTVDKAIEVAYAEADA--WNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDK 1158
Cdd:cd07119 21 ANGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEIDIDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1159 TIQQVAYYCLQAKKEfaHPELLPGPTGEIDELSLKGRGVVVSMSSSCDLLIRFVGQTTAALLAGNTVVAKPAYTGSLTAY 1238
Cdd:cd07119 101 VANCFRYYAGLATKE--TGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTI 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 754263081 1239 NIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALA 1294
Cdd:cd07119 179 ALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAA 234
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
1081-1311 |
6.16e-15 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 79.19 E-value: 6.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1081 ADGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDKTI 1160
Cdd:cd07099 4 ATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1161 QQVAYYCLQAKKEFAHPELLPGPT--GEIDELSLKGRGVV---------VSMSsscdllirfVGQTTAALLAGNTVVAKP 1229
Cdd:cd07099 84 EAIDWAARNAPRVLAPRKVPTGLLmpNKKATVEYRPYGVVgvispwnypLLTP---------MGDIIPALAAGNAVVLKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1230 AYTGSLTAYNIVKLMLKAGVDPKVINLILSDDEeiTSALLFNSKVALVTFSGSISAVKQVHQALALRrgaIIPFVAESVA 1309
Cdd:cd07099 155 SEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGA--TGAALIDAGVDKVAFTGSVATGRKVMAAAAER---LIPVVLELGG 229
|
..
gi 754263081 1310 KD 1311
Cdd:cd07099 230 KD 231
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
577-988 |
6.22e-15 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 79.08 E-value: 6.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 577 PNT-GDTIGTVINADAKMAKRALKNAQSAFEDWNntpasQRANILEKFANLLEKNTDEFIAIAMIE--AGKTLSNAIDEV 653
Cdd:cd07126 29 PDTdEDEINEFVDSLRQCPKSGLHNPLKNPERYL-----LYGDVSHRVAHELRKPEVEDFFARLIQrvAPKSDAQALGEV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 654 REAVDFCRYYAA-QAR---REFNGPielpalSDHLKQIEFTGR---GAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKP 726
Cdd:cd07126 104 VVTRKFLENFAGdQVRflaRSFNVP------GDHQGQQSSGYRwpyGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 727 AEQTPIIAYKAIKLLFKAGLPKGVLQFTPGDGATVGSALVQSPVcKGVIFTGSTEVAGIINQTLASKSS-EIVPFIAETG 805
Cdd:cd07126 178 DSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANP-RMTLFTGSSKVAERLALELHGKVKlEDAGFDWKIL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 806 GQNAMIVDssslpeQVTGDVIRSAFDSAGQRCSALRILCLQEdiadNYIKM-IVGAMKELKiGDSKYIDTDVGPVID--- 881
Cdd:cd07126 257 GPDVSDVD------YVAWQCDQDAYACSGQKCSAQSILFAHE----NWVQAgILDKLKALA-EQRKLEDLTIGPVLTwtt 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 882 ---KEAADNLNAyIEEKKKQF---KLVYQAQPnedTQKGTfVMPTA-------FEIEKLSDL-GREQFGPILHILRFKAN 947
Cdd:cd07126 326 eriLDHVDKLLA-IPGAKVLFggkPLTNHSIP---SIYGA-YEPTAvfvpleeIAIEENFELvTTEVFGPFQVVTEYKDE 400
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 754263081 948 ELSKLIKDINSTGYGLTAGVHSRINEVMNYVKNNIKAGNVY 988
Cdd:cd07126 401 QLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNGTTY 441
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
1082-1297 |
9.84e-15 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 78.55 E-value: 9.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1082 DGKNIGKKYVASVSTVDKAIEVAYAEAdawNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDKTIQ 1161
Cdd:cd07146 8 TGEVVGTVPAGTEEALREALALAASYR---STLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1162 QVAYYCLQAKKEfahpellpgpTGEIDELSL----KGR---------GVVVSMSSSCDLLIRFVGQTTAALLAGNTVVAK 1228
Cdd:cd07146 85 VLRFAAAEALRD----------DGESFSCDLtangKARkiftlreplGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 754263081 1229 PAYTGSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALALRR 1297
Cdd:cd07146 155 PSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYKR 223
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
1097-1282 |
1.30e-14 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 77.96 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1097 VDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDKTIQQV---AYYCLQakke 1173
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILreaAGLPRR---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1174 fAHPELLpgPTGEIDELSLKGR---GVVVSMSS-SCDLL--IRFVGqttAALLAGNTVVAKPA----YTGSLTaynIVKL 1243
Cdd:cd07104 78 -PEGEIL--PSDVPGKESMVRRvplGVVGVISPfNFPLIlaMRSVA---PALALGNAVVLKPDsrtpVTGGLL---IAEI 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 754263081 1244 MLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGS 1282
Cdd:cd07104 149 FEEAGLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGS 187
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
1081-1294 |
1.46e-14 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 77.67 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1081 ADGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDKTI 1160
Cdd:cd07102 4 IDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGML 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1161 QQVAYYCLQAKKEFAhPELLPGPTGeidelsLKGR------GVVVSMSS-SCDLLIRfVGQTTAALLAGNTVVAKPAYTG 1233
Cdd:cd07102 84 ERARYMISIAEEALA-DIRVPEKDG------FERYirreplGVVLIIAPwNYPYLTA-VNAVIPALLAGNAVILKHSPQT 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754263081 1234 SLTAYNIVKLMLKAGVDPKVINLILSDDeEITSALLFNSKVALVTFSGSISAVKQVHQALA 1294
Cdd:cd07102 156 PLCGERFAAAFAEAGLPEGVFQVLHLSH-ETSAALIADPRIDHVSFTGSVAGGRAIQRAAA 215
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
1081-1294 |
2.69e-14 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 76.80 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1081 ADGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDKTI 1160
Cdd:cd07106 5 ATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1161 QQVAYYclqAKKEFAhPELLPGPTGEIDELSLKGRGVVVSMSSSCDLLIRFVGQTTAALLAGNTVVAKPAYTGSLTAYNI 1240
Cdd:cd07106 85 AWLRYT---ASLDLP-DEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 754263081 1241 VKLMLKAgVDPKVINlILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALA 1294
Cdd:cd07106 161 GELAQEV-LPPGVLN-VVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAA 212
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
1078-1294 |
2.73e-14 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 77.09 E-value: 2.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1078 LKSADGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDA-HIQI 1156
Cdd:cd07115 2 LNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRLDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1157 DKTIQQVAYYCLQAKKEFAhpELLPGPTGEIDELSLKGRGVVVSMssscdLLIRFVGQTTA-----ALLAGNTVVAKPAY 1231
Cdd:cd07115 82 PRAADTFRYYAGWADKIEG--EVIPVRGPFLNYTVREPVGVVGAI-----VPWNFPLMFAAwkvapALAAGNTVVLKPAE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754263081 1232 TGSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALA 1294
Cdd:cd07115 155 LTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAA 217
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
1075-1286 |
3.25e-14 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 76.60 E-value: 3.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1075 FVDLKSADGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHI 1154
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1155 QIDKTIQQVAyyclQAKKEFAHP--ELLP-GPTGEIDELSLKGRGVVVSMSSSCDLLIRFVGQTTAALLAGNTVVAKPAY 1231
Cdd:cd07150 81 ETTFTPELLR----AAAGECRRVrgETLPsDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 754263081 1232 TGSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSiSAV 1286
Cdd:cd07150 157 ETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGS-TAV 210
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
1086-1299 |
8.38e-14 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 75.75 E-value: 8.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1086 IGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDKTIQQVAY 1165
Cdd:cd07097 28 VGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARGEVTRAGQIFRY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1166 YclqakkefahpellpgpTGEIdeLSLKGRgVVVSMSSSCDLLIR-----FVGQTTA--------------ALLAGNTVV 1226
Cdd:cd07097 108 Y-----------------AGEA--LRLSGE-TLPSTRPGVEVETTreplgVVGLITPwnfpiaipawkiapALAYGNTVV 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754263081 1227 AKPAYTGSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQAlALRRGA 1299
Cdd:cd07097 168 FKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAA-AAARGA 239
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
1063-1291 |
2.41e-13 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 74.09 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1063 NIVAGE--KAKKDKFVDLKS-ADGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIAS 1139
Cdd:cd07085 3 LFINGEwvESKTTEWLDVYNpATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1140 CLVTESNVSVEDAHIQIDKTIQQVAYYClqakkefAHPELLPGPTGE-----IDELSLKG-RGVV-----------VSMS 1202
Cdd:cd07085 83 LITLEHGKTLADARGDVLRGLEVVEFAC-------SIPHLLKGEYLEnvargIDTYSYRQpLGVVagitpfnfpamIPLW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1203 SscdllirfvgqTTAALLAGNTVVAKPAYTGSLTAYNIVKLMLKAGVDPKVINLILSDDEEITsALLFNSKVALVTFSGS 1282
Cdd:cd07085 156 M-----------FPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVN-ALLDHPDIKAVSFVGS 223
|
....*....
gi 754263081 1283 ISAVKQVHQ 1291
Cdd:cd07085 224 TPVGEYIYE 232
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
1065-1297 |
4.86e-13 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 72.99 E-value: 4.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1065 VAGE--KAKKDKFVDLKS-ADGKNIGKKYVASVSTVDKAIEVAYAEADA--WNHINAEDRALIVEKFLDLLEKERHLIAS 1139
Cdd:cd07139 3 IGGRwvAPSGSETIDVVSpATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1140 cLVTESN----VSVEDAHIQIdkTIQQVAYYcLQAKKEFAHPELLPGPTGEIDELSLKGRGVVVSMSSSCDLLIRFVGQT 1215
Cdd:cd07139 83 -LWTAENgmpiSWSRRAQGPG--PAALLRYY-AALARDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1216 TAALLAGNTVVAKPAYTGSLTAYNIVKLMLKAGVDPKVINlILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALA- 1294
Cdd:cd07139 159 APALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVN-VVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGe 237
|
....
gi 754263081 1295 -LRR 1297
Cdd:cd07139 238 rLAR 241
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
1081-1282 |
5.36e-13 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 72.76 E-value: 5.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1081 ADGKNIGKKYVASVSTVDKAIEVAYA--EADAWNHiNAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDK 1158
Cdd:cd07120 5 ATGEVIGTYADGGVAEAEAAIAAARRafDETDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEARFEISG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1159 TIQQVAYYCLQAKKEFAHP-ELLPGptgeidELSLKGR------GVVVSMSSSCDLLIRfvgQTTAALLAGNTVVAKPAY 1231
Cdd:cd07120 84 AISELRYYAGLARTEAGRMiEPEPG------SFSLVLRepmgvaGIIVPWNSPVVLLVR---SLAPALAAGCTVVVKPAG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 754263081 1232 TGSLTAYNIVKLMLKAGVDPK-VINLILSDDEEITSALLFNSKVALVTFSGS 1282
Cdd:cd07120 155 QTAQINAAIIRILAEIPSLPAgVVNLFTESGSEGAAHLVASPDVDVISFTGS 206
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
1070-1289 |
8.24e-13 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 72.47 E-value: 8.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1070 AKKDKFVDLKS-ADGKNIGKKYVASVSTVDKAIEVAYAEAD-AWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNV 1147
Cdd:cd07113 11 GQSEKRLDITNpATEQVIASVASATEADVDAAVASAWRAFVsAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1148 SVE-DAHIQIDKTIQQVAYYCLQAKK---EFAHPELlPGPTGE-IDELSLKGR-GVVVSMSSSCDLLIRFVGQTTAALLA 1221
Cdd:cd07113 91 SIHlSRAFEVGQSANFLRYFAGWATKingETLAPSI-PSMQGErYTAFTRREPvGVVAGIVPWNFSVMIAVWKIGAALAT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 754263081 1222 GNTVVAKPAYTGSLTAYNIVKLMLKAGVDPKVINLIlSDDEEITSALLFNSKVALVTFSGSISAVKQV 1289
Cdd:cd07113 170 GCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVV-NGKGAVGAQLISHPDVAKVSFTGSVATGKKI 236
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
1081-1294 |
9.65e-13 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 72.15 E-value: 9.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1081 ADGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDA-HIQIDKT 1159
Cdd:cd07138 22 ATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPITLArAAQVGLG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1160 IQQVAYYcLQAKKEFAHPELLPGptgeiDELSLKGRGVVVsmssscdlLI--------RFVGQTTAALLAGNTVVAKPAY 1231
Cdd:cd07138 102 IGHLRAA-ADALKDFEFEERRGN-----SLVVREPIGVCG--------LItpwnwplnQIVLKVAPALAAGCTVVLKPSE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754263081 1232 TGSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALA 1294
Cdd:cd07138 168 VAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAA 230
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
1068-1294 |
1.50e-12 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 71.61 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1068 EKAKKDKFVDLKSADGKNIGKKYVAS-VSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESN 1146
Cdd:cd07131 9 DSASGETFDSRNPADLEEVVGTFPLStASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1147 VSVEDAHIQIDKTIQQVAYYCLQAKKEFAH--PELLPgptgEIDELS-LKGRGVV-------VSMSSSCDLLIrfvgqtt 1216
Cdd:cd07131 89 KPLAEGRGDVQEAIDMAQYAAGEGRRLFGEtvPSELP----NKDAMTrRQPIGVValitpwnFPVAIPSWKIF------- 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 754263081 1217 AALLAGNTVVAKPAYTGSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALA 1294
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCA 235
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
1082-1306 |
1.72e-12 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 71.19 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1082 DGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDKTIQ 1161
Cdd:cd07101 5 TGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1162 QVAYYCLQAKKEFA---HPELLPGPTGEIDELSLKGrgvVVSMSSSCDL-LIRFVGQTTAALLAGNTVVAKPAYTGSLTA 1237
Cdd:cd07101 85 VARYYARRAERLLKprrRRGAIPVLTRTTVNRRPKG---VVGVISPWNYpLTLAVSDAIPALLAGNAVVLKPDSQTALTA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 754263081 1238 YNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKvaLVTFSGSISAVKQVHQALALRrgaIIPFVAE 1306
Cdd:cd07101 162 LWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNAD--YVMFTGSTATGRVVAERAGRR---LIGCSLE 225
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
1081-1301 |
2.83e-12 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 70.67 E-value: 2.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1081 ADGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIAScLVTesnvsvedahiqidkti 1160
Cdd:cd07086 21 ANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGR-LVS----------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1161 qqvayycLQAKKEFahPELLpgptGEIDE----------LS--LKGRgVVVSMSSSCDLLIRF-----VGQTTA------ 1217
Cdd:cd07086 83 -------LEMGKIL--PEGL----GEVQEmidicdyavgLSrmLYGL-TIPSERPGHRLMEQWnplgvVGVITAfnfpva 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1218 --------ALLAGNTVVAKPAYTGSLTAYNIVKLMLKA----GVDPKVINLILSDDeEITSALLFNSKVALVTFSGSISA 1285
Cdd:cd07086 149 vpgwnaaiALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGG-DGGELLVHDPRVPLVSFTGSTEV 227
|
250
....*....|....*.
gi 754263081 1286 VKQVHQALALRRGAII 1301
Cdd:cd07086 228 GRRVGETVARRFGRVL 243
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
1081-1294 |
3.11e-12 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 70.51 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1081 ADGKNIGKKYVASVSTVDKAIEVAY-AEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVE-DAHIQIDK 1158
Cdd:cd07144 31 STGEVIASVYAAGEEDVDKAVKAARkAFESWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYHsNALGDLDE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1159 TIQQVAYYCLQAKKEFahpellpgptGEIDELSLKGRGVVVSMSsscdllIRFVGQTT--------------AALLAGNT 1224
Cdd:cd07144 111 IIAVIRYYAGWADKIQ----------GKTIPTSPNKLAYTLHEP------YGVCGQIIpwnyplamaawklaPALAAGNT 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1225 VVAKPAYTGSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALA 1294
Cdd:cd07144 175 VVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAA 244
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
1083-1292 |
5.12e-12 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 69.63 E-value: 5.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1083 GKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDKTIQQ 1162
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1163 vayyCLQAKKEFAHP--ELLPGPTGEideLSLKGR------GVVVSMSSSCDLLIRFVGqttAALLAGNTVVAKP----A 1230
Cdd:cd07152 81 ----LHEAAGLPTQPqgEILPSAPGR---LSLARRvplgvvGVISPFNFPLILAMRSVA---PALALGNAVVLKPdprtP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 754263081 1231 YTGSLTaynIVKLMLKAGVDPKVINlILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQA 1292
Cdd:cd07152 151 VSGGVV---IARLFEEAGLPAGVLH-VLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEA 208
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
1097-1300 |
6.47e-12 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 69.22 E-value: 6.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1097 VDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDKTIQQVAYyCLQAKKEFAH 1176
Cdd:cd07095 2 VDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDI-SIKAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1177 PELLPGPTGEiDELSLKGRGVVvsmssscdllirFV------------GQTTAALLAGNTVVAKPAYTGSLTAYNIVKLM 1244
Cdd:cd07095 81 ERATPMAQGR-AVLRHRPHGVM------------AVfgpfnfpghlpnGHIVPALLAGNTVVFKPSELTPAVAELMVELW 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 754263081 1245 LKAGVDPKVINLILSDDEEiTSALLFNSKVALVTFSGSISAVKQVHQALALRRGAI 1300
Cdd:cd07095 148 EEAGLPPGVLNLVQGGRET-GEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKI 202
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
248-476 |
1.57e-11 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 68.19 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 248 SIKLSALH-PRYEVAKHQ--------RVHEELYPKLLKLTQLAKEYNVGMNIDAEETeRLQISLE-LVERLAHEPSLDgf 317
Cdd:PLN02681 187 SFPLFADSsPLYHATSEPepltaeeeRLLELAHERLQKLCERAAQLGVPLLIDAEYT-SLQPAIDyITYDLAREFNKG-- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 318 DGIGIV---VQAYQKRAPYVLDYLANLAKKTNRRFMIRLVKGAYWDAEIKHAQEQGLaDYPVFTRKYHTDVSYQACVKQL 394
Cdd:PLN02681 264 KDRPIVygtYQAYLKDARERLRLDLERSEREGVPLGAKLVRGAYLSLERRLAASLGV-PSPVHDTIQDTHACYNRCAEFL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 395 FEH-----HQYIypqFATHNAQTVAVVMELAN------GNKDFEFQCLHGMGDPLyDNIVGKEGYedipcRI--YAPVGG 461
Cdd:PLN02681 343 LEKasngdGEVM---LATHNVESGELAAAKMNelglhkGDPRVQFAQLLGMSDNL-SFGLGNAGF-----RVskYLPYGP 413
|
250
....*....|....*
gi 754263081 462 HKHLLAYLVRRLLEN 476
Cdd:PLN02681 414 VEEVIPYLLRRAEEN 428
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
1086-1297 |
1.88e-11 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 68.38 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1086 IGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLE-KERH-LIASCLVTESnvsvedahiqidKTIQQV 1163
Cdd:cd07123 60 LATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSgKYRYeLNAATMLGQG------------KNVWQA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1164 ---------------AYYClqakKEFAHPELLPGPTGEIDELSLKG-RGVVVSMSSscdllirF----VGQT--TAALLA 1221
Cdd:cd07123 128 eidaacelidflrfnVKYA----EELYAQQPLSSPAGVWNRLEYRPlEGFVYAVSP-------FnftaIGGNlaGAPALM 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1222 GNTVVAKPAYTGSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSiSAV-----KQVHQALALR 1296
Cdd:cd07123 197 GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGS-TPTfkslwKQIGENLDRY 275
|
.
gi 754263081 1297 R 1297
Cdd:cd07123 276 R 276
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
1081-1294 |
3.40e-11 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 67.24 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1081 ADGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASclvTES-------NVSVEDah 1153
Cdd:PRK13473 25 ATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFAR---LESlncgkplHLALND-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1154 iQIDKTIQQVAYY-----CLQAKkefAHPELLPGPTGEIdelslkgR----GVVVSMSSSCDLLIRFVGQTTAALLAGNT 1224
Cdd:PRK13473 100 -EIPAIVDVFRFFagaarCLEGK---AAGEYLEGHTSMI-------RrdpvGVVASIAPWNYPLMMAAWKLAPALAAGNT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1225 VVAKPAYTGSLTAYNIVKLMLKAgVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALA 1294
Cdd:PRK13473 169 VVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAA 237
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
1081-1294 |
3.67e-11 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 67.21 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1081 ADGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIAsclVTESN---VSVEDA-HIQI 1156
Cdd:cd07093 5 ATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELA---LLESLdtgKPITLArTRDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1157 DKTIQQV---AYYCLQAkkefaHPELLPGPTGEIDELSLKGRGVVVSMS--SSCDLLIRFvgQTTAALLAGNTVVAKPAY 1231
Cdd:cd07093 82 PRAAANFrffADYILQL-----DGESYPQDGGALNYVLRQPVGVAGLITpwNLPLMLLTW--KIAPALAFGNTVVLKPSE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754263081 1232 TGSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALA 1294
Cdd:cd07093 155 WTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAA 217
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
1081-1295 |
5.32e-11 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 66.75 E-value: 5.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1081 ADGKNIGKKYVASVSTVDKAIEVAYA--EADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDA-HIQID 1157
Cdd:cd07140 29 TDGSVICKVSLATVEDVDRAVAAAKEafENGEWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLAlKTHVG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1158 KTIQQVAYYCLQAKKefahpelLPGPTGEIDE------LSLKGR---GVVVSMSSSCDLLIRFVGQTTAALLAGNTVVAK 1228
Cdd:cd07140 109 MSIQTFRYFAGWCDK-------IQGKTIPINQarpnrnLTLTKRepiGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754263081 1229 PAYTGSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALAL 1295
Cdd:cd07140 182 PAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAV 248
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
1081-1294 |
6.23e-11 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 66.22 E-value: 6.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1081 ADGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDKTI 1160
Cdd:cd07110 5 ATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDDVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1161 QQVAYYCLQAKKEFAH-PELLPGPTGEIDELSLKGRGVVVSMSSSCDL-LIRFVGQTTAALLAGNTVVAKPAYTGSLTAY 1238
Cdd:cd07110 85 GCFEYYADLAEQLDAKaERAVPLPSEDFKARVRREPVGVVGLITPWNFpLLMAAWKVAPALAAGCTVVLKPSELTSLTEL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 754263081 1239 NIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALA 1294
Cdd:cd07110 165 ELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAA 220
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
1074-1294 |
8.06e-11 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 65.98 E-value: 8.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1074 KFVDLKSA---------DGKNIGKKYVASVSTVDKAIEVAYAEAD--AWNHINAEDRALIVEKFLDLLEKERHLIAScLV 1142
Cdd:cd07142 11 QFVDAASGktfptidprNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADELAA-LE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1143 TESNVSVED--AHIQIDKTIQQVAYYCLQAKKefAHPELLPGpTGEIDELSLKGR-GVVVSMSSSCDLLIRFVGQTTAAL 1219
Cdd:cd07142 90 TWDNGKPYEqaRYAEVPLAARLFRYYAGWADK--IHGMTLPA-DGPHHVYTLHEPiGVVGQIIPWNFPLLMFAWKVGPAL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754263081 1220 LAGNTVVAKPAYTGSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALA 1294
Cdd:cd07142 167 ACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAA 241
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
1081-1306 |
1.09e-10 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 65.72 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1081 ADGKNIGKKYVASVSTVDKAIEVAY-AEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDKT 1159
Cdd:cd07109 5 STGEVFARIARGGAADVDRAVQAARrAFESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1160 IQQVAYYCLQAKKefAHPELLP--------------GPTGEI----DELSLKGRGVvvsmssscdllirfvgqtTAALLA 1221
Cdd:cd07109 85 ARYFEYYGGAADK--LHGETIPlgpgyfvytvrephGVTGHIipwnYPLQITGRSV------------------APALAA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1222 GNTVVAKPAYTGSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALALRrgaII 1301
Cdd:cd07109 145 GNAVVVKPAEDAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAEN---VV 221
|
....*
gi 754263081 1302 PFVAE 1306
Cdd:cd07109 222 PVTLE 226
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
1081-1282 |
2.01e-10 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 64.93 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1081 ADGKNIGKKYVASVSTVDKAIEVAYA--EADAWNHINAEDRALIVEKFLDLLEKERH------------LIASCLvtesN 1146
Cdd:cd07112 10 ATGRVLAEVAACDAADVDRAVAAARRafESGVWSRLSPAERKAVLLRLADLIEAHRDelalletldmgkPISDAL----A 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1147 VSVEDA--HIQ-----IDKTIQQVAyyclqakkefahpellpgPTGEiDELSLKGR---GVVVSMSSSCDLLIRFVGQTT 1216
Cdd:cd07112 86 VDVPSAanTFRwyaeaIDKVYGEVA------------------PTGP-DALALITReplGVVGAVVPWNFPLLMAAWKIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 754263081 1217 AALLAGNTVVAKPAYTGSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGS 1282
Cdd:cd07112 147 PALAAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGS 212
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
1092-1309 |
5.32e-10 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 63.44 E-value: 5.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1092 ASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDKTIQQVAYyCLQAK 1171
Cdd:PRK09457 34 ATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEVTAMINKIAI-SIQAY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1172 KEFAHPELLPGPTGEIdELSLKGRGVVVsmssscdllirfV------------GQTTAALLAGNTVVAKPAYTGSLTAYN 1239
Cdd:PRK09457 113 HERTGEKRSEMADGAA-VLRHRPHGVVA------------VfgpynfpghlpnGHIVPALLAGNTVVFKPSELTPWVAEL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 754263081 1240 IVKLMLKAGVDPKVINLILSDDEEiTSALLFNSKVALVTFSGSISAVKQVHQALALRRGAII--------PFVAESVA 1309
Cdd:PRK09457 180 TVKLWQQAGLPAGVLNLVQGGRET-GKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEKILalemggnnPLVIDEVA 256
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
1082-1282 |
5.45e-10 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 63.21 E-value: 5.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1082 DGKNIGKKYVASVSTVDKAIEVAYA---EADAWnhINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDK 1158
Cdd:cd07148 8 DLKPIGEVPTVDWAAIDKALDTAHAlflDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1159 TIQQVAYyCLQAKKEFAHPE----LLPGPTGEIDELSLKGRGVVVSMSSSCDLLIRFVGQTTAALLAGNTVVAKPAYTGS 1234
Cdd:cd07148 86 AIDGVEL-AADELGQLGGREipmgLTPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 754263081 1235 LTAYNIVKLMLKAGVDPKVINLILSDDeEITSALLFNSKVALVTFSGS 1282
Cdd:cd07148 165 LSCLAFVDLLHEAGLPEGWCQAVPCEN-AVAEKLVTDPRVAFFSFIGS 211
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
1063-1302 |
8.32e-10 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 62.75 E-value: 8.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1063 NIVAGE--KAKKDKFVD-LKSADGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIAS 1139
Cdd:cd07559 3 NFINGEwvAPSKGEYFDnYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1140 CLVTESNVSV-EDAHIQIDKTIQQVAYY--CLQAKKefahpellpGPTGEIDE--LSLKGR---GVVvsmssscdllirf 1211
Cdd:cd07559 83 AETLDNGKPIrETLAADIPLAIDHFRYFagVIRAQE---------GSLSEIDEdtLSYHFHeplGVV------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1212 vGQTTA--------------ALLAGNTVVAKPAytgSLTAYNIVKLM-LKAGVDPK-VINLILSDDEEITSALLFNSKVA 1275
Cdd:cd07559 141 -GQIIPwnfpllmaawklapALAAGNTVVLKPA---SQTPLSILVLMeLIGDLLPKgVVNVVTGFGSEAGKPLASHPRIA 216
|
250 260
....*....|....*....|....*..
gi 754263081 1276 LVTFSGSISAVKQVHQALALRrgaIIP 1302
Cdd:cd07559 217 KLAFTGSTTVGRLIMQYAAEN---LIP 240
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
1092-1282 |
9.06e-10 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 62.71 E-value: 9.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1092 ASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDKTIQqvayyCLQAK 1171
Cdd:cd07151 29 ASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANIEWGAAMA-----ITREA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1172 KEFAH-------PELLPGPTGEIDELSLkgrGVVVSMSS---SCDLLIRFVGqttAALLAGNTVVAKPA----YTGSLTa 1237
Cdd:cd07151 104 ATFPLrmegrilPSDVPGKENRVYREPL---GVVGVISPwnfPLHLSMRSVA---PALALGNAVVLKPAsdtpITGGLL- 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 754263081 1238 ynIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGS 1282
Cdd:cd07151 177 --LAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGS 219
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
1063-1291 |
2.25e-09 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 61.31 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1063 NIVAGE---KAKKDKFVDLKSADGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIAS 1139
Cdd:cd07116 3 NFIGGEwvaPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1140 CLVTESNVSV-EDAHIQIDKTIQQVAYY--CLQAKKefahpellpGPTGEIDELSL-----KGRGVVVSMSSSCDLLIRF 1211
Cdd:cd07116 83 AETWDNGKPVrETLAADIPLAIDHFRYFagCIRAQE---------GSISEIDENTVayhfhEPLGVVGQIIPWNFPLLMA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1212 VGQTTAALLAGNTVVAKPAytgSLTAYNIVKLMLKAG--VDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQV 1289
Cdd:cd07116 154 TWKLAPALAAGNCVVLKPA---EQTPASILVLMELIGdlLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLI 230
|
..
gi 754263081 1290 HQ 1291
Cdd:cd07116 231 MQ 232
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
1081-1344 |
3.07e-09 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 61.26 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1081 ADGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIAsclVTESNVS------VEDAHI 1154
Cdd:cd07111 45 ATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFA---VLESLDNgkpireSRDCDI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1155 QIdkTIQQVAYYCLQAKKEfahPELLPGPtgeidelslKGRGVVVSMSSSCDLLIRFVGQTTAALLAGNTVVAKPAYTGS 1234
Cdd:cd07111 122 PL--VARHFYHHAGWAQLL---DTELAGW---------KPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1235 LTAYNIVKLMLKAGVDPKVINlILSDDEEITSALLFNSKVALVTFSGSISAVKqvhqalALRRgaiipfvaeSVAKDGKC 1314
Cdd:cd07111 188 LTALLFAEICAEAGLPPGVLN-IVTGNGSFGSALANHPGVDKVAFTGSTEVGR------ALRR---------ATAGTGKK 251
|
250 260 270
....*....|....*....|....*....|
gi 754263081 1315 TSLAIETASPlylrrFVVEKTVSVDTTASG 1344
Cdd:cd07111 252 LSLELGGKSP-----FIVFDDADLDSAVEG 276
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
1097-1282 |
4.37e-09 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 60.33 E-value: 4.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1097 VDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSvEDAHIQIDKTIQQVAYYCLQAKKEFAH 1176
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKG-WMFAENICGDQVQLRARAFVIYSYRIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1177 PELL--PGPTGEID-ELSLKGRGVVVSMSSSCDLLIRFVGQTTAALLAGNTVVAKPAYTGSLTAYNIVKLMLKAGVDPKV 1253
Cdd:cd07084 80 HEPGnhLGQGLKQQsHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLLPPE 159
|
170 180
....*....|....*....|....*....
gi 754263081 1254 INLILSDDEEITSALLFNSKVALVTFSGS 1282
Cdd:cd07084 160 DVTLINGDGKTMQALLLHPNPKMVLFTGS 188
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
1081-1294 |
5.05e-09 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 60.23 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1081 ADGKNIGKKYVASVSTVDKAIEVAYA--EADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVED-AHIQID 1157
Cdd:cd07143 30 STGKLITKIAEATEADVDIAVEVAHAafETDWGLKVSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTFGTaKRVDVQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1158 KTIQQVAYYCLQAKKEFahpellpGPTGEIDELSL-----KGRGVVVSMSSSCDLLIRFVGQTTAALLAGNTVVAKPAYT 1232
Cdd:cd07143 110 ASADTFRYYGGWADKIH-------GQVIETDIKKLtytrhEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSEL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 754263081 1233 GSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALA 1294
Cdd:cd07143 183 TPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAA 244
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
1081-1306 |
5.42e-09 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 60.28 E-value: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1081 ADGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHiqidKTI 1160
Cdd:PRK09407 40 FTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAF----EEV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1161 QQVA----YYCLQAKKEFA---HPELLPGPTgEIDELSLKgRGVV---------VSMSsscdllirfVGQTTAALLAGNT 1224
Cdd:PRK09407 116 LDVAltarYYARRAPKLLAprrRAGALPVLT-KTTELRQP-KGVVgvispwnypLTLA---------VSDAIPALLAGNA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1225 VVAKPAYTGSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNskVALVTFSGSISAVKQVHQALALRrgaIIPFV 1304
Cdd:PRK09407 185 VVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAGRR---LIGFS 259
|
..
gi 754263081 1305 AE 1306
Cdd:PRK09407 260 LE 261
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
1097-1282 |
5.62e-09 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 59.90 E-value: 5.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1097 VDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDKTIQQVAYYClqakkefAH 1176
Cdd:cd07105 2 ADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAA-------SL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1177 PELLPG---PTGEIDELSLKGR---GVVVSMS---SSCDLLIRFVgqtTAALLAGNTVVAKPAYTGSLTAYNIVKLMLKA 1247
Cdd:cd07105 75 ITQIIGgsiPSDKPGTLAMVVKepvGVVLGIApwnAPVILGTRAI---AYPLAAGNTVVLKASELSPRTHWLIGRVFHEA 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 754263081 1248 GVDPKVINLILSDDE---EITSALLFNSKVALVTFSGS 1282
Cdd:cd07105 152 GLPKGVLNVVTHSPEdapEVVEALIAHPAVRKVNFTGS 189
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
1074-1294 |
7.29e-09 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 59.92 E-value: 7.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1074 KFVDLKS---------ADGKNIGKKYVASVSTVDKAIEVAYA--EADAWNHINAEDRALIVEKFLDLLEKERHLIAScLV 1142
Cdd:cd07091 11 EFVDSVSgktfptinpATEEVICQVAEADEEDVDAAVKAARAafETGWWRKMDPRERGRLLNKLADLIERDRDELAA-LE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1143 TESN--VSVEDAHIQIDKTIQQVAYYCLQAKKefahpelLPGPTGEIDE--LSLKGR---GVVVSMSSSCDLLIRFVGQT 1215
Cdd:cd07091 90 SLDNgkPLEESAKGDVALSIKCLRYYAGWADK-------IQGKTIPIDGnfLAYTRRepiGVCGQIIPWNFPLLMLAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1216 TAALLAGNTVVAKPAYTGSLTAYNIVKLMLKAGVDPKVINLI----------LSDDEEItsallfnSKVAlvtFSGSISA 1285
Cdd:cd07091 163 APALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVpgfgptagaaISSHMDV-------DKIA---FTGSTAV 232
|
....*....
gi 754263081 1286 VKQVHQALA 1294
Cdd:cd07091 233 GRTIMEAAA 241
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
1081-1282 |
1.04e-08 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 59.10 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1081 ADGKNIGKKYVASVSTVDKAIEVAYA--EADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDK 1158
Cdd:cd07114 5 ATGEPWARVPEASAADVDRAVAAARAafEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVRY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1159 TIQQVAYYCLQAKKEFAhpELLPGPTGeiDELSLKGR---GVVVSMSSSCDLLIRFVGQTTAALLAGNTVVAKPAYTGSL 1235
Cdd:cd07114 85 LAEWYRYYAGLADKIEG--AVIPVDKG--DYLNFTRReplGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 754263081 1236 TAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGS 1282
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGG 207
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
1081-1296 |
1.89e-08 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 58.47 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1081 ADGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDKTI 1160
Cdd:cd07090 5 ATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDSSA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1161 QQVAYYC-LQAKKEFAHPELLPGPTGEIDELSLkgrGVVVSMSSsCDLLIRFVGQTTA-ALLAGNTVVAKPAYTGSLTAY 1238
Cdd:cd07090 85 DCLEYYAgLAPTLSGEHVPLPGGSFAYTRREPL---GVCAGIGA-WNYPIQIASWKSApALACGNAMVYKPSPFTPLTAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 754263081 1239 NIVKLMLKAGVDPKVINLILSDDEeiTSALLF-NSKVALVTFSGSISAVKQVHQALALR 1296
Cdd:cd07090 161 LLAEILTEAGLPDGVFNVVQGGGE--TGQLLCeHPDVAKVSFTGSVPTGKKVMSAAAKG 217
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
1081-1348 |
3.34e-08 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 57.61 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1081 ADGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDKTI 1160
Cdd:PRK11241 34 ANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1161 QQVAYYCLQAKKEFAhpELLPGPTGEIDELSLKGR-GVVVSMSS---SCDLLIRFVGqttAALLAGNTVVAKPAYTGSLT 1236
Cdd:PRK11241 114 SFIEWFAEEGKRIYG--DTIPGHQADKRLIVIKQPiGVTAAITPwnfPAAMITRKAG---PALAAGCTMVLKPASQTPFS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1237 AYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQvhqalalrrgaiipfVAESVAKDGKCTS 1316
Cdd:PRK11241 189 ALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQ---------------LMEQCAKDIKKVS 253
|
250 260 270
....*....|....*....|....*....|..
gi 754263081 1317 LAIETASPlylrrFVVEKTVSVDTTASGGNAS 1348
Cdd:PRK11241 254 LELGGNAP-----FIVFDDADLDKAVEGALAS 280
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
1081-1294 |
3.45e-08 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 57.72 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1081 ADGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEK--ERHLIASCLVT--ESNVSVEDahiQI 1156
Cdd:cd07092 5 ATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEEnaEELAALESRNTgkPLHLVRDD---EL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1157 DKTIQQVAYY-----CLQAKkefAHPELLPGPTGEIDELSLkgrGVVVSMSSSCDLLIRFVGQTTAALLAGNTVVAKPAY 1231
Cdd:cd07092 82 PGAVDNFRFFagaarTLEGP---AAGEYLPGHTSMIRREPI---GVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754263081 1232 TGSLTAYNIVKLmLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALA 1294
Cdd:cd07092 156 TTPLTTLLLAEL-AAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAA 217
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
1081-1302 |
4.33e-08 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 57.37 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1081 ADGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTES-NVSVEDAHIQIDKT 1159
Cdd:cd07108 5 ATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETgNALRTQARPEAAVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1160 IQQVAYYCLQAKKefAHPELLPGPTGEIDELSLKGRGVVVSMSSSCDLLIRFVGQTTAALLAGNTVVAKPAYTGSLTAYN 1239
Cdd:cd07108 85 ADLFRYFGGLAGE--LKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 754263081 1240 IVKLM---LKAGVdpkvINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALALRrgaIIP 1302
Cdd:cd07108 163 LAEILaqvLPAGV----LNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADR---LIP 221
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
1097-1289 |
4.96e-08 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 57.08 E-value: 4.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1097 VDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDKTIQQVAYYCLQAKkEFAH 1176
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAE-AFLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1177 PELLPGPTGE--IDELSLkgrGVVvsmssscdLLI-----------RFVGqttAALLAGNTVVAKPAYTGSLTAYNIVKL 1243
Cdd:cd07100 80 DEPIETDAGKayVRYEPL---GVV--------LGImpwnfpfwqvfRFAA---PNLMAGNTVLLKHASNVPGCALAIEEL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 754263081 1244 MLKAGVDPKV-INLILSDDEeiTSALLFNSKVALVTFSGSISAVKQV 1289
Cdd:cd07100 146 FREAGFPEGVfQNLLIDSDQ--VEAIIADPRVRGVTLTGSERAGRAV 190
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
1097-1306 |
9.40e-08 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 56.40 E-value: 9.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1097 VDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVedAHIQ--IDKTIQQ--------VAYY 1166
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPE--ARLQgeLGRTTGQlrlfadlvREGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1167 CLQAKKEFAHPELLPGPTGEIdELSLKGRGVVVSMSSScdlliRF-----V--GQTTAALLAGNTVVAK--PAY--TGSL 1235
Cdd:cd07129 79 WLDARIDPADPDRQPLPRPDL-RRMLVPLGPVAVFGAS-----NFplafsVagGDTASALAAGCPVVVKahPAHpgTSEL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754263081 1236 TAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVhQALALRRGAIIPFVAE 1306
Cdd:cd07129 153 VARAIRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRAL-FDAAAARPEPIPFYAE 222
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
1092-1294 |
1.20e-07 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 55.81 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1092 ASVSTVDKAIEVAYAEADA--WNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDKTIQQVAYYCLQ 1169
Cdd:cd07118 16 GTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1170 AKKEF--AHPELLPGPTGeideLSLKGRGVVVSMSSSCDLLIRFVGQTTA-ALLAGNTVVAKPAYTGSLTAYNIVKLMLK 1246
Cdd:cd07118 96 ARTLHgdSYNNLGDDMLG----LVLREPIGVVGIITPWNFPFLILSQKLPfALAAGCTVVVKPSEFTSGTTLMLAELLIE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 754263081 1247 AGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALA 1294
Cdd:cd07118 172 AGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAA 219
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
1218-1294 |
4.34e-07 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 53.97 E-value: 4.34e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754263081 1218 ALLAGNTVVAKPAYTGSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALA 1294
Cdd:PRK10090 95 ALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIMAAAA 171
|
|
| PRODH |
pfam18327 |
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain ... |
20-61 |
5.38e-07 |
|
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain found in Proline utilization A (PutA) proteins. Proline utilization A (PutA) is a flavoprotein that has mutually exclusive roles as a transcriptional repressor of the put regulon and a membrane-associated enzyme that catalyzes the oxidation of proline to glutamate. The N-terminal region carries the flavoenzyme proline dehydrogenase (PRODH) domain which catalyzes the 2-electron oxidation of proline with the concomitant reduction of a flavin cofactor.
Pssm-ID: 465712 [Multi-domain] Cd Length: 48 Bit Score: 47.46 E-value: 5.38e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 754263081 20 ISKYWLIEEKEAVTKLVDKAHMSSVQKAQVRERAYGLVEKVR 61
Cdd:pfam18327 7 ITAAYRRPEAECVAPLLEAARLPPAERAAIRALARKLVEALR 48
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
1074-1304 |
8.84e-07 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 53.27 E-value: 8.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1074 KFVDlkSADGKNI------GKKYVASVST-----VDKAIEVAYAEAD--AWNHINAEDRALIVEKFLDLLEKERHLIASC 1140
Cdd:PLN02466 65 QFVD--AASGKTFptldprTGEVIAHVAEgdaedVNRAVAAARKAFDegPWPKMTAYERSRILLRFADLLEKHNDELAAL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1141 LVTESNVSVED-AHIQIDKTIQQVAYYCLQAKKEFA---------HPELLPGPTGEIdelslkgrGVVVSMSSScdlLIR 1210
Cdd:PLN02466 143 ETWDNGKPYEQsAKAELPMFARLFRYYAGWADKIHGltvpadgphHVQTLHEPIGVA--------GQIIPWNFP---LLM 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1211 FVGQTTAALLAGNTVVAKPAYTGSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVH 1290
Cdd:PLN02466 212 FAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVL 291
|
250 260
....*....|....*....|..
gi 754263081 1291 QALA--------LRRGAIIPFV 1304
Cdd:PLN02466 292 ELAAksnlkpvtLELGGKSPFI 313
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
1074-1292 |
2.26e-06 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 51.97 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1074 KFVDLKSADGKNIGKKYVASVSTVDKAIEV---AYAEADAWNHINAEDRALIVEKFLDLLEKERHLIAScLVTESNVS-- 1148
Cdd:cd07141 23 TFPTINPATGEKICEVQEGDKADVDKAVKAaraAFKLGSPWRTMDASERGRLLNKLADLIERDRAYLAS-LETLDNGKpf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1149 VEDAHIQIDKTIQQVAYYCLQAKKefAHPELLPGPTGEIDELSLKGRGVVVSMSSSCDLLIRFVGQTTAALLAGNTVVAK 1228
Cdd:cd07141 102 SKSYLVDLPGAIKVLRYYAGWADK--IHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLK 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 754263081 1229 PAYTGSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQA 1292
Cdd:cd07141 180 PAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQA 243
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
1061-1296 |
2.36e-06 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 52.06 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1061 ITNIVAGE--KAKKDKFVD-LKSADGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLI 1137
Cdd:PLN02419 114 VPNLIGGSfvESQSSSFIDvINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1138 ASCLVTESNVSVEDAHIQIDKTIQQVAYYCLQAKKEFAhpELLPGPTGEIDELSLKGR-GVVVSMSSSCDLLIRFVGQTT 1216
Cdd:PLN02419 194 AMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMG--EYLPNVSNGVDTYSIREPlGVCAGICPFNFPAMIPLWMFP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1217 AALLAGNTVVAKPAYTGSLTAYNIVKLMLKAGVDPKVINLILSDDEEItSALLFNSKVALVTFSGSISAVKQVHQALALR 1296
Cdd:PLN02419 272 VAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAAAK 350
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
1215-1301 |
6.80e-06 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 50.28 E-value: 6.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1215 TTAALLAGNTVVAKPAYTGSLTAYNIVKLMLKA----GVDPKVINLILSdDEEITSALLFNSKVALVTFSGSISAVKQVH 1290
Cdd:cd07130 153 AAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVG 231
|
90
....*....|.
gi 754263081 1291 QALALRRGAII 1301
Cdd:cd07130 232 QAVAARFGRSL 242
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
1081-1294 |
1.33e-05 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 49.30 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1081 ADGKNIGKKYVASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSVEDAHIQIDKTI 1160
Cdd:cd07107 5 ATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMVAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1161 QQVAYYCLQAKKefAHPELLPGPTGEIDELSLKGRGVVVSMSSSCDLLIRFVGQTTAALLAGNTVVAKPAYTGSLTAYNI 1240
Cdd:cd07107 85 ALLDYFAGLVTE--LKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 754263081 1241 VKLMLKAgVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALA 1294
Cdd:cd07107 163 AELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAA 215
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
1097-1289 |
1.66e-05 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 49.12 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1097 VDKAIEVAYA--EADAWNHINAEDRALIVEKFLDLLEKERHLIA--SCLVTESNV--SVEDahiQIDKTIQQVAYYCLQA 1170
Cdd:PRK09847 59 IDRAVSAARGvfERGDWSLSSPAKRKAVLNKLADLMEAHAEELAllETLDTGKPIrhSLRD---DIPGAARAIRWYAEAI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1171 KKEFAHPellpGPTGEiDELSLKGR---GVVVSMSSSCDLLIRFVGQTTAALLAGNTVVAKPAYTGSLTAYNIVKLMLKA 1247
Cdd:PRK09847 136 DKVYGEV----ATTSS-HELAMIVRepvGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEA 210
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 754263081 1248 GVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQV 1289
Cdd:PRK09847 211 GLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQL 252
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
598-839 |
3.97e-05 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 47.86 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 598 LKNAQSAFEDWNNTPASQRANILEKFANLLEKNTDEFIAIAMIEAGKTL--------SNAIDEVREAVDfcryYAAQARR 669
Cdd:cd07127 90 LAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFmmafqaggPHAQDRGLEAVA----YAWREMS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 670 EF------------NGPIELPalsdhlKQIEFTGRGAMVCIS-----PWNFPLAIFlgqitAVLAAGNTVVAKPAEQT-- 730
Cdd:cd07127 166 RIpptaewekpqgkHDPLAME------KTFTVVPRGVALVIGcstfpTWNGYPGLF-----ASLATGNPVIVKPHPAAil 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 731 --PIIAYKAIKLLFKAGL-PKGVL--QFTPGDGATvgSALVQSPVCKGVIFTGSTEVAGIINQTLASKSseivpFIAETG 805
Cdd:cd07127 235 plAITVQVAREVLAEAGFdPNLVTlaADTPEEPIA--QTLATRPEVRIIDFTGSNAFGDWLEANARQAQ-----VYTEKA 307
|
250 260 270
....*....|....*....|....*....|....*..
gi 754263081 806 GQNAMIVDSSSlpeQVTGDVIRSAFDSA---GQRCSA 839
Cdd:cd07127 308 GVNTVVVDSTD---DLKAMLRNLAFSLSlysGQMCTT 341
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
1092-1306 |
1.37e-04 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 46.29 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1092 ASVSTVDKAIEVAYAEADAWNHINAEDRALIVEKFLDLLEKERHLIASCLVTESNVSV-EDAHIQIDKTIQQVAYY--CL 1168
Cdd:cd07117 35 ATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIrETRAVDIPLAADHFRYFagVI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1169 QAKKefahpellpGPTGEIDE--LSLKGR---GVVVSMSSSCDLLIRFVGQTTAALLAGNTVVAKPAYTGSLTAYNIVKL 1243
Cdd:cd07117 115 RAEE---------GSANMIDEdtLSIVLRepiGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKI 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 754263081 1244 MlkAGVDPK-VINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALALRrgaIIPFVAE 1306
Cdd:cd07117 186 I--QDVLPKgVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKK---LIPATLE 244
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
1074-1294 |
3.42e-04 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 44.81 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1074 KFVDlkSADGKNIGKK------YVASVSTVDKA-IEVAYAEA-DAWNH-----INAEDRALIVEKFLDLLEKE-RHLIAS 1139
Cdd:PLN02766 28 EFVD--AASGKTFETRdprtgeVIARIAEGDKEdVDLAVKAArEAFDHgpwprMSGFERGRIMMKFADLIEEHiEELAAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1140 CLVTESNVSVEDAHIQIDKTIQQVAYYCLQAKKefAHPELLPgPTGEIDELSLKGR-GVVVSMSSSCDLLIRFVGQTTAA 1218
Cdd:PLN02766 106 DTIDAGKLFALGKAVDIPAAAGLLRYYAGAADK--IHGETLK-MSRQLQGYTLKEPiGVVGHIIPWNFPSTMFFMKVAPA 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 754263081 1219 LLAGNTVVAKPAYTGSLTAYNIVKLMLKAGVDPKVINLILSDDEEITSALLFNSKVALVTFSGSISAVKQVHQALA 1294
Cdd:PLN02766 183 LAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAA 258
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
1091-1336 |
4.06e-04 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 44.57 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1091 VASVST--VDKAIEVAYAEADAWNHINA---EDRALIVEKF-LDLLEKERHLIASCLVTESNVSveDAHIQIDKTIQQVA 1164
Cdd:cd07128 28 VARVSSegLDFAAAVAYAREKGGPALRAltfHERAAMLKALaKYLMERKEDLYALSAATGATRR--DSWIDIDGGIGTLF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1165 YYCLQAKKEFAHPELLPgpTGEIDELSLKG-----------RGVVVSMSS----SCDLLIRFvgqtTAALLAGNTVVAKP 1229
Cdd:cd07128 106 AYASLGRRELPNAHFLV--EGDVEPLSKDGtfvgqhiltprRGVAVHINAfnfpVWGMLEKF----APALLAGVPVIVKP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1230 AYTGSLTAYNIVKLMLKAGVDPK-VINLILSDDEEITSALLFNSkvaLVTFSGSISAVKQ--VHQALaLRRGaiIPFVAE 1306
Cdd:cd07128 180 ATATAYLTEAVVKDIVESGLLPEgALQLICGSVGDLLDHLGEQD---VVAFTGSAATAAKlrAHPNI-VARS--IRFNAE 253
|
250 260 270
....*....|....*....|....*....|....*.
gi 754263081 1307 svAKDGKCTSLAiETASP------LYLRRFVVEKTV 1336
Cdd:cd07128 254 --ADSLNAAILG-PDATPgtpefdLFVKEVAREMTV 286
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
693-990 |
1.95e-03 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 42.25 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 693 GAMVCISPWNFPLAIFLGQITAVLAAGNTVVAKPAEQTPIIAYKAIKLLF----KAGLPKGVLQFTPGDGATVGSALVQS 768
Cdd:cd07081 97 GVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLqaavAAGAPENLIGWIDNPSIELAQRLMKF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 769 PVCKGVIFTGSTEVagiinqtLASKSSEIVPFIAETGGQNAMIVDSSSLPEQVTGDVIRSAFDSAGQRCSALRILCLQED 848
Cdd:cd07081 177 PGIGLLLATGGPAV-------VKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVVDS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 849 IADnyikmivgAMKELKIGDSKYIDT-----DVGPVIDKEAADNLNAYIEEKKKQFKLVYQAQPNEdtQKGTFVMPTAFE 923
Cdd:cd07081 250 VYD--------EVMRLFEGQGAYKLTaeelqQVQPVILKNGDVNRDIVGQDAYKIAAAAGLKVPQE--TRILIGEVTSLA 319
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 754263081 924 IEKLsdLGREQFGPILHILRFK--ANELSKLIKDINSTGYGLTAGVHSR---INEVMNYVKNNIKAGNVYVN 990
Cdd:cd07081 320 EHEP--FAHEKLSPVLAMYRAAnfADADAKALALKLEGGCGHTSAMYSDnikAIENMNQFANAMKTSRFVKN 389
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
1217-1294 |
9.53e-03 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 40.01 E-value: 9.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754263081 1217 AALLAGNTVVAKPaytgSLTAYNIVKLMLK---AGVDPKVINLILSDDEEITSALLFnsKVALVTFSGSISAVKQVHQAL 1293
Cdd:PTZ00381 132 GAIAAGNTVVLKP----SELSPHTSKLMAKlltKYLDPSYVRVIEGGVEVTTELLKE--PFDHIFFTGSPRVGKLVMQAA 205
|
.
gi 754263081 1294 A 1294
Cdd:PTZ00381 206 A 206
|
|
| |
