|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
424-950 |
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: 543.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 424 APQNFLYALFapeeqalkdQEEVFREAVAQRWDTFagprraqnrleeaeqaagrqaprtgrFANEPDTDPALEANR-EWA 502
Cdd:cd07125 1 ANSSFVNRIF---------DLEVPLEALADALKAF--------------------------DEKEWEAIPIINGEEtETG 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 503 LKALATDPGEHG--VEEVTDAG--VVDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQ 578
Cdd:cd07125 46 EGAPVIDPADHErtIGEVSLADaeDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLAD 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 579 TDPEISEAIDFCTYYAQSARLLDSY-----------AAEFTPYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQ 647
Cdd:cd07125 126 ADAEVREAIDFCRYYAAQARELFSDpelpgptgelnGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQ 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 648 VVHCAKLVVKAFRaglEAqGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLFRSWKPE-----LNIMAETS 722
Cdd:cd07125 206 TPLIAARAVELLH---EA-GVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAErdgpiLPLIAETG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 723 GKNALIITPSADPDLAIQDLYLSAFGHSGQKCSASSLVIFVGAAgeSQRLRSQLVDAVKTLIPGPGYEITTTMNGLAEAP 802
Cdd:cd07125 282 GKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEI--AERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKP 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 803 GEKLLRGLTQLEPGETWLVKPEKLNE-DGTLWSPGIRDNVrpGSWFHVNECFGPVLGIMHAE--TLEQAIEWQNSTGYGL 879
Cdd:cd07125 360 AGKLLRAHTELMRGEAWLIAPAPLDDgNGYFVAPGIIEIV--GIFDLTTEVFGPILHVIRFKaeDLDEAIEDINATGYGL 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1196634871 880 TGGIHSLDDDEIQYWIDNVEVGNAYVNRGITGAIVQRQSFGGWKKSVMGPgaKAGGPNYVPQMGTWADGEL 950
Cdd:cd07125 438 TLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGP--KAGGPNYLLRFGNEKTVSL 506
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
28-960 |
2.61e-121 |
|
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: 397.88 E-value: 2.61e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 28 HSWLASTADEQDPATEQ-LADLLRNPDGVAFTMDFVDRVMRPEDDKVAAHALKSVTTTYDASFlglINGSLVGLG-GFFG 105
Cdd:COG0506 18 RRLVEAIRAAPEGGVEAlLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLAKSPSFL---VNASTWGLMlTLVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 106 PILPNLVMPLARMRMRQMVGHLVLDAESDALNKTLDKAAESGEQLNLNLLGEAVLGDDEARSRAERTLKLIK-----NPR 180
Cdd:COG0506 95 RLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAARKLRAKGYRVSLDLLGEAVLTEAEAERYLDAYLEALEaigaaGVD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 181 VTYVSVKASSMVAQLNPWDIEGSLVRLKERLRPLYEAAARRPdrVFINLDMEEYHDLHLTVRLFTELLSEPEFTN-LEAG 259
Cdd:COG0506 175 RPGVSVKLSALGPRYSPAQRERVVEELLERLRPLARAAREAG--IFVTIDMEEYDRLDLTLDVFERLLADPELAGwPGVG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 260 IVLQAYLPDTFDALAHLAEFAKqrvaEGGSHIKIRIVKGANLSMEHVQGEIHGWPAAPYSTKDEVDANYYRLLDYILrpE 339
Cdd:COG0506 253 IVLQAYLKRAEADLDRLAALAR----RGGRRIRVRLVKGAYWDPEIVRAQVHGWPYPVFTRKADTDANYLRCARKLL--E 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 340 FADCVRIGVATHNLYTAAFAYKLGTKRGVMRmmDS---EMLQGMSPAQQTAVRKAFEGRQILYTPVVHMEDFDVAVSYLV 416
Cdd:COG0506 327 AGDAIYPQFATHNARTIAAALALAGERGRPP--DRfefQMLYGMGEDLQRALAAVDGGRLLLYCPVVAPVGGDAALAYLL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 417 RRLEENSAPQNFLYALFAPEEQALKDQEE--VFREAVAQRWDTFAGPRRAQNRLEEAEQAAGRQAPRTGRFANEPDTDPA 494
Cdd:COG0506 405 RRLLENNSFLNFFVADFDDDEDLLEFPREppRFLAALAAPTPPPPPPLRRQRRRRRRARGGALAAALAAAAAAAALAAAA 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 495 LEANREWALKAL--------------ATDPGEHGVEEVTDAGVVDKHVSRAAELGAEWGARPAEDRARALEAVADELANR 560
Cdd:COG0506 485 AAAAALAAAAAGaaaaaaaaavavvpAAAAAVVAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAEAAE 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 561 RGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSARLLdsYAAEFTPYRVTVVTPPWNFPVAIPTGGIAAALAAGSAV 640
Cdd:COG0506 565 AALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAAR--AAAPPPPPPGGLVALLPLGPLAAAAAAAAAAAAAAAAA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 641 IIKPAPQVVHCAKLVVKA-----FRAGLEAQGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLFRSWKPEL 715
Cdd:COG0506 643 AAAAAAAAAAAAAAAAAAaaaalAAAALAALLLLLGGAGGGVLVLGAGGGAGGAAALTLAAAAAAATAATAAAAAAAAAL 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 716 NIMAETSGKNALIITPSADPDLAIQDLYLS-------AFGHSGQKCSASSLVIFVGAAGESQRLRSQLVDAVKTLIPGPG 788
Cdd:COG0506 723 AAAAAAAAAAAAAAAGGAAAAAAAAAAAAAvaavaasAAASASASASLLSLLALLLLDADLVILLLALAAAAAALLVGGP 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 789 YEITTTMNGLAEAPGEKLLRGLTQLEPGETWLVKPEKLNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQA 868
Cdd:COG0506 803 GAAALALGIVEDAAAAALLLALAALELGEEELLLPGGGPLVPGLLTAPLLVALILGLIVLVLLEIVLVLALVLALALDLA 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 869 IEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVGNAYVNRGITGAIVQRQSFGGWKKSVMGPGAKAGGPNYVPQMGTWADG 948
Cdd:COG0506 883 ALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGTLALAAAAA 962
|
970
....*....|..
gi 1196634871 949 ELRPREVDVPAA 960
Cdd:COG0506 963 AATALAAAAAAA 974
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
485-941 |
6.58e-90 |
|
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: 299.14 E-value: 6.58e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 485 FANEPDTDPALEANREWALKALATDPGEHGVE-------------------------EV------TDAGVVDKHVSRAAE 533
Cdd:cd07124 1 FRNEPFTDFADEENRAAFRAALARVREELGREyplviggkevrteekiesrnpadpsEVlgtvqkATKEEAEAAVQAARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 534 LGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSARLLDSYAAE------- 606
Cdd:cd07124 81 AFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEmvpgedn 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 607 ---FTPYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFRaglEAqGLDPDLVQLVfTDEGDA 683
Cdd:cd07124 161 ryvYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILE---EA-GLPPGVVNFL-PGPGEE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 684 -GRALVSHADVDAVILTGASDTG----KLFRSWKPELN----IMAETSGKNALIITPSADPDLAIQDLYLSAFGHSGQKC 754
Cdd:cd07124 236 vGDYLVEHPDVRFIAFTGSREVGlriyERAAKVQPGQKwlkrVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKC 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 755 SASSLVIFVGAAgeSQRLRSQLVDAVKTLIPGPGYEITTTMNGLAEAPGEKLLRGLTQLEPGETWLV---KPEKLNEDGT 831
Cdd:cd07124 316 SACSRVIVHESV--YDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEGRLLlggEVLELAAEGY 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 832 LWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVGNAYVNRGITG 911
Cdd:cd07124 394 FVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITG 473
|
490 500 510
....*....|....*....|....*....|
gi 1196634871 912 AIVQRQSFGGWKKSvmGPGAKAGGPNYVPQ 941
Cdd:cd07124 474 ALVGRQPFGGFKMS--GTGSKAGGPDYLLQ 501
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
517-935 |
1.85e-83 |
|
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: 280.09 E-value: 1.85e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 517 EVTDAGV--VDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYA 594
Cdd:COG1012 36 RVPAATAedVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARGEVDRAADFLRYYA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 595 QSARLLDSYAAE-----------FTPYRVTVVTPPWNFPVAIP------------TggiaaalaagsaVIIKPAPQVVHC 651
Cdd:COG1012 116 GEARRLYGETIPsdapgtrayvrREPLGVVGAITPWNFPLALAawklapalaagnT------------VVLKPAEQTPLS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 652 AKLVVKAFRaglEAqGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLFRSW-----KPelnIMAETSGKNA 726
Cdd:COG1012 184 ALLLAELLE---EA-GLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAaaenlKR---VTLELGGKNP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 727 LIITPSADPDLAIQDLYLSAFGHSGQKCSASSlVIFVgAAGESQRLRSQLVDAVKTLIPGPGYEITTTMNGLAEAPGEKL 806
Cdd:COG1012 257 AIVLDDADLDAAVEAAVRGAFGNAGQRCTAAS-RLLV-HESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLER 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 807 LRGLTQ--LEPGETWLVKPEKLN-EDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGI 883
Cdd:COG1012 335 VLAYIEdaVAEGAELLTGGRRPDgEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASV 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1196634871 884 HSLDDDEIQYWIDNVEVGNAYVNRGITGAiVQRQSFGGWKKSvmGPGAKAGG 935
Cdd:COG1012 415 FTRDLARARRVARRLEAGMVWINDGTTGA-VPQAPFGGVKQS--GIGREGGR 463
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
207-1133 |
8.83e-80 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 285.61 E-value: 8.83e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 207 LKERLRPLYEAAARRpdRVFINLDMEEYHDLHLTVRLFTELLSEPEFTNLEA-GIVLQAYL---PDTFDALAHLAEFAKQ 282
Cdd:PRK11905 269 LLPRLKALALLAKAY--DIGLNIDAEEADRLELSLDLLEALCSDPDLAGWNGiGFVVQAYQkrcPFVIDYLIDLARRSGR 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 283 RvaeggshIKIRIVKGANLSME----HVQGeIHGWPAapYSTKDEVDANYY----RLLDYilrpefADCVRIGVATHNLY 354
Cdd:PRK11905 347 R-------LMVRLVKGAYWDAEikraQVDG-LEGFPV--FTRKVHTDVSYIacarKLLAA------RDVIYPQFATHNAQ 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 355 TAAFAYKLGTKRGvmrmmDSEM--LQGM-SPAQQTAVRKAFEGRQI-LYTPVVHMEDFdvaVSYLVRRLEENSAPQNFLY 430
Cdd:PRK11905 411 TLAAIYELAGGKG-----DFEFqcLHGMgEPLYDQVVGKEKLGRPCrIYAPVGTHETL---LAYLVRRLLENGANSSFVN 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 431 AL----FAPEEQALKDQEEVFREAVAQR------WDTFAGPRR--------AQNRLeeAEQAAGRQAPRTGRFANEP--D 490
Cdd:PRK11905 483 RIvdenVPVEELIADPVEKVAAMGVAPHpqiplpRDLYGPERRnskgldlsDEATL--AALDEALNAFAAKTWHAAPllA 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 491 TDPALEANREwalkalATDPGEHG--VEEVT--DAGVVDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFIS 566
Cdd:PRK11905 561 GGDVDGGTRP------VLNPADHDdvVGTVTeaSAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFA 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 567 VAAYEANKTVTQTDPEISEAIDFCTYYAQSARLLDSyAAEFTPYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAP 646
Cdd:PRK11905 635 LAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLN-GPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAE 713
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 647 QVVHCAKLVVKAFRaglEAqGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLFRSW-----KPELNIMAET 721
Cdd:PRK11905 714 QTPLIAARAVRLLH---EA-GVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTlakrsGPPVPLIAET 789
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 722 SGKNALIITPSADPDLAIQDLYLSAFGHSGQKCSAssL-VIFVgaagesQ-----RLRSQLVDAVKTLIPGPGYEITTTM 795
Cdd:PRK11905 790 GGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSA--LrVLCL------QedvadRVLTMLKGAMDELRIGDPWRLSTDV 861
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 796 ---------NGLAE--APGEKLLRGLTQLE-PGETwlvkpeklnEDGTLWSP------GIRDNVRpgswfhvnECFGPVL 857
Cdd:PRK11905 862 gpvidaeaqANIEAhiEAMRAAGRLVHQLPlPAET---------EKGTFVAPtlieidSISDLER--------EVFGPVL 924
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 858 GIM--HAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVGNAYVNRGITGAIVQRQSFGGWKKSvmGPGAKAGG 935
Cdd:PRK11905 925 HVVrfKADELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLS--GTGPKAGG 1002
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 936 PNYVPQMgtwadgeLRPREVDVPAAVANELRNLASRAALSDAD-VEWLWRAAELDQLAWMEEFGRDHDRTGLISEANIFR 1014
Cdd:PRK11905 1003 PLYLGRL-------VREAPTPIPPAHESVDTDAAARDFLAWLDkEGKAALAAAARDARARSALGLEQELPGPTGESNLLS 1075
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 1015 YVPlldklRVRI---GEGfaLRDVIRQALAAAVTGTTVEFSATPALAEQLAVL------GIEVRQ--LSDAAFASELSRA 1083
Cdd:PRK11905 1076 LHP-----RGRVlcvADT--EEALLRQLAAALATGNVAVVAADSGLAAALADLpglvaaRIDWTQdwEADDPFAGALLEG 1148
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|
gi 1196634871 1084 ESARVRTLgavadtTREAAVESNSVILDQPVLADGRRELLPYLLEQAVSV 1133
Cdd:PRK11905 1149 DAERARAV------RQALAARPGAIVPLIAAEPTDAYDLARLVEERSVSI 1192
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
517-939 |
1.06e-75 |
|
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: 257.84 E-value: 1.06e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 517 EVTDAGV--VDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYA 594
Cdd:pfam00171 22 TVPAATAedVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGEVDRAIDVLRYYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 595 QSARLLDSYAAEFTPYRVTVVT--P--------PWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFRaglE 664
Cdd:pfam00171 102 GLARRLDGETLPSDPGRLAYTRrePlgvvgaitPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFE---E 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 665 AqGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLF-----RSWKPelnIMAETSGKNALIITPSADPDLAI 739
Cdd:pfam00171 179 A-GLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIaeaaaQNLKR---VTLELGGKNPLIVLEDADLDAAV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 740 QDLYLSAFGHSGQKCSASSLVIFVgaagES--QRLRSQLVDAVKTLIPGPGYEITTTMNGLAEAPGEKLLRGLTQ--LEP 815
Cdd:pfam00171 255 EAAVFGAFGNAGQVCTATSRLLVH----ESiyDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEdaKEE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 816 GETWLVKPEKLNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWI 895
Cdd:pfam00171 331 GAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVA 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1196634871 896 DNVEVGNAYVNRGITGAIVQRqSFGGWKKSVMGpgaKAGGPNYV 939
Cdd:pfam00171 411 RRLEAGMVWINDYTTGDADGL-PFGGFKQSGFG---REGGPYGL 450
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
48-940 |
1.04e-71 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 259.75 E-value: 1.04e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 48 LLRNPDgvAFTmdfVDRVMRpedDKVA-----AHALKSVTTTYDASFLGL-INGSLVGL----GGFFGPILPNLV----M 113
Cdd:PRK11904 91 LLRIPD--AAT---ADALIR---DKLSgadwkKHLGRSDSLFVNASTWGLmLTGKVVKLdkkaDGTPSGVLKRLVnrlgE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 114 PLARMRMRQ----MVGHLVLDAESDALNKTLDKAAESGEQLNLNLLGEAVLGDDEARS-------------RAERTLKLI 176
Cdd:PRK11904 163 PVIRKAMRQamkiMGKQFVLGRTIEEALKRARSARNKGYRYSFDMLGEAALTAADAERyfkayaraieaigRAAGGADLP 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 177 KNPRVtyvSVKASSM-----VAQlnpwdIEGSLVRLKERLRPLYEAAARRpdRVFINLDMEEYHDLHLTVRLFTELLSEP 251
Cdd:PRK11904 243 ARPGI---SIKLSALhpryeAAQ-----RERVLAELVPRVLELARLAKEA--NIGLTIDAEEADRLELSLDLFEALFRDP 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 252 EFTNLEA-GIVLQAYLPDTFDALAHLAEFAKQRvaegGSHIKIRIVKGANLSMEHVQGEIHGWPAAP-YSTKDEVDANYY 329
Cdd:PRK11904 313 SLKGWGGfGLAVQAYQKRALPVLDWLADLARRQ----GRRIPVRLVKGAYWDSEIKRAQELGLPGYPvFTRKAATDVSYL 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 330 RLLDYILR------PEFAdcvrigvaTHNLYTAAFayklgtkrgVMRMMDSE-----MLQGMSPAQQTAVRKAFEGRQIL 398
Cdd:PRK11904 389 ACARKLLSargaiyPQFA--------THNAHTVAA---------ILEMAGHRgfefqRLHGMGEALYDALLDAPGIPCRI 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 399 YTPVVHMEDFdvaVSYLVRRLEENSAPQNFLYALFAPE---EQALKDQEEVFREAVAQR-------WDTFAGPRR----- 463
Cdd:PRK11904 452 YAPVGSHKDL---LPYLVRRLLENGANSSFVHRLVDPDvpiEELVADPVEKLRSFETLPnpkiplpRDIFGPERKnskgl 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 464 ------AQNRLEEAEQAAGRQAPRTGRFANEPDTdpaleanrewalKALATDPGEHG--VEEVTDAGV--VDKHVSRAAE 533
Cdd:PRK11904 529 nlndrsELEPLAAAIAAFLEKQWQAGPIINGEGE------------ARPVVSPADRRrvVGEVAFADAeqVEQALAAARA 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 534 LGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSARLLDSyAAEFTP---- 609
Cdd:PRK11904 597 AFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFG-APEKLPgptg 675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 610 ----YR-----VTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFragLEAqGLDPDLVQLVFTDE 680
Cdd:PRK11904 676 esneLRlhgrgVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLL---HEA-GIPKDVLQLLPGDG 751
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 681 GDAGRALVSHADVDAVILTGASDTGKLF-RS--WK--PELNIMAETSGKNALIITPSADPDLAIQDLYLSAFGHSGQKCS 755
Cdd:PRK11904 752 ATVGAALTADPRIAGVAFTGSTETARIInRTlaARdgPIVPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCS 831
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 756 AssL-VIFV-------------GAAGEsqrLRSQLVDAVKTLIpGPgyEITttmnglAEAPgEKLLRGLTQLEPGETWLV 821
Cdd:PRK11904 832 A--LrVLFVqediadrviemlkGAMAE---LKVGDPRLLSTDV-GP--VID------AEAK-ANLDAHIERMKREARLLA 896
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 822 KPE--KLNEDGTLWSP------GIRDNVRpgswfhvnECFGPVLGIMH--AETLEQAIEWQNSTGYGLTGGIHSLDDDEI 891
Cdd:PRK11904 897 QLPlpAGTENGHFVAPtafeidSISQLER--------EVFGPILHVIRykASDLDKVIDAINATGYGLTLGIHSRIEETA 968
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*....
gi 1196634871 892 QYWIDNVEVGNAYVNRGITGAIVQRQSFGGWKKSvmGPGAKAGGPNYVP 940
Cdd:PRK11904 969 DRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLS--GTGPKAGGPHYLL 1015
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
138-429 |
3.08e-71 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 239.70 E-value: 3.08e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 138 KTLDKAAESGEQLNLNLLGEAVLGDDEARSRAERTLKLI----------KNPRVTYVSVKASSMVAQLNPWDIEGSLVRL 207
Cdd:pfam01619 3 KTIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIdalgkaagpwPLGPRPGISVKLSALHPRYEPLERERVMAEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 208 KERLRPLYEAAARRPdrVFINLDMEEYHDLHLTVRLFTELLSEPEFTNLE-AGIVLQAYLPDTFDALAHLAEFAKQRvae 286
Cdd:pfam01619 83 LERLRPLCRLAKELG--VRLNIDAEEADRLDLTLDLFERLLAEPELRGWNgVGITLQAYLKDALAVLDWLLELARRR--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 287 gGSHIKIRIVKGANLSMEHVQGEIHGWPAAPYSTKDEVDANYYRLLDYILrpEFADCVRIGVATHNLYTAAFAYKLGTKR 366
Cdd:pfam01619 158 -GRPLGVRLVKGAYWDSEIKRAQQGGWPYPVFTRKEATDANYEACARFLL--ENHDRIYPQFATHNARSVAAALALAEEL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1196634871 367 GV-MRMMDSEMLQGMSPAQQTAVRKAfeGRQ-ILYTPVVHMEDFdvaVSYLVRRLEENSAPQNFL 429
Cdd:pfam01619 235 GIpPRRFEFQQLYGMGDNLSFALVAA--GYRvRKYAPVGPHEEL---LAYLVRRLLENTANSSFV 294
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
485-941 |
5.46e-70 |
|
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: 243.62 E-value: 5.46e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 485 FANEPDTDPALEANREWALKALATDPGEHGV--------EEVTDAGVVD-------------------KHVSRAAELGA- 536
Cdd:TIGR01237 1 YKHEPFTDFADEENRQAFFKALATVKEQLGKtyplvingERVETENKIVsinpcdksevvgtvskasqEHAEHALQAAAk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 537 ---EWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSARLLD------SYAAE- 606
Cdd:TIGR01237 81 afeAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAkgkpvnSREGEt 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 607 ----FTPYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPApqvvHCAKLVVKAFRAGLEAQGLDPDLVQLVFTDEGD 682
Cdd:TIGR01237 161 nqyvYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPA----EAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 683 AGRALVSHADVDAVILTGASDTG--------KLFRSWKPELNIMAETSGKNALIITPSADPDLAIQDLYLSAFGHSGQKC 754
Cdd:TIGR01237 237 VGDYLVDHPKTSLITFTGSREVGtriferaaKVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKC 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 755 SASSLVIFVGAAGESqrLRSQLVDAVKTLIPGPGYEITTTMNGLAEAPGEKLLRGLTQLEPGETWLVKPEKLN-EDGTLW 833
Cdd:TIGR01237 317 SAGSRAVVHEKVYDE--VVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEGRLVSGGCGDdSKGYFI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 834 SPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVGNAYVNRGITGAI 913
Cdd:TIGR01237 395 GPTIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAI 474
|
490 500
....*....|....*....|....*...
gi 1196634871 914 VQRQSFGGWKKSvmGPGAKAGGPNYVPQ 941
Cdd:TIGR01237 475 VGYQPFGGFKMS--GTDSKAGGPDYLAL 500
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
525-936 |
6.99e-67 |
|
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: 232.10 E-value: 6.99e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 525 DKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSARLL--DS 602
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLhgEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 603 YAAEFT---------PYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFRaglEAqGLDPDLV 673
Cdd:cd07078 81 IPSPDPgelaivrrePLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLA---EA-GLPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 674 QLVFTDEGDAGRALVSHADVDAVILTGASDTGK-LFRSWKPEL-NIMAETSGKNALIITPSADPDLAIQDLYLSAFGHSG 751
Cdd:cd07078 157 NVVTGDGDEVGAALASHPRVDKISFTGSTAVGKaIMRAAAENLkRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 752 QKCSASSlVIFVgAAGESQRLRSQLVDAVKTLIPGPGYEITTTMNGL---------------AEAPGEKLLRGLTQLEPG 816
Cdd:cd07078 237 QVCTAAS-RLLV-HESIYDEFVERLVERVKALKVGNPLDPDTDMGPLisaaqldrvlayiedAKAEGAKLLCGGKRLEGG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 817 ETWLVKPeklnedgtlwspGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWID 896
Cdd:cd07078 315 KGYFVPP------------TVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAE 382
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1196634871 897 NVEVGNAYVNRGITGAIVQrQSFGGWKKSVMGpgaKAGGP 936
Cdd:cd07078 383 RLEAGTVWINDYSVGAEPS-APFGGVKQSGIG---REGGP 418
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
74-1088 |
1.72e-65 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 242.15 E-value: 1.72e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 74 AAHALKSVTTTYDASFLGLINGSLVGLGGffgpilPNLVMPLARMRMRQMVGHLVLDAESDALNKTLDKAAESGEQLNLN 153
Cdd:COG4230 133 LLLGLLLLTALESSLSLASGLLRLLGRLG------RPGIRRAMRAAMMMMMGLFGVGFVTEEAAEAARKAARKREYYYYD 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 154 LLGEAVLGDDEARSRAERTLKLIKN----------PRVTYVSVKASSMVAQLNPWDIEGSLVRLKERLRPLYEAAARrpD 223
Cdd:COG4230 207 MLGEAAAAAADAAAYAYAYAAAAAAaiaaagggsgGPGPSISSSLSVLLSARHPRYRRRREERLLLLLLPLLALLAL--A 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 224 RVFINLDMEEYHDLHLTVRLFTELLSEPEFTNLEAGIVLQAY--------LPDTFDALAHLAEFAKQRVaeggshiKIRI 295
Cdd:COG4230 285 AININIDEEEDAEELLLLLLLLDLLAALLLDGGLGGGGGVGQavqayakaLLLVLDLLARRRRRRRRRL-------VVRL 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 296 VKGANLSMEHVQGEIHGWPAAPYSTKDEVDANYYRLLdyiLRPEFADCVRI--GVATHNLYTAAFAYKLGT-----KRGV 368
Cdd:COG4230 358 VKGAEWDREIQRAQVLGYVVYPVTTRKVLYDAAALAL---ALLLLAAQPAFapQFATHAAATAAAAAAAGGggefeFQCL 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 369 MRMMDSEMLQGMSPAQQTAVRkafegrqiLYTPVVHMEDFdvaVSYLVRRLEENSAPQNFLYALF---APEEQALKDQEE 445
Cdd:COG4230 435 HGMGEYLYDQVGRGKLGRPCR--------IYAPVGSHEDL---LAYLVRRLLENGANSSFVNRIAdedVPVEELIADPVE 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 446 VFREAVAQR-------WDTFAGPRRAQ------NRLEEAEQAAGRQAPRTGRFANEP--DTDPALEANREwalkalATDP 510
Cdd:COG4230 504 KARALGGAPhpriplpRDLYGPERRNSagldlsDEAVLAALSAALAAAAEKQWQAAPliAGEAASGEARP------VRNP 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 511 GEHG--VEEVTDAGV--VDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEA 586
Cdd:COG4230 578 ADHSdvVGTVVEATAadVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAIAEVREA 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 587 IDFCTYYAQSARLLDSYAAEFTPyRVTVVT-PPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFragLEA 665
Cdd:COG4230 658 VDFCRYYAAQARRLFAAPTVLRG-RGVFVCiSPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLL---HEA 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 666 qGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGK-----LFRSWKPELNIMAETSGKNALIITPSADPDLAIQ 740
Cdd:COG4230 734 -GVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARlinrtLAARDGPIVPLIAETGGQNAMIVDSSALPEQVVD 812
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 741 DLYLSAFGHSGQKCSAsslvifvgaagesqrLRSQLV--DAVKTLIpgpgyeitttmnglaeapgeKLLRGLTQ-LEPGE 817
Cdd:COG4230 813 DVLASAFDSAGQRCSA---------------LRVLCVqeDIADRVL--------------------EMLKGAMAeLRVGD 857
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 818 TWL----VKP--------------EKLNEDGTL-WSPGIRDNVRPGSWF--------HVN----ECFGPVLGIM--HAET 864
Cdd:COG4230 858 PADlstdVGPvidaearanleahiERMRAEGRLvHQLPLPEECANGTFVaptlieidSISdlerEVFGPVLHVVryKADE 937
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 865 LEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVGNAYVNRGITGAIVQRQSFGGWKKSvmGPGAKAGGPNYVPQMGT 944
Cdd:COG4230 938 LDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLS--GTGPKAGGPHYLLRFAT 1015
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 945 wadgeLRPREVDVPAAVANelrnlASRAALSDadvewlWRAAELDQLAWmeefgrdhdrTGLISEANIFRYVPlldklRV 1024
Cdd:COG4230 1016 -----ERTVTVNTTAAGGN-----ASLLALGD------WLASLLGALTL----------PGPTGERNTLTLRP-----RG 1064
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1196634871 1025 RI-GEGFALRDVIRQALAAAVTGTTVEFSATPALAEqlavLGIEVRQLSDAAFASELSRAESARV 1088
Cdd:COG4230 1065 RVlCLADSLEALLAQLAAALATGNRAVVAADLALAG----LPAVLLPPFDAVLFEGRLRALRQAL 1125
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
520-939 |
4.75e-65 |
|
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: 229.00 E-value: 4.75e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 520 DAGVVDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSARL 599
Cdd:cd07083 53 DKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 600 LDSYAAEFTPYR------------VTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFRaglEAqG 667
Cdd:cd07083 133 LRYPAVEVVPYPgednesfyvglgAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFH---EA-G 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 668 LDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLF----------RSWKPELniMAETSGKNALIITPSADPDL 737
Cdd:cd07083 209 FPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIyeaaarlapgQTWFKRL--YVETGGKNAIIVDETADFEL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 738 AIQDLYLSAFGHSGQKCSASSLVIFVGAAGEsqRLRSQLVDAVKTLIPGPGYEITTTMNGLAEAPGEKLLRGLTQLEPGE 817
Cdd:cd07083 287 VVEGVVVSAFGFQGQKCSAASRLILTQGAYE--PVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 818 TWLVKPEKLNE-DGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMH--AETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYW 894
Cdd:cd07083 365 GQLVLGGKRLEgEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRykDDDFAEALEVANSTPYGLTGGVYSRKREHLEEA 444
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1196634871 895 IDNVEVGNAYVNRGITGAIVQRQSFGGWKKSvmGPGAKAGGPNYV 939
Cdd:cd07083 445 RREFHVGNLYINRKITGALVGVQPFGGFKLS--GTNAKTGGPHYL 487
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
485-938 |
2.97e-64 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 227.13 E-value: 2.97e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 485 FANEPDTDPALEANREW---ALKALATDPGEH-----GVEEVTDA---------------GVVDK----HVSRAAELGAE 537
Cdd:PRK03137 5 YKHEPFTDFSVEENVEAfeeALKKVEKELGQDypliiGGERITTEdkivsinpanksevvGRVSKatkeLAEKAMQAALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 538 ----WGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSA-RLLD-----SYAAE- 606
Cdd:PRK03137 85 afetWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMlKLADgkpveSRPGEh 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 607 ----FTPYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAfragLEAQGLDPDLVQLVFTDEGD 682
Cdd:PRK03137 165 nryfYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEV----LEEAGLPAGVVNFVPGSGSE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 683 AGRALVSHADVDAVILTGASDTG-KLF-RSWK--PELN----IMAETSGKNALIITPSADPDLAIQDLYLSAFGHSGQKC 754
Cdd:PRK03137 241 VGDYLVDHPKTRFITFTGSREVGlRIYeRAAKvqPGQIwlkrVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 755 SASSLVIFVGAAGEsqRLRSQLVDAVKTLIPGPGyEITTTMNGLAEAPGEKLLRGLTQLEPGETWLVK-PEKLNEDGTLW 833
Cdd:PRK03137 321 SACSRAIVHEDVYD--EVLEKVVELTKELTVGNP-EDNAYMGPVINQASFDKIMSYIEIGKEEGRLVLgGEGDDSKGYFI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 834 SPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVGNAYVNRGITGAI 913
Cdd:PRK03137 398 QPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAI 477
|
490 500
....*....|....*....|....*
gi 1196634871 914 VQRQSFGGWKKSvmGPGAKAGGPNY 938
Cdd:PRK03137 478 VGYHPFGGFNMS--GTDSKAGGPDY 500
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
519-936 |
2.37e-58 |
|
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: 209.13 E-value: 2.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 519 TDAGVVDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSAR 598
Cdd:cd07131 34 STASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 599 LL--DSYAAE------FT---PYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFRAGleaqG 667
Cdd:cd07131 114 RLfgETVPSElpnkdaMTrrqPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEA----G 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 668 LDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLFRSWKPELNIMA--ETSGKNALIITPSADPDLAIQDLYLS 745
Cdd:cd07131 190 LPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRValEMGGKNPIIVMDDADLDLALEGALWS 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 746 AFGHSGQKCSASS-LVIFVGAAGEsqrLRSQLVDAVKTLIPGPGYEITTTMNGL-AEAPGEKLLR--GLTQLEpGETWLV 821
Cdd:cd07131 270 AFGTTGQRCTATSrLIVHESVYDE---FLKRFVERAKRLRVGDGLDEETDMGPLiNEAQLEKVLNynEIGKEE-GATLLL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 822 KPEKLN----EDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDN 897
Cdd:cd07131 346 GGERLTgggyEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRD 425
|
410 420 430
....*....|....*....|....*....|....*....
gi 1196634871 898 VEVGNAYVNRGITGAIVQrQSFGGWKKSvmGPGAKAGGP 936
Cdd:cd07131 426 LEAGITYVNAPTIGAEVH-LPFGGVKKS--GNGHREAGT 461
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
530-934 |
9.87e-57 |
|
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: 200.92 E-value: 9.87e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 530 RAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSARLL--------- 600
Cdd:cd06534 2 AARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLggpelpspd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 601 ---DSYAaEFTPYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFRaglEAqGLDPDLVQLVF 677
Cdd:cd06534 82 pggEAYV-RREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQ---EA-GLPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 678 TDEGDAGRALVSHADVDAVILTGASDTGK-LFRSWKPEL-NIMAETSGKNALIITPSADPDLAIQDLYLSAFGHSGQKCS 755
Cdd:cd06534 157 GGGDEVGAALLSHPRVDKISFTGSTAVGKaIMKAAAENLkPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 756 ASSLVIFVGAAGEsqrlrsQLVDAVKTLIpgpgyeitttmnglaeapgekllrgltqlepgetwlvkpeklnedgtlwsp 835
Cdd:cd06534 237 AASRLLVHESIYD------EFVEKLVTVL--------------------------------------------------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 836 girDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVGNAYVNRGITGAIVQ 915
Cdd:cd06534 260 ---VDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPE 336
|
410
....*....|....*....
gi 1196634871 916 rQSFGGWKKSvmGPGAKAG 934
Cdd:cd06534 337 -APFGGVKNS--GIGREGG 352
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
508-939 |
2.57e-54 |
|
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: 198.21 E-value: 2.57e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 508 TDPGEH----GVEEVTDAGVVDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEI 583
Cdd:TIGR01238 56 TNPADRrdivGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 584 SEAIDFCTYYAQSAR-LLDSYAAEftPYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFrag 662
Cdd:TIGR01238 136 REAVDFCRYYAKQVRdVLGEFSVE--SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELM--- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 663 LEAqGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLF-----RSWKPELNIMAETSGKNALIITPSADPDL 737
Cdd:TIGR01238 211 QEA-GFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLInqtlaQREDAPVPLIAETGGQNAMIVDSTALPEQ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 738 AIQDLYLSAFGHSGQKCSAssLVIFVGAAGESQRLRSQLVDAVKTLIPGPGYEITTTMNGLAEAPG-EKLLRGLTQLEpg 816
Cdd:TIGR01238 290 VVRDVLRSAFDSAGQRCSA--LRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAkQNLLAHIEHMS-- 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 817 ETWLVKPEKLNEDGTLWSPGirDNVRPgSWFHVN-------ECFGPVLGIM--HAETLEQAIEWQNSTGYGLTGGIHSLD 887
Cdd:TIGR01238 366 QTQKKIAQLTLDDSRACQHG--TFVAP-TLFELDdiaelseEVFGPVLHVVryKARELDQIVDQINQTGYGLTMGVHSRI 442
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1196634871 888 DDEIQYWIDNVEVGNAYVNRGITGAIVQRQSFGGwkKSVMGPGAKAGGPNYV 939
Cdd:TIGR01238 443 ETTYRWIEKHARVGNCYVNRNQVGAVVGVQPFGG--QGLSGTGPKAGGPHYL 492
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
207-1133 |
6.22e-53 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 203.28 E-value: 6.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 207 LKERLRPLYEAAaRRPDrVFINLDMEEYHDLHLTVRLFTELLSEPEFTNLEA-GIVLQAYL---PDTFDALAHLAEFAKQ 282
Cdd:PRK11809 349 LYPRLKSLTLLA-RQYD-IGINIDAEEADRLEISLDLLEKLCFEPELAGWNGiGFVIQAYQkrcPFVIDYLIDLARRSRR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 283 RvaeggshIKIRIVKGANLSMEHVQGEIHGWPAAP-YSTKDEVDANYY----RLL---DYILrPEFAdcvrigvaTHNLY 354
Cdd:PRK11809 427 R-------LMIRLVKGAYWDSEIKRAQVDGLEGYPvYTRKVYTDVSYLacarKLLavpNLIY-PQFA--------THNAH 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 355 TAAFAYKLGTKRGVMRMMDSEMLQGM-SPAQQTAVRKAFEGR-----QIlYTPV-VHmedfDVAVSYLVRRLEENSAPQN 427
Cdd:PRK11809 491 TLAAIYHLAGQNYYPGQYEFQCLHGMgEPLYEQVVGKVADGKlnrpcRI-YAPVgTH----ETLLAYLVRRLLENGANTS 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 428 FLYAL---FAPEEQALKDQEEVFREAVAQRWDTFA------------GPRRA---------QNRLEEAEQAAGRQAPRTG 483
Cdd:PRK11809 566 FVNRIadtSLPLDELVADPVEAVEKLAQQEGQLGLphpkiplprdlyGKGRAnsagldlanEHRLASLSSALLASAHQKW 645
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 484 RFAnepdtdPALEANREWALKALATDPGEHG--VEEVTDAGV--VDKHVSRAAELGAEWGARPAEDRARALEAVADELAN 559
Cdd:PRK11809 646 QAA------PMLEDPVAAGEMSPVINPADPRdiVGYVREATPaeVEQALESAVNAAPIWFATPPAERAAILERAADLMEA 719
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 560 RRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSARlldsyaAEFT-----PYRVTVVTPPWNFPVAIPTGGIAAAL 634
Cdd:PRK11809 720 QMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVR------DDFDndthrPLGPVVCISPWNFPLAIFTGQVAAAL 793
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 635 AAGSAVIIKPAPQVVHCAKLVVKAFRaglEAqGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLF-RSWKP 713
Cdd:PRK11809 794 AAGNSVLAKPAEQTPLIAAQAVRILL---EA-GVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLqRNLAG 869
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 714 ELN-------IMAETSGKNALIITPSADPDLAIQDLYLSAFGHSGQKCSAssLVIFVGAAGESQRLRSQLVDAVKTLIPG 786
Cdd:PRK11809 870 RLDpqgrpipLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSA--LRVLCLQDDVADRTLKMLRGAMAECRMG 947
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 787 -PGY---EITTTMNGLAEAPGEKLL-------RGLTQLEP--GETW----LVKPeklnedgTLWSPGIRDNVRpgswfhv 849
Cdd:PRK11809 948 nPDRlstDIGPVIDAEAKANIERHIqamrakgRPVFQAARenSEDWqsgtFVPP-------TLIELDSFDELK------- 1013
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 850 NECFGPVLGIMH--AETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVGNAYVNRGITGAIVQRQSFGGWKKSvm 927
Cdd:PRK11809 1014 REVFGPVLHVVRynRNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLS-- 1091
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 928 GPGAKAGGPNYV-------PQMGTWADGELRPREVDVPAAVANELrnLASRAALSDadvewlWRAAELDQLAWMEEFGRD 1000
Cdd:PRK11809 1092 GTGPKAGGPLYLyrllatrPEDALAVTLARQDAEYPVDAQLRAAL--LAPLTALRE------WAAEREPELAALCDQYAE 1163
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 1001 HDRTGLI-------SEANIFRYVPlldklRVRIgegFAL----RDVIRQALAAAVTGTTVEFSATPALAEQLAVLGIEVR 1069
Cdd:PRK11809 1164 LAQAGTTrllpgptGERNTYTLLP-----RERV---LCLadteQDALTQLAAVLAVGSQALWPDDALHRALVAALPAAVQ 1235
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1196634871 1070 ---------QLSDAAFASELSRAESARVRTL-GAVAdtTREAAvesnsVILDQPVLADGRRELLPYLL-EQAVSV 1133
Cdd:PRK11809 1236 ariqlakdwQLADQPFDAVLFHGDSDQLRALcEQVA--QRDGP-----IVSVQGFARGETNILLERLLiERSLSV 1303
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
520-929 |
3.05e-50 |
|
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: 185.53 E-value: 3.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 520 DAGVVDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYA----- 594
Cdd:cd07097 35 SAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARGEVTRAGQIFRYYAgealr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 595 QSARLLDSY--AAEFTPYR-----VTVVTPpWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFraglEAQG 667
Cdd:cd07097 115 LSGETLPSTrpGVEVETTReplgvVGLITP-WNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEIL----EEAG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 668 LDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKlfRSWKPELNIMA----ETSGKNALIITPSADPDLAIQDLY 743
Cdd:cd07097 190 LPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGR--RIAAAAAARGArvqlEMGGKNPLVVLDDADLDLAVECAV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 744 LSAFGHSGQKCSASSLVIFVgaAGESQRLRSQLVDAVKTLIPGPGYEITTTMNGLA-EAPGEKLLR--GLTQLEPGEtwL 820
Cdd:cd07097 268 QGAFFSTGQRCTASSRLIVT--EGIHDRFVEALVERTKALKVGDALDEGVDIGPVVsERQLEKDLRyiEIARSEGAK--L 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 821 V---KPEKLNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDN 897
Cdd:cd07097 344 VyggERLKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRR 423
|
410 420 430
....*....|....*....|....*....|..
gi 1196634871 898 VEVGNAYVNRGITGAIVQrQSFGGWKKSVMGP 929
Cdd:cd07097 424 VEAGVVMVNLPTAGVDYH-VPFGGRKGSSYGP 454
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
524-925 |
4.92e-49 |
|
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: 181.99 E-value: 4.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 524 VDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSARLL--D 601
Cdd:cd07086 37 VEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLygL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 602 SYAAE------FTPYR----VTVVTPpWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFRAGLEAQGLDPD 671
Cdd:cd07086 117 TIPSErpghrlMEQWNplgvVGVITA-FNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 672 LVQLVfTDEGDAGRALVSHADVDAVILTGASDTGKLF------RSWKPELnimaETSGKNALIITPSADPDLAIQDLYLS 745
Cdd:cd07086 196 VVNLV-TGGGDGGELLVHDPRVPLVSFTGSTEVGRRVgetvarRFGRVLL----ELGGNNAIIVMDDADLDLAVRAVLFA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 746 AFGHSGQKC-SASSLVIFVGAAGEsqrLRSQLVDAVKTLIPGPGYEITTTMNGL-AEAPGEKLLRGLTQL-EPGETWLVK 822
Cdd:cd07086 271 AVGTAGQRCtTTRRLIVHESVYDE---FLERLVKAYKQVRIGDPLDEGTLVGPLiNQAAVEKYLNAIEIAkSQGGTVLTG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 823 PEKL--NEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDN--V 898
Cdd:cd07086 348 GKRIdgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPkgS 427
|
410 420
....*....|....*....|....*..
gi 1196634871 899 EVGNAYVNRGITGAIVQrQSFGGWKKS 925
Cdd:cd07086 428 DCGIVNVNIPTSGAEIG-GAFGGEKET 453
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
524-925 |
5.02e-45 |
|
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: 168.99 E-value: 5.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 524 VDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEA---IDFctyyaqSARLL 600
Cdd:cd07095 2 VDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMagkIDI------SIKAY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 601 DSYAAE-------------FTPYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFraglEAQG 667
Cdd:cd07095 76 HERTGEratpmaqgravlrHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELW----EEAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 668 LDPDLVQLVfTDEGDAGRALVSHADVDAVILTGASDTGKLFR---SWKPELNIMAETSGKNALIITPSADPDLAIQDLYL 744
Cdd:cd07095 152 LPPGVLNLV-QGGRETGEALAAHEGIDGLLFTGSAATGLLLHrqfAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 745 SAFGHSGQKCSASSLVIFVGAAgESQRLRSQLVDAVKTLIPGPGYEITTTMNGL--AEAPGEKLLRGLTQLEPGETWLVK 822
Cdd:cd07095 231 SAFLTAGQRCTCARRLIVPDGA-VGDAFLERLVEAAKRLRIGAPDAEPPFMGPLiiAAAAARYLLAQQDLLALGGEPLLA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 823 PEKLNEDGTLWSPGIRD----NVRPGSwfhvnECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNV 898
Cdd:cd07095 310 MERLVAGTAFLSPGIIDvtdaADVPDE-----EIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARI 384
|
410 420
....*....|....*....|....*..
gi 1196634871 899 EVGNAYVNRGITGAiVQRQSFGGWKKS 925
Cdd:cd07095 385 RAGIVNWNRPTTGA-SSTAPFGGVGLS 410
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
515-928 |
9.37e-42 |
|
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: 160.12 E-value: 9.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 515 VEEVTDAGV--VDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTY 592
Cdd:cd07088 26 VATVPAATAedADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARVEVEFTADYIDY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 593 YAQSARlldSYAAEF--------------TPYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKA 658
Cdd:cd07088 106 MAEWAR---RIEGEIipsdrpnenififkVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAEL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 659 FRAGleaqGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTG-KLFRSWKPELNIMA-ETSGKNALIITPSADPD 736
Cdd:cd07088 183 VDEA----GLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGqKIMEAAAENITKVSlELGGKAPAIVMKDADLD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 737 LAIQDLYLSAFGHSGQKCSASSlVIFVGAAGESQRLRsQLVDAVKTLIPGPGYEITTTMNGLAEAPGEKLLRGLTQ--LE 814
Cdd:cd07088 259 LAVKAIVDSRIINCGQVCTCAE-RVYVHEDIYDEFME-KLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMVEraVE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 815 PGETWLVKPEKLN-EDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQY 893
Cdd:cd07088 337 AGATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMR 416
|
410 420 430
....*....|....*....|....*....|....*.
gi 1196634871 894 WIDNVEVGNAYVNRGITGAIvqrQSF-GGWKKSVMG 928
Cdd:cd07088 417 ATNELEFGETYINRENFEAM---QGFhAGWKKSGLG 449
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
524-928 |
8.09e-40 |
|
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: 153.84 E-value: 8.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 524 VDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSArlLDSY 603
Cdd:cd07106 21 LDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGAVAWLRYTASLD--LPDE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 604 AAEFTPYRVTVV--TP--------PWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKafragLEAQGLDPDLV 673
Cdd:cd07106 99 VIEDDDTRRVELrrKPlgvvaaivPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGE-----LAQEVLPPGVL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 674 QLVfTDEGDAGRALVSHADVDAVILTGASDTGKlfrswkpelNIMA-----------ETSGKNALIITPSADPDLAIQDL 742
Cdd:cd07106 174 NVV-SGGDELGPALTSHPDIRKISFTGSTATGK---------KVMAsaaktlkrvtlELGGNDAAIVLPDVDIDAVAPKL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 743 YLSAFGHSGQKCSASSLViFVgaaGESQ--RLRSQLVDAVKTLIPGPGYEITTTM------------NGL---AEAPGEK 805
Cdd:cd07106 244 FWGAFINSGQVCAAIKRL-YV---HESIydEFCEALVALAKAAVVGDGLDPGTTLgpvqnkmqydkvKELvedAKAKGAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 806 LLRGltqlepGETwlvkpekLNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHS 885
Cdd:cd07106 320 VLAG------GEP-------LDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWS 386
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1196634871 886 LDDDEIQYWIDNVEVGNAYVNRgiTGAIVQRQSFGGWKKSVMG 928
Cdd:cd07106 387 SDLERAEAVARRLEAGTVWINT--HGALDPDAPFGGHKQSGIG 427
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
524-925 |
1.08e-37 |
|
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: 147.22 E-value: 1.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 524 VDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSA------ 597
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAeaflad 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 598 RLLDSYAAE----FTPYRVTVVTPPWNFP------VAIPTGGIAAAlaagsaVIIKPAPQVVHCAKLVVKAFRAGleaqG 667
Cdd:cd07100 81 EPIETDAGKayvrYEPLGVVLGIMPWNFPfwqvfrFAAPNLMAGNT------VLLKHASNVPGCALAIEELFREA----G 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 668 LDPDLVQLVFTDEGDAGrALVSHADVDAVILTGASDTGKlfrswkpelnIMAETSGKN------------ALIITPSADP 735
Cdd:cd07100 151 FPEGVFQNLLIDSDQVE-AIIADPRVRGVTLTGSERAGR----------AVAAEAGKNlkksvlelggsdPFIVLDDADL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 736 DLAIQDLYLSAFGHSGQKCSASSLVIFVGAAGEsqRLRSQLVDAVKTLIPGPGYEITTTMNGLAEapgEKLLRGLTQ--- 812
Cdd:cd07100 220 DKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYD--EFLEKFVEAMAALKVGDPMDEDTDLGPLAR---KDLRDELHEqve 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 813 --LEPGETWLVKPEKLNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDE 890
Cdd:cd07100 295 eaVAAGATLLLGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLER 374
|
410 420 430
....*....|....*....|....*....|....*
gi 1196634871 891 IQYWIDNVEVGNAYVNrGITGAiVQRQSFGGWKKS 925
Cdd:cd07100 375 AERVARRLEAGMVFIN-GMVKS-DPRLPFGGVKRS 407
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
520-928 |
4.48e-37 |
|
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: 146.56 E-value: 4.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 520 DAGVVDKHVSRAAELG-AEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSAR 598
Cdd:cd07082 36 SALEILEAAETAYDAGrGWWPTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 599 LLDSYAAEFT---------------PYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFRagl 663
Cdd:cd07082 116 RLDGDSLPGDwfpgtkgkiaqvrrePLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFH--- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 664 EAqGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLFRSWKPELNIMAETSGKNALIITPSADPDLAIQDLY 743
Cdd:cd07082 193 DA-GFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHPMKRLVLELGGKDPAIVLPDADLELAAKEIV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 744 LSAFGHSGQKCSASSLViFV--GAAGEsqrLRSQLVDAVKTLIPGPGYEITTTMNGLAEAPGEKLLRGLTQ--LEPGETw 819
Cdd:cd07082 272 KGALSYSGQRCTAIKRV-LVheSVADE---LVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDdaVAKGAT- 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 820 LVKPEKlNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVE 899
Cdd:cd07082 347 VLNGGG-REGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALE 425
|
410 420 430
....*....|....*....|....*....|...
gi 1196634871 900 VGNAYVNRGitgaiVQRQ----SFGGWKKSVMG 928
Cdd:cd07082 426 VGTVNINSK-----CQRGpdhfPFLGRKDSGIG 453
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
524-928 |
5.25e-37 |
|
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: 146.51 E-value: 5.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 524 VDKHVSRAAELGAEWGARPAEDRAR-------ALEAVADELANrrgefisVAAYEANKTVTQTDPEIS---EAIDFCT-- 591
Cdd:cd07085 40 VDAAVAAAKAAFPAWSATPVLKRQQvmfkfrqLLEENLDELAR-------LITLEHGKTLADARGDVLrglEVVEFACsi 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 592 -------YYAQSARLLDSYAaEFTPYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFRaglE 664
Cdd:cd07085 113 phllkgeYLENVARGIDTYS-YRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQ---E 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 665 AqGLDPDLVQLVFTDeGDAGRALVSHADVDAV-----------ILTGASDTGKlfrswkpelNIMAETSGKNALIITPSA 733
Cdd:cd07085 189 A-GLPDGVLNVVHGG-KEAVNALLDHPDIKAVsfvgstpvgeyIYERAAANGK---------RVQALGGAKNHAVVMPDA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 734 DPDLAIQDLYLSAFGHSGQKCSASSLVIFVGaaGESQRLRSQLVDAVKTLIPGPGYEITTTMNGLAEAPGEKLLRGLTQ- 812
Cdd:cd07085 258 DLEQTANALVGAAFGAAGQRCMALSVAVAVG--DEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIEs 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 813 -LEPGETWLV-----KPEKLnEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSL 886
Cdd:cd07085 336 gVEEGAKLVLdgrgvKVPGY-ENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTR 414
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1196634871 887 DDDEIQYWIDNVEVGNAYVNRGITgAIVQRQSFGGWKKSVMG 928
Cdd:cd07085 415 SGAAARKFQREVDAGMVGINVPIP-VPLAFFSFGGWKGSFFG 455
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
527-934 |
1.24e-36 |
|
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: 144.81 E-value: 1.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 527 HVSRAAELGAEWGAR-PAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSARL------ 599
Cdd:cd07146 22 ALREALALAASYRSTlTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAADVLRFAAAEALRddgesf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 600 -LDSYAAE-----FT---PYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFRaglEAqGLDP 670
Cdd:cd07146 102 sCDLTANGkarkiFTlrePLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLY---EA-GLPP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 671 DLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLFRSWKPELNIMAETSGKNALIITPSADPDLAIQDLYLSAFGHS 750
Cdd:cd07146 178 DMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANS 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 751 GQKCSASSLVIfvgaAGES--QRLRSQLVDAVKTLIPGPGYEITTTMNGLAEAPGEKLLRGLTQ--LEPGETWLVKPEKl 826
Cdd:cd07146 258 GQRCTAVKRIL----VHESvaDEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEeaIAQGARVLLGNQR- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 827 neDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVGNAYVN 906
Cdd:cd07146 333 --QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVN 410
|
410 420
....*....|....*....|....*...
gi 1196634871 907 rGITGAIVQRQSFGGWKKSvmGPGAKAG 934
Cdd:cd07146 411 -EVPGFRSELSPFGGVKDS--GLGGKEG 435
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
511-928 |
9.02e-36 |
|
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: 142.19 E-value: 9.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 511 GEHGVE-EVTDAGVVDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDF 589
Cdd:cd07094 9 GEVIGKvPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRAIDT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 590 CTYYAQSARL-------LDSYAAEFTPYRVTVVTP--------PWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKL 654
Cdd:cd07094 89 LRLAAEEAERirgeeipLDATQGSDNRLAWTIREPvgvvlaitPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 655 VVKAfragLEAQGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLFRSWKPELNIMAETSGKNALIITPSAD 734
Cdd:cd07094 169 LAKI----LVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKRIALELGGNAPVIVDRDAD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 735 PDLAIQDLYLSAFGHSGQKCSASSLVIFVGAAGEsqRLRSQLVDAVKTLIPG-PGYEITTTMNGLAEAPGEKLLRGLTQ- 812
Cdd:cd07094 245 LDAAIEALAKGGFYHAGQVCISVQRIYVHEELYD--EFIEAFVAAVKKLKVGdPLDEDTDVGPLISEEAAERVERWVEEa 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 813 LEPGETWLVKPEKlneDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQ 892
Cdd:cd07094 323 VEAGARLLCGGER---DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAF 399
|
410 420 430
....*....|....*....|....*....|....*.
gi 1196634871 893 YWIDNVEVGNAYVNRGiTGAIVQRQSFGGWKKSVMG 928
Cdd:cd07094 400 KAAEKLEVGGVMVNDS-SAFRTDWMPFGGVKESGVG 434
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
520-912 |
1.32e-35 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 142.40 E-value: 1.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 520 DAGVVDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISE-----AIDFCTY-- 592
Cdd:PRK09457 35 TAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEVTAminkiAISIQAYhe 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 593 --YAQSARLLDSYAA-EFTPYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFRaglEAqGLD 669
Cdd:PRK09457 115 rtGEKRSEMADGAAVlRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQ---QA-GLP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 670 PDLVQLVfTDEGDAGRALVSHADVDAVILTGASDTGKLFR---SWKPELNIMAETSGKNALIITPSADPDLAIQDLYLSA 746
Cdd:PRK09457 191 AGVLNLV-QGGRETGKALAAHPDIDGLLFTGSANTGYLLHrqfAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 747 FGHSGQKCS-ASSLVIFVGAAGesQRLRSQLVDAVKTLIPGPGYEITTTMNG--LAEAPGEKLLRGLTQL-EPGETWLVK 822
Cdd:PRK09457 270 FISAGQRCTcARRLLVPQGAQG--DAFLARLVAVAKRLTVGRWDAEPQPFMGavISEQAAQGLVAAQAQLlALGGKSLLE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 823 PEKLNEDGTLWSPGIRD--NV--RPGSwfhvnECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNV 898
Cdd:PRK09457 348 MTQLQAGTGLLTPGIIDvtGVaeLPDE-----EYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEI 422
|
410
....*....|....
gi 1196634871 899 EVGNAYVNRGITGA 912
Cdd:PRK09457 423 RAGIVNWNKPLTGA 436
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
512-929 |
3.45e-34 |
|
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: 137.35 E-value: 3.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 512 EHGVEEVTDAgvvdkhVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCT 591
Cdd:cd07099 14 VTDPAEVAAA------VARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLALEAID 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 592 YYAQSA-RLLDSYAA-------------EFTPYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVK 657
Cdd:cd07099 88 WAARNApRVLAPRKVptgllmpnkkatvEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 658 AFRAGleaqGLDPDLVQLVfTDEGDAGRALVShADVDAVILTGASDTGKlfrswkpelNIMA-----------ETSGKNA 726
Cdd:cd07099 168 AWAAA----GPPQGVLQVV-TGDGATGAALID-AGVDKVAFTGSVATGR---------KVMAaaaerlipvvlELGGKDP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 727 LIITPSADPDLAIQDLYLSAFGHSGQKCsASSLVIFVgAAGESQRLRSQLVDAVKTLIPGPGYEITTTMNGLAEAPGEKL 806
Cdd:cd07099 233 MIVLADADLERAAAAAVWGAMVNAGQTC-ISVERVYV-HESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 807 LRGLTQ--LEPGETWLVKPEKLNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIH 884
Cdd:cd07099 311 VRRHVDdaVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVF 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1196634871 885 SLDDDEIQYWIDNVEVGNAYVNRGITGAIVQRQSFGGWKKS----VMGP 929
Cdd:cd07099 391 SRDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSgggrRHGA 439
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
518-945 |
3.65e-34 |
|
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: 137.04 E-value: 3.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 518 VTDAGVVDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSA 597
Cdd:cd07152 9 VADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEAAGLP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 598 -----RLLDSYA-----AEFTPYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFragLEAQG 667
Cdd:cd07152 89 tqpqgEILPSAPgrlslARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIARL---FEEAG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 668 LDPDLVQlVFTDEGDAGRALVSHADVDAVILTGASDTGKLF-----RSWKpelNIMAETSGKNALIITPSADPDLAIQDL 742
Cdd:cd07152 166 LPAGVLH-VLPGGADAGEALVEDPNVAMISFTGSTAVGRKVgeaagRHLK---KVSLELGGKNALIVLDDADLDLAASNG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 743 YLSAFGHSGQKCSASSLVIFvgAAGESQRLRSQLVDAVKTLIPGPGYEITTTMNGL---------------AEAPGEKLL 807
Cdd:cd07152 242 AWGAFLHQGQICMAAGRHLV--HESVADAYTAKLAAKAKHLPVGDPATGQVALGPLinarqldrvhaivddSVAAGARLE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 808 RGLTQlepgetwlvkpeklneDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLD 887
Cdd:cd07152 320 AGGTY----------------DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRD 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1196634871 888 DDEIQYWIDNVEVGNAYVNRGITGAIVQrQSFGGWKKSvmGPGAKAGGPNYVPQMGTW 945
Cdd:cd07152 384 VGRAMALADRLRTGMLHINDQTVNDEPH-NPFGGMGAS--GNGSRFGGPANWEEFTQW 438
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
518-928 |
6.25e-33 |
|
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: 133.49 E-value: 6.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 518 VTDAGVVDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSA 597
Cdd:cd07149 17 VASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDRAIETLRLSAEEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 598 RLL-------DSYAAE-----FT---PYRVTVVTPPWNFPV---------AIptggiaaalAAGSAVIIKPAPQVVHCAK 653
Cdd:cd07149 97 KRLagetipfDASPGGegrigFTirePIGVVAAITPFNFPLnlvahkvgpAI---------AAGNAVVLKPASQTPLSAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 654 LVVKAFragLEAqGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLFRSWKPELNIMAETSGKNALIITPSA 733
Cdd:cd07149 168 KLAELL---LEA-GLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLKKVTLELGSNAAVIVDADA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 734 DPDLAIQDLYLSAFGHSGQKCsASSLVIFVgAAGESQRLRSQLVDAVKTLIPGPGYEITTTMNGL--------------- 798
Cdd:cd07149 244 DLEKAVERCVSGAFANAGQVC-ISVQRIFV-HEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMiseaeaerieewvee 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 799 AEAPGEKLLRGLTQlepgetwlvkpeklneDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYG 878
Cdd:cd07149 322 AVEGGARLLTGGKR----------------DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYG 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1196634871 879 LTGGIHSLDDDEIQYWIDNVEVGNAYVNrGITGAIVQRQSFGGWKKSVMG 928
Cdd:cd07149 386 LQAGVFTNDLQKALKAARELEVGGVMIN-DSSTFRVDHMPYGGVKESGTG 434
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
524-945 |
9.27e-33 |
|
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: 132.65 E-value: 9.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 524 VDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSARLL--- 600
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPege 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 601 ---------DSYAaeftpYRVTV----VTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQV-VHCAKLVVKAFraglEAQ 666
Cdd:cd07104 82 ilpsdvpgkESMV-----RRVPLgvvgVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTpVTGGLLIAEIF----EEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 667 GLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLF-----RSWKPelnIMAETSGKNALIITPSADPDLAIQD 741
Cdd:cd07104 153 GLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIgelagRHLKK---VALELGGNNPLIVLDDADLDLAVSA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 742 LYLSAFGHSGQKCSASSLVIfVGAAGESQRLRsQLVDAVKTLIPGPGYEITTTMNGL-AEAPGEKLLRGLTQ-------L 813
Cdd:cd07104 230 AAFGAFLHQGQICMAAGRIL-VHESVYDEFVE-KLVAKAKALPVGDPRDPDTVIGPLiNERQVDRVHAIVEDavaagarL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 814 EPGETWlvkpeklneDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQY 893
Cdd:cd07104 308 LTGGTY---------EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMA 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1196634871 894 WIDNVEVGNAYVNrGIT---GAIVqrqSFGGWKKSVMGpgaKAGGPNYVPQMGTW 945
Cdd:cd07104 379 FAERLETGMVHIN-DQTvndEPHV---PFGGVKASGGG---RFGGPASLEEFTEW 426
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
508-928 |
1.11e-32 |
|
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: 132.94 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 508 TDP--GEHgVEEVTDAGV--VDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEI 583
Cdd:cd07103 2 INPatGEV-IGEVPDAGAadADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 584 SEAIDFCTYYAQSARLL--DSYAAEFTPYRVTVVT-P--------PWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCA 652
Cdd:cd07103 81 DYAASFLEWFAEEARRIygRTIPSPAPGKRILVIKqPvgvvaaitPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 653 KLVVKAFRaglEAqGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLfrswkpelnIMAETS---------- 722
Cdd:cd07103 161 LALAELAE---EA-GLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKL---------LMAQAAdtvkrvslel 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 723 GKNA-LIITPSADPDLAIQDLYLSAFGHSGQKCSASSLvIFVgAAGESQRLRSQLVDAVKTLIPGPGYEITTTMNGLAEA 801
Cdd:cd07103 228 GGNApFIVFDDADLDKAVDGAIASKFRNAGQTCVCANR-IYV-HESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 802 PGEKLLRGLTQ--LEPGETWLVKPEKLNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGL 879
Cdd:cd07103 306 RAVEKVEALVEdaVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGL 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1196634871 880 TGGIHSLDDDEIQYWIDNVEVGNAYVNRGITGAIVqrQSFGGWKKSVMG 928
Cdd:cd07103 386 AAYVFTRDLARAWRVAEALEAGMVGINTGLISDAE--APFGGVKESGLG 432
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
520-925 |
4.02e-32 |
|
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: 131.20 E-value: 4.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 520 DAGVVDKHVSRAAE-LGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSAR 598
Cdd:cd07109 17 GAADVDRAVQAARRaFESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEAAARYFEYYGGAAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 599 --------LLDSYAAeFT---PYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQvvhcAKLVVKAFRAGLEAQG 667
Cdd:cd07109 97 klhgetipLGPGYFV-YTvrePHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAED----APLTALRLAELAEEAG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 668 LDPDLVQLVfTDEG-DAGRALVSHADVDAVILTGASDTGKLF-RSWKPELN-IMAETSGKNALIITPSADPDLAIQDLYL 744
Cdd:cd07109 172 LPAGALNVV-TGLGaEAGAALVAHPGVDHISFTGSVETGIAVmRAAAENVVpVTLELGGKSPQIVFADADLEAALPVVVN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 745 SAFGHSGQKCSASSLVIFVGAAGEsqRLRSQLVDAVKTLIPGPG--------------YEITTTMNGLAEAPGEKLLRGL 810
Cdd:cd07109 251 AIIQNAGQTCSAGSRLLVHRSIYD--EVLERLVERFRALRVGPGledpdlgplisakqLDRVEGFVARARARGARIVAGG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 811 TQLEPgetwlvkpekLNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDE 890
Cdd:cd07109 329 RIAEG----------APAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDR 398
|
410 420 430
....*....|....*....|....*....|....*.
gi 1196634871 891 iQYWI-DNVEVGNAYVNRGITGAIVQRqSFGGWKKS 925
Cdd:cd07109 399 -ALRVaRRLRAGQVFVNNYGAGGGIEL-PFGGVKKS 432
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
524-925 |
6.04e-31 |
|
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: 127.31 E-value: 6.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 524 VDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSARLL--- 600
Cdd:cd07105 2 ADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIigg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 601 -------DSYAAEF-TPYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFRaglEAqGLDPDL 672
Cdd:cd07105 82 sipsdkpGTLAMVVkEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFH---EA-GLPKGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 673 VQLVFTDEGDAGR---ALVSHADVDAVILTGASDTGKLFRSW-----KPELnimAETSGKNALIITPSADPDLAIQDLYL 744
Cdd:cd07105 158 LNVVTHSPEDAPEvveALIAHPAVRKVNFTGSTRVGRIIAETaakhlKPVL---LELGGKAPAIVLEDADLDAAANAALF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 745 SAFGHSGQKCSASSLVIFVGAAGEsqRLRSQLVDAVKTLIPGPGYEI-------TTTMNGL---AEAPGEKLLRGltqle 814
Cdd:cd07105 235 GAFLNSGQICMSTERIIVHESIAD--EFVEKLKAAAEKLFAGPVVLGslvsaaaADRVKELvddALSKGAKLVVG----- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 815 pgetwlvKPEKLNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYW 894
Cdd:cd07105 308 -------GLADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAV 380
|
410 420 430
....*....|....*....|....*....|....
gi 1196634871 895 IDNVEVGNAYVNrgitGAIVQRQS---FGGWKKS 925
Cdd:cd07105 381 AKRIESGAVHIN----GMTVHDEPtlpHGGVKSS 410
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
524-925 |
6.17e-31 |
|
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: 127.80 E-value: 6.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 524 VDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKT-VTQTDPEI---SEAIDFCTYYAQ---- 595
Cdd:cd07098 20 VDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTmVDASLGEIlvtCEKIRWTLKHGEkalr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 596 ----SARLLDSY---AAEFTPYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFRAGLEAQGL 668
Cdd:cd07098 100 pesrPGGLLMFYkraRVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIRECLAACGH 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 669 DPDLVQLVfTDEGDAGRALVSHADVDAVILTGASDTGKLfrswkpelnIMA-----------ETSGKNALIITPSADPDL 737
Cdd:cd07098 180 DPDLVQLV-TCLPETAEALTSHPVIDHITFIGSPPVGKK---------VMAaaaesltpvvlELGGKDPAIVLDDADLDQ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 738 AIQDLYLSAFGHSGQKCSASSLVIfvgaAGESQ--RLRSQLVDAVKTLIPGPGYEITT-----TMNGLAEAPgEKLLRgl 810
Cdd:cd07098 250 IASIIMRGTFQSSGQNCIGIERVI----VHEKIydKLLEILTDRVQALRQGPPLDGDVdvgamISPARFDRL-EELVA-- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 811 TQLEPGETWLV--KPEKLNED--GTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSL 886
Cdd:cd07098 323 DAVEKGARLLAggKRYPHPEYpqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGK 402
|
410 420 430
....*....|....*....|....*....|....*....
gi 1196634871 887 DDDEIQYWIDNVEVGNAYVNRGITGAIVQRQSFGGWKKS 925
Cdd:cd07098 403 DIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGS 441
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
524-928 |
8.70e-31 |
|
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: 127.71 E-value: 8.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 524 VDKHV--SRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQT-DPEISEAIDFCTYYAQSA--- 597
Cdd:cd07091 43 VDAAVkaARAAFETGWWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEESaKGDVALSIKCLRYYAGWAdki 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 598 --RLLDSYAAEFT-----PYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQ----VVHCAKLVVKAfragleaq 666
Cdd:cd07091 123 qgKTIPIDGNFLAytrrePIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQtplsALYLAELIKEA-------- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 667 GLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLFRSWKPELNIMA---ETSGKNALIITPSADPDLAIQDLY 743
Cdd:cd07091 195 GFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSNLKKvtlELGGKSPNIVFDDADLDKAVEWAA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 744 LSAFGHSGQKCSASSLvIFVgAAGESQRLRSQLVDAVKTLIPGPGYEITTTMNGL-AEAPGEKLLRGLTQ-LEPGETWLV 821
Cdd:cd07091 275 FGIFFNQGQCCCAGSR-IFV-QESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQvSKAQFDKILSYIESgKKEGATLLT 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 822 KPEKLNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVG 901
Cdd:cd07091 353 GGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAG 432
|
410 420
....*....|....*....|....*...
gi 1196634871 902 NAYVNrgiTGAIVQRQS-FGGWKKSVMG 928
Cdd:cd07091 433 TVWVN---TYNVFDAAVpFGGFKQSGFG 457
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
520-939 |
9.47e-31 |
|
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: 128.47 E-value: 9.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 520 DAGVVDKHVSRAAELGAEWGARPAEDRARALEAVADELANR-RGEFISVAAYEANKTVTQTdpEI---SEAIDFCTYYAQ 595
Cdd:cd07123 67 DAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKyRYELNAATMLGQGKNVWQA--EIdaaCELIDFLRFNVK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 596 SARLLDSYAAEFTP--------YR-----VTVVTPpWNFpVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFRag 662
Cdd:cd07123 145 YAEELYAQQPLSSPagvwnrleYRplegfVYAVSP-FNF-TAIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILE-- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 663 lEAqGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTgklFRS-WK------------PElnIMAETSGKNALII 729
Cdd:cd07123 221 -EA-GLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPT---FKSlWKqigenldryrtyPR--IVGETGGKNFHLV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 730 TPSADPDLAIQDLYLSAFGHSGQKCSASSLViFVgAAGESQRLRSQLVDAVKTLIPGPGYEITTTMNGL----------- 798
Cdd:cd07123 294 HPSADVDSLVTATVRGAFEYQGQKCSAASRA-YV-PESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVidekafdrikg 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 799 -----AEAPGEKLLRGltqlepGET-----WLVKPeklnedgTLwspgIRDNVrPGSWFHVNECFGPVLGIM------HA 862
Cdd:cd07123 372 yidhaKSDPEAEIIAG------GKCddsvgYFVEP-------TV----IETTD-PKHKLMTEEIFGPVLTVYvypdsdFE 433
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1196634871 863 ETLEQAiewQNSTGYGLTGGIHSLDDDEIQYWIDNVE--VGNAYVNRGITGAIVQRQSFGGWKKSvmGPGAKAGGPNYV 939
Cdd:cd07123 434 ETLELV---DTTSPYALTGAIFAQDRKAIREATDALRnaAGNFYINDKPTGAVVGQQPFGGARAS--GTNDKAGSPLNL 507
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
513-928 |
2.46e-30 |
|
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: 125.91 E-value: 2.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 513 HGVEeVT---DAGV--VDKHVS---RAAELGaEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEIS 584
Cdd:cd07118 6 HGVV-VAryaEGTVedVDAAVAaarKAFDKG-PWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 585 EAIDFCTYYAQSARLL--DSYAA-----------EftPYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAP----Q 647
Cdd:cd07118 84 GAADLWRYAASLARTLhgDSYNNlgddmlglvlrE--PIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEftsgT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 648 VVHCAKLVVKAfragleaqGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLF-----RSWKpelNIMAETS 722
Cdd:cd07118 162 TLMLAELLIEA--------GLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIaaaaaRNLK---KVSLELG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 723 GKNALIITPSADPDLAIQDLYLSAFGHSGQKC-SASSLVIFVGAAGEsqrLRSQLVDAVKTLIPGPGYEITTTMNGL-AE 800
Cdd:cd07118 231 GKNPQIVFADADLDAAADAVVFGVYFNAGECCnSGSRLLVHESIADA---FVAAVVARSRKVRVGDPLDPETKVGAIiNE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 801 APGEKLLRGLTQ-LEPGETWLVKPEKLNE-DGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYG 878
Cdd:cd07118 308 AQLAKITDYVDAgRAEGATLLLGGERLASaAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYG 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1196634871 879 LTGGIHSLDDDEIQYWIDNVEVGNAYVNRGITGAivQRQSFGGWKKSVMG 928
Cdd:cd07118 388 LSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGS--PELPFGGFKQSGIG 435
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
524-928 |
3.84e-30 |
|
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: 125.57 E-value: 3.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 524 VDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSARLL--- 600
Cdd:cd07107 21 VDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMVAAALLDYFAGLVTELkge 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 601 ----DSYAAEFT---PYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQvvhcAKLvvKAFRAGLEAQG-LDPDL 672
Cdd:cd07107 101 tipvGGRNLHYTlrePYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQ----APL--SALRLAELAREvLPPGV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 673 VQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLF-----RSWKPelnIMAETSGKNALIITPSADPDLAIQDLYLSA- 746
Cdd:cd07107 175 FNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAImraaaEGIKH---VTLELGGKNALIVFPDADPEAAADAAVAGMn 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 747 FGHSGQKCSASSLViFVGAAGESQRLrSQLVDAVKTLIPGPGYEITTTMNGL---------------AEAPGEKLLRGlt 811
Cdd:cd07107 252 FTWCGQSCGSTSRL-FVHESIYDEVL-ARVVERVAAIKVGDPTDPATTMGPLvsrqqydrvmhyidsAKREGARLVTG-- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 812 qlepGetwlVKPE-KLNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDE 890
Cdd:cd07107 328 ----G----GRPEgPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQ 399
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1196634871 891 IQYWIDNVEVGNAYVN---RGITGAivqrqSFGGWKKSVMG 928
Cdd:cd07107 400 AHRTARRVEAGYVWINgssRHFLGA-----PFGGVKNSGIG 435
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
517-928 |
2.36e-29 |
|
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: 123.18 E-value: 2.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 517 EVTDAG--VVDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYA 594
Cdd:cd07090 12 TVHCAGaeDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDSSADCLEYYA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 595 QSARLL---------DSYAaeFT---PYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFR-A 661
Cdd:cd07090 92 GLAPTLsgehvplpgGSFA--YTrrePLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTeA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 662 GLeaqgldPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKlfrswkpelNIMA-----------ETSGKNALIIT 730
Cdd:cd07090 170 GL------PDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGK---------KVMSaaakgikhvtlELGGKSPLIIF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 731 PSADPDLAIQDLYLSAFGHSGQKCSASSLViFVgAAGESQRLRSQLVDAVKTLIPGPGYEITTTMNGLAEAP-------- 802
Cdd:cd07090 235 DDADLENAVNGAMMANFLSQGQVCSNGTRV-FV-QRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEhlekvlgy 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 803 -------GEKLLRGltqlepGEtwLVKPEKLNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNST 875
Cdd:cd07090 313 iesakqeGAKVLCG------GE--RVVPEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDT 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1196634871 876 GYGLTGGIHSLDDDEIQYWIDNVEVGNAYVNR-GITGAIVqrqSFGGWKKSVMG 928
Cdd:cd07090 385 TYGLAAGVFTRDLQRAHRVIAQLQAGTCWINTyNISPVEV---PFGGYKQSGFG 435
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
518-928 |
3.00e-29 |
|
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: 122.80 E-value: 3.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 518 VTDAGVVDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSA 597
Cdd:cd07101 14 QSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVARYYARRA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 598 R-------------LLDSYAAEFTPYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAfragLE 664
Cdd:cd07101 94 ErllkprrrrgaipVLTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVEL----LI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 665 AQGLDPDLVQLVFTDEGDAGRALVSHADVdaVILTGASDTGKLF--RSWKPELNIMAETSGKNALIITPSADPDLAIQDL 742
Cdd:cd07101 170 EAGLPRDLWQVVTGPGSEVGGAIVDNADY--VMFTGSTATGRVVaeRAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 743 YLSAFGHSGQKCsASSLVIFVGAAgESQRLRSQLVDAVKTLIPGPGYEITTTMNGLAeapGEKLLRGLTQ-----LEPGE 817
Cdd:cd07101 248 VRACFSNAGQLC-VSIERIYVHES-VYDEFVRRFVARTRALRLGAALDYGPDMGSLI---SQAQLDRVTAhvddaVAKGA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 818 TWLVKPEKLNEDGTL-WSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWID 896
Cdd:cd07101 323 TVLAGGRARPDLGPYfYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAA 402
|
410 420 430
....*....|....*....|....*....|...
gi 1196634871 897 NVEVGNAYVNRGITGAIVQRQS-FGGWKKSVMG 928
Cdd:cd07101 403 RLRAGTVNVNEGYAAAWASIDApMGGMKDSGLG 435
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
524-907 |
7.51e-29 |
|
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: 121.58 E-value: 7.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 524 VDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSAR--LLD 601
Cdd:cd07102 20 VRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMISIAEeaLAD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 602 SYAAE---FT------PYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFraglEAQGLDPDL 672
Cdd:cd07102 100 IRVPEkdgFEryirrePLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAF----AEAGLPEGV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 673 VQlVFTDEGDAGRALVSHADVDAVILTGASDTGK-LFRSWKPEL-NIMAETSGKNALIITPSADPDLAIQDLYLSAFGHS 750
Cdd:cd07102 176 FQ-VLHLSHETSAALIADPRIDHVSFTGSVAGGRaIQRAAAGRFiKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNS 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 751 GQKCSAsslV--IFVGAAGESQRLrSQLVDAVKTLIPGPGYEITTTMNGLAEAPGEKLLRGLTQ--LEPGETWLVKPEKL 826
Cdd:cd07102 255 GQSCCS---IerIYVHESIYDAFV-EAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIAdaIAKGARALIDGALF 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 827 NED---GTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVGNA 903
Cdd:cd07102 331 PEDkagGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTV 410
|
....
gi 1196634871 904 YVNR 907
Cdd:cd07102 411 FMNR 414
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
514-928 |
8.09e-29 |
|
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: 121.30 E-value: 8.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 514 GVEEVTDAgvVDkhVSRAAELGAEWgARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYY 593
Cdd:cd07120 17 GVAEAEAA--IA--AARRAFDETDW-AHDPRLRARVLLELADAFEANAERLARLLALENGKILGEARFEISGAISELRYY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 594 AQSARLLDSYAAEFTPYRVTVVTP----------PWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFRagl 663
Cdd:cd07120 92 AGLARTEAGRMIEPEPGSFSLVLRepmgvagiivPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILA--- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 664 EAQGLDPDLVQLvFTDEG-DAGRALVSHADVDAVILTGASDTGK-LFRSWKPELNIMA-ETSGKNALIITPSADPDLAIQ 740
Cdd:cd07120 169 EIPSLPAGVVNL-FTESGsEGAAHLVASPDVDVISFTGSTATGRaIMAAAAPTLKRLGlELGGKTPCIVFDDADLDAALP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 741 DLYLSAFGHSGQKCSASSLVIFvgAAGESQRLRSQLVDAVKTLIPGPGYEITTTMNGLAEAPGEKLLRGLTQ--LEPGET 818
Cdd:cd07120 248 KLERALTIFAGQFCMAGSRVLV--QRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVEraIAAGAE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 819 WLVKPEKLNED---GTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWI 895
Cdd:cd07120 326 VVLRGGPVTEGlakGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVA 405
|
410 420 430
....*....|....*....|....*....|...
gi 1196634871 896 DNVEVGNAYVNRgiTGAIVQRQSFGGWKKSVMG 928
Cdd:cd07120 406 RAIRAGTVWIND--WNKLFAEAEEGGYRQSGLG 436
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
524-928 |
8.76e-29 |
|
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: 121.31 E-value: 8.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 524 VDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTV-TQTDPEISEAIDFCTYYAQSARLLDs 602
Cdd:cd07108 21 VDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPEAAVLADLFRYFGGLAGELK- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 603 yaAEFTPYRVTVVT-----P--------PWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVvkafrAGLEAQGLd 669
Cdd:cd07108 100 --GETLPFGPDVLTytvrePlgvvgailPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLL-----AEILAQVL- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 670 PDLVQLVFTDEG-DAGRALVSHADVDAVILTGASDTGK-LFRSWKPEL-NIMAETSGKNALIITPSADPDLAIQDLYLSA 746
Cdd:cd07108 172 PAGVLNVITGYGeECGAALVDHPDVDKVTFTGSTEVGKiIYRAAADRLiPVSLELGGKSPMIVFPDADLDDAVDGAIAGM 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 747 -FGHSGQKCSASSLvIFVGAAGESQRLRsQLVDAVKTLIPGPGYEITTTMNGL----------------AEAPGEKLLRG 809
Cdd:cd07108 252 rFTRQGQSCTAGSR-LFVHEDIYDAFLE-KLVAKLSKLKIGDPLDEATDIGAIisekqfakvcgyidlgLSTSGATVLRG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 810 LTQLEPGEtwlvkpeklNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDD 889
Cdd:cd07108 330 GPLPGEGP---------LADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLG 400
|
410 420 430
....*....|....*....|....*....|....*....
gi 1196634871 890 EIQYWIDNVEVGNAYVNRGitGAIVQRQSFGGWKKSVMG 928
Cdd:cd07108 401 RALRAAHALEAGWVQVNQG--GGQQPGQSYGGFKQSGLG 437
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
489-936 |
9.30e-29 |
|
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: 121.28 E-value: 9.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 489 PDTDPAleANREWALKALAtdpgehGVEEVTDAgvvdkhVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVA 568
Cdd:cd07150 2 DDLNPA--DGSVYARVAVG------SRQDAERA------IAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 569 AYEANKTVTQTDPEISEAIDFCTYYAQSARLL------DSYAAEFT-----PYRVTVVTPPWNFPVAIPTGGIAAALAAG 637
Cdd:cd07150 68 IDEGGSTYGKAWFETTFTPELLRAAAGECRRVrgetlpSDSPGTVSmsvrrPLGVVAGITPFNYPLILATKKVAFALAAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 638 SAVIIKPAPQVVHCAKLVVKAFraglEAQGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLF-----RSWK 712
Cdd:cd07150 148 NTVVLKPSEETPVIGLKIAEIM----EEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIaekagRHLK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 713 PelnIMAETSGKNALIITPSADPDLAIQDLYLSAFGHSGQKCSASSLVI------------FVGAAG------------- 767
Cdd:cd07150 224 K---ITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIveepvydefvkkFVARASklkvgdprdpdtv 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 768 --------ESQRLRSQLVDAVktlipgpgyeitttmnglaeAPGEKLLrgltqlePGETWlvkpeklneDGTLWSPGIRD 839
Cdd:cd07150 301 igplisprQVERIKRQVEDAV--------------------AKGAKLL-------TGGKY---------DGNFYQPTVLT 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 840 NVRPG-SWFHvNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVGNAYVNrgitGAIVQRQS 918
Cdd:cd07150 345 DVTPDmRIFR-EETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESGMVHIN----DPTILDEA 419
|
490 500
....*....|....*....|.
gi 1196634871 919 ---FGGWKKSVMGpgaKAGGP 936
Cdd:cd07150 420 hvpFGGVKASGFG---REGGE 437
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
520-928 |
2.18e-28 |
|
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: 120.15 E-value: 2.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 520 DAGVVDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSARL 599
Cdd:cd07110 17 TAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDDVAGCFEYYADLAEQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 600 LDSYAAE--------FTPYR------VTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPApqvvHCAKLVVKAFRAGLEA 665
Cdd:cd07110 97 LDAKAERavplpsedFKARVrrepvgVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPS----ELTSLTELELAEIAAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 666 QGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLFRSWKPEL--NIMAETSGKNALIITPSADPDLAIQDLY 743
Cdd:cd07110 173 AGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDikPVSLELGGKSPIIVFDDADLEKAVEWAM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 744 LSAFGHSGQKCSASSLVIFvgAAGESQRLRSQLVDAVKTLIPGPGYEITTTMNGLA-EAPGEKLLRGLTQ-LEPGETWL- 820
Cdd:cd07110 253 FGCFWNNGQICSATSRLLV--HESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVsQAQYEKVLSFIARgKEEGARLLc 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 821 --VKPEKLnEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNV 898
Cdd:cd07110 331 ggRRPAHL-EKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEAL 409
|
410 420 430
....*....|....*....|....*....|
gi 1196634871 899 EVGNAYVNrgITGAIVQRQSFGGWKKSVMG 928
Cdd:cd07110 410 EAGIVWIN--CSQPCFPQAPWGGYKRSGIG 437
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
520-928 |
9.18e-28 |
|
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: 118.47 E-value: 9.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 520 DAGVVDKHVS---RAAELGAeWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQT-DPEISEAIDFCTYYAQ 595
Cdd:cd07112 22 DAADVDRAVAaarRAFESGV-WSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDAlAVDVPSAANTFRWYAE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 596 SA-RLLDSYAAEfTPYRVTVVT--P--------PWNFPVAIPTGGIAAALAAGSAVIIKPAPQ----VVHCAKLvvkAFR 660
Cdd:cd07112 101 AIdKVYGEVAPT-GPDALALITrePlgvvgavvPWNFPLLMAAWKIAPALAAGNSVVLKPAEQspltALRLAEL---ALE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 661 AGLeaqgldPDLVQLVFTDEGD-AGRALVSHADVDAVILTGASDTGKLFRSWKPELN---IMAETSGKNALIITPSA-DP 735
Cdd:cd07112 177 AGL------PAGVLNVVPGFGHtAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNlkrVWLECGGKSPNIVFADApDL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 736 DLAIQDLYLSAFGHSGQKCSASSLVIFvgAAGESQRLRSQLVDAVKTLIPGPGYEITTTMNGL-AEAPGEKLLRGLTQLE 814
Cdd:cd07112 251 DAAAEAAAAGIFWNQGEVCSAGSRLLV--HESIKDEFLEKVVAAAREWKPGDPLDPATRMGALvSEAHFDKVLGYIESGK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 815 PGETWLV---KPEKLNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEI 891
Cdd:cd07112 329 AEGARLVaggKRVLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRA 408
|
410 420 430
....*....|....*....|....*....|....*..
gi 1196634871 892 QYWIDNVEVGNAYVNrgITGAIVQRQSFGGWKKSVMG 928
Cdd:cd07112 409 HRVARRLRAGTVWVN--CFDEGDITTPFGGFKQSGNG 443
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
509-879 |
1.07e-27 |
|
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: 117.81 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 509 DP--GEhGVEEVTDAGV--VDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQT-DPEI 583
Cdd:cd07092 3 DPatGE-EIATVPDASAadVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVrDDEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 584 SEAIDFCTYYAQSARLLDSYAA-EFTPYRVTVV----------TPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQvVHCA 652
Cdd:cd07092 82 PGAVDNFRFFAGAARTLEGPAAgEYLPGHTSMIrrepigvvaqIAPWNYPLMMAAWKIAPALAAGNTVVLKPSET-TPLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 653 KLVVkafrAGLEAQGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKlfrswkpelNIMA-----------ET 721
Cdd:cd07092 161 TLLL----AELAAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGK---------KVARaaadtlkrvhlEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 722 SGKNALIITPSADPDLAIQDLYLSAFGHSGQKCSASSLVIFvgAAGESQRLRSQLVDAVKTLIPGPGYEITTTMNGLA-E 800
Cdd:cd07092 228 GGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYV--HESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNsA 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1196634871 801 APGEKLLRGLTQLEPGETWLVKPEKLNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGL 879
Cdd:cd07092 306 AQRERVAGFVERAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGL 384
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
514-939 |
3.01e-27 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 117.48 E-value: 3.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 514 GVEEVTDAgvvdkhVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYY 593
Cdd:PLN02278 60 GRAETNDA------IASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 594 AQSARLL--DSYAAEFTPYRVTVV---------TPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCA-KLVVKAFRA 661
Cdd:PLN02278 134 AEEAKRVygDIIPSPFPDRRLLVLkqpvgvvgaITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTAlAAAELALQA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 662 GLEaqgldPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLfrswkpelnIMAETS----------GKNA-LIIT 730
Cdd:PLN02278 214 GIP-----PGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKK---------LMAGAAatvkrvslelGGNApFIVF 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 731 PSADPDLAIQDLYLSAFGHSGQKCSASSLVIFvgAAGESQRLRSQLVDAVKTLIPGPGYEITTTMNGLAEAPGEKLLRGL 810
Cdd:PLN02278 280 DDADLDVAVKGALASKFRNSGQTCVCANRILV--QEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESH 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 811 TQ--LEPGETWLVKPEKLNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDD 888
Cdd:PLN02278 358 VQdaVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDL 437
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1196634871 889 DEIQYWIDNVEVGNAYVNRGITGAIVqrQSFGGWKKSVMG-PGAKAGGPNYV 939
Cdd:PLN02278 438 QRAWRVSEALEYGIVGVNEGLISTEV--APFGGVKQSGLGrEGSKYGIDEYL 487
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
520-939 |
3.36e-27 |
|
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: 116.73 E-value: 3.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 520 DAGVVDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQT-DPEISEAIDFCTYYAQSAR 598
Cdd:cd07111 57 EEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESrDCDIPLVARHFYHHAGWAQ 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 599 LLDSYAAEFTPYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQvvhcAKLVVKAFRAGLEAQGLDPDLVQLVfT 678
Cdd:cd07111 137 LLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEY----TPLTALLFAEICAEAGLPPGVLNIV-T 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 679 DEGDAGRALVSHADVDAVILTGASDTGKLFRS----WKPELNImaETSGKNALIITPSADPDLAIQDLYLSAFGHSGQKC 754
Cdd:cd07111 212 GNGSFGSALANHPGVDKVAFTGSTEVGRALRRatagTGKKLSL--ELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVC 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 755 SASS-LVIFVGAAGES-QRLRSQLvdavKTLIPGPGYEITTTMNGLAEAPGEKLLRGLTQLEPGETWLV--KPEKLNEDG 830
Cdd:cd07111 290 CAGSrLLVQESVAEELiRKLKERM----SHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVfqPGADLPSKG 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 831 TLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVGNAYVNRgiT 910
Cdd:cd07111 366 PFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWING--H 443
|
410 420 430
....*....|....*....|....*....|
gi 1196634871 911 GAIVQRQSFGGWKKSVMG-PGAKAGGPNYV 939
Cdd:cd07111 444 NLFDAAAGFGGYRESGFGrEGGKEGLYEYL 473
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
520-928 |
9.63e-27 |
|
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: 115.28 E-value: 9.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 520 DAGVVDKHV--SRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTD-PEISEAIDFCTYYAQS 596
Cdd:cd07142 39 DAEDVDRAVkaARKAFDEGPWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQARyAEVPLAARLFRYYAGW 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 597 ARLLDSYAAEFT-PYRV-TVVTP--------PWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVK-AFRAGLea 665
Cdd:cd07142 119 ADKIHGMTLPADgPHHVyTLHEPigvvgqiiPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKlAAEAGL-- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 666 qgldPDLVQLVFTDEGD-AGRALVSHADVDAVILTGASDTGKLFRSWKPELNIMA---ETSGKNALIITPSADPDLAIQD 741
Cdd:cd07142 197 ----PDGVLNIVTGFGPtAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKSNLKPvtlELGGKSPFIVCEDADVDKAVEL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 742 LYLSAFGHSGQKCSASSLViFVGAAGESQRLRSQLVDAVKTLIPGP---GYEitttmNG--LAEAPGEKLLRGLTQ-LEP 815
Cdd:cd07142 273 AHFALFFNQGQCCCAGSRT-FVHESIYDEFVEKAKARALKRVVGDPfrkGVE-----QGpqVDKEQFEKILSYIEHgKEE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 816 GETWLVKPEKLNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWI 895
Cdd:cd07142 347 GATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLS 426
|
410 420 430
....*....|....*....|....*....|....*
gi 1196634871 896 DNVEVGNAYVN--RGITGAIvqrqSFGGWKKSVMG 928
Cdd:cd07142 427 RALKAGTVWVNcyDVFDASI----PFGGYKMSGIG 457
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
524-928 |
1.28e-26 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 114.96 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 524 VDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQ-------- 595
Cdd:PRK13968 31 IENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYAEhgpamlka 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 596 SARLLDSYAA--EFTPYRVTVVTPPWNFPV------AIPTGGIAAAlaagsaVIIKPAPQVVHCAKLVVKAFR-AGLeaq 666
Cdd:PRK13968 111 EPTLVENQQAviEYRPLGTILAIMPWNFPLwqvmrgAVPILLAGNG------YLLKHAPNVMGCAQLIAQVFKdAGI--- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 667 gldPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLF--RSWKPELNIMAETSGKNALIITPSADPDLAIQDLYL 744
Cdd:PRK13968 182 ---PQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIgaQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 745 SAFGHSGQKCSASSLviFVGAAGESQRLRSQLVDAVKTLIPGPGYEITTTMNGLAEAPGEKLLRGLTQ--LEPGETWLVK 822
Cdd:PRK13968 259 GRYQNTGQVCAAAKR--FIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEatLAEGARLLLG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 823 PEKLNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVGN 902
Cdd:PRK13968 337 GEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGG 416
|
410 420
....*....|....*....|....*.
gi 1196634871 903 AYVNrGITgAIVQRQSFGGWKKSVMG 928
Cdd:PRK13968 417 VFIN-GYC-ASDARVAFGGVKKSGFG 440
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
517-928 |
2.55e-26 |
|
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: 113.81 E-value: 2.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 517 EVTDAGV--VDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDP-EISEAIDFCTYY 593
Cdd:cd07093 12 KVPEGGAaeVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTrDIPRAAANFRFF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 594 AQSARLLDSYAAE----------FTPYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFRAGl 663
Cdd:cd07093 92 ADYILQLDGESYPqdggalnyvlRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEA- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 664 eaqGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLfrswkpelnIMA-----------ETSGKNALIITPS 732
Cdd:cd07093 171 ---GLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRT---------IMRaaapnlkpvslELGGKNPNIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 733 ADPDLAIQDLYLSAFGHSGQKCSASSLvIFVgaagesQR-----LRSQLVDAVKTLIPGPGYEITTTMNGL--------- 798
Cdd:cd07093 239 ADLDRAVDAAVRSSFSNNGEVCLAGSR-ILV------QRsiydeFLERFVERAKALKVGDPLDPDTEVGPLiskehlekv 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 799 ------AEAPGEKLLRGltqlepGETWlvkPEKLNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQ 872
Cdd:cd07093 312 lgyvelARAEGATILTG------GGRP---ELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELA 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 873 NSTGYGLTGGIHSLDDDEIQYWIDNVEVGNAYVN----RGItgaivqRQSFGGWKKSVMG 928
Cdd:cd07093 383 NDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNcwlvRDL------RTPFGGVKASGIG 436
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
516-928 |
2.65e-26 |
|
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: 114.04 E-value: 2.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 516 EEVTDAGVVdkhVSRAAeLGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKT-VTQTDPEISEAIDFCTYYA 594
Cdd:cd07144 44 EEDVDKAVK---AARKA-FESWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPyHSNALGDLDEIIAVIRYYA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 595 QSARLL--DSYAAEFTPYRVTVVTP--------PWNFPVAIPTGGIAAALAAGSAVIIKPAPQ----VVHCAKLVVKAfr 660
Cdd:cd07144 120 GWADKIqgKTIPTSPNKLAYTLHEPygvcgqiiPWNYPLAMAAWKLAPALAAGNTVVIKPAENtplsLLYFANLVKEA-- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 661 agleaqGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLF-----RSWKpelNIMAETSGKNALIITPSADP 735
Cdd:cd07144 198 ------GFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVmkaaaQNLK---AVTLECGGKSPALVFEDADL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 736 DLAIQDLYLSAFGHSGQKCSASSLVI------------FVGAAGESQRLRSQLVDavKTLIpGP-----GYEITTTMNGL 798
Cdd:cd07144 269 DQAVKWAAAGIMYNSGQNCTATSRIYvqesiydkfvekFVEHVKQNYKVGSPFDD--DTVV-GPqvsktQYDRVLSYIEK 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 799 AEAPGEKLLRGLTQLEPGetwlvkpeklNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYG 878
Cdd:cd07144 346 GKKEGAKLVYGGEKAPEG----------LGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYG 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1196634871 879 LTGGIHSLDDDEIQYWIDNVEVGNAYVNRGITGAIvqRQSFGGWKKSVMG 928
Cdd:cd07144 416 LAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDV--GVPFGGFKMSGIG 463
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
530-906 |
6.00e-26 |
|
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: 113.17 E-value: 6.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 530 RAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSA-----RLLDSYA 604
Cdd:cd07119 45 RRAFDSGEWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEIDIDDVANCFRYYAGLAtketgEVYDVPP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 605 AEFT-----PYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQvvhcAKLVVKAFRAGLEAQGLDPDLVQLVFTD 679
Cdd:cd07119 125 HVISrtvrePVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEV----TPLTTIALFELIEEAGLPAGVVNLVTGS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 680 EGDAGRALVSHADVDAVILTGASDTGK-LFRSWKPEL-NIMAETSGKNALIITPSADPDLAIQDLYLSAFGHSGQKCSAS 757
Cdd:cd07119 201 GATVGAELAESPDVDLVSFTGGTATGRsIMRAAAGNVkKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 758 SLVIfvgaAGES--QRLRSQLVDAVKTLIPGPGYEITTTMNGL-AEAPGEKLLRgLTQL--EPGETWLVKPEKLNED--- 829
Cdd:cd07119 281 SRLL----VEESihDKFVAALAERAKKIKLGNGLDADTEMGPLvSAEHREKVLS-YIQLgkEEGARLVCGGKRPTGDela 355
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1196634871 830 -GTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVGNAYVN 906
Cdd:cd07119 356 kGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIN 433
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
520-928 |
1.52e-25 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 112.22 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 520 DAGVVDKHV--SRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDP-EISEAIDFCTYYAQS 596
Cdd:PLN02766 56 DKEDVDLAVkaAREAFDHGPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 597 A-----------RLLDSYAAEfTPYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQV-------VHCAKLvvka 658
Cdd:PLN02766 136 AdkihgetlkmsRQLQGYTLK-EPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTplsalfyAHLAKL---- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 659 frAGLeaqgldPDLVQLVFTDEG-DAGRALVSHADVDAVILTGASDTGKLFRSWKPELN---IMAETSGKNALIITPSAD 734
Cdd:PLN02766 211 --AGV------PDGVINVVTGFGpTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSNlkqVSLELGGKSPLLIFDDAD 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 735 PDLAIQDLYLSAFGHSGQKCSASSLViFVgAAGESQRLRSQLVDAVKTLIPGPGYEITTTMNglAEAPGEKLLRGLTQLE 814
Cdd:PLN02766 283 VDMAVDLALLGIFYNKGEICVASSRV-YV-QEGIYDEFVKKLVEKAKDWVVGDPFDPRARQG--PQVDKQQFEKILSYIE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 815 PGE----TWLVKPEKLNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDE 890
Cdd:PLN02766 359 HGKregaTLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDV 438
|
410 420 430
....*....|....*....|....*....|....*...
gi 1196634871 891 IQYWIDNVEVGNAYVNrgITGAIVQRQSFGGWKKSVMG 928
Cdd:PLN02766 439 ANTVSRSIRAGTIWVN--CYFAFDPDCPFGGYKMSGFG 474
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
517-928 |
5.70e-25 |
|
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: 109.64 E-value: 5.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 517 EVTDAGVVDKH----VSRAAELGAEWgARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDP-EISEAIDFCT 591
Cdd:cd07089 12 TAPDAGAADVDaaiaAARRAFDTGDW-STDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAmQVDGPIGHLR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 592 YYAQsarLLDSYAAEFT------------------PYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAK 653
Cdd:cd07089 91 YFAD---LADSFPWEFDlpvpalrggpgrrvvrrePVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 654 LVVKAFraglEAQGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLfrswkpelnIMA-----------ETS 722
Cdd:cd07089 168 LLGEII----AETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRR---------IMAqaaatlkrvllELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 723 GKNALIITPSADPDLAIQDLYLSAFGHSGQKCSASSLVIfvgaAGESqrLRSQLVDAVKTLIP----GPGYEITTTMNGL 798
Cdd:cd07089 235 GKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLL----VPRS--RYDEVVEALAAAFEalpvGDPADPGTVMGPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 799 AEAPGEKLLRGLTQL--EPGETWLV---KPEKLnEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQN 873
Cdd:cd07089 309 ISAAQRDRVEGYIARgrDEGARLVTgggRPAGL-DKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIAN 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1196634871 874 STGYGLTGGIHSLDDDEIQYWIDNVEVGNAYVNRGITGAIvqRQSFGGWKKSVMG 928
Cdd:cd07089 388 DSDYGLSGGVWSADVDRAYRVARRIRTGSVGINGGGGYGP--DAPFGGYKQSGLG 440
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
524-928 |
6.63e-25 |
|
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: 109.74 E-value: 6.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 524 VDKHV---SRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTV-TQTDPEISEAIDFCTYYAQSA-- 597
Cdd:cd07141 46 VDKAVkaaRAAFKLGSPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFsKSYLVDLPGAIKVLRYYAGWAdk 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 598 ---RLLDSYAAEFTPYR---VTVVTP--PWNFPVAIPTGGIAAALAAGSAVIIKPAPQ----VVHCAKLVVKAfraglea 665
Cdd:cd07141 126 ihgKTIPMDGDFFTYTRhepVGVCGQiiPWNFPLLMAAWKLAPALACGNTVVLKPAEQtpltALYLASLIKEA------- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 666 qGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLFR--SWKPELN-IMAETSGKNALIITPSADPDLAIQDL 742
Cdd:cd07141 199 -GFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQqaAGKSNLKrVTLELGGKSPNIVFADADLDYAVEQA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 743 YLSAFGHSGQKCSASSLViFVGAAGESQRLRsQLVDAVKTLIPGPGYEiTTTMNGlAEAPGEKLLRGLTQLEPGETWLVK 822
Cdd:cd07141 278 HEALFFNMGQCCCAGSRT-FVQESIYDEFVK-RSVERAKKRVVGNPFD-PKTEQG-PQIDEEQFKKILELIESGKKEGAK 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 823 PE----KLNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNV 898
Cdd:cd07141 354 LEcggkRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNAL 433
|
410 420 430
....*....|....*....|....*....|.
gi 1196634871 899 EVGNAYVNrgiTGAIVQRQS-FGGWKKSVMG 928
Cdd:cd07141 434 RAGTVWVN---CYNVVSPQApFGGYKMSGNG 461
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
524-925 |
8.98e-25 |
|
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: 109.13 E-value: 8.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 524 VDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISvaayeankTVTQtdpEISEAIDFC---------TYYA 594
Cdd:cd07138 38 VDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ--------AITL---EMGAPITLAraaqvglgiGHLR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 595 QSARLLDSYAAEFTPYRVTVV---------TPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQvvhcAKLVVKAFRAGLEA 665
Cdd:cd07138 107 AAADALKDFEFEERRGNSLVVrepigvcglITPWNWPLNQIVLKVAPALAAGCTVVLKPSEV----APLSAIILAEILDE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 666 QGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLfrswkpelnIMA-----------ETSGKNALIITPSAD 734
Cdd:cd07138 183 AGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKR---------VAEaaadtvkrvalELGGKSANIILDDAD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 735 PDLAIQDLYLSAFGHSGQKCSASS--LVifvgaagESQRL---RSQLVDAVKTLIPGPGYEITTTMNGLAEAPGEKLLRG 809
Cdd:cd07138 254 LEKAVPRGVAACFANSGQSCNAPTrmLV-------PRSRYaeaEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 810 LTQ--LEPGETWLV----KPEKLnEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGI 883
Cdd:cd07138 327 YIQkgIEEGARLVAggpgRPEGL-ERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYV 405
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1196634871 884 HSLDDDEIQYWIDNVEVGNAYVNRGITGAivqRQSFGGWKKS 925
Cdd:cd07138 406 WSADPERARAVARRLRAGQVHINGAAFNP---GAPFGGYKQS 444
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
537-928 |
9.13e-25 |
|
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: 109.45 E-value: 9.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 537 EWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTqtdpeISEAIDFctyyAQSARLLDSYA------------ 604
Cdd:cd07113 53 AWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIH-----LSRAFEV----GQSANFLRYFAgwatkingetla 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 605 --------AEFT------PYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKP---AP-QVVHCAKLvvkAFRAGLeaq 666
Cdd:cd07113 124 psipsmqgERYTaftrrePVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPsefTPlTLLRVAEL---AKEAGI--- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 667 gldPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGK-LFRSWKPELN-IMAETSGKNALIITPSADPDLAIQDLYL 744
Cdd:cd07113 198 ---PDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKkIGRQAASDLTrVTLELGGKNAAAFLKDADIDWVVEGLLT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 745 SAFGHSGQKCSASSLViFVGAAgESQRLRSQLVDAVKTLIPGPGYEITTTMNGLAEAPG-EKLLRGLTQL-EPGETWLVK 822
Cdd:cd07113 275 AGFLHQGQVCAAPERF-YVHRS-KFDELVTKLKQALSSFQVGSPMDESVMFGPLANQPHfDKVCSYLDDArAEGDEIVRG 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 823 PEKLNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVGN 902
Cdd:cd07113 353 GEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGT 432
|
410 420
....*....|....*....|....*..
gi 1196634871 903 AYVN-RGITGAIVqrqSFGGWKKSVMG 928
Cdd:cd07113 433 VWVNmHTFLDPAV---PFGGMKQSGIG 456
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
518-928 |
1.27e-24 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 109.58 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 518 VTDAGVVDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSA 597
Cdd:PRK09407 50 VSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLDVALTARYYARRA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 598 RLLdsyaaeFTPYRVTVVTP-------------------PWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKA 658
Cdd:PRK09407 130 PKL------LAPRRRAGALPvltkttelrqpkgvvgvisPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVEL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 659 fragLEAQGLDPDLVQLVFTDEGDAGRALVSHADVdaVILTGASDTGKLF--RSWKPELNIMAETSGKNALIITPSADPD 736
Cdd:PRK09407 204 ----LYEAGLPRDLWQVVTGPGPVVGTALVDNADY--LMFTGSTATGRVLaeQAGRRLIGFSLELGGKNPMIVLDDADLD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 737 LAIQDLYLSAFGHSGQKCsASSLVIFVgaaGES--QRLRSQLVDAVKTLIPGPGYEITTTMNGLAEAPgekllrgltQLE 814
Cdd:PRK09407 278 KAAAGAVRACFSNAGQLC-ISIERIYV---HESiyDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEA---------QLE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 815 -----------PGETWLVKPEKLNEDGTL-WSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGG 882
Cdd:PRK09407 345 tvsahvddavaKGATVLAGGKARPDLGPLfYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNAS 424
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1196634871 883 IHSLDDDEIQYWIDNVEVGNAYVNRGITGAIVQRQS-FGGWKKSVMG 928
Cdd:PRK09407 425 VWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSVDApMGGMKDSGLG 471
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
524-923 |
1.37e-24 |
|
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: 108.83 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 524 VDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSARLLD-- 601
Cdd:cd07130 36 YESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLGEVQEMIDICDFAVGLSRQLYgl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 602 SYAAE---------FTPYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQV----VHCAKLVVKAfragLEAQGL 668
Cdd:cd07130 116 TIPSErpghrmmeqWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTpltaIAVTKIVARV----LEKNGL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 669 DPDLVQLVfTDEGDAGRALVSHADVDAVILTGASDTGKLF------RSWKPELnimaETSGKNALIITPSADPDLAIQDL 742
Cdd:cd07130 192 PGAIASLV-CGGADVGEALVKDPRVPLVSFTGSTAVGRQVgqavaaRFGRSLL----ELGGNNAIIVMEDADLDLAVRAV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 743 YLSAFGHSGQKCSASSLVIFvgaaGES--QRLRSQLVDAVKTLIPGPGYEITTTMNGL-AEAPGEKLLRGLTQL-EPGET 818
Cdd:cd07130 267 LFAAVGTAGQRCTTTRRLIV----HESiyDEVLERLKKAYKQVRIGDPLDDGTLVGPLhTKAAVDNYLAAIEEAkSQGGT 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 819 WLVKPEKLNEDGTLWSPGIRDNVRPGSWFHvNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNV 898
Cdd:cd07130 343 VLFGGKVIDGPGNYVEPTIVEGLSDAPIVK-EETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPK 421
|
410 420
....*....|....*....|....*..
gi 1196634871 899 --EVGNAYVNRGITGAIVQrQSFGGWK 923
Cdd:cd07130 422 gsDCGIVNVNIGTSGAEIG-GAFGGEK 447
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
520-928 |
3.01e-24 |
|
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: 107.52 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 520 DAGVVDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQT-DPEISEAIDFCTYYAQSAr 598
Cdd:cd07115 17 SAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRLDVPRAADTFRYYAGWA- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 599 llDSYAAEFTPYR-----VTVVTP--------PWNFPVAIPTGGIAAALAAGSAVIIKPAPQvvhcAKLVVKAFRAGLEA 665
Cdd:cd07115 96 --DKIEGEVIPVRgpflnYTVREPvgvvgaivPWNFPLMFAAWKVAPALAAGNTVVLKPAEL----TPLSALRIAELMAE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 666 QGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTG-KLFRSWKPELN-IMAETSGKNALIITPSADPDLAIQDLY 743
Cdd:cd07115 170 AGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGrKIMQGAAGNLKrVSLELGGKSANIVFADADLDAAVRAAA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 744 LSAFGHSGQKCSASSLVIfvgaAGES--QRLRSQLVDAVKTLIPGPGYEITTTMNGL-AEAPGEKLL----RGLTQlepG 816
Cdd:cd07115 250 TGIFYNQGQMCTAGSRLL----VHESiyDEFLERFTSLARSLRPGDPLDPKTQMGPLvSQAQFDRVLdyvdVGREE---G 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 817 ETWLVKPEKLNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWID 896
Cdd:cd07115 323 ARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAA 402
|
410 420 430
....*....|....*....|....*....|..
gi 1196634871 897 NVEVGNAYVNrgITGAIVQRQSFGGWKKSVMG 928
Cdd:cd07115 403 ALKAGTVWIN--TYNRFDPGSPFGGYKQSGFG 432
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
524-928 |
1.64e-23 |
|
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: 105.33 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 524 VDKHVS--RAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSARLLD 601
Cdd:cd07114 21 VDRAVAaaRAAFEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVRYLAEWYRYYAGLADKIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 602 ---------SYAAeFT---PYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQ----VVHCAKLVVKAfraglea 665
Cdd:cd07114 101 gavipvdkgDYLN-FTrrePLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHtpasTLELAKLAEEA------- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 666 qGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLF-----RSWKPelnIMAETSGKNALIITPSADPDLAIQ 740
Cdd:cd07114 173 -GFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIaraaaENLAP---VTLELGGKSPNIVFDDADLDAAVN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 741 DLYLSAFGHSGQKCSASSLvIFVgAAGESQRLRSQLVDAVKTLIPGPGYEITTTMNGLAEAP---------------GEK 805
Cdd:cd07114 249 GVVAGIFAAAGQTCVAGSR-LLV-QRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERqlekveryvarareeGAR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 806 LLRGLTQLEPGEtwlvkpeklNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHS 885
Cdd:cd07114 327 VLTGGERPSGAD---------LGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWT 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1196634871 886 LDDDEIQYWIDNVEVGNAYVN--RgitgAIVQRQSFGGWKKSVMG 928
Cdd:cd07114 398 RDLARAHRVARAIEAGTVWVNtyR----ALSPSSPFGGFKDSGIG 438
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
515-928 |
2.82e-23 |
|
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: 104.74 E-value: 2.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 515 VEEVTDAGVVD-KHVSRAAELGAE-WGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTY 592
Cdd:cd07145 12 IDTVPSLSREEvREAIEVAEKAKDvMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVERTIRLFKL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 593 YAQSARLL-------DSYAAE-----FT---PYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQ----VVHCAK 653
Cdd:cd07145 92 AAEEAKVLrgetipvDAYEYNerriaFTvrePIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNtpltAIELAK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 654 LVVKAfragleaqGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLFRSWKPEL--NIMAETSGKNALIITP 731
Cdd:cd07145 172 ILEEA--------GLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTgkKVALELGGSDPMIVLK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 732 SADPDLAIQDLYLSAFGHSGQKCSASSLVIfvgaAGES--QRLRSQLVDAVKTLIPGPGYEITTTMNGL----------- 798
Cdd:cd07145 244 DADLERAVSIAVRGRFENAGQVCNAVKRIL----VEEEvyDKFLKLLVEKVKKLKVGDPLDESTDLGPLispeavermen 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 799 ----AEAPGEKLLRGltqlepGEtwlvkpeklNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNS 874
Cdd:cd07145 320 lvndAVEKGGKILYG------GK---------RDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANS 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1196634871 875 TGYGLTGGIHSLDDDEIQYWIDNVEVGNAYVNRGITgaivQRQS---FGGWKKSVMG 928
Cdd:cd07145 385 TEYGLQASVFTNDINRALKVARELEAGGVVINDSTR----FRWDnlpFGGFKKSGIG 437
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
514-906 |
3.14e-23 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 105.20 E-value: 3.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 514 GVEEVTDAGVVDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYY 593
Cdd:PLN02467 42 ATAEDVDAAVEAARKAFKRNKGKDWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 594 AQSARLLDSYA--------AEFT------PYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQV-VHCAKLVVKA 658
Cdd:PLN02467 122 ADLAEALDAKQkapvslpmETFKgyvlkePLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELAsVTCLELADIC 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 659 FRAGLeaqgldPDLVQLVFTDEG-DAGRALVSHADVDAVILTGASDTGKLFRSW-----KPelnIMAETSGKNALIITPS 732
Cdd:PLN02467 202 REVGL------PPGVLNVVTGLGtEAGAPLASHPGVDKIAFTGSTATGRKIMTAaaqmvKP---VSLELGGKSPIIVFDD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 733 ADPDLAIQDLYLSAFGHSGQKCSASS-LVIFVGAAGESQRlrsQLVDAVKTLIPGPGYEITTTMNGL-AEAPGEKLLRGL 810
Cdd:PLN02467 273 VDLDKAVEWAMFGCFWTNGQICSATSrLLVHERIASEFLE---KLVKWAKNIKISDPLEEGCRLGPVvSEGQYEKVLKFI 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 811 -TQLEPGETWL---VKPEKLNEdGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSL 886
Cdd:PLN02467 350 sTAKSEGATILcggKRPEHLKK-GFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISN 428
|
410 420
....*....|....*....|
gi 1196634871 887 DDDEIQYWIDNVEVGNAYVN 906
Cdd:PLN02467 429 DLERCERVSEAFQAGIVWIN 448
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
530-928 |
1.05e-22 |
|
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: 102.77 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 530 RAAELG-AEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQ-----SARLLDSY 603
Cdd:cd07151 39 RAAAAAqKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANIEWGAAMAITREAATfplrmEGRILPSD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 604 --AAEFTPYRVTV----VTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQV-VHCAKLVVKAFraglEAQGLDPDLVQLV 676
Cdd:cd07151 119 vpGKENRVYREPLgvvgVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTpITGGLLLAKIF----EEAGLPKGVLNVV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 677 FTDEGDAGRALVSHADVDAVILTGASDTGK-LFRSWKPELNIMA-ETSGKNALIITPSADPDLAIQDLYLSAFGHSGQKC 754
Cdd:cd07151 195 VGAGSEIGDAFVEHPVPRLISFTGSTPVGRhIGELAGRHLKKVAlELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQIC 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 755 SASSLVIfVGAAGESQRLRsQLVDAVKTLIPG----PGYEITTTMNglaeapgEKLLRGLTQL-----EPGETWLVKPEK 825
Cdd:cd07151 275 MAINRII-VHEDVYDEFVE-KFVERVKALPYGdpsdPDTVVGPLIN-------ESQVDGLLDKieqavEEGATLLVGGEA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 826 lneDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVGNAYV 905
Cdd:cd07151 346 ---EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHI 422
|
410 420
....*....|....*....|....*.
gi 1196634871 906 NRGitgaIVQRQ---SFGGWKKSVMG 928
Cdd:cd07151 423 NDQ----PVNDEphvPFGGEKNSGLG 444
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
524-889 |
4.73e-22 |
|
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: 101.11 E-value: 4.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 524 VDKHVS--RAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVT-QTDPEISEAIDFCTYYAQSARll 600
Cdd:cd07139 38 VDAAVAaaRRAFDNGPWPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISwSRRAQGPGPAALLRYYAALAR-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 601 dSYAAEFT--------------PYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAfragLEAQ 666
Cdd:cd07139 116 -DFPFEERrpgsggghvlvrrePVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEA----AEEA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 667 GLDPDLVQLVFTDEgDAGRALVSHADVDAVILTGASDTGKLFRSWKPEL--NIMAETSGKNALIITPSADPDLAIQDLYL 744
Cdd:cd07139 191 GLPPGVVNVVPADR-EVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERlaRVTLELGGKSAAIVLDDADLDAAVPGLVP 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 745 SAFGHSGQKCSASSLVIFvgAAGESQRLRSQLVDAVKTLIPGPGYEITTTMNGLA---------------EAPGEKLLRG 809
Cdd:cd07139 270 ASLMNNGQVCVALTRILV--PRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLAsarqrervegyiakgRAEGARLVTG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 810 ---LTQLEPGetWLVKPeklnedgTLWSpgirdNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSL 886
Cdd:cd07139 348 ggrPAGLDRG--WFVEP-------TLFA-----DVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTA 413
|
...
gi 1196634871 887 DDD 889
Cdd:cd07139 414 DVE 416
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
550-931 |
6.95e-22 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 99.81 E-value: 6.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 550 LEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSARlldSYAAEF--------------TPYRVTVV 615
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWAR---RYEGEIiqsdrpgenillfkRALGVTTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 616 TPPWNFPVAIPTGGIAAALAAGSAVIIKPA---PQVVHC-AKLVVKAfragleaqGLDPDLVQLVFTDEGDAGRALVSHA 691
Cdd:PRK10090 78 ILPWNFPFFLIARKMAPALLTGNTIVIKPSeftPNNAIAfAKIVDEI--------GLPKGVFNLVLGRGETVGQELAGNP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 692 DVDAVILTGASDTGK--LFRSWKPELNIMAETSGKNALIITPSADPDLAIQDLYLSAFGHSGQKCSASSLViFVgAAGES 769
Cdd:PRK10090 150 KVAMVSMTGSVSAGEkiMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERV-YV-QKGIY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 770 QRLRSQLVDAVKTLIPG-PGYEITTTMNGLAEAPGEKLLRGLTQ--LEPGETWLVKPEKLNEDGTLWSPGIRDNVRPGSW 846
Cdd:PRK10090 228 DQFVNRLGEAMQAVQFGnPAERNDIAMGPLINAAALERVEQKVAraVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 847 FHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVGNAYVNRGITGAIvqrQSF-GGWKKS 925
Cdd:PRK10090 308 IMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAM---QGFhAGWRKS 384
|
....*.
gi 1196634871 926 VMGpGA 931
Cdd:PRK10090 385 GIG-GA 389
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
520-928 |
1.71e-21 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 99.88 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 520 DAGVVDKHVSRAAELGAE--WGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQT-DPEISEAIDFCTYYAQS 596
Cdd:PLN02466 93 DAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSaKAELPMFARLFRYYAGW 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 597 A-RLLDSYAAEFTPYRV-TVVTP--------PWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFragLEAq 666
Cdd:PLN02466 173 AdKIHGLTVPADGPHHVqTLHEPigvagqiiPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLL---HEA- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 667 GLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLFRSWKPELNIMA---ETSGKNALIITPSADPDLAIQDLY 743
Cdd:PLN02466 249 GLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKSNLKPvtlELGGKSPFIVCEDADVDKAVELAH 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 744 LSAFGHSGQKCSASSLViFVgaageSQRLRSQLVD-----AVKTLIPGPgyeittTMNGLAEAPG------EKLLRGL-T 811
Cdd:PLN02466 329 FALFFNQGQCCCAGSRT-FV-----HERVYDEFVEkakarALKRVVGDP------FKKGVEQGPQidseqfEKILRYIkS 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 812 QLEPGETWLVKPEKLNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEI 891
Cdd:PLN02466 397 GVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTA 476
|
410 420 430
....*....|....*....|....*....|....*....
gi 1196634871 892 QYWIDNVEVGNAYVN--RGITGAIvqrqSFGGWKKSVMG 928
Cdd:PLN02466 477 NTLSRALRVGTVWVNcfDVFDAAI----PFGGYKMSGIG 511
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
515-928 |
4.04e-21 |
|
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: 98.37 E-value: 4.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 515 VEEVTDAGVvDKHVSRA-AELGAEWGAR-PAEDRARALEAVADELANRRGEFISVAAYEANKTV-TQTDPEISEAIDFCT 591
Cdd:cd07143 38 IAEATEADV-DIAVEVAhAAFETDWGLKvSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTFgTAKRVDVQASADTFR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 592 YYAQSA-----RLLDSYAAEFT-----PYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFRa 661
Cdd:cd07143 117 YYGGWAdkihgQVIETDIKKLTytrhePIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIP- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 662 glEAqGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGK--LFRSWKPEL-NIMAETSGKNALIITPSADPDLA 738
Cdd:cd07143 196 --EA-GFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRkvMEAAAKSNLkKVTLELGGKSPNIVFDDADLESA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 739 IQDLYLSAFGHSGQKCSASSLvIFVgAAGESQRLRSQLVDAVKTLIPGPGYEITTTMNglAEAPGEKLLRGLTQLEPGE- 817
Cdd:cd07143 273 VVWTAYGIFFNHGQVCCAGSR-IYV-QEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQG--PQVSQIQYERIMSYIESGKa 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 818 ---TWLVKPEKLNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYW 894
Cdd:cd07143 349 egaTVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRV 428
|
410 420 430
....*....|....*....|....*....|....
gi 1196634871 895 IDNVEVGNAYVNrgITGAIVQRQSFGGWKKSVMG 928
Cdd:cd07143 429 ANALKAGTVWVN--CYNLLHHQVPFGGYKQSGIG 460
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
530-906 |
4.45e-21 |
|
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: 97.70 E-value: 4.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 530 RAAELGAEWGAR-PAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSARL-------LD 601
Cdd:cd07147 28 AAAVKAFRPMRAlPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDTFRIAAEEATRiygevlpLD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 602 SYAA---------EFTPYRVTVVTPpWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLvvkaFRAGLEAQGLDPDL 672
Cdd:cd07147 108 ISARgegrqglvrRFPIGPVSAITP-FNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALI----LGEVLAETGLPKGA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 673 VQLVFTDEGDAGRaLVSHADVDAVILTGASDTGKLFRSWKPELNIMAETSGKNALIITPSADPDLAIQDLYLSAFGHSGQ 752
Cdd:cd07147 183 FSVLPCSRDDADL-LVTDERIKLLSFTGSPAVGWDLKARAGKKKVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQ 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 753 KCsASSLVIFVGAAGESQrLRSQLVDAVKTLIPGPGYEITTTMNGLAEAPGEKLLRGLTQ--LEPGETWLVKPEKlneDG 830
Cdd:cd07147 262 SC-ISVQRVLVHRSVYDE-FKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNeaVDAGAKLLTGGKR---DG 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1196634871 831 TLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVGNAYVN 906
Cdd:cd07147 337 ALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVIN 412
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
524-906 |
9.00e-21 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 97.13 E-value: 9.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 524 VDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSA-RLL-- 600
Cdd:PLN00412 55 VNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGvRILge 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 601 ------DSYA---------AEFTPYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFRAGlea 665
Cdd:PLN00412 135 gkflvsDSFPgnernkyclTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLA--- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 666 qGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGAsDTGKLFRSWKPELNIMAETSGKNALIITPSADPDLAIQDLYLS 745
Cdd:PLN00412 212 -GFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIAISKKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 746 AFGHSGQKCSASSLVIFVGAAGEsqRLRSQLVDAVKTLIPGPGyEITTTMNGLAEAPGEKLLRGLTQ--LEPGETWLvkP 823
Cdd:PLN00412 290 GFSYSGQRCTAVKVVLVMESVAD--ALVEKVNAKVAKLTVGPP-EDDCDITPVVSESSANFIEGLVMdaKEKGATFC--Q 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 824 EKLNEDGTLWsPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVGNA 903
Cdd:PLN00412 365 EWKREGNLIW-PLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTV 443
|
...
gi 1196634871 904 YVN 906
Cdd:PLN00412 444 QIN 446
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
517-928 |
4.58e-20 |
|
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: 95.10 E-value: 4.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 517 EVTDAGV--VDKHVSRAAELGAEWGARPAEDRARALEAVADEL-ANRrgEFISVA-AYEANKTVTQT-DPEISEAIDFCT 591
Cdd:cd07559 31 EIPRSTAedVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIeENL--ELLAVAeTLDNGKPIRETlAADIPLAIDHFR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 592 YYAQSARLLDSYAAEF----------TPYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQ----VVHCAKLVvk 657
Cdd:cd07559 109 YFAGVIRAQEGSLSEIdedtlsyhfhEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQtplsILVLMELI-- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 658 afragleAQGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLFRSWKPELNIMA--ETSGKNALIITPSA-D 734
Cdd:cd07559 187 -------GDLLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENLIPVtlELGGKSPNIFFDDAmD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 735 PDLAIQDLYLSAFG----HSGQKCSASSLvIFVgAAGESQRLRSQLVDAVKTLIPGPGYEiTTTMNGlAEAPGEKLLRGL 810
Cdd:cd07559 260 ADDDFDDKAEEGQLgfafNQGEVCTCPSR-ALV-QESIYDEFIERAVERFEAIKVGNPLD-PETMMG-AQVSKDQLEKIL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 811 TQL----EPGETWLVKPEKLNEDGTL----WSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGG 882
Cdd:cd07559 336 SYVdigkEEGAEVLTGGERLTLGGLDkgyfYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGG 415
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1196634871 883 IHSLDDDEIQYWIDNVEVGNAYVNrgITGAIVQRQSFGGWKKSVMG 928
Cdd:cd07559 416 VWTRDINRALRVARGIQTGRVWVN--CYHQYPAHAPFGGYKKSGIG 459
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
515-879 |
4.78e-20 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 94.98 E-value: 4.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 515 VEEVTDAGV--VDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQT-DPEISEAIDFCT 591
Cdd:PRK13473 30 LAEIAEASAaqVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLAlNDEIPAIVDVFR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 592 YYAQSARLLDS-----YAAEFTPY-R---VTVVT--PPWNFPVAIPTGGIAAALAAGSAVIIKPAPQ----VVHCAKLVV 656
Cdd:PRK13473 110 FFAGAARCLEGkaageYLEGHTSMiRrdpVGVVAsiAPWNYPLMMAAWKLAPALAAGNTVVLKPSEItpltALKLAELAA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 657 KAFRAGleaqgldpdLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKlfrswkpelNIMAETS-----------GKN 725
Cdd:PRK13473 190 DILPPG---------VLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGK---------HVLSAAAdsvkrthlelgGKA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 726 ALIITPSADPDLAIQDLYLSAFGHSGQKCSASSLVIfvGAAGESQRLRSQLVDAVKTLIPGPGYEITTTMNGL------- 798
Cdd:PRK13473 252 PVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIY--AQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLisaahrd 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 799 ------AEAPGEKLLRGLTqlepgetwlvKPEKLNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQ 872
Cdd:PRK13473 330 rvagfvERAKALGHIRVVT----------GGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWA 399
|
....*..
gi 1196634871 873 NSTGYGL 879
Cdd:PRK13473 400 NDSDYGL 406
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
517-928 |
6.01e-20 |
|
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: 94.44 E-value: 6.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 517 EVTDAGV--VDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDP-EISEAIDFCTYY 593
Cdd:cd07117 31 EITDATDadVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRAvDIPLAADHFRYF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 594 AQSARLLDSYAAEFT----------PYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQ----VVHCAKLVVKAF 659
Cdd:cd07117 111 AGVIRAEEGSANMIDedtlsivlrePIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTtslsLLELAKIIQDVL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 660 RAGleaqgldpdLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLFRSWKPELNIMA--ETSGKNALIITPSADPDL 737
Cdd:cd07117 191 PKG---------VVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIPAtlELGGKSANIIFDDANWDK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 738 AIQDLYLSAFGHSGQKCSASSLvIFVgAAGESQRLRSQLVDAVKTLIPGPGYEITTTMNG-LAEAPGEKLLRGL-TQLEP 815
Cdd:cd07117 262 ALEGAQLGILFNQGQVCCAGSR-IFV-QEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAqVNKDQLDKILSYVdIAKEE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 816 GETWLVKPEKLNED----GTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEI 891
Cdd:cd07117 340 GAKILTGGHRLTENgldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRA 419
|
410 420 430
....*....|....*....|....*....|....*..
gi 1196634871 892 QYWIDNVEVGNAYVNrgITGAIVQRQSFGGWKKSVMG 928
Cdd:cd07117 420 LRVARAVETGRVWVN--TYNQIPAGAPFGGYKKSGIG 454
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
524-936 |
1.21e-18 |
|
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: 90.37 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 524 VDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDpEISEAIDFCTYYAQSARLLDSY 603
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAE-NICGDQVQLRARAFVIYSYRIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 604 AA---------------EFTPYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFRaglEAQGL 668
Cdd:cd07084 80 HEpgnhlgqglkqqshgYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLH---YAGLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 669 DPDLVQLVFTDeGDAGRALVSHADVDAVILTGASDTGKLFRSWKPELNIMAETSGKNALIITPSADP-DLAIQDLYLSAF 747
Cdd:cd07084 157 PPEDVTLINGD-GKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQARIYLELAGFNWKVLGPDAQAvDYVAWQCVQDMT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 748 GHSGQKCSASSlVIFVGAAGESQRLRSQLVDAVKTLIPGP---GYEIT-TTMNGLAEAP--GEKLLRGLTQLEPGETWLV 821
Cdd:cd07084 236 ACSGQKCTAQS-MLFVPENWSKTPLVEKLKALLARRKLEDlllGPVQTfTTLAMIAHMEnlLGSVLLFSGKELKNHSIPS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 822 KPEKLnEDGTLWSPGIRDNVRPGSWfhVNECFGPVLGIMH------AETLEQAIEWQNStgygLTGGIHSLDDDEIQYWI 895
Cdd:cd07084 315 IYGAC-VASALFVPIDEILKTYELV--TEEIFGPFAIVVEykkdqlALVLELLERMHGS----LTAAIYSNDPIFLQELI 387
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1196634871 896 DNVEV-GNAY-VNRGITGAIVQRQSFGGWKKSvmGPGAKAGGP 936
Cdd:cd07084 388 GNLWVaGRTYaILRGRTGVAPNQNHGGGPAAD--PRGAGIGGP 428
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
515-942 |
6.85e-18 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 88.35 E-value: 6.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 515 VEEVTDAGVVDKHVS-RAAELGAE-WGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTY 592
Cdd:PLN02315 47 IAEVVEASLEDYEEGlRACEEAAKiWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDF 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 593 YAQSARLLDSYAAE-----------FTPYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFRA 661
Cdd:PLN02315 127 AVGLSRQLNGSIIPserpnhmmmevWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 662 GLEAQGLdPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLF------RSWKPELnimaETSGKNALIITPSADP 735
Cdd:PLN02315 207 VLEKNNL-PGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVqqtvnaRFGKCLL----ELSGNNAIIVMDDADI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 736 DLAIQDLYLSAFGHSGQKCSASSLVIFvgaaGES--QRLRSQLVDAVKTLIPGPGYEITTTMNGL-AEAPGEKLLRGLTQ 812
Cdd:PLN02315 282 QLAVRSVLFAAVGTAGQRCTTCRRLLL----HESiyDDVLEQLLTVYKQVKIGDPLEKGTLLGPLhTPESKKNFEKGIEI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 813 LEP-GETWLVKPEKLNEDGTLWSPGIRDnVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEI 891
Cdd:PLN02315 358 IKSqGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETI 436
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1196634871 892 QYWI--DNVEVGNAYVNRGITGAIVQrQSFGGWKKSvmGPGAKAGGPNYVPQM 942
Cdd:PLN02315 437 FKWIgpLGSDCGIVNVNIPTNGAEIG-GAFGGEKAT--GGGREAGSDSWKQYM 486
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
524-928 |
1.16e-17 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 87.10 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 524 VDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSAR--LLD 601
Cdd:PRK09406 25 VDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYYAEHAEalLAD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 602 SYA-----------AEFTPYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFRAGleaqGLDP 670
Cdd:PRK09406 105 EPAdaaavgasrayVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRA----GFPD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 671 DLVQLVFTDEGdAGRALVSHADVDAVILTGASDTGKLF-----RSWKPelnIMAETSGKNALIITPSADPDLAIQDLYLS 745
Cdd:PRK09406 181 GCFQTLLVGSG-AVEAILRDPRVAAATLTGSEPAGRAVaaiagDEIKK---TVLELGGSDPFIVMPSADLDRAAETAVTA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 746 AFGHSGQKCSASSLviFVGAAGESQRLRSQLVDAVKTLIPGPGYEITTTMNGLAEAPG----EKLLRGltQLEPGETWLV 821
Cdd:PRK09406 257 RVQNNGQSCIAAKR--FIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGrdevEKQVDD--AVAAGATILC 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 822 KPEKLNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVG 901
Cdd:PRK09406 333 GGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAG 412
|
410 420
....*....|....*....|....*..
gi 1196634871 902 NAYVNrGITgAIVQRQSFGGWKKSVMG 928
Cdd:PRK09406 413 QVFIN-GMT-VSYPELPFGGVKRSGYG 437
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
538-939 |
9.34e-17 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 84.57 E-value: 9.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 538 WGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSARLL--DSYAAEFT------- 608
Cdd:PRK11241 64 WRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIygDTIPGHQAdkrlivi 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 609 --PYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCA-KLVVKAFRAGLEAqgldpDLVQLVFTDEGDAGR 685
Cdd:PRK11241 144 kqPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSAlALAELAIRAGIPA-----GVFNVVTGSAGAVGG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 686 ALVSHADVDAVILTGASDTGK--LFRSWKPELNIMAETSGKNALIITPSADPDLAIQDLYLSAFGHSGQKCSASSLvIFV 763
Cdd:PRK11241 219 ELTSNPLVRKLSFTGSTEIGRqlMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANR-LYV 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 764 gAAGESQRLRSQLVDAVKTLIPGPGYEITTTMNGL---------AEAPGEKLLRGLTQLEPGetwlvKPEKLneDGTLWS 834
Cdd:PRK11241 298 -QDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLidekavakvEEHIADALEKGARVVCGG-----KAHEL--GGNFFQ 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 835 PGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVGNAYVNRGITGAIV 914
Cdd:PRK11241 370 PTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEV 449
|
410 420
....*....|....*....|....*.
gi 1196634871 915 qrQSFGGWKKSVMG-PGAKAGGPNYV 939
Cdd:PRK11241 450 --APFGGIKASGLGrEGSKYGIEDYL 473
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
528-906 |
9.66e-17 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 85.18 E-value: 9.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 528 VSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSARL-------- 599
Cdd:PLN02419 157 VSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLqmgeylpn 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 600 ----LDSYAAEfTPYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVK-AFRAGLeaqgldPDLVQ 674
Cdd:PLN02419 237 vsngVDTYSIR-EPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAElAMEAGL------PDGVL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 675 LVFTDEGDAGRALVSHADVDAVILTGASDTGKLF--RSWKPELNIMAETSGKNALIITPSADPDLAIQDLYLSAFGHSGQ 752
Cdd:PLN02419 310 NIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIyaRAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQ 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 753 KCSASSLVIFVgaaGESQRLRSQLVDAVKTLIPGPGYEITTTMNGLAEAPGEKLLRGLTQ--LEPGETWLVKPEKL---- 826
Cdd:PLN02419 390 RCMALSTVVFV---GDAKSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQsgVDDGAKLLLDGRDIvvpg 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 827 NEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVGNAYVN 906
Cdd:PLN02419 467 YEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
524-928 |
1.06e-16 |
|
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: 84.47 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 524 VDKHVSRAAEL--GAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVT-QTDPEISEAIDFCTYYA------ 594
Cdd:cd07140 45 VDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTlALKTHVGMSIQTFRYFAgwcdki 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 595 QSARLLDSYAAE-----FT---PYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPApQV-----VHCAKLVVKAfra 661
Cdd:cd07140 125 QGKTIPINQARPnrnltLTkrePIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPA-QVtpltaLKFAELTVKA--- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 662 gleaqGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLFRSWKPELNIMA---ETSGKNALIITPSADPDLA 738
Cdd:cd07140 201 -----GFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAVSNLKKvslELGGKSPLIIFADCDMDKA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 739 IQDLYLSAFGHSGQKCSASSLvIFVGAAGESQRLRsQLVDAVKTLIPGPGYEiTTTMNGLA--EAPGEKLLRGLTQ-LEP 815
Cdd:cd07140 276 VRMGMSSVFFNKGENCIAAGR-LFVEESIHDEFVR-RVVEEVKKMKIGDPLD-RSTDHGPQnhKAHLDKLVEYCERgVKE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 816 GETWLVKPEKLNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGI--MHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQY 893
Cdd:cd07140 353 GATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIIskFDDGDVDGVLQRANDTEYGLASGVFTKDINKALY 432
|
410 420 430
....*....|....*....|....*....|....*
gi 1196634871 894 WIDNVEVGNAYVNRGITGAIVqrQSFGGWKKSVMG 928
Cdd:cd07140 433 VSDKLEAGTVFVNTYNKTDVA--APFGGFKQSGFG 465
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
612-928 |
1.19e-15 |
|
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: 80.73 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 612 VTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFRagleaQGLDPDLVQLVFTDEGDAGRALVSHa 691
Cdd:cd07135 111 VVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVP-----KYLDPDAFQVVQGGVPETTALLEQK- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 692 dVDAVILTGASDTGKlfrswkpelnIMA------------ETSGKNALIITPSADPDLAIQDLYLSAFGHSGQKCSASSL 759
Cdd:cd07135 185 -FDKIFYTGSGRVGR----------IIAeaaakhltpvtlELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDY 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 760 VI--------FVGAAGES-QRLRSQLVDAVKTL---IPGPGYEITTTMngLAEAPGEKLLRGLTqlepgetwlvkpekln 827
Cdd:cd07135 254 VLvdpsvydeFVEELKKVlDEFYPGGANASPDYtriVNPRHFNRLKSL--LDTTKGKVVIGGEM---------------- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 828 EDGTLW-SPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVGNAYVN 906
Cdd:cd07135 316 DEATRFiPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVIN 395
|
330 340
....*....|....*....|..
gi 1196634871 907 RGITGAIVQRQSFGGWKKSVMG 928
Cdd:cd07135 396 DTLIHVGVDNAPFGGVGDSGYG 417
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
609-925 |
7.06e-15 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 78.78 E-value: 7.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 609 PYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPApqvvhcAKLVVKAFR-AGLEAQGLDPDLVQLVFTDEG-DAGRA 686
Cdd:PRK09847 157 PVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPS------EKSPLSAIRlAGLAKEAGLPDGVLNVVTGFGhEAGQA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 687 LVSHADVDAVILTGASDTGKLFRSWKPELN---IMAETSGKNALIITpsAD-PDL--AIQDLYLSAFGHSGQKCSASSLV 760
Cdd:PRK09847 231 LSRHNDIDAIAFTGSTRTGKQLLKDAGDSNmkrVWLEAGGKSANIVF--ADcPDLqqAASATAAGIFYNQGQVCIAGTRL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 761 IFVGAAGES--QRLRSQlvdaVKTLIPGPGYEITTTMNGLAE-APGEKLLRGLTQLEPGETWLVKPEKLNEDGTLwSPGI 837
Cdd:PRK09847 309 LLEESIADEflALLKQQ----AQNWQPGHPLDPATTMGTLIDcAHADSVHSFIREGESKGQLLLDGRNAGLAAAI-GPTI 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 838 RDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVGNAYVNRGITGAIVqrQ 917
Cdd:PRK09847 384 FVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMT--V 461
|
....*...
gi 1196634871 918 SFGGWKKS 925
Cdd:PRK09847 462 PFGGYKQS 469
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
524-928 |
1.62e-14 |
|
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: 77.49 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 524 VDKHVSRAAELGAEWGARPAEDRARALEAVADELaNRRGEFISVA-AYEANKTVTQT-DPEISEAIDFCTYYAQSARLLD 601
Cdd:cd07116 40 IELALDAAHAAKEAWGKTSVAERANILNKIADRM-EANLEMLAVAeTWDNGKPVRETlAADIPLAIDHFRYFAGCIRAQE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 602 SYAAE----------FTPYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKafragLEAQGLDPD 671
Cdd:cd07116 119 GSISEidentvayhfHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLME-----LIGDLLPPG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 672 LVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKLFRSWKPElNIMA---ETSGKNALIITPS---ADPDL---AIQDL 742
Cdd:cd07116 194 VVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASE-NIIPvtlELGGKSPNIFFADvmdADDAFfdkALEGF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 743 YLSAFgHSGQKCSASSLVIFvgaaGES--QRLRSQLVDAVKTLIPGPGYEiTTTMNGlAEAPGEKLLRGLTQL----EPG 816
Cdd:cd07116 273 VMFAL-NQGEVCTCPSRALI----QESiyDRFMERALERVKAIKQGNPLD-TETMIG-AQASLEQLEKILSYIdigkEEG 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 817 ETWLVKPEKLNEDGTLWSPGIrdnVRPGSWFHVN------ECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDE 890
Cdd:cd07116 346 AEVLTGGERNELGGLLGGGYY---VPTTFKGGNKmrifqeEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNT 422
|
410 420 430
....*....|....*....|....*....|....*...
gi 1196634871 891 IQYWIDNVEVGNAYVNrgITGAIVQRQSFGGWKKSVMG 928
Cdd:cd07116 423 AYRMGRGIQAGRVWTN--CYHLYPAHAAFGGYKQSGIG 458
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
517-928 |
3.07e-14 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 76.84 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 517 EVTDAGVVDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEfisVAAYEanktVTQTDPEISEAI--------D 588
Cdd:PRK13252 39 QAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDE---LAALE----TLDTGKPIQETSvvdivtgaD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 589 FCTYYAQsarLLDSYAAEFTPYR-------------VTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLV 655
Cdd:PRK13252 112 VLEYYAG---LAPALEGEQIPLRggsfvytrreplgVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 656 VKAFR-AGLeaqgldPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGKlfrswkpelNIMA-----------ETSG 723
Cdd:PRK13252 189 AEIYTeAGL------PDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGK---------KVMAaaaaslkevtmELGG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 724 KNALIITPSADPDLAIQDLYLSAFGHSGQKCSASSLViFVgAAGESQRLRSQLVDAVKTLIPGPGYEITTTMNGLAEAPG 803
Cdd:PRK13252 254 KSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRV-FV-QKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAH 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 804 -EKLLRGLTQ-LEPGETWLVKPEKLNED----GTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGY 877
Cdd:PRK13252 332 rDKVLGYIEKgKAEGARLLCGGERLTEGgfanGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEY 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1196634871 878 GLTGGIHSLDDDEIQYWIDNVEVGNAYVNR-GITGAivqRQSFGGWKKSVMG 928
Cdd:PRK13252 412 GLAAGVFTADLSRAHRVIHQLEAGICWINTwGESPA---EMPVGGYKQSGIG 460
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
524-890 |
4.89e-13 |
|
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: 72.57 E-value: 4.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 524 VDKHVSRAAELGAEWGARPAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQSAR----- 598
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVRegswl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 599 --LLDSYAAEFTP--------YRVTV----VTPPWNFPVAI---------------PtggiaaalaagsaVIIKPAPQVV 649
Cdd:cd07129 81 daRIDPADPDRQPlprpdlrrMLVPLgpvaVFGASNFPLAFsvaggdtasalaagcP-------------VVVKAHPAHP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 650 HCAKLVVKAFRAGLEAQGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGASDTGK-LFR--SWKPE-LNIMAETSGKN 725
Cdd:cd07129 148 GTSELVARAIRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRaLFDaaAARPEpIPFYAELGSVN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 726 ALIITPSA---DPDLAIQDLYLSAFGHSGQKCSASSLViFVGAAGESQRLRSQLVDAVKTLIPGP--------GYEitTT 794
Cdd:cd07129 228 PVFILPGAlaeRGEAIAQGFVGSLTLGAGQFCTNPGLV-LVPAGPAGDAFIAALAEALAAAPAQTmltpgiaeAYR--QG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 795 MNGLAEAPGEKLLrgLTQLEPGETWLVKPeklnedgTLWSPGIRDNVRPGSWFHvnECFGPVLGIMHAETLEQAIEWQNS 874
Cdd:cd07129 305 VEALAAAPGVRVL--AGGAAAEGGNQAAP-------TLFKVDAAAFLADPALQE--EVFGPASLVVRYDDAAELLAVAEA 373
|
410
....*....|....*.
gi 1196634871 875 TGYGLTGGIHSLDDDE 890
Cdd:cd07129 374 LEGQLTATIHGEEDDL 389
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
618-928 |
3.92e-12 |
|
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 275104 Cd Length: 480 Bit Score: 70.18 E-value: 3.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 618 PWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFragLEAQGLDPDLVQLVFTDEGDAGRALVSHADVDAVI 697
Cdd:TIGR04284 150 PWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAVLGELI---AEHTDFPPGVVNIVTSSDHRLGALLAKDPRVDMVS 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 698 LTGASDTGKlfrswkpelNIMA-----------ETSGKNALIITPSADPDLAIQDLYLSAFGHSGQKCSASSlvifvgaa 766
Cdd:TIGR04284 227 FTGSTATGR---------AVMAdaaatlkkvflELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITT-------- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 767 gesqRL---RSQLVDAVKTLipgpgyeiTTTMNGLaeAPGEKLLRGLT--------QLEPGETWLVKPEKlnEDGTLWSP 835
Cdd:TIGR04284 290 ----RLvvpRARYDEAVAAA--------AATMGSI--KPGDPADPGTVcgpvisarQRDRVQSYLDLAVA--EGGRFACG 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 836 GIRDNVRPGSWF---------------HVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEV 900
Cdd:TIGR04284 354 GGRPADRDRGFFveptviagldnnarvAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVFGADPERAAAVAARVRT 433
|
330 340
....*....|....*....|....*....
gi 1196634871 901 GNAYVNRGI-TGAIVqrqSFGGWKKSVMG 928
Cdd:TIGR04284 434 GTVNVNGGVwYSADA---PFGGYKQSGIG 459
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
609-928 |
3.00e-11 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 67.36 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 609 PYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVvkafrAGLEAQGLDPDLVQLVftdEGDA--GRA 686
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLM-----AKLLTKYLDPSYVRVI---EGGVevTTE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 687 LVSHAdVDAVILTGASDTGKLfrswkpelnIMA-----------ETSGKNALIITPSADPDLAIQDLYLSAFGHSGQKCS 755
Cdd:PTZ00381 181 LLKEP-FDHIFFTGSPRVGKL---------VMQaaaenltpctlELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCV 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 756 ASSLVIFvgaageSQRLRSQLVDAVKTLIP---GPGYEITTTMNGLAEAPGEKLLRGLTQLEPGEtwLVKPEKLNEDGTL 832
Cdd:PTZ00381 251 APDYVLV------HRSIKDKFIEALKEAIKeffGEDPKKSEDYSRIVNEFHTKRLAELIKDHGGK--VVYGGEVDIENKY 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 833 WSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVGNAYVNRGITGA 912
Cdd:PTZ00381 323 VAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHL 402
|
330
....*....|....*.
gi 1196634871 913 IVQRQSFGGWKKSVMG 928
Cdd:PTZ00381 403 LNPNLPFGGVGNSGMG 418
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
609-928 |
3.84e-11 |
|
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: 66.78 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 609 PYRVTVVTPPWNFPV---------AIP---TggiaaalaagsaVIIKPAPQVVHCAKLVVKAFragleAQGLDPDLVQLV 676
Cdd:cd07087 100 PLGVVLIIGPWNYPLqlalapligAIAagnT------------VVLKPSELAPATSALLAKLI-----PKYFDPEAVAVV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 677 ftdEGDA--GRALVSHAdVDAVILTGASDTGKLfrswkpelnIMA-----------ETSGKNALIITPSADPDLAIQDLY 743
Cdd:cd07087 163 ---EGGVevATALLAEP-FDHIFFTGSPAVGKI---------VMEaaakhltpvtlELGGKSPCIVDKDANLEVAARRIA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 744 LSAFGHSGQKCSASSLViFVgaageSQRLRSQLVDAVKTLIpgpgyeitTTMNGlaEAPGE-----------------KL 806
Cdd:cd07087 230 WGKFLNAGQTCIAPDYV-LV-----HESIKDELIEELKKAI--------KEFYG--EDPKEspdygriinerhfdrlaSL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 807 LRGLTQLEPGETwlvkpeklNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSL 886
Cdd:cd07087 294 LDDGKVVIGGQV--------DKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSE 365
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1196634871 887 DDDEIQYWIDNVEVGNAYVNRGITGAIVQRQSFGGWKKSVMG 928
Cdd:cd07087 366 DKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGGVGNSGMG 407
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
609-928 |
1.16e-10 |
|
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: 65.32 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 609 PYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKafragLEAQGLDPDLVQLVFTDEGDAGRALv 688
Cdd:cd07132 100 PLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAE-----LIPKYLDKECYPVVLGGVEETTELL- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 689 sHADVDAVILTGASDTGKLfrswkpelnIMA-----------ETSGKNALIITPSADPDLAIQDLYLSAFGHSGQKCSAS 757
Cdd:cd07132 174 -KQRFDYIFYTGSTSVGKI---------VMQaaakhltpvtlELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAP 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 758 SLVIFvgaageSQRLRSQLVDAVKTLI---------PGPGYEITTTMNGLAEApgEKLLRGLTQLEPGETwlvkpeklNE 828
Cdd:cd07132 244 DYVLC------TPEVQEKFVEALKKTLkefygedpkESPDYGRIINDRHFQRL--KKLLSGGKVAIGGQT--------DE 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 829 DGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVGNAYVNRG 908
Cdd:cd07132 308 KERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDT 387
|
330 340
....*....|....*....|
gi 1196634871 909 ITGAIVQRQSFGGWKKSVMG 928
Cdd:cd07132 388 IMHYTLDSLPFGGVGNSGMG 407
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
517-874 |
2.74e-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: 63.98 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 517 EVTDAGVVDKHVSRAAELGAEWGAR-PAEDRARALEAVADELANRRGEFISVAAYEANKTVTQTDPEISEAIDFCTYYAQ 595
Cdd:cd07148 16 PTVDWAAIDKALDTAHALFLDRNNWlPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVELAAD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 596 SARLL-------DSYAAE-----FT---PYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFR 660
Cdd:cd07148 96 ELGQLggreipmGLTPASagriaFTtrePIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLH 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 661 aglEAqGLDPDLVQLVFTDEgDAGRALVSHADVDAVILTGASDTGKLFRS-WKPELNIMAETSGKNALIITPSADPDLAI 739
Cdd:cd07148 176 ---EA-GLPEGWCQAVPCEN-AVAEKLVTDPRVAFFSFIGSARVGWMLRSkLAPGTRCALEHGGAAPVIVDRSADLDAMI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 740 QDLYLSAFGHSGQKCsASSLVIFVGAAgESQRLRSQLVDAVKTLIPGPGYEITTTMNGL---------------AEAPGE 804
Cdd:cd07148 251 PPLVKGGFYHAGQVC-VSVQRVFVPAE-IADDFAQRLAAAAEKLVVGDPTDPDTEVGPLirprevdrveewvneAVAAGA 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 805 KLLRGLTQLepgetwlvkpeklneDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNS 874
Cdd:cd07148 329 RLLCGGKRL---------------SDTTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANS 383
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
612-928 |
3.50e-10 |
|
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: 63.78 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 612 VTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKafragLEAQGLDPDLVQLVftdEGDA--GRALVS 689
Cdd:cd07134 103 VCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAK-----IIREAFDEDEVAVF---EGDAevAQALLE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 690 HAdVDAVILTGASDTGKLfrswkpelnIMA-----------ETSGKNALIITPSADPDLAIQDLYLSAFGHSGQKCSASS 758
Cdd:cd07134 175 LP-FDHIFFTGSPAVGKI---------VMAaaakhlasvtlELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 759 LViFVGAAgesqrLRSQLVDAVKTLI-----------PGPGY-EITTTMN-----GLAEapgEKLLRGLTQLEPGETwlv 821
Cdd:cd07134 245 YV-FVHES-----VKDAFVEHLKAEIekfygkdaarkASPDLaRIVNDRHfdrlkGLLD---DAVAKGAKVEFGGQF--- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 822 kpeklNEDGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVG 901
Cdd:cd07134 313 -----DAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSG 387
|
330 340
....*....|....*....|....*..
gi 1196634871 902 NAYVNRGITGAIVQRQSFGGWKKSVMG 928
Cdd:cd07134 388 GVVVNDVVLHFLNPNLPFGGVNNSGIG 414
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
640-767 |
5.04e-09 |
|
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: 60.18 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 640 VIIKPAPQVVHCAKLVVKAFRAGLEAQGLDPDLVQLV-FTDEGDAGRALVSHADVDAVILTGASDTGKLFRSWKPELNIM 718
Cdd:cd07127 224 VIVKPHPAAILPLAITVQVAREVLAEAGFDPNLVTLAaDTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQAQVY 303
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1196634871 719 AETSGKNALIITPSADPDLAIQDLYLSAFGHSGQKCSASSlVIFVGAAG 767
Cdd:cd07127 304 TEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQ-NIYVPRDG 351
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
201-423 |
5.94e-09 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 59.71 E-value: 5.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 201 EGSLVRLKERLRPLYEAAARRPDRVFInlDMEEYHdLHLTVRLFTELLSEPEFTNLEAGIVL---QAYLPDTFDALAHLA 277
Cdd:PLN02681 212 ERLLELAHERLQKLCERAAQLGVPLLI--DAEYTS-LQPAIDYITYDLAREFNKGKDRPIVYgtyQAYLKDARERLRLDL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 278 EFAKQRvaegGSHIKIRIVKGANLSMEHVQGEIHGWPAAPYSTKDEVDANYYRLLDYILRPEFADCVRIGVATHNLYT-- 355
Cdd:PLN02681 289 ERSERE----GVPLGAKLVRGAYLSLERRLAASLGVPSPVHDTIQDTHACYNRCAEFLLEKASNGDGEVMLATHNVESge 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1196634871 356 --AAFAYKLGTKRGVMRMMDSEMLqGMSPAQQTAVRKAfeGRQIL-YTPvvhMEDFDVAVSYLVRRLEENS 423
Cdd:PLN02681 365 laAAKMNELGLHKGDPRVQFAQLL-GMSDNLSFGLGNA--GFRVSkYLP---YGPVEEVIPYLLRRAEENR 429
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
545-891 |
1.50e-07 |
|
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: 55.35 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 545 DRARALEAVADELANRRGEFISVAAyeaNKTVTQTDP--EISEAIDFCTYYAQSAR--------LLD----------SYA 604
Cdd:cd07128 60 ERAAMLKALAKYLMERKEDLYALSA---ATGATRRDSwiDIDGGIGTLFAYASLGRrelpnahfLVEgdveplskdgTFV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 605 AE--FTPYR-VTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFraglEAQGLDPD-LVQLVFTDE 680
Cdd:cd07128 137 GQhiLTPRRgVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDI----VESGLLPEgALQLICGSV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 681 GDagraLVSH-ADVDAVILTGASDTGKLFRSwKPELN-----IMAETSGKNALIITPSADP-----DLAIQDLYLSAFGH 749
Cdd:cd07128 213 GD----LLDHlGEQDVVAFTGSAATAAKLRA-HPNIVarsirFNAEADSLNAAILGPDATPgtpefDLFVKEVAREMTVK 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 750 SGQKCSASSLvIFVGAAgesqrlrsqLVDAV---------KTLIPGPGYEiTTTMNGLA--------EAPGEKLLRGLTQ 812
Cdd:cd07128 288 AGQKCTAIRR-AFVPEA---------RVDAViealkarlaKVVVGDPRLE-GVRMGPLVsreqredvRAAVATLLAEAEV 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 813 LEPGETWLVKPEKLNEDGTLWSPGI--RDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDE 890
Cdd:cd07128 357 VFGGPDRFEVVGADAEKGAFFPPTLllCDDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAF 436
|
.
gi 1196634871 891 I 891
Cdd:cd07128 437 A 437
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
640-921 |
2.15e-07 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, 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: 143440 [Multi-domain] Cd Length: 436 Bit Score: 54.80 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 640 VIIKPAPQVVHCAKLVVKAFRAGLEAQGLDPDLVQLVFTDEGDAGRALVSHADVDAVILTGAsdtgklfrswkPELNIMA 719
Cdd:cd07122 126 IIFSPHPRAKKCSIEAAKIMREAAVAAGAPEGLIQWIEEPSIELTQELMKHPDVDLILATGG-----------PGMVKAA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 720 ETSGKNAL---------IITPSADPDLAIQDLYLS-AFGHsGQKCSASSLVIFV--------------GA----AGESQR 771
Cdd:cd07122 195 YSSGKPAIgvgpgnvpaYIDETADIKRAVKDIILSkTFDN-GTICASEQSVIVDdeiydevraelkrrGAyflnEEEKEK 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 772 LRSQLVDAVKTL---IPG-PGYEItttmnglAEAPGEKLLRGlTQLepgetwLVKPEklnedgtlwspgirDNVRPGSWF 847
Cdd:cd07122 274 LEKALFDDGGTLnpdIVGkSAQKI-------AELAGIEVPED-TKV------LVAEE--------------TGVGPEEPL 325
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1196634871 848 hVNECFGPVLGIMHAETLEQAIE----WQNSTGYGLTGGIHSLDDDEIQYWIDNVEVGNAYVNrgitgaivQRQSFGG 921
Cdd:cd07122 326 -SREKLSPVLAFYRAEDFEEALEkareLLEYGGAGHTAVIHSNDEEVIEEFALRMPVSRILVN--------TPSSLGG 394
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
609-928 |
1.72e-06 |
|
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: 52.03 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 609 PYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKP---APqvvhcaklVVKAFRAGLEAQGLDPDLVQLVftdEG--DA 683
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPselAP--------ATSALLAKLIPEYLDTKAIKVI---EGgvPE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 684 GRALVSHaDVDAVILTGASDTGKLfrswkpelnIMA-----------ETSGKNALIITPSADPDLAIQDLYLSAFG-HSG 751
Cdd:cd07137 170 TTALLEQ-KWDKIFFTGSPRVGRI---------IMAaaakhltpvtlELGGKCPVIVDSTVDLKVAVRRIAGGKWGcNNG 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 752 QKCSASSLVIFvgaageSQRLRSQLVDAVKTLIP---GPGYEITTTMNGLAEAPGEKLLRGLTQLEPGETWLVKPEKLNE 828
Cdd:cd07137 240 QACIAPDYVLV------EESFAPTLIDALKNTLEkffGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERDE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 829 DGTLWSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVGNAYVNRG 908
Cdd:cd07137 314 KNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDT 393
|
330 340
....*....|....*....|
gi 1196634871 909 ITGAIVQRQSFGGWKKSVMG 928
Cdd:cd07137 394 VVQYAIDTLPFGGVGESGFG 413
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
618-928 |
5.44e-06 |
|
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: 50.18 E-value: 5.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 618 PWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKAFragleAQGLDPDLVQlVFTDEGDAGRAlVSHADVDAVI 697
Cdd:cd07133 110 PWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELL-----AEYFDEDEVA-VVTGGADVAAA-FSSLPFDHLL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 698 LTGASDTGKLfrswkpelnIMA-----------ETSGKNALIITPSADPDLAIQDLYLSAFGHSGQKCSA--------SS 758
Cdd:cd07133 183 FTGSTAVGRH---------VMRaaaenltpvtlELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVApdyvlvpeDK 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 759 LVIFVGAAgesqrlRSQLVDAVKTLIPGPGYeiTTTMN--------GL---AEAPGEKLLrgltQLEPGETWLVKPEKLn 827
Cdd:cd07133 254 LEEFVAAA------KAAVAKMYPTLADNPDY--TSIINerhyarlqGLledARAKGARVI----ELNPAGEDFAATRKL- 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 828 edgtlwSPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVGNAYVNR 907
Cdd:cd07133 321 ------PPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTIND 394
|
330 340
....*....|....*....|.
gi 1196634871 908 GITGAIVQRQSFGGWKKSVMG 928
Cdd:cd07133 395 TLLHVAQDDLPFGGVGASGMG 415
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
609-928 |
6.07e-06 |
|
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: 50.20 E-value: 6.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 609 PYRVTVVTPPWNFPV---------AIP---TggiaaalaagsaVIIKPAPQVVHCAKLVVKAFRagleaQGLDPDLVQLV 676
Cdd:cd07136 100 PYGVVLIIAPWNYPFqlalapligAIAagnT------------AVLKPSELTPNTSKVIAKIIE-----ETFDEEYVAVV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 677 ftdEGDAG--RALVsHADVDAVILTGASDTGKLfrswkpelnIMA-----------ETSGKNALIITPSADPDLAIQDLY 743
Cdd:cd07136 163 ---EGGVEenQELL-DQKFDYIFFTGSVRVGKI---------VMEaaakhltpvtlELGGKSPCIVDEDANLKLAAKRIV 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 744 LSAFGHSGQKCSASSLvIFVgaageSQRLRSQLVDAVKTLIpgpgyeitTTMNGlaEAP----------GEKLLRGLTQl 813
Cdd:cd07136 230 WGKFLNAGQTCVAPDY-VLV-----HESVKEKFIKELKEEI--------KKFYG--EDPlespdygriiNEKHFDRLAG- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 814 epgetwLVKPEKL-----NEDGTLW-SPGIRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLD 887
Cdd:cd07136 293 ------LLDNGKIvfggnTDRETLYiEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSED 366
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1196634871 888 DDEIQYWIDNVEVGNAYVNRGITGAIVQRQSFGGWKKSVMG 928
Cdd:cd07136 367 KKVEKKVLENLSFGGGCINDTIMHLANPYLPFGGVGNSGMG 407
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
609-928 |
5.23e-03 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 40.80 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 609 PYRVTVVTPPWNFPVAIPTGGIAAALAAGSAVIIKPAPQVVHCAKLVVKafragLEAQGLDPDLVQLVftdEGDAGR--A 686
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAK-----LLEQYLDSSAVRVV---EGAVTEttA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 687 LVSHaDVDAVILTGASDTGKLFR--SWKPELNIMAETSGKNALIITPSADPDLAIQDLYLSAFG-HSGQKCSASSLVIfv 763
Cdd:PLN02174 184 LLEQ-KWDKIFYTGSSKIGRVIMaaAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYIL-- 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 764 gaagESQRLRSQLVDAVKTLI-------PGPGYEITTTMNglaEAPGEKLLRGLTQLEPGETWLVKPEKLNEDGTLwSPG 836
Cdd:PLN02174 261 ----TTKEYAPKVIDAMKKELetfygknPMESKDMSRIVN---STHFDRLSKLLDEKEVSDKIVYGGEKDRENLKI-APT 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196634871 837 IRDNVRPGSWFHVNECFGPVLGIMHAETLEQAIEWQNSTGYGLTGGIHSLDDDEIQYWIDNVEVGNAYVNRGITGAIVQR 916
Cdd:PLN02174 333 ILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHT 412
|
330
....*....|..
gi 1196634871 917 QSFGGWKKSVMG 928
Cdd:PLN02174 413 LPFGGVGESGMG 424
|
|
| |
