|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
476-985 |
0e+00 |
|
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: 803.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 476 FSNEPVIDFTREEQRQAFREHIGQVRSRFGRKYPLFIGGQELETEDLLPSMNPSDPSEIVGWVCQAGTDEVAQAIGAARK 555
Cdd:cd07124 1 FRNEPFTDFADEENRAAFRAALARVREELGREYPLVIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 556 SFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADVTEAIDFLEYYAREMIRL-GSPRSMgkVAGE 634
Cdd:cd07124 81 AFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLrGFPVEM--VPGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 635 TNQYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGD 714
Cdd:cd07124 159 DNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 715 YLVDHPHVSLIAFTGSMEVGLRIIERAAKVQPGQEMVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSAC 794
Cdd:cd07124 239 YLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSAC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 795 SRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQKRIMNYIEVGRQEGRLLYQGHVPEV---GFFVPLT 871
Cdd:cd07124 319 SRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEVLELaaeGYFVQPT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 872 IIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNRNCTGALVGR 951
Cdd:cd07124 399 IFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGR 478
|
490 500 510
....*....|....*....|....*....|....
gi 221564986 952 QPFGGFRLSGAGTKAGGPDYLLHFMDPRVVTENT 985
Cdd:cd07124 479 QPFGGFKMSGTGSKAGGPDYLLQFMQPKTVTENF 512
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
472-983 |
0e+00 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 712.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 472 KVIPFSNEPVIDFTREEQRQAFREHIGQVRSRFGRKYPLFIGGQELETEDLLPSMNPSDPSEIVGWVCQAGTDEVAQAIG 551
Cdd:PRK03137 1 MVVPYKHEPFTDFSVEENVEAFEEALKKVEKELGQDYPLIIGGERITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 552 AARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADVTEAIDFLEYYAREMIRLGSPRSMGKV 631
Cdd:PRK03137 81 AALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLKLADGKPVESR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 632 AGETNQYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGI 711
Cdd:PRK03137 161 PGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 712 MGDYLVDHPHVSLIAFTGSMEVGLRIIERAAKVQPGQEMVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKC 791
Cdd:PRK03137 241 VGDYLVDHPKTRFITFTGSREVGLRIYERAAKVQPGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 792 SACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLiGAVAEENAQKRIMNYIEVGRQEGRLLYQGHV-PEVGFFVPL 870
Cdd:PRK03137 321 SACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNAYM-GPVINQASFDKIMSYIEIGKEEGRLVLGGEGdDSKGYFIQP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 871 TIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNRNCTGALVG 950
Cdd:PRK03137 400 TIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVG 479
|
490 500 510
....*....|....*....|....*....|...
gi 221564986 951 RQPFGGFRLSGAGTKAGGPDYLLHFMDPRVVTE 983
Cdd:PRK03137 480 YHPFGGFNMSGTDSKAGGPDYLLLFLQAKTVSE 512
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
476-984 |
0e+00 |
|
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: 636.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 476 FSNEPVIDFTREEQRQAFREHIGQVRSRFGRKYPLFIGGQELETEDLLPSMNPSDPSEIVGWVCQAGTDEVAQAIGAARK 555
Cdd:TIGR01237 1 YKHEPFTDFADEENRQAFFKALATVKEQLGKTYPLVINGERVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 556 SFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADVTEAIDFLEYYAREMIRLGSPRSMGKVAGET 635
Cdd:TIGR01237 81 AFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNSREGET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 636 NQYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDY 715
Cdd:TIGR01237 161 NQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 716 LVDHPHVSLIAFTGSMEVGLRIIERAAKVQPGQEMVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACS 795
Cdd:TIGR01237 241 LVDHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 796 RVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQKRIMNYIEVGRQEGRLLYQGH-VPEVGFFVPLTIIG 874
Cdd:TIGR01237 321 RAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEGRLVSGGCgDDSKGYFIGPTIFA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 875 DIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNRNCTGALVGRQPF 954
Cdd:TIGR01237 401 DVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPF 480
|
490 500 510
....*....|....*....|....*....|
gi 221564986 955 GGFRLSGAGTKAGGPDYLLHFMDPRVVTEN 984
Cdd:TIGR01237 481 GGFKMSGTDSKAGGPDYLALFMQAKTVTEM 510
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
103-985 |
1.06e-173 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 534.39 E-value: 1.06e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 103 RKAVSTAIRKMAQQFIVGENTTEAISNIERLRHQGFAAVVDVLGEATLSEKEADAYVDQYLDLIGSIeramgrwkplgaG 182
Cdd:PRK11904 166 RKAMRQAMKIMGKQFVLGRTIEEALKRARSARNKGYRYSFDMLGEAALTAADAERYFKAYARAIEAI------------G 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 183 RTSGSMDWGHAPRInvSVKATALSclasPMdYEGS-----VAAILRRLRLICRRVREVNGFLCLDMETYRYKEIILEVYR 257
Cdd:PRK11904 234 RAAGGADLPARPGI--SIKLSALH----PR-YEAAqrervLAELVPRVLELARLAKEANIGLTIDAEEADRLELSLDLFE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 258 RLKLEN--PDYHHLGLVLQSYLRDTDHDLDNLVTWARENCLGISIRLVKGAYWDYEMIRSRQSGLPE-PVWTMKAETDAA 334
Cdd:PRK11904 307 ALFRDPslKGWGGFGLAVQAYQKRALPVLDWLADLARRQGRRIPVRLVKGAYWDSEIKRAQELGLPGyPVFTRKAATDVS 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 335 FERQARRIMENSDVCHFACASHNIRSISAVIELArelavSDDRYEFQVLYGMAEPVRKAILNRTG-RLRLYCPYGP---M 410
Cdd:PRK11904 387 YLACARKLLSARGAIYPQFATHNAHTVAAILEMA-----GHRGFEFQRLHGMGEALYDALLDAPGiPCRIYAPVGShkdL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 411 VPgmgYLVRRLLENTSNVSFLRQtFVDA-AGAEKLLEDPLHVVERQRLAVQPRlregakssgkvIPF---------SNEP 480
Cdd:PRK11904 462 LP---YLVRRLLENGANSSFVHR-LVDPdVPIEELVADPVEKLRSFETLPNPK-----------IPLprdifgperKNSK 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 481 VIDFTREEQRQAFREHIGQVRSRFGRKYPLFIGGQELEtedllPSMNPSDPSEIVGWVCQAGTDEVAQAIGAARKSFETW 560
Cdd:PRK11904 527 GLNLNDRSELEPLAAAIAAFLEKQWQAGPIINGEGEAR-----PVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAW 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 561 RDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADVTEAIDFLEYYAREMIRL-GSPRSMGKVAGETNQYF 639
Cdd:PRK11904 602 SRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLfGAPEKLPGPTGESNELR 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 640 YEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDH 719
Cdd:PRK11904 682 LHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTAD 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 720 PHVSLIAFTGSMEVGlRIIER--AAKVQPgqemVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACsRV 797
Cdd:PRK11904 762 PRIAGVAFTGSTETA-RIINRtlAARDGP----IVPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSAL-RV 835
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 798 IVL-DGIYDKFVQRLTALAEAVPVGpveDPANL---IGAVAEENAQKRIMNYIEVGRQEGRLLYQGHVP---EVGFFVPL 870
Cdd:PRK11904 836 LFVqEDIADRVIEMLKGAMAELKVG---DPRLLstdVGPVIDAEAKANLDAHIERMKREARLLAQLPLPagtENGHFVAP 912
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 871 TI--IGDIrpehRLAQEEIFGPLLAVMR--ARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNRNCTG 946
Cdd:PRK11904 913 TAfeIDSI----SQLEREVFGPILHVIRykASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIG 988
|
890 900 910
....*....|....*....|....*....|....*....
gi 221564986 947 ALVGRQPFGGFRLSGAGTKAGGPDYLLHFMDPRVVTENT 985
Cdd:PRK11904 989 AVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTVTVNT 1027
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
506-985 |
2.15e-167 |
|
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: 498.88 E-value: 2.15e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 506 RKYPLFIGGQELE--TEDLLPSMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRI 583
Cdd:COG1012 4 PEYPLFIGGEWVAaaSGETFDVINPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 584 YELSALQVLEIGKQWDQAYADVTEAIDFLEYYAREMIRLGSPRSMGKVAGETNQYFYEPKGVAAVIAPWNFPLAISMGMV 663
Cdd:COG1012 83 EELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 664 SAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAk 743
Cdd:COG1012 163 APALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 744 vqpgqEMVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPV 823
Cdd:COG1012 242 -----ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 824 EDPANLIGAVAEENAQKRIMNYIEVGRQEG-RLLYQGHVPEV--GFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDF 900
Cdd:COG1012 317 LDPGTDMGPLISEAQLERVLAYIEDAVAEGaELLTGGRRPDGegGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 901 NEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNRNCTGAlVGRQPFGGFRLSGAGTKaGGPDYLLHFMDPRV 980
Cdd:COG1012 397 EEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGA-VPQAPFGGVKQSGIGRE-GGREGLEEYTETKT 474
|
....*
gi 221564986 981 VTENT 985
Cdd:COG1012 475 VTIRL 479
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
490-984 |
1.76e-159 |
|
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: 479.38 E-value: 1.76e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 490 RQAFREHIGQVRSRFGRKYPLFIGGQELETEDLLPSMNPSDPSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRA 569
Cdd:cd07083 1 RRAMREALRRVKEEFGRAYPLVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 570 EFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADVTEAIDFLEYYAREMIRL-GSPRSMGKVAGETNQYFYEPKGVAAV 648
Cdd:cd07083 81 RLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLrYPAVEVVPYPGEDNESFYVGLGAGVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 649 IAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFT 728
Cdd:cd07083 161 ISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 729 GSMEVGLRIIERAAKVQPGQEMVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFV 808
Cdd:cd07083 241 GSLETGKKIYEAAARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 809 QRLTALAEAVPVGPVEDPANLIGAVAEENAQKRIMNYIEVGRQEGRLLYQGHVPE-VGFFVPLTIIGDIRPEHRLAQEEI 887
Cdd:cd07083 321 ERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLEgEGYFVAPTVVEEVPPKARIAQEEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 888 FGPLLAVMR--ARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNRNCTGALVGRQPFGGFRLSGAGTK 965
Cdd:cd07083 401 FGPVLSVIRykDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAK 480
|
490
....*....|....*....
gi 221564986 966 AGGPDYLLHFMDPRVVTEN 984
Cdd:cd07083 481 TGGPHYLRRFLEMKAVAER 499
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
103-976 |
1.93e-156 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 494.00 E-value: 1.93e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 103 RKAVSTAIRKMAQQFIVGENTTEAISNIERLRHQGFAAVVDVLGEATLSEKEADAYVDQYLDLIGSIeramgrwkplgaG 182
Cdd:PRK11905 165 RKAVDMAMRMMGEQFVTGETIEEALKRARELEARGYRYSYDMLGEAARTAADAERYYRDYERAIHAI------------G 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 183 RTSGSMDWGHAPRInvSVKATALSclasPMdYEGS------------VAAilrrlrlicrrvrevngfLCL-----DM-- 243
Cdd:PRK11905 233 KAATGRGVYDGPGI--SVKLSALH----PR-YERAqrervmaellprLKA------------------LALlakayDIgl 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 244 -----ETYRYkEIILEVYRRLkLENPD---YHHLGLVLQSYLRDTDHDLDNLVTWARENCLGISIRLVKGAYWDYEMIRS 315
Cdd:PRK11905 288 nidaeEADRL-ELSLDLLEAL-CSDPDlagWNGIGFVVQAYQKRCPFVIDYLIDLARRSGRRLMVRLVKGAYWDAEIKRA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 316 RQSGLPE-PVWTMKAETDAAFERQARRIMENSDVCHFACASHNIRSISAVIELARElavsDDRYEFQVLYGMAEP----- 389
Cdd:PRK11905 366 QVDGLEGfPVFTRKVHTDVSYIACARKLLAARDVIYPQFATHNAQTLAAIYELAGG----KGDFEFQCLHGMGEPlydqv 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 390 VRKAILNRtgRLRLYCPYGPMVPGMGYLVRRLLENTSNVSFLRQTFVDAAGAEKLLEDPLHVVERQRLAVQPRLREGAK- 468
Cdd:PRK11905 442 VGKEKLGR--PCRIYAPVGTHETLLAYLVRRLLENGANSSFVNRIVDENVPVEELIADPVEKVAAMGVAPHPQIPLPRDl 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 469 -------SSGkvIPFSNEPVIDfTREEQRQAFREHIGQVRsrfgrkyPLFIGGQEleTEDLLPSMNPSDPSEIVGWVCQA 541
Cdd:PRK11905 520 ygperrnSKG--LDLSDEATLA-ALDEALNAFAAKTWHAA-------PLLAGGDV--DGGTRPVLNPADHDDVVGTVTEA 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 542 GTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADVTEAIDFLEYYAREMIR 621
Cdd:PRK11905 588 SAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARR 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 622 LGSPRSmgkvagetnqyfYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGV 701
Cdd:PRK11905 668 LLNGPG------------HKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDA 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 702 FNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRI----IERAAKVQPgqemvkkVICEMGGKNAIIIDDDADLDEAVP 777
Cdd:PRK11905 736 LQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIqrtlAKRSGPPVP-------LIAETGGQNAMIVDSSALPEQVVA 808
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 778 HVFNSAFGFQGQKCSACsRVIVL-DGIYDKFVQRLT-ALAEAVpVGpveDPANL---IGAVAEENAQKRIMNYIEVGRQE 852
Cdd:PRK11905 809 DVIASAFDSAGQRCSAL-RVLCLqEDVADRVLTMLKgAMDELR-IG---DPWRLstdVGPVIDAEAQANIEAHIEAMRAA 883
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 853 GRLLYQGHVPEV---GFFVPLTII--GDIrpehRLAQEEIFGPLLAVMR-ARDFNEALVWA-NSTRYALTGGLFSRSPEH 925
Cdd:PRK11905 884 GRLVHQLPLPAEtekGTFVAPTLIeiDSI----SDLEREVFGPVLHVVRfKADELDRVIDDiNATGYGLTFGLHSRIDET 959
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|.
gi 221564986 926 IAIATKRFRVGNLYLNRNCTGALVGRQPFGGFRLSGAGTKAGGPDYLLHFM 976
Cdd:PRK11905 960 IAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLV 1010
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
523-981 |
1.33e-153 |
|
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: 462.39 E-value: 1.33e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 523 LPSMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAY 602
Cdd:pfam00171 9 IEVINPAT-GEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 603 ADVTEAIDFLEYYAREMIRLgSPRSMGKVAGETNQYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTS 682
Cdd:pfam00171 88 GEVDRAIDVLRYYAGLARRL-DGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 683 IIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAKvqpgqeMVKKVICEMGGKN 762
Cdd:pfam00171 167 LTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ------NLKRVTLELGGKN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 763 AIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQKRI 842
Cdd:pfam00171 241 PLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 843 MNYIEVGRQEG-RLLYQGH-VPEVGFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFS 920
Cdd:pfam00171 321 LKYVEDAKEEGaKLLTGGEaGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFT 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221564986 921 RSPEHIAIATKRFRVGNLYLNRNCTGALVGRqPFGGFRLSGAGtKAGGPDYLLHFMDPRVV 981
Cdd:pfam00171 401 SDLERALRVARRLEAGMVWINDYTTGDADGL-PFGGFKQSGFG-REGGPYGLEEYTEVKTV 459
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
490-989 |
2.29e-143 |
|
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: 438.17 E-value: 2.29e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 490 RQAFREHIGQVRSRFGRKYPlFIGGQELETEDLLPSMNPSDPSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRA 569
Cdd:cd07125 16 LEALADALKAFDEKEWEAIP-IINGEETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 570 EFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADVTEAIDFLEYYAREMIRLGSPRSMGKVAGETNQYFYEPKGVAAVI 649
Cdd:cd07125 95 EILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPELPGPTGELNGLELHGRGVFVCI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 650 APWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTG 729
Cdd:cd07125 175 SPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 730 SMEVGLRIIE-RAAKVQPgqemVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFV 808
Cdd:cd07125 255 STETAKLINRaLAERDGP----ILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 809 QRLTALAEAVPVGPVEDPANLIGAVAEENAQKRIMNYIEVGRQEGRLLYQGHVPEV-GFFVPLTII-GDIRPEHrlaQEE 886
Cdd:cd07125 331 EMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDGnGYFVAPGIIeIVGIFDL---TTE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 887 IFGPLLAVMRAR--DFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNRNCTGALVGRQPFGGFRLSGAGT 964
Cdd:cd07125 408 VFGPILHVIRFKaeDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGP 487
|
490 500
....*....|....*....|....*
gi 221564986 965 KAGGPDYLLHFMDPRVVTENTMRRG 989
Cdd:cd07125 488 KAGGPNYLLRFGNEKTVSLNTTAAG 512
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
3-995 |
1.40e-141 |
|
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: 448.34 E-value: 1.40e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 3 DSELNRRIVSCGREMFAGIYGETPSLFDKgrwlgkLMAWSMSDEEFKTRLFRFVDVFPTLSTDRMVADHLEEYFDGAQPP 82
Cdd:COG0506 6 DEALRARAVALARRLVEAIRAAPEGGVEA------LLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLAKSPSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 83 VLALLRQA--AGVFGPFGNFIQRKAVSTAIRKMAQQFIVGENTTEAISNIERLRHQGFAAVVDVLGEATLSEKEADAYVD 160
Cdd:COG0506 80 LVNASTWGlmLTLVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAARKLRAKGYRVSLDLLGEAVLTEAEAERYLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 161 QYLDLIGSIERAmgrwkplgagrtsgsmdwgHAPRINVSVKATALSCLASPMDYEGSVAAILRRLRLICRRVREVNGFLC 240
Cdd:COG0506 160 AYLEALEAIGAA-------------------GVDRPGVSVKLSALGPRYSPAQRERVVEELLERLRPLARAAREAGIFVT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 241 LDMETYRYKEIILEVYRRL--KLENPDYHHLGLVLQSYLRDTDHDLDNLVTWARENCLGISIRLVKGAYWDYEMIRSRQS 318
Cdd:COG0506 221 IDMEEYDRLDLTLDVFERLlaDPELAGWPGVGIVLQAYLKRAEADLDRLAALARRGGRRIRVRLVKGAYWDPEIVRAQVH 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 319 GLPEPVWTMKAETDAAFERQARRIMENSDVCHFACASHNIRSISAVIELARELAVSDDRYEFQVLYGMAEPVRKAILN-R 397
Cdd:COG0506 301 GWPYPVFTRKADTDANYLRCARKLLEAGDAIYPQFATHNARTIAAALALAGERGRPPDRFEFQMLYGMGEDLQRALAAvD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 398 TGRLRLYCPYGPMVPGMGYLVRRLLENTSNVSFLRQTFVDAAGAEKLLEDPlhVVERQRLAVQPRLREGAKSSGKVIPFS 477
Cdd:COG0506 381 GGRLLLYCPVVAPVGGDAALAYLLRRLLENNSFLNFFVADFDDDEDLLEFP--REPPRFLAALAAPTPPPPPPLRRQRRR 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 478 NEPVIDFTREEQRQAFREHIGQVRSRFGRKYPLFIGGQELETEDLLPSMNPSDPS--EIVGWVCQAGTDEVAQAIGAARK 555
Cdd:COG0506 459 RRRARGGALAAALAAAAAAAALAAAAAAAAALAAAAAGAAAAAAAAAVAVVPAAAaaVVAAAAAAAAAAAAAAAAAAAAA 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 556 SFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADVTEAIDFLEYYAREMIRLGSPRSMGKVAGET 635
Cdd:COG0506 539 AAAAAAAAAAAAAAAAAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAARAAAPPPPPPGGLVA 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 636 NQYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDY 715
Cdd:COG0506 619 LLPLGPLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAGGGVLVLGAGGGAGGAAA 698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 716 LVDHPHVSLIAFTGSMEVGLRIIERAAKVQPGQEmvkkVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACS 795
Cdd:COG0506 699 LTLAAAAAAATAATAAAAAAAAALAAAAAAAAAA----AAAAAGGAAAAAAAAAAAAAVAAVAASAAASASASASLLSLL 774
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 796 RVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQKRIMNYIEVGRQEGRLLYQGHVPEV-GFFVPLTIIG 874
Cdd:COG0506 775 ALLLLDADLVILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLPGGGPLVpGLLTAPLLVA 854
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 875 DIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNRNCTGALVGRQPF 954
Cdd:COG0506 855 LILGLIVLVLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGGGGGGGGGGGGG 934
|
970 980 990 1000
....*....|....*....|....*....|....*....|.
gi 221564986 955 GGFRLSGAGTKAGGPDYLLHFMDPRVVTENTMRRGFAPAGA 995
Cdd:COG0506 935 GGGGGGGGGGGGGGGGGAGTLALAAAAAAATALAAAAAAAA 975
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
103-985 |
5.61e-137 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 440.91 E-value: 5.61e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 103 RKAVSTAIRKMAQQFIVGENTTEAISNIERLRHQGFAAVVDVLGEATLSEKEADAYVDQYLDLIGSIERAmgrwkplgAG 182
Cdd:COG4230 166 RRAMRAAMMMMMGLFGVGFVTEEAAEAARKAARKREYYYYDMLGEAAAAAADAAAYAYAYAAAAAAAIAA--------AG 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 183 RTSGSMDWGHAPRInvSVKATALSCLASPMDYEGSVAAILRRLRLICRRVREVNGFLCLDMETYRYKEIILEVYRRLKLE 262
Cdd:COG4230 238 GGSGGPGPSISSSL--SVLLSARHPRYRRRREERLLLLLLPLLALLALAAININIDEEEDAEELLLLLLLLDLLAALLLD 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 263 NP--DYHHLGLVLQSYLRDTDHDLDnlvtWARENCLGISIRLVKGAYWDYE--MIRSRQSGLPEPVWTMKAETDAAFERQ 338
Cdd:COG4230 316 GGlgGGGGVGQAVQAYAKALLLVLD----LLARRRRRRRRRLVVRLVKGAEwdREIQRAQVLGYVVYPVTTRKVLYDAAA 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 339 ARRIMENSDVCHFACASHNirSISAVIELARELAVSDDRYEFQVLYGMAEP----VRKAILNRtgRLRLYCPYG------ 408
Cdd:COG4230 392 LALALLLLAAQPAFAPQFA--THAAATAAAAAAAGGGGEFEFQCLHGMGEYlydqVGRGKLGR--PCRIYAPVGshedll 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 409 PmvpgmgYLVRRLLENTSNVSFLRQtFVDAA-GAEKLLEDPLHVVERQRLAVQPRLR--------EGAKSSGkvipfsne 479
Cdd:COG4230 468 A------YLVRRLLENGANSSFVNR-IADEDvPVEELIADPVEKARALGGAPHPRIPlprdlygpERRNSAG-------- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 480 pvIDFTREEQRQAFREHIGQVRSRFGRKYPLfIGGqELETEDLLPSMNPSDPSEIVGWVCQAGTDEVAQAIGAARKSFET 559
Cdd:COG4230 533 --LDLSDEAVLAALSAALAAAAEKQWQAAPL-IAG-EAASGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPA 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 560 WRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADVTEAIDFLEYYAREMIRLGSprsmgkvagetNQYF 639
Cdd:COG4230 609 WSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFA-----------APTV 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 640 YEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDH 719
Cdd:COG4230 678 LRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVAD 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 720 PHVSLIAFTGSMEVGlRIIERAAKVQPGQEMVkkVICEMGGKNaiiidddadldeaVPHVFNSAFGFQGQKCSACsRVIV 799
Cdd:COG4230 758 PRIAGVAFTGSTETA-RLINRTLAARDGPIVP--LIAETGGQNamivdssalpeqvVDDVLASAFDSAGQRCSAL-RVLC 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 800 L-DGIYDKFVQRLT-ALAEAVpVGpveDPANL---IGAVAEENAQKRIMNYIEVGRQEGRLLYQGHVPEV---GFFVPLT 871
Cdd:COG4230 834 VqEDIADRVLEMLKgAMAELR-VG---DPADLstdVGPVIDAEARANLEAHIERMRAEGRLVHQLPLPEEcanGTFVAPT 909
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 872 I--IGDIRpehRLaQEEIFGPLLAVMR--ARDFnEALVWA-NSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNRNCTG 946
Cdd:COG4230 910 LieIDSIS---DL-EREVFGPVLHVVRykADEL-DKVIDAiNATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIG 984
|
890 900 910
....*....|....*....|....*....|....*....
gi 221564986 947 ALVGRQPFGGFRLSGAGTKAGGPDYLLHFMDPRVVTENT 985
Cdd:COG4230 985 AVVGVQPFGGEGLSGTGPKAGGPHYLLRFATERTVTVNT 1023
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
548-983 |
3.91e-132 |
|
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: 405.82 E-value: 3.91e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 548 QAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADVTEAIDFLEYYAREMIRLGSPRS 627
Cdd:cd07078 2 AAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 628 MGKVAGETNQYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPG 707
Cdd:cd07078 82 PSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 708 RSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAkvqpgqEMVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQ 787
Cdd:cd07078 162 DGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAA------ENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 788 GQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQKRIMNYIEVGRQEG-RLLYQGHVPE--V 864
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGaKLLCGGKRLEggK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 865 GFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNrNC 944
Cdd:cd07078 316 GYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIN-DY 394
|
410 420 430
....*....|....*....|....*....|....*....
gi 221564986 945 TGALVGRQPFGGFRLSGAGtKAGGPDYLLHFMDPRVVTE 983
Cdd:cd07078 395 SVGAEPSAPFGGVKQSGIG-REGGPYGLEEYTEPKTVTI 432
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
103-996 |
1.80e-128 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 421.30 E-value: 1.80e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 103 RKAVSTAIRKMAQQFIVGENTTEAISNIERLRHQGFAAVVDVLGEATLSEKEADAYVDQYLDLIGSIERAMGrwkplGAG 182
Cdd:PRK11809 245 RKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTEADAQAYLASYEQAIHAIGKASN-----GRG 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 183 RTSGsmdwghaPRInvSVKATALSCLASPMDYEGSVAAILRRLRLICRRVREVNGFLCLDMETYRYKEIILEVYRRLKLE 262
Cdd:PRK11809 320 IYEG-------PGI--SIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 263 nPD---YHHLGLVLQSYLRDTDHDLDNLVTWARENCLGISIRLVKGAYWDYEMIRSRQSGLPE-PVWTMKAETDAAFERQ 338
Cdd:PRK11809 391 -PElagWNGIGFVIQAYQKRCPFVIDYLIDLARRSRRRLMIRLVKGAYWDSEIKRAQVDGLEGyPVYTRKVYTDVSYLAC 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 339 ARRIMENSDVCHFACASHNIRSISAVIELARELAVSDdRYEFQVLYGMAEP-----VRKAI---LNRTgrLRLYCPYGPM 410
Cdd:PRK11809 470 ARKLLAVPNLIYPQFATHNAHTLAAIYHLAGQNYYPG-QYEFQCLHGMGEPlyeqvVGKVAdgkLNRP--CRIYAPVGTH 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 411 VPGMGYLVRRLLENTSNVSFLRQTFVDAAGAEKLLEDPLHVVERqrLAVQ--------PRL--------REGAKSSGkvi 474
Cdd:PRK11809 547 ETLLAYLVRRLLENGANTSFVNRIADTSLPLDELVADPVEAVEK--LAQQegqlglphPKIplprdlygKGRANSAG--- 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 475 pfsnepvIDFTREEQRQAFREHIGQVRSRFGRKYPLFigGQELETEDLLPSMNPSDPSEIVGWVCQAGTDEVAQAIGAAR 554
Cdd:PRK11809 622 -------LDLANEHRLASLSSALLASAHQKWQAAPML--EDPVAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAV 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 555 KSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADVTEAIDFLEYYAremirlgsprsmGKVAGE 634
Cdd:PRK11809 693 NAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYA------------GQVRDD 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 635 TNQYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGD 714
Cdd:PRK11809 761 FDNDTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGA 840
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 715 YLVDHPHVSLIAFTGSMEVGlRIIER--AAKVQPgQEMVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCS 792
Cdd:PRK11809 841 ALVADARVRGVMFTGSTEVA-RLLQRnlAGRLDP-QGRPIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCS 918
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 793 ACsRVIVL-DGIYDKFVQRLT-ALAEAVpvgpVEDPANL---IGAVAEENAQKRIMNYIEVGRQEGRLLYQGHVPEV--- 864
Cdd:PRK11809 919 AL-RVLCLqDDVADRTLKMLRgAMAECR----MGNPDRLstdIGPVIDAEAKANIERHIQAMRAKGRPVFQAARENSedw 993
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 865 --GFFVPLTII--GDIrpeHRLaQEEIFGPLLAVMRAR--DFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNL 938
Cdd:PRK11809 994 qsGTFVPPTLIelDSF---DEL-KREVFGPVLHVVRYNrnQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNL 1069
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*...
gi 221564986 939 YLNRNCTGALVGRQPFGGFRLSGAGTKAGGPDYLLHFMDPRvvTENTMRRGFAPAGAG 996
Cdd:PRK11809 1070 YVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLATR--PEDALAVTLARQDAE 1125
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
508-970 |
2.49e-122 |
|
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: 381.60 E-value: 2.49e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 508 YPLFIGGQELETEDLLPSMNPSDPSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELS 587
Cdd:cd07097 1 YRNYIDGEWVAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 588 ALQVLEIGKQWDQAYADVTEAIDFLEYYAREMIRLGS---PRSMGKVAGETNQyfyEPKGVAAVIAPWNFPLAISMGMVS 664
Cdd:cd07097 81 RLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGetlPSTRPGVEVETTR---EPLGVVGLITPWNFPIAIPAWKIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 665 AAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAKV 744
Cdd:cd07097 158 PALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 745 QpgqemvKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVE 824
Cdd:cd07097 238 G------ARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDAL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 825 DPANLIGAVAEENAQKRIMNYIEVGRQEG-RLLYQGHV---PEVGFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDF 900
Cdd:cd07097 312 DEGVDIGPVVSERQLEKDLRYIEIARSEGaKLVYGGERlkrPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDY 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 901 NEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNRNCTGALVgRQPFGGFRLSGAGTKAGGPD 970
Cdd:cd07097 392 DEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDY-HVPFGGRKGSSYGPREQGEA 460
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
126-433 |
8.87e-113 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 349.87 E-value: 8.87e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 126 AISNIERLRHQGFAAVVDVLGEATLSEKEADAYVDQYLDLIGSIERAMGRWKPlgagrtsgsmdwghAPRINVSVKATAL 205
Cdd:pfam01619 1 ALKTIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDALGKAAGPWPL--------------GPRPGISVKLSAL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 206 SCLASPMDYEGSVAAILRRLRLICRRVREVNGFLCLDMETYRYKEIILEVYRRL--KLENPDYHHLGLVLQSYLRDTDHD 283
Cdd:pfam01619 67 HPRYEPLERERVMAELLERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLlaEPELRGWNGVGITLQAYLKDALAV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 284 LDNLVTWARENCLGISIRLVKGAYWDYEMIRSRQSGLPEPVWTMKAETDAAFERQARRIMENSDVCHFACASHNIRSISA 363
Cdd:pfam01619 147 LDWLLELARRRGRPLGVRLVKGAYWDSEIKRAQQGGWPYPVFTRKEATDANYEACARFLLENHDRIYPQFATHNARSVAA 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 364 VIELARELAVSDDRYEFQVLYGMAEPVRKAILNRTGRLRLYCPYGPMVPGMGYLVRRLLENTSNVSFLRQ 433
Cdd:pfam01619 227 ALALAEELGIPPRRFEFQQLYGMGDNLSFALVAAGYRVRKYAPVGPHEELLAYLVRRLLENTANSSFVRR 296
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
511-984 |
2.29e-109 |
|
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: 347.80 E-value: 2.29e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 511 FIGGQELE--TEDLLPSMNPSDPSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSA 588
Cdd:cd07131 2 YIGGEWVDsaSGETFDSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 589 LQVLEIGKQWDQAYADVTEAIDFLEYYAREMIRLGSPRSMGKVAGETNQYFYEPKGVAAVIAPWNFPLAISMGMVSAAIV 668
Cdd:cd07131 82 LVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 669 TGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAKVQpgq 748
Cdd:cd07131 162 CGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPN--- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 749 emvKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPAN 828
Cdd:cd07131 239 ---KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEET 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 829 LIGAVAEENAQKRIMNYIEVGRQEGRLLYQG------HVPEVGFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNE 902
Cdd:cd07131 316 DMGPLINEAQLEKVLNYNEIGKEEGATLLLGgerltgGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 903 ALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNRNCTGALVgRQPFGGFRLSGAGTKAGGPDYLLHFMDPRVVT 982
Cdd:cd07131 396 AIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEV-HLPFGGVKKSGNGHREAGTTALDAFTEWKAVY 474
|
..
gi 221564986 983 EN 984
Cdd:cd07131 475 VD 476
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
478-984 |
1.37e-105 |
|
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: 339.18 E-value: 1.37e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 478 NEPVIDFTR-EEQRQAFREHIGQVRSRFgRKYPLFIGGQELETEDLLPSMNPSDPSEIVGWVCQAGTDEVAQAIGAARKS 556
Cdd:cd07123 3 NEPVLSYAPgSPERAKLQEALAELKSLT-VEIPLVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 557 FETWrDITP-EIRAEFLLKACTVV--RRRiYELSALQVLEIGKQWDQAYAD-VTEAIDFLE---YYAREMIRlGSPRSmg 629
Cdd:cd07123 82 RKEW-ARMPfEDRAAIFLKAADLLsgKYR-YELNAATMLGQGKNVWQAEIDaACELIDFLRfnvKYAEELYA-QQPLS-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 630 KVAGETNQYFYEP-KGVAAVIAPWNFPlAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGR 708
Cdd:cd07123 157 SPAGVWNRLEYRPlEGFVYAVSPFNFT-AIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 709 SGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAA------KVQPgqemvkKVICEMGGKNAIIIDDDADLDEAVPHVFNS 782
Cdd:cd07123 236 GPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGenldryRTYP------RIVGETGGKNFHLVHPSADVDSLVTATVRG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 783 AFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQKRIMNYIEVGRQ--EGRLLYQGH 860
Cdd:cd07123 310 AFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSdpEAEIIAGGK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 861 V-PEVGFFVPLTIIGDIRPEHRLAQEEIFGPLLA--VMRARDFNEAL-VWANSTRYALTGGLFSRSPEHIAIATKRFR-- 934
Cdd:cd07123 390 CdDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTvyVYPDSDFEETLeLVDTTSPYALTGAIFAQDRKAIREATDALRna 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 221564986 935 VGNLYLNRNCTGALVGRQPFGGFRLSGAGTKAGGPDYLLHFMDPRVVTEN 984
Cdd:cd07123 470 AGNFYINDKPTGAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPRTIKET 519
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
552-983 |
1.70e-102 |
|
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: 325.34 E-value: 1.70e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 552 AARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADVTEAIDFLEYYAREMIRLGSPRSMGKV 631
Cdd:cd06534 2 AARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 632 AGETNQYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGI 711
Cdd:cd06534 82 PGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 712 MGDYLVDHPHVSLIAFTGSMEVGLRIIERAAkvqpgqEMVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKC 791
Cdd:cd06534 162 VGAALLSHPRVDKISFTGSTAVGKAIMKAAA------ENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQIC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 792 SACSRVIVLDGIYDKFVQRLtalaeavpvgpvedpanligavaeenaqkrimnyievgrqegrllyqghvpevgffvpLT 871
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKL----------------------------------------------------------VT 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 872 IIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNRNCTGAlVGR 951
Cdd:cd06534 258 VLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGV-GPE 336
|
410 420 430
....*....|....*....|....*....|..
gi 221564986 952 QPFGGFRLSGAGtKAGGPDYLLHFMDPRVVTE 983
Cdd:cd06534 337 APFGGVKNSGIG-REGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
525-982 |
1.61e-98 |
|
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: 317.97 E-value: 1.61e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 525 SMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQ-WDQAYA 603
Cdd:cd07093 1 NFNPAT-GEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPiTLARTR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 604 DVTEAIDFLEYYArEMIRLGSPRSMGKVAGETNQYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSI 683
Cdd:cd07093 80 DIPRAAANFRFFA-DYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 684 IGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAKvqpgqeMVKKVICEMGGKNA 763
Cdd:cd07093 159 TAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAP------NLKPVSLELGGKNP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 764 IIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQKRIM 843
Cdd:cd07093 233 NIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 844 NYIEVGRQEG-RLLYQGHVPEV-----GFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGG 917
Cdd:cd07093 313 GYVELARAEGaTILTGGGRPELpdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAY 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221564986 918 LFSRSPEHIAIATKRFRVGNLYLNRNCTGALvgRQPFGGFRLSGAGTKagGPDYLLHF-MDPRVVT 982
Cdd:cd07093 393 VWTRDLGRAHRVARRLEAGTVWVNCWLVRDL--RTPFGGVKASGIGRE--GGDYSLEFyTELKNVC 454
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
527-981 |
7.83e-97 |
|
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: 313.80 E-value: 7.83e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 527 NPSDpSEIVGWVCQAGTDEVAQAIGAARKSFETW-RDITPEIRAEFLLKACTVVRRRIYELSALQVLEIG--------KQ 597
Cdd:cd07089 3 NPAT-EEVIGTAPDAGAADVDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGapvmtaraMQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 598 WDQAYADVTEAIDFLEYYAREMIRLGSP----RSMGKVAgetnqyfYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCV 673
Cdd:cd07089 82 VDGPIGHLRYFADLADSFPWEFDLPVPAlrggPGRRVVR-------REPVGVVAAITPWNFPFFLNLAKLAPALAAGNTV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 674 VFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAkvqpgqEMVKK 753
Cdd:cd07089 155 VLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAA------ATLKR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 754 VICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAV 833
Cdd:cd07089 229 VLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 834 AEENAQKRIMNYIEVGRQEG-RLLYQGHVP---EVGFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANS 909
Cdd:cd07089 309 ISAAQRDRVEGYIARGRDEGaRLVTGGGRPaglDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIAND 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221564986 910 TRYALTGGLFSRSPEH-IAIAtKRFRVGNLYLNrncTGALVGRQ-PFGGFRLSGAGtKAGGPDYLLHFMDPRVV 981
Cdd:cd07089 389 SDYGLSGGVWSADVDRaYRVA-RRIRTGSVGIN---GGGGYGPDaPFGGYKQSGLG-RENGIEGLEEFLETKSI 457
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
510-967 |
1.49e-96 |
|
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: 313.38 E-value: 1.49e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 510 LFIGGQ--ELETEDLLPSMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFET--WRDITPEIRAEFLLKACTVVRRRIYE 585
Cdd:cd07091 6 LFINNEfvDSVSGKTFPTINPAT-EEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 586 LSALQVLEIGKQWDQAY-ADVTEAIDFLEYYAremirlgsprsmG---KVAGET-----NQYFY---EPKGVAAVIAPWN 653
Cdd:cd07091 85 LAALESLDNGKPLEESAkGDVALSIKCLRYYA------------GwadKIQGKTipidgNFLAYtrrEPIGVCGQIIPWN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 654 FPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEV 733
Cdd:cd07091 153 FPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 734 GLRIIERAAKVQpgqemVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTA 813
Cdd:cd07091 233 GRTIMEAAAKSN-----LKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 814 LAEAVPVGPVEDPANLIGAVAEENAQKRIMNYIEVGRQEG-RLLYQG-HVPEVGFFVPLTIIGDIRPEHRLAQEEIFGPL 891
Cdd:cd07091 308 RAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYIESGKKEGaTLLTGGeRHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPV 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221564986 892 LAVMRARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLnrNCTGALVGRQPFGGFRLSGAGTKAG 967
Cdd:cd07091 388 VTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWV--NTYNVFDAAVPFGGFKQSGFGRELG 461
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
525-981 |
5.03e-96 |
|
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: 311.30 E-value: 5.03e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 525 SMNPSDPSEIvGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQW-DQAYA 603
Cdd:cd07115 1 TLNPATGELI-ARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIrAARRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 604 DVTEAIDFLEYYAremirlGSPRsmgKVAGET--------NQYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVF 675
Cdd:cd07115 80 DVPRAADTFRYYA------GWAD---KIEGEVipvrgpflNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 676 KPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAkvqpgqEMVKKVI 755
Cdd:cd07115 151 KPAELTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAA------GNLKRVS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 756 CEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAE 835
Cdd:cd07115 225 LELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 836 ENAQKRIMNYIEVGRQEG-RLLYQGHVP-EVGFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYA 913
Cdd:cd07115 305 QAQFDRVLDYVDVGREEGaRLLTGGKRPgARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYG 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221564986 914 LTGGLFSRSPEHIAIATKRFRVGNLYLnrNCTGALVGRQPFGGFRLSGAGtKAGGPDYLLHFMDPRVV 981
Cdd:cd07115 385 LAAGVWTRDLGRAHRVAAALKAGTVWI--NTYNRFDPGSPFGGYKQSGFG-REMGREALDEYTEVKSV 449
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
527-967 |
2.44e-93 |
|
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: 304.16 E-value: 2.44e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 527 NPSDpSEIVGWVCQAGTDEVAQAIGAARKSFET-WRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADV 605
Cdd:cd07109 3 DPST-GEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 606 TEAIDFLEYYARemirlgsprSMGKVAGET----NQYF----YEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKP 677
Cdd:cd07109 82 EAAARYFEYYGG---------AADKLHGETiplgPGYFvytvREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 678 SGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAkvqpgqEMVKKVICE 757
Cdd:cd07109 153 AEDAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAA------ENVVPVTLE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 758 MGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLiGAVAEEN 837
Cdd:cd07109 227 LGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPDL-GPLISAK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 838 AQKRIMNYIEVGRQEG-RLLYQGHV----PEVGFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRY 912
Cdd:cd07109 306 QLDRVEGFVARARARGaRIVAGGRIaegaPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDY 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 221564986 913 ALTGGLFSRSPEHIAIATKRFRVGNLYLnrNCTGALVGRQ-PFGGFRLSGAGTKAG 967
Cdd:cd07109 386 GLVAGVWTRDGDRALRVARRLRAGQVFV--NNYGAGGGIElPFGGVKKSGHGREKG 439
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
511-967 |
4.45e-93 |
|
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: 304.10 E-value: 4.45e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 511 FIGGQELE-TEDLLPSMNPSDPSEIVGwVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSAL 589
Cdd:cd07086 2 VIGGEWVGsGGETFTSRNPANGEPIAR-VFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 590 QVLEIGKQWDQAYADVTEAIDFLEYYAREMIRLG-----SPRSmGKVAGEtnqyFYEPKGVAAVIAPWNFPLAISMGMVS 664
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYgltipSERP-GHRLME----QWNPLGVVGVITAFNFPVAVPGWNAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 665 AAIVTGNCVVFKPSGLTSIIGWQLVDIFREV----GLPDGVFNFVPGRSGImGDYLVDHPHVSLIAFTGSMEVGLRIIER 740
Cdd:cd07086 156 IALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDG-GELLVHDPRVPLVSFTGSTEVGRRVGET 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 741 AAKvqpgqeMVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPV 820
Cdd:cd07086 235 VAR------RFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 821 GPVEDPANLIGAVAEENAQKRIMNYIEVGRQEG-RLLYQGHVPEV---GFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMR 896
Cdd:cd07086 309 GDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGgTVLTGGKRIDGgepGNYVEPTIVTGVTDDARIVQEETFAPILYVIK 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221564986 897 ARDFNEALVWANSTRYALTGGLFSRSPEHIAiatkRFR------VGNLYLNRNCTGALVGrQPFGGFRLSGAGTKAG 967
Cdd:cd07086 389 FDSLEEAIAINNDVPQGLSSSIFTEDLREAF----RWLgpkgsdCGIVNVNIPTSGAEIG-GAFGGEKETGGGRESG 460
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
511-981 |
1.41e-92 |
|
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: 302.65 E-value: 1.41e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 511 FIGGQ--ELETEDLLPSMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSA 588
Cdd:cd07088 1 YINGEfvPSSSGETIDVLNPAT-GEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 589 LQVLEIGKQWDQAYADVTEAIDFLEYYArEMIRlgspRSMGKV-----AGETNQYFYEPKGVAAVIAPWNFPLAISMGMV 663
Cdd:cd07088 80 LIVEEQGKTLSLARVEVEFTADYIDYMA-EWAR----RIEGEIipsdrPNENIFIFKVPIGVVAGILPWNFPFFLIARKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 664 SAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAk 743
Cdd:cd07088 155 APALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAA- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 744 vqpgqEMVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPV 823
Cdd:cd07088 234 -----ENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 824 EDPANLIGAVAEENAQKRIMNYIEVGRQEG-RLLYQGHVPEV--GFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDF 900
Cdd:cd07088 309 FDAATDMGPLVNEAALDKVEEMVERAVEAGaTLLTGGKRPEGekGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 901 NEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNRNCTGALvgrQPF-GGFRLSGAGtKAGGPDYLLHFMDPR 979
Cdd:cd07088 389 DEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAM---QGFhAGWKKSGLG-GADGKHGLEEYLQTK 464
|
..
gi 221564986 980 VV 981
Cdd:cd07088 465 VV 466
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
510-963 |
2.20e-92 |
|
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: 301.73 E-value: 2.20e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 510 LFIGGQ--ELETEDLLPSMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELS 587
Cdd:cd07138 1 FYIDGAwvAPAGTETIDVINPAT-EEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 588 ALQVLEIG-----KQWDQA---------YADVTEAIDFLEYYAREMIRlgsprsmgkvagetnqyfYEPKGVAAVIAPWN 653
Cdd:cd07138 80 QAITLEMGapitlARAAQVglgighlraAADALKDFEFEERRGNSLVV------------------REPIGVCGLITPWN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 654 FPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEV 733
Cdd:cd07138 142 WPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 734 GLRIIERAAkvqpgqEMVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTA 813
Cdd:cd07138 222 GKRVAEAAA------DTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 814 LAEAVPVGPVEDPANLIGAVAEENAQKRIMNYIEVGRQEG-RLLYQG----HVPEVGFFVPLTIIGDIRPEHRLAQEEIF 888
Cdd:cd07138 296 AAEAYVVGDPRDPATTLGPLASAAQFDRVQGYIQKGIEEGaRLVAGGpgrpEGLERGYFVKPTVFADVTPDMTIAREEIF 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221564986 889 GPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNRnctGALVGRQPFGGFRLSGAG 963
Cdd:cd07138 376 GPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHING---AAFNPGAPFGGYKQSGNG 447
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
527-982 |
1.35e-91 |
|
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: 299.35 E-value: 1.35e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 527 NPSDpSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADVT 606
Cdd:cd07103 3 NPAT-GEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 607 EAIDFLEYYAREmirlgSPRSMGKV-----AGETNQYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLT 681
Cdd:cd07103 82 YAASFLEWFAEE-----ARRIYGRTipspaPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 682 SIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAkvqpgqEMVKKVICEMGGk 761
Cdd:cd07103 157 PLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAA------DTVKRVSLELGG- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 762 naiiidddadldeavpH----VFNSA-------------FGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVE 824
Cdd:cd07103 230 ----------------NapfiVFDDAdldkavdgaiaskFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 825 DPANLIGAVAEENAQKRIMNYIEVGRQEG-RLLYQGH-VPEVGFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNE 902
Cdd:cd07103 294 DEGTDMGPLINERAVEKVEALVEDAVAKGaKVLTGGKrLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 903 ALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNrncTGALVGRQ-PFGGFRLSGAGtKAGGPDYLLHFMDPRVV 981
Cdd:cd07103 374 VIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGIN---TGLISDAEaPFGGVKESGLG-REGGKEGLEEYLETKYV 449
|
.
gi 221564986 982 T 982
Cdd:cd07103 450 S 450
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
526-967 |
2.11e-91 |
|
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: 298.88 E-value: 2.11e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 526 MNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADV 605
Cdd:cd07110 2 INPAT-EATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 606 TEAIDFLEYYAR--EMIRLGSPRSmgkVAGETNQY----FYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSG 679
Cdd:cd07110 81 DDVAGCFEYYADlaEQLDAKAERA---VPLPSEDFkarvRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 680 LTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAkvqpgqEMVKKVICEMG 759
Cdd:cd07110 158 LTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAA------QDIKPVSLELG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 760 GKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQ 839
Cdd:cd07110 232 GKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 840 KRIMNYIEVGRQEG-RLLYQGHVPEV---GFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALT 915
Cdd:cd07110 312 EKVLSFIARGKEEGaRLLCGGRRPAHlekGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLA 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 221564986 916 GGLFSRSPEHIAIATKRFRVGNLYLnrNCTGALVGRQPFGGFRLSGAGTKAG 967
Cdd:cd07110 392 AAVISRDAERCDRVAEALEAGIVWI--NCSQPCFPQAPWGGYKRSGIGRELG 441
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
511-985 |
3.81e-90 |
|
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: 296.53 E-value: 3.81e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 511 FIGGQ--ELETEDLLPSMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFET--WRDITPEIRAEFLLKACTVVRRRIYEL 586
Cdd:cd07119 1 YIDGEwvEAASGKTRDIINPAN-GEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 587 SALQVLEIGKQWDQAYADVTEAIDFLEYYAREMIRLGSprSMGKVAGETNQY-FYEPKGVAAVIAPWNFPLAISMGMVSA 665
Cdd:cd07119 80 ARLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETG--EVYDVPPHVISRtVREPVGVCGLITPWNYPLLQAAWKLAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 666 AIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAkvq 745
Cdd:cd07119 158 ALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAA--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 746 pgqEMVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVED 825
Cdd:cd07119 235 ---GNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 826 PANLIGAVAEENAQKRIMNYIEVGRQEG-RLLYQGHVPE-----VGFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARD 899
Cdd:cd07119 312 ADTEMGPLVSAEHREKVLSYIQLGKEEGaRLVCGGKRPTgdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 900 FNEALVWANSTRYALTGGLFSRSpehIAIA---TKRFRVGNLYLnrNCTGALVGRQPFGGFRLSGAGtKAGGPDYLLHFM 976
Cdd:cd07119 392 EEEAIRLANDTPYGLAGAVWTKD---IARAnrvARRLRAGTVWI--NDYHPYFAEAPWGGYKQSGIG-RELGPTGLEEYQ 465
|
....*....
gi 221564986 977 DPRVVTENT 985
Cdd:cd07119 466 ETKHININL 474
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
510-982 |
1.75e-89 |
|
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: 294.48 E-value: 1.75e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 510 LFIGGQ--ELETEDLLPSMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFE--TWRDITPEIRAEFLLKACTVVRRRIYE 585
Cdd:cd07139 1 LFIGGRwvAPSGSETIDVVSPAT-EEVVGRVPEATPADVDAAVAAARRAFDngPWPRLSPAERAAVLRRLADALEARADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 586 LSALQVLEIGK-QWDQAYADVTEAIDFLEYYAR-------EMIRLGSPRSMGKVAgetnqyfYEPKGVAAVIAPWNFPLA 657
Cdd:cd07139 80 LARLWTAENGMpISWSRRAQGPGPAALLRYYAAlardfpfEERRPGSGGGHVLVR-------REPVGVVAAIVPWNAPLF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 658 ISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGImGDYLVDHPHVSLIAFTGSMEVGLRI 737
Cdd:cd07139 153 LAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREV-GEYLVRHPGVDKVSFTGSTAAGRRI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 738 IERAAkvqpgqEMVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEA 817
Cdd:cd07139 232 AAVCG------ERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 818 VPVGPVEDPANLIGAVAEENAQKRIMNYIEVGRQEG-RLLYQGHVPEV---GFFVPLTIIGDIRPEHRLAQEEIFGPLLA 893
Cdd:cd07139 306 LKVGDPLDPATQIGPLASARQRERVEGYIAKGRAEGaRLVTGGGRPAGldrGWFVEPTLFADVDNDMRIAQEEIFGPVLS 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 894 VMRARDFNEALVWANSTRYALTGGLFSRSPEH-IAIAtKRFRVGNLYLN--RNCTGAlvgrqPFGGFRLSGAGtKAGGPD 970
Cdd:cd07139 386 VIPYDDEDDAVRIANDSDYGLSGSVWTADVERgLAVA-RRIRTGTVGVNgfRLDFGA-----PFGGFKQSGIG-REGGPE 458
|
490
....*....|..
gi 221564986 971 YLLHFMDPRVVT 982
Cdd:cd07139 459 GLDAYLETKSIY 470
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
523-982 |
2.93e-89 |
|
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: 293.08 E-value: 2.93e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 523 LPSMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAY 602
Cdd:cd07150 1 FDDLNPAD-GSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 603 ADVTEAIDFLEYyAREMIRlgspRSMGKV-----AGETNQYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKP 677
Cdd:cd07150 80 FETTFTPELLRA-AAGECR----RVRGETlpsdsPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 678 SGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAKvqpgqeMVKKVICE 757
Cdd:cd07150 155 SEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGR------HLKKITLE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 758 MGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEEN 837
Cdd:cd07150 229 LGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 838 AQKRIMNYIEVGRQEG-RLLYQGHVpEVGFFVPlTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTG 916
Cdd:cd07150 309 QVERIKRQVEDAVAKGaKLLTGGKY-DGNFYQP-TVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSA 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221564986 917 GLFSRSpEHIAIA-TKRFRVGNLYLnrNCTGALVGRQ-PFGGFRLSGAGtKAGGPDYLLHFMDPRVVT 982
Cdd:cd07150 387 AILTND-LQRAFKlAERLESGMVHI--NDPTILDEAHvPFGGVKASGFG-REGGEWSMEEFTELKWIT 450
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
545-969 |
5.26e-89 |
|
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: 291.74 E-value: 5.26e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 545 EVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADVTEAIDFLeyyaREMIRLGS 624
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAIL----REAAGLPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 625 pRSMGKV-----AGETNQYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSI-IGWQLVDIFREVGLP 698
Cdd:cd07104 77 -RPEGEIlpsdvPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVtGGLLIAEIFEEAGLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 699 DGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAKvqpgqeMVKKVICEMGGKNaiiidddadldeavPH 778
Cdd:cd07104 156 KGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGR------HLKKVALELGGNN--------------PL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 779 V---------------FnSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQKRIM 843
Cdd:cd07104 216 IvlddadldlavsaaaF-GAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVH 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 844 NYIEVGRQEG-RLLYQGHVpeVGFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRS 922
Cdd:cd07104 295 AIVEDAVAAGaRLLTGGTY--EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRD 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 221564986 923 PEH-IAIAtKRFRVGNLYLNR---NCtGALVgrqPFGGFRLSGaGTKAGGP 969
Cdd:cd07104 373 LERaMAFA-ERLETGMVHINDqtvND-EPHV---PFGGVKASG-GGRFGGP 417
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
477-979 |
1.37e-88 |
|
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: 292.97 E-value: 1.37e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 477 SNEPVIDFTREEQRQAFREHIGQVRSRFGRKYPLfIGGQELETEDLLPSMNPSDPSEIVGWVCQAGTDEVAQAIGAARKS 556
Cdd:TIGR01238 8 KNSLGIDLDNESELKPLEAQIHAWADKTWQAAPI-IGHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAIDSAQQA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 557 FETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADVTEAIDFLEYYAremirlgsprsmGKVAGETN 636
Cdd:TIGR01238 87 FPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYA------------KQVRDVLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 637 QYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYL 716
Cdd:TIGR01238 155 EFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 717 VDHPHVSLIAFTGSMEVGLRIIERAAKVQPGQemvKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSR 796
Cdd:TIGR01238 235 TSDPRIAGVAFTGSTEVAQLINQTLAQREDAP---VPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 797 VIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQKRIMNYIEVGRQEGRLLYQ-----GHVPEVGFFVPLT 871
Cdd:TIGR01238 312 LCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQltlddSRACQHGTFVAPT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 872 IIgDIRPEHRLaQEEIFGPLLAVMR--ARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNRNCTGALV 949
Cdd:TIGR01238 392 LF-ELDDIAEL-SEEVFGPVLHVVRykARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVV 469
|
490 500 510
....*....|....*....|....*....|
gi 221564986 950 GRQPFGGFRLSGAGTKAGGPDYLLHFMDPR 979
Cdd:TIGR01238 470 GVQPFGGQGLSGTGPKAGGPHYLYRLTQVQ 499
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
525-967 |
9.64e-86 |
|
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: 283.67 E-value: 9.64e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 525 SMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFET--WRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAY 602
Cdd:cd07114 1 SINPAT-GEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 603 ADVTEAIDFLEYYA--REMIRlGS--PRSMGKVAGETNqyfYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPS 678
Cdd:cd07114 80 AQVRYLAEWYRYYAglADKIE-GAviPVDKGDYLNFTR---REPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 679 GLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAKVqpgqemVKKVICEM 758
Cdd:cd07114 156 EHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAEN------LAPVTLEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 759 GGKNaiiidddadldeavPH-VFNSA-------------FGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVE 824
Cdd:cd07114 230 GGKS--------------PNiVFDDAdldaavngvvagiFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 825 DPANLIGAVAEENAQKRIMNYIEVGRQEG-RLLYQGHVPEV-----GFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRAR 898
Cdd:cd07114 296 DPETQMGPLATERQLEKVERYVARAREEGaRVLTGGERPSGadlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFD 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221564986 899 DFNEALVWANSTRYALTGGLFSRSpehIAIA---TKRFRVGNLYLN--RnctgALVGRQPFGGFRLSGAGTKAG 967
Cdd:cd07114 376 DEEEAIALANDSEYGLAAGIWTRD---LARAhrvARAIEAGTVWVNtyR----ALSPSSPFGGFKDSGIGRENG 442
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
540-967 |
1.09e-85 |
|
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: 283.46 E-value: 1.09e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 540 QAGTDEVAQAIGAARKSFET--WRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADVTEAIDFLEYYAr 617
Cdd:cd07118 15 EGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAA- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 618 emirlGSPRSMgkvAGETNQ---------YFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQL 688
Cdd:cd07118 94 -----SLARTL---HGDSYNnlgddmlglVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLML 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 689 VDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAKvqpgqeMVKKVICEMGGKNAIIIDD 768
Cdd:cd07118 166 AELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR------NLKKVSLELGGKNPQIVFA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 769 DADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQKRIMNYIEV 848
Cdd:cd07118 240 DADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 849 GRQEGRLLYQGH---VPEVGFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEH 925
Cdd:cd07118 320 GRAEGATLLLGGerlASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDT 399
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 221564986 926 IAIATKRFRVGNLYLNRNCTGAlvGRQPFGGFRLSGAGTKAG 967
Cdd:cd07118 400 ALTVARRIRAGTVWVNTFLDGS--PELPFGGFKQSGIGRELG 439
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
523-977 |
7.50e-85 |
|
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: 281.41 E-value: 7.50e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 523 LPSMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFE--TWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQ 600
Cdd:cd07112 4 FATINPAT-GRVLAEVAACDAADVDRAVAAARRAFEsgVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 601 AYA-DVTEAIDFLEYYArEMIrlgsPRSMGKVAGETNQYF----YEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVF 675
Cdd:cd07112 83 ALAvDVPSAANTFRWYA-EAI----DKVYGEVAPTGPDALalitREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 676 KPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAakvqpGQEMVKKVI 755
Cdd:cd07112 158 KPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYS-----GQSNLKRVW 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 756 CEMGGKNAIIIDD-DADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVA 834
Cdd:cd07112 233 LECGGKSPNIVFAdAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 835 EENAQKRIMNYIEVGRQEG-RLLYQG---HVPEVGFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANST 910
Cdd:cd07112 313 SEAHFDKVLGYIESGKAEGaRLVAGGkrvLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221564986 911 RYALTGGLFSRSPEHIAIATKRFRVGNLYLnrNCTGALVGRQPFGGFRLSGagtkaGGPDYLLHFMD 977
Cdd:cd07112 393 VYGLAASVWTSDLSRAHRVARRLRAGTVWV--NCFDEGDITTPFGGFKQSG-----NGRDKSLHALD 452
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
509-983 |
1.51e-83 |
|
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: 278.63 E-value: 1.51e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 509 PLFIGGQ--ELETEDLLPSMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYEL 586
Cdd:cd07085 2 KLFINGEwvESKTTEWLDVYNPAT-GEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 587 SALQVLEIGKQWDQAYADVTEAIDFLEYyAREMIRLGSPRSMGKVAGETNQYFY-EPKGVAAVIAPWNFPLAISMGMVSA 665
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEF-ACSIPHLLKGEYLENVARGIDTYSYrQPLGVVAGITPFNFPAMIPLWMFPM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 666 AIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGrSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAKVQ 745
Cdd:cd07085 160 AIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 746 pgqemvKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVED 825
Cdd:cd07085 239 ------KRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 826 PANLIGAVAEENAQKRIMNYIEVGRQEG-RLLYQGHVPEV-----GFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARD 899
Cdd:cd07085 313 PGADMGPVISPAAKERIEGLIESGVEEGaKLVLDGRGVKVpgyenGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 900 FNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNrncTG--ALVGRQPFGGFRLSGAG-TKAGGPDYLLHFM 976
Cdd:cd07085 393 LDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN---VPipVPLAFFSFGGWKGSFFGdLHFYGKDGVRFYT 469
|
....*..
gi 221564986 977 DPRVVTE 983
Cdd:cd07085 470 QTKTVTS 476
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
533-982 |
4.96e-83 |
|
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: 276.40 E-value: 4.96e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 533 EIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADVTEAIDFL 612
Cdd:cd07149 10 EVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDRAIETL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 613 EYYAREMIRL--------GSPRSMGKVAgetnqYFY-EPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSI 683
Cdd:cd07149 90 RLSAEEAKRLagetipfdASPGGEGRIG-----FTIrEPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 684 IGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAkvqpgqemVKKVICEMGGKNA 763
Cdd:cd07149 165 SALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--------LKKVTLELGSNAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 764 IIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQKRIM 843
Cdd:cd07149 237 VIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 844 NYIEVGRQEGRLLYQGHVPEVGFFVPlTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSP 923
Cdd:cd07149 317 EWVEEAVEGGARLLTGGKRDGAILEP-TVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDL 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 924 EHIAIATKRFRVGNLYLNRNCTgALVGRQPFGGFRLSGAGTKagGPDYLLHFM-DPRVVT 982
Cdd:cd07149 396 QKALKAARELEVGGVMINDSST-FRVDHMPYGGVKESGTGRE--GPRYAIEEMtEIKLVC 452
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
527-981 |
7.38e-83 |
|
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: 275.56 E-value: 7.38e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 527 NPSDPsEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADVT 606
Cdd:cd07106 3 NPATG-EVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 607 EAIDFLEYYAR-----EMIRLGSPRsmgKVAGEtnqyfYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLT 681
Cdd:cd07106 82 GAVAWLRYTASldlpdEVIEDDDTR---RVELR-----RKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 682 SIIGWQLVDIFREVgLPDGVFNFVPGRSGImGDYLVDHPHVSLIAFTGSMEVGLRIIERAAKVqpgqemVKKVICEMGGK 761
Cdd:cd07106 154 PLCTLKLGELAQEV-LPPGVLNVVSGGDEL-GPALTSHPDIRKISFTGSTATGKKVMASAAKT------LKRVTLELGGN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 762 NAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVaeENAQ-- 839
Cdd:cd07106 226 DAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPV--QNKMqy 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 840 KRIMNYIEVGRQEG-RLLYQGHVPEV-GFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGG 917
Cdd:cd07106 304 DKVKELVEDAKAKGaKVLAGGEPLDGpGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGAS 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221564986 918 LFSRSPEH-IAIAtKRFRVGNLYLNRNctGALVGRQPFGGFRLSGAGTkAGGPDYLLHFMDPRVV 981
Cdd:cd07106 384 VWSSDLERaEAVA-RRLEAGTVWINTH--GALDPDAPFGGHKQSGIGV-EFGIEGLKEYTQTQVI 444
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
515-963 |
1.79e-82 |
|
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: 274.95 E-value: 1.79e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 515 QELETEDLLPSMNPSDPSEIVGwVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEI 594
Cdd:cd07151 4 RDGTSERTIDVLNPYTGETLAE-IPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 595 GK-------QWDQAYADVTEAIDFleyyareMIRLGSPRSMGKVAGETNQYFYEPKGVAAVIAPWNFPLAISMGMVSAAI 667
Cdd:cd07151 83 GStrikaniEWGAAMAITREAATF-------PLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 668 VTGNCVVFKPSGLTSIIGWQLV-DIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAKVqp 746
Cdd:cd07151 156 ALGNAVVLKPASDTPITGGLLLaKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRH-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 747 gqemVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDP 826
Cdd:cd07151 234 ----LKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 827 ANLIGAVAEENAQKRIMNYIEVGRQEG-RLLYQGHVpeVGFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALV 905
Cdd:cd07151 310 DTVVGPLINESQVDGLLDKIEQAVEEGaTLLVGGEA--EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALE 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221564986 906 WANSTRYALTGGLFSRSPEH-IAIAtKRFRVGNLYLNRNCtgalVGRQP---FGGFRLSGAG 963
Cdd:cd07151 388 LANDTEYGLSGAVFTSDLERgVQFA-RRIDAGMTHINDQP----VNDEPhvpFGGEKNSGLG 444
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
530-964 |
6.33e-82 |
|
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: 273.05 E-value: 6.33e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 530 DPS--EIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYAD-VT 606
Cdd:cd07092 3 DPAtgEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDeLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 607 EAIDFLEYYAremirlGSPRSM-GKVAGE-----TNQYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGL 680
Cdd:cd07092 83 GAVDNFRFFA------GAARTLeGPAAGEylpghTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 681 TSIIGWQLVDIFREVgLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAKvqpgqeMVKKVICEMGG 760
Cdd:cd07092 157 TPLTTLLLAELAAEV-LPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAAD------TLKRVHLELGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 761 KNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQK 840
Cdd:cd07092 230 KAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 841 RIMNYIEVGRQEGRLLYQGHVPEV-GFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLF 919
Cdd:cd07092 310 RVAGFVERAPAHARVLTGGRRAEGpGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVW 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 221564986 920 SRSPEHIAIATKRFRVGNLYLnrNCTGALVGRQPFGGFRLSGAGT 964
Cdd:cd07092 390 TRDVGRAMRLSARLDFGTVWV--NTHIPLAAEMPHGGFKQSGYGK 432
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
511-967 |
1.35e-81 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 272.84 E-value: 1.35e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 511 FIGGQ--ELETEDLLPSMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSA 588
Cdd:TIGR01804 1 FIDGEyvEDSAGTTREIINPAN-GEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 589 LQVLEIGKQWDQA-YADVTEAIDFLEYYAR-------EMIRLGSPrSMGKVAgetnqyfYEPKGVAAVIAPWNFPLAISM 660
Cdd:TIGR01804 80 LETLDTGKTLQETiVADMDSGADVFEFFAGlapalngEIIPLGGP-SFAYTI-------REPLGVCVGIGAWNYPLQIAS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 661 GMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIER 740
Cdd:TIGR01804 152 WKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 741 AAkvqpgqEMVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPV 820
Cdd:TIGR01804 232 AA------GHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 821 GPVEDPANLIGAVAEENAQKRIMNYIEVGRQEG-RLLYQGHVPEV-----GFFVPLTIIGDIRPEHRLAQEEIFGPLLAV 894
Cdd:TIGR01804 306 GDPFDEATEMGPLISAAHRDKVLSYIEKGKAEGaTLATGGGRPENvglqnGFFVEPTVFADCTDDMTIVREEIFGPVMTV 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221564986 895 MRARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNR-NCTGALVgrqPFGGFRLSGAGTKAG 967
Cdd:TIGR01804 386 LTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTyNLYPAEA---PFGGYKQSGIGRENG 456
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
525-967 |
1.56e-81 |
|
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: 272.33 E-value: 1.56e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 525 SMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYAD 604
Cdd:cd07107 1 VINPAT-GQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 605 VTEAIDFLEYYAREMIRLGSpRSMGKVAGETNQYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSII 684
Cdd:cd07107 80 VMVAAALLDYFAGLVTELKG-ETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 685 GWQLVDIFREVgLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGlRIIERAAKvqpgqEMVKKVICEMGGKNAI 764
Cdd:cd07107 159 ALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTG-RAIMRAAA-----EGIKHVTLELGGKNAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 765 IIDDDADLDEAV-PHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQKRIM 843
Cdd:cd07107 232 IVFPDADPEAAAdAAVAGMNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVM 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 844 NYIEVGRQEG-RLLY-----QGHVPEVGFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGG 917
Cdd:cd07107 312 HYIDSAKREGaRLVTgggrpEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAA 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 221564986 918 LFSRSPEHIAIATKRFRVGNLYLN---RNCTGAlvgrqPFGGFRLSGAGTKAG 967
Cdd:cd07107 392 IWTNDISQAHRTARRVEAGYVWINgssRHFLGA-----PFGGVKNSGIGREEC 439
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
505-967 |
1.10e-79 |
|
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: 268.12 E-value: 1.10e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 505 GRKY--P--LFIGGQELETED--LLPSMNPSDPSEIVGWVCqAGTDEVAQAIGAARKSFET-WRDITPEIRAEFLLKACT 577
Cdd:cd07144 1 GKSYdqPtgLFINNEFVKSSDgeTIKTVNPSTGEVIASVYA-AGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 578 VVRRRIYELSALQVLEIGKQWDQ-AYADVTEAIDFLEYYAremirlGSPRSM-GKVAGETNQYF----YEPKGVAAVIAP 651
Cdd:cd07144 80 LVEKNRDLLAAIEALDSGKPYHSnALGDLDEIIAVIRYYA------GWADKIqGKTIPTSPNKLaytlHEPYGVCGQIIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 652 WNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSM 731
Cdd:cd07144 154 WNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGST 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 732 EVGlRIIERAAkvqpGQEMvKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRL 811
Cdd:cd07144 234 ATG-RLVMKAA----AQNL-KAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 812 TA-LAEAVPVGPVEDPANLIGAVAEENAQKRIMNYIEVGRQEG-RLLYQGHV----PEVGFFVPLTIIGDIRPEHRLAQE 885
Cdd:cd07144 308 VEhVKQNYKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGaKLVYGGEKapegLGKGYFIPPTIFTDVPQDMRIVKE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 886 EIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSrspEHIAIA---TKRFRVGNLYLNRNCTGALvgRQPFGGFRLSGA 962
Cdd:cd07144 388 EIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFT---KDIRRAhrvARELEAGMVWINSSNDSDV--GVPFGGFKMSGI 462
|
....*
gi 221564986 963 GTKAG 967
Cdd:cd07144 463 GRELG 467
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
527-967 |
2.06e-78 |
|
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: 263.78 E-value: 2.06e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 527 NPSDpSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADVT 606
Cdd:cd07090 3 EPAT-GEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 607 EAIDFLEYYARemirlgsprSMGKVAGETNQ-----YFY---EPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPS 678
Cdd:cd07090 82 SSADCLEYYAG---------LAPTLSGEHVPlpggsFAYtrrEPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 679 GLTSIIGWQLVDIFREVGLPDGVFNFVPGrSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAKvqpgqeMVKKVICEM 758
Cdd:cd07090 153 PFTPLTALLLAEILTEAGLPDGVFNVVQG-GGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAK------GIKHVTLEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 759 GGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENA 838
Cdd:cd07090 226 GGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEH 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 839 QKRIMNYIEVGRQEG-RLLYQGHVPEV------GFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTR 911
Cdd:cd07090 306 LEKVLGYIESAKQEGaKVLCGGERVVPedglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTT 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 221564986 912 YALTGGLFSR--SPEHIAIAtkRFRVGNLYLNR-NCTGALVgrqPFGGFRLSGAGTKAG 967
Cdd:cd07090 386 YGLAAGVFTRdlQRAHRVIA--QLQAGTCWINTyNISPVEV---PFGGYKQSGFGRENG 439
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
526-963 |
2.66e-78 |
|
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: 263.44 E-value: 2.66e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 526 MNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADV 605
Cdd:cd07145 4 RNPAN-GEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 606 TEAIDFLEYYAREmirlgSPRSMGKV----AGETNQYFY-----EPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFK 676
Cdd:cd07145 83 ERTIRLFKLAAEE-----AKVLRGETipvdAYEYNERRIaftvrEPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 677 PSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAKvqpgqeMVKKVIC 756
Cdd:cd07145 158 PSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGG------TGKKVAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 757 EMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVG-PVEDPAN---LIGA 832
Cdd:cd07145 232 ELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGdPLDESTDlgpLISP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 833 VAEENAQKRIMNYIEVGrqeGRLLYQGHVPEvGFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRY 912
Cdd:cd07145 312 EAVERMENLVNDAVEKG---GKILYGGKRDE-GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEY 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 221564986 913 ALTGGLFSrspEHIAIATK---RFRVGNLYLNrNCTGALVGRQPFGGFRLSGAG 963
Cdd:cd07145 388 GLQASVFT---NDINRALKvarELEAGGVVIN-DSTRFRWDNLPFGGFKKSGIG 437
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
510-974 |
4.09e-78 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 264.67 E-value: 4.09e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 510 LFIGGQELE--TEDLLPSMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFET-----WRDITPEIRAEFLLKACTVVRRR 582
Cdd:PLN02467 10 LFIGGEWREpvLGKRIPVVNPAT-EETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 583 IYELSALQVLEIGKQWDQAYADVTEAIDFLEYYAR--EMI--RLGSPRSMGKVAGETNqYFYEPKGVAAVIAPWNFPLAI 658
Cdd:PLN02467 89 KSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADlaEALdaKQKAPVSLPMETFKGY-VLKEPLGVVGLITPWNYPLLM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 659 SMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRII 738
Cdd:PLN02467 168 ATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 739 ERAAkvqpgqEMVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAV 818
Cdd:PLN02467 248 TAAA------QMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 819 PVG-PVEDPANLiGAVAEENAQKRIMNYIEVGRQEG-RLLYQGHVPEV---GFFVPLTIIGDIRPEHRLAQEEIFGPLLA 893
Cdd:PLN02467 322 KISdPLEEGCRL-GPVVSEGQYEKVLKFISTAKSEGaTILCGGKRPEHlkkGFFIEPTIITDVTTSMQIWREEVFGPVLC 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 894 VMRARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLnrNCTGALVGRQPFGGFRLSGAGTKAG--GPDY 971
Cdd:PLN02467 401 VKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWI--NCSQPCFCQAPWGGIKRSGFGRELGewGLEN 478
|
...
gi 221564986 972 LLH 974
Cdd:PLN02467 479 YLS 481
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
508-963 |
8.28e-78 |
|
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: 263.05 E-value: 8.28e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 508 YPLFIGGQELETED--LLPSMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYE 585
Cdd:cd07559 1 YDNFINGEWVAPSKgeYFDNYNPVN-GKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 586 LSALQVLEIGKQWDQAY-ADVTEAIDFLEYYArEMIRLGSPrSMGKVAGET-NQYFYEPKGVAAVIAPWNFPLAISMGMV 663
Cdd:cd07559 80 LAVAETLDNGKPIRETLaADIPLAIDHFRYFA-GVIRAQEG-SLSEIDEDTlSYHFHEPLGVVGQIIPWNFPLLMAAWKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 664 SAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVgLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAk 743
Cdd:cd07559 158 APALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAA- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 744 vqpgqEMVKKVICEMGGK--NAIIIDDDADLDEAVPHVFNSAFGF---QGQKCSACSRVIVLDGIYDKFVQRLTALAEAV 818
Cdd:cd07559 236 -----ENLIPVTLELGGKspNIFFDDAMDADDDFDDKAEEGQLGFafnQGEVCTCPSRALVQESIYDEFIERAVERFEAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 819 PVGPVEDPANLIGAVAEENAQKRIMNYIEVGRQEG-RLLYQGH-----VPEVGFFVPLTIIGDIRPEHRLAQEEIFGPLL 892
Cdd:cd07559 311 KVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGaEVLTGGErltlgGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVL 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221564986 893 AVMRARDFNEALVWANSTRYALTGGLFSRSpehiaiATKRFRVGN-LYLNR---NCTGALVGRQPFGGFRLSGAG 963
Cdd:cd07559 391 AVITFKDEEEAIAIANDTEYGLGGGVWTRD------INRALRVARgIQTGRvwvNCYHQYPAHAPFGGYKKSGIG 459
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
507-963 |
3.58e-77 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 261.35 E-value: 3.58e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 507 KYPLFIGGQELE--TEDLLPSMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIY 584
Cdd:PRK13252 6 LQSLYIDGAYVEatSGETFEVINPAT-GEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERND 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 585 ELSALQVLEIGKQWDQA-YADVTEAIDFLEYYAR-------EMIRLGSprsmgkvagetNQYFY---EPKGVAAVIAPWN 653
Cdd:PRK13252 85 ELAALETLDTGKPIQETsVVDIVTGADVLEYYAGlapalegEQIPLRG-----------GSFVYtrrEPLGVCAGIGAWN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 654 FPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGrSGIMGDYLVDHPHVSLIAFTGSMEV 733
Cdd:PRK13252 154 YPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQG-DGRVGAWLTEHPDIAKVSFTGGVPT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 734 GLRIIERAAkvqpgqEMVKKVICEMGGKNAIIidddadldeavphVFNSA-------------FGFQGQKCSACSRVIVL 800
Cdd:PRK13252 233 GKKVMAAAA------ASLKEVTMELGGKSPLI-------------VFDDAdldraadiamlanFYSSGQVCTNGTRVFVQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 801 DGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQKRIMNYIEVGRQEG-RLLYQGH-----VPEVGFFVPLTIIG 874
Cdd:PRK13252 294 KSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGaRLLCGGErltegGFANGAFVAPTVFT 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 875 DIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSR--SPEHIAIAtkRFRVGNLYLnrNCTGALVGRQ 952
Cdd:PRK13252 374 DCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTAdlSRAHRVIH--QLEAGICWI--NTWGESPAEM 449
|
490
....*....|.
gi 221564986 953 PFGGFRLSGAG 963
Cdd:PRK13252 450 PVGGYKQSGIG 460
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
507-964 |
1.44e-75 |
|
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: 256.34 E-value: 1.44e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 507 KYPLFIGGQELETE-DLLPSMNPSDPsEIVGWVCQAGTDEVAQAIGAARKSFE-TWRDITPEIRAEFLLKACTVVRRRIY 584
Cdd:cd07082 1 QFKYLINGEWKESSgKTIEVYSPIDG-EVIGSVPALSALEILEAAETAYDAGRgWWPTMPLEERIDCLHKFADLLKENKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 585 ELSALQVLEIGKQWDQAYADVTEAIDFLEYYAREMIRL--------GSPRSMGKVAgetnQYFYEPKGVAAVIAPWNFPL 656
Cdd:cd07082 80 EVANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLdgdslpgdWFPGTKGKIA----QVRREPLGVVLAIGPFNYPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 657 AISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLR 736
Cdd:cd07082 156 NLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 737 IIERAAkvqpgqemVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAE 816
Cdd:cd07082 236 LKKQHP--------MKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 817 AVPVGPVEDPANLIGAVAEENA----QKRIMNYIEVGrqeGRLLYQGHVPEVGFFVPlTIIGDIRPEHRLAQEEIFGPLL 892
Cdd:cd07082 308 KLKVGMPWDNGVDITPLIDPKSadfvEGLIDDAVAKG---ATVLNGGGREGGNLIYP-TLLDPVTPDMRLAWEEPFGPVL 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221564986 893 AVMRARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNRNCtgalvgrQ------PFGGFRLSGAGT 964
Cdd:cd07082 384 PIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKC-------QrgpdhfPFLGRKDSGIGT 454
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
526-982 |
4.49e-75 |
|
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: 254.45 E-value: 4.49e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 526 MNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKactvVRRRIY----ELSALQVLEIGKQWDQA 601
Cdd:cd07099 1 RNPAT-GEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLR----WKRALAdhadELAELLHAETGKPRADA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 602 YADVTEAIDFLEYYAREMIRLGSPRSMG---KVAGETNQYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPS 678
Cdd:cd07099 76 GLEVLLALEAIDWAARNAPRVLAPRKVPtglLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 679 GLTSIIGWQLVDIFREVGLPDGVFNFVPGrSGIMGDYLVDHPhVSLIAFTGSMEVGLRIIERAAkvqpgqEMVKKVICEM 758
Cdd:cd07099 156 EVTPLVGELLAEAWAAAGPPQGVLQVVTG-DGATGAALIDAG-VDKVAFTGSVATGRKVMAAAA------ERLIPVVLEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 759 GGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEEN- 837
Cdd:cd07099 228 GGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARq 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 838 ---AQKRIMNYIEVGrqeGRLLYQGHVPEV-GFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYA 913
Cdd:cd07099 308 ldiVRRHVDDAVAKG---AKALTGGARSNGgGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYG 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 914 LTGGLFSRSPEHI-AIATkRFRVGNLYLNRNCTGALVGRQPFGGFRLSGAGTKaGGPDYLLHFMDPRVVT 982
Cdd:cd07099 385 LSASVFSRDLARAeAIAR-RLEAGAVSINDVLLTAGIPALPFGGVKDSGGGRR-HGAEGLREFCRPKAIA 452
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
524-967 |
1.52e-74 |
|
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: 253.81 E-value: 1.52e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 524 PSMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFE---TWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQW-D 599
Cdd:cd07141 25 PTINPAT-GEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFsK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 600 QAYADVTEAIDFLEYYAremirlgsprsmG---KVAGET----NQYF----YEPKGVAAVIAPWNFPLAISMGMVSAAIV 668
Cdd:cd07141 104 SYLVDLPGAIKVLRYYA------------GwadKIHGKTipmdGDFFtytrHEPVGVCGQIIPWNFPLLMAAWKLAPALA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 669 TGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGlRIIERAAkvqpGQ 748
Cdd:cd07141 172 CGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVG-KLIQQAA----GK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 749 EMVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPAN 828
Cdd:cd07141 247 SNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 829 LIGAVAEENAQKRIMNYIEVGRQEGRLLYQG--HVPEVGFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVW 906
Cdd:cd07141 327 EQGPQIDEEQFKKILELIESGKKEGAKLECGgkRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIER 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221564986 907 ANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLnrNCTGALVGRQPFGGFRLSGAGTKAG 967
Cdd:cd07141 407 ANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWV--NCYNVVSPQAPFGGYKMSGNGRELG 465
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
510-974 |
7.18e-74 |
|
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: 252.06 E-value: 7.18e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 510 LFIGGQELETED--LLPSMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFET-W-RDITPEIRAEFLLKACTVVRRRIYE 585
Cdd:cd07143 9 LFINGEFVDSVHggTVKVYNPST-GKLITKIAEATEADVDIAVEVAHAAFETdWgLKVSGSKRGRCLSKLADLMERNLDY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 586 LSALQVLEIGKQWDQAYA-DVTEAIDFLEYYAremirlG-SPRSMGKVAgETNQ-----YFYEPKGVAAVIAPWNFPLAI 658
Cdd:cd07143 88 LASIEALDNGKTFGTAKRvDVQASADTFRYYG------GwADKIHGQVI-ETDIkkltyTRHEPIGVCGQIIPWNFPLLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 659 SMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRII 738
Cdd:cd07143 161 CAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 739 ERAAKVQpgqemVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAV 818
Cdd:cd07143 241 EAAAKSN-----LKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 819 PVGPVEDPANLIGAVAEENAQKRIMNYIEVGRQEGRLLYQG---HVPEvGFFVPLTIIGDIRPEHRLAQEEIFGPLLAVM 895
Cdd:cd07143 316 KVGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGgkrHGNE-GYFIEPTIFTDVTEDMKIVKEEIFGPVVAVI 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221564986 896 RARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLnrNCTGALVGRQPFGGFRLSGAGTKAGgpDYLLH 974
Cdd:cd07143 395 KFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWV--NCYNLLHHQVPFGGYKQSGIGRELG--EYALE 469
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
505-978 |
1.47e-73 |
|
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: 251.16 E-value: 1.47e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 505 GRKYPLFIGGQELETED--LLPSMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRR 582
Cdd:cd07111 19 DRSFGHFINGKWVKPENrkSFPTINPAT-GEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 583 IYELSALQVLEIGKQWDQAY-ADVTEAIDFLEYYAremirlGSPRSMgkvagETNQYFYEPKGVAAVIAPWNFPLAISMG 661
Cdd:cd07111 98 QRLFAVLESLDNGKPIRESRdCDIPLVARHFYHHA------GWAQLL-----DTELAGWKPVGVVGQIVPWNFPLLMLAW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 662 MVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGrSGIMGDYLVDHPHVSLIAFTGSMEVGlRIIERA 741
Cdd:cd07111 167 KICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTG-NGSFGSALANHPGVDKVAFTGSTEVG-RALRRA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 742 AKvqpGQemVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVG 821
Cdd:cd07111 245 TA---GT--GKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 822 PVEDPANLIGAVAEENAQKRIMNYIEVGRQEGRLLYQ--GHVPEVGFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARD 899
Cdd:cd07111 320 DPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQpgADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 900 FNEALVWANSTRYALTGGLFSrspEHIAIATK---RFRVGNLYLnrNCTGALVGRQPFGGFRLSGAGtKAGGPDYLLHFM 976
Cdd:cd07111 400 AKEAVALANNTPYGLAASVWS---ENLSLALEvalSLKAGVVWI--NGHNLFDAAAGFGGYRESGFG-REGGKEGLYEYL 473
|
..
gi 221564986 977 DP 978
Cdd:cd07111 474 RP 475
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
510-967 |
2.90e-73 |
|
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: 250.10 E-value: 2.90e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 510 LFIGGQELETED--LLPSMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFE--TWRDITPEIRAEFLLKACTVVRRRIYE 585
Cdd:cd07142 6 LFINGQFVDAASgkTFPTIDPRN-GEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 586 LSALQVLEIGKQWDQA-YADVTEAIDFLEYYARemirlgsprSMGKVAGET--------NQYFYEPKGVAAVIAPWNFPL 656
Cdd:cd07142 85 LAALETWDNGKPYEQArYAEVPLAARLFRYYAG---------WADKIHGMTlpadgphhVYTLHEPIGVVGQIIPWNFPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 657 AISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLR 736
Cdd:cd07142 156 LMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 737 IIERAAKVQpgqemVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAE 816
Cdd:cd07142 236 IMQLAAKSN-----LKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARAL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 817 AVPVGPVEDPANLIGAVAEENAQKRIMNYIEVGRQEGRLLYQG--HVPEVGFFVPLTIIGDIRPEHRLAQEEIFGPLLAV 894
Cdd:cd07142 311 KRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGgdRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSI 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221564986 895 MRARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLnrNCTGALVGRQPFGGFRLSGAGTKAG 967
Cdd:cd07142 391 LKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWV--NCYDVFDASIPFGGYKMSGIGREKG 461
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
508-963 |
6.30e-73 |
|
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: 249.29 E-value: 6.30e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 508 YPLFIGGQELETE--DLLPSMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYE 585
Cdd:cd07117 1 YGLFINGEWVKGSsgETIDSYNPAN-GETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 586 LSALQVLEIGKQWDQAYA-DVTEAIDFLEYYArEMIRLGSPRSMGKVAGETNQYFYEPKGVAAVIAPWNFPLAISMGMVS 664
Cdd:cd07117 80 LAMVETLDNGKPIRETRAvDIPLAADHFRYFA-GVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 665 AAIVTGNCVVFKPSGLTSIIGWQLVDIFREVgLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAKv 744
Cdd:cd07117 159 PALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 745 qpgqemvkKVI---CEMGGKNAIIIDDDADLDEAVPHV-----FNsafgfQGQKCSACSRVIVLDGIYDKFVQRLTALAE 816
Cdd:cd07117 237 --------KLIpatLELGGKSANIIFDDANWDKALEGAqlgilFN-----QGQVCCAGSRIFVQEGIYDEFVAKLKEKFE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 817 AVPVGPVEDPANLIGAVAEENAQKRIMNYIEVGRQEG-RLLYQGH-----VPEVGFFVPLTIIGDIRPEHRLAQEEIFGP 890
Cdd:cd07117 304 NVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGaKILTGGHrltenGLDKGFFIEPTLIVNVTNDMRVAQEEIFGP 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221564986 891 LLAVMRARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLnrNCTGALVGRQPFGGFRLSGAG 963
Cdd:cd07117 384 VATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWV--NTYNQIPAGAPFGGYKKSGIG 454
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
527-982 |
8.78e-72 |
|
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: 245.73 E-value: 8.78e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 527 NPSDpSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQW-DQAYADV 605
Cdd:cd07108 3 NPAT-GQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 606 TEAIDFLEYYARemirLGsprsmGKVAGET-----NQYFY---EPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKP 677
Cdd:cd07108 82 AVLADLFRYFGG----LA-----GELKGETlpfgpDVLTYtvrEPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 678 SGLTSIIGWQLVDIFREVgLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGlRIIERAA--KVQPgqemvkkVI 755
Cdd:cd07108 153 AEDAPLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVG-KIIYRAAadRLIP-------VS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 756 CEMGGKNAIIIDDDADLDEAVPHVFNSA-FGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVA 834
Cdd:cd07108 224 LELGGKSPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAII 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 835 EENAQKRIMNYIEVGR--QEGRLLYQGHVPEV-----GFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWA 907
Cdd:cd07108 304 SEKQFAKVCGYIDLGLstSGATVLRGGPLPGEgpladGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMA 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221564986 908 NSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNRNcTGALVGrQPFGGFRLSGAGTKAGGPDYLLHFMDPRVVT 982
Cdd:cd07108 384 NDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQG-GGQQPG-QSYGGFKQSGLGREASLEGMLEHFTQKKTVN 456
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
508-963 |
1.12e-71 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 245.97 E-value: 1.12e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 508 YPLFIGGQELETE-DLLPSMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYEL 586
Cdd:PRK13473 3 TKLLINGELVAGEgEKQPVYNPAT-GEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 587 SALQVLEIGKQWDQAYAD-VTEAIDFLEYYAremirlGSPRSM-GKVAGE-----TNQYFYEPKGVAAVIAPWNFPLAIS 659
Cdd:PRK13473 82 ARLESLNCGKPLHLALNDeIPAIVDVFRFFA------GAARCLeGKAAGEyleghTSMIRRDPVGVVASIAPWNYPLMMA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 660 MGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVgLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIE 739
Cdd:PRK13473 156 AWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 740 RAAKvqpgqeMVKKVICEMGGKnaiiidddadldeaVPH-VFNSA-----------FGF--QGQKCSACSRVIVLDGIYD 805
Cdd:PRK13473 235 AAAD------SVKRTHLELGGK--------------APViVFDDAdldavvegirtFGYynAGQDCTAACRIYAQRGIYD 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 806 KFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQKRIMNYIEVGRQEG--RLLYQGHVPEV-GFFVPLTIIGDIRPEHRL 882
Cdd:PRK13473 295 DLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGhiRVVTGGEAPDGkGYYYEPTLLAGARQDDEI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 883 AQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLnrNCTGALVGRQPFGGFRLSGA 962
Cdd:PRK13473 375 VQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWV--NTHFMLVSEMPHGGQKQSGY 452
|
.
gi 221564986 963 G 963
Cdd:PRK13473 453 G 453
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
525-982 |
1.52e-70 |
|
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: 242.25 E-value: 1.52e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 525 SMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFE--TWRDiTPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAY 602
Cdd:cd07120 1 SIDPAT-GEVIGTYADGGVAEAEAAIAAARRAFDetDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 603 ADVTEAIDFLEYYArEMIRLGSPRSMGKVAGETNQYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTS 682
Cdd:cd07120 79 FEISGAISELRYYA-GLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 683 IIGWQLVDIFREV-GLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAKvqpgqeMVKKVICEMGGK 761
Cdd:cd07120 158 QINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAP------TLKRLGLELGGK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 762 NAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQKR 841
Cdd:cd07120 232 TPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 842 IMNYIEVGRQEGR--LLYQGHVPEV---GFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTG 916
Cdd:cd07120 312 VDRMVERAIAAGAevVLRGGPVTEGlakGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221564986 917 GLFSRSPEHIAIATKRFRVGNLYLNRNctGALVGRQPFGGFRLSGAGtKAGGPDYLLHFMDPRVVT 982
Cdd:cd07120 392 SVWTRDLARAMRVARAIRAGTVWINDW--NKLFAEAEEGGYRQSGLG-RLHGVAALEDFIEYKHIY 454
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
545-961 |
1.27e-68 |
|
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: 236.01 E-value: 1.27e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 545 EVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQ-WDQAyadvTEA------IDFLEYYAR 617
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPlWEAQ----TEVaamagkIDISIKAYH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 618 EmiRLGSPR-SMGKVAGETNqyfYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVG 696
Cdd:cd07095 77 E--RTGERAtPMAQGRAVLR---HRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 697 LPDGVFNFVPGrSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAKvQPGqemvKKVICEMGGKNAIIIDDDADLDEAV 776
Cdd:cd07095 152 LPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAG-RPG----KILALEMGGNNPLVVWDVADIDAAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 777 PHVFNSAFGFQGQKCSACSRVIVLDGIY-DKFVQRLTALAEAVPVG-PVEDPANLIGAVAEENAQKRIMNYIEVGRQEGR 854
Cdd:cd07095 226 YLIVQSAFLTAGQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGaPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 855 LLYQGH-VPEVGFFVPLTIIgDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRF 933
Cdd:cd07095 306 PLLAMErLVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARI 384
|
410 420
....*....|....*....|....*...
gi 221564986 934 RVGNLYLNRNCTGAlVGRQPFGGFRLSG 961
Cdd:cd07095 385 RAGIVNWNRPTTGA-SSTAPFGGVGLSG 411
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
533-982 |
8.95e-67 |
|
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: 231.03 E-value: 8.95e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 533 EIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADVTEAIDFL 612
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 613 eyyaREMIRLGSpRSMGKV----AGETNQYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQL 688
Cdd:cd07152 82 ----HEAAGLPT-QPQGEIlpsaPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 689 V-DIFREVGLPDGVFNFVPGRSGImGDYLVDHPHVSLIAFTGSMEVGLRIIERAAKvqpgqeMVKKVICEMGGKNAIIID 767
Cdd:cd07152 157 IaRLFEEAGLPAGVLHVLPGGADA-GEALVEDPNVAMISFTGSTAVGRKVGEAAGR------HLKKVSLELGGKNALIVL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 768 DDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVG-PVEDPANLiGAVAEENAQKRIMNYI 846
Cdd:cd07152 230 DDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGdPATGQVAL-GPLINARQLDRVHAIV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 847 EVGRQEGRLLYQGHVPEVGFFVPlTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEHI 926
Cdd:cd07152 309 DDSVAAGARLEAGGTYDGLFYRP-TVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRA 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 221564986 927 AIATKRFRVGNLYLNrNCTGALVGRQPFGGFRLSGAGTKAGGPDYLLHFMDPRVVT 982
Cdd:cd07152 388 MALADRLRTGMLHIN-DQTVNDEPHNPFGGMGASGNGSRFGGPANWEEFTQWQWVT 442
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
530-967 |
9.44e-67 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 232.79 E-value: 9.44e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 530 DP--SEIVGWVCQAGTDEVAQAIGAARKSFE--TWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQA-YAD 604
Cdd:PLN02766 42 DPrtGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGkAVD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 605 VTEAIDFLEYYA--REMIRLGSPRSMGKVAGETnqyFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTS 682
Cdd:PLN02766 122 IPAAAGLLRYYAgaADKIHGETLKMSRQLQGYT---LKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 683 IIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAKVQpgqemVKKVICEMGGKN 762
Cdd:PLN02766 199 LSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSN-----LKQVSLELGGKS 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 763 AIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQKRI 842
Cdd:PLN02766 274 PLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKI 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 843 MNYIEVGRQEGRLLYQGHVP--EVGFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFS 920
Cdd:PLN02766 354 LSYIEHGKREGATLLTGGKPcgDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVT 433
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 221564986 921 RSPEHIAIATKRFRVGNLYLnrNCTGALVGRQPFGGFRLSGAGTKAG 967
Cdd:PLN02766 434 KDLDVANTVSRSIRAGTIWV--NCYFAFDPDCPFGGYKMSGFGRDQG 478
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
511-986 |
3.15e-66 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 231.50 E-value: 3.15e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 511 FIGGQELETED--LLPSMNPSDPSEIVGWVCQaGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSA 588
Cdd:PLN02278 28 LIGGKWTDAYDgkTFPVYNPATGEVIANVPCM-GRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 589 LQVLEIGKQWDQAYADVTEAIDFLEYYAREMIR-----LGSPRSMGKVAGeTNQyfyePKGVAAVIAPWNFPLAISMGMV 663
Cdd:PLN02278 107 LMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRvygdiIPSPFPDRRLLV-LKQ----PVGVVGAITPWNFPLAMITRKV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 664 SAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAK 743
Cdd:PLN02278 182 GPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 744 VqpgqemVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPV 823
Cdd:PLN02278 262 T------VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 824 EDPANLIGAVAEENAQKRIMNYIEVGRQEG-RLLYQGHVPEVG--FFVPlTIIGDIRPEHRLAQEEIFGPLLAVMRARDF 900
Cdd:PLN02278 336 FEEGVTQGPLINEAAVQKVESHVQDAVSKGaKVLLGGKRHSLGgtFYEP-TVLGDVTEDMLIFREEVFGPVAPLTRFKTE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 901 NEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNRNCTGALVGrqPFGGFRLSGAGtKAGGPDYLLHFMDPRV 980
Cdd:PLN02278 415 EEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA--PFGGVKQSGLG-REGSKYGIDEYLEIKY 491
|
....*.
gi 221564986 981 VTENTM 986
Cdd:PLN02278 492 VCLGNM 497
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
510-982 |
1.01e-65 |
|
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: 229.25 E-value: 1.01e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 510 LFIGGQEL--ETEDLLPSMNPSDPSEIvGWVCQAGTDEVAQAIGAARKSFET-WRDITPEIRAEFLLKACTVVRRRIYEL 586
Cdd:cd07113 2 HFIDGRPVagQSEKRLDITNPATEQVI-ASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 587 SALQVLEIGKQWDQAYA-DVTEAIDFLEYYAR-------EMIRLGSPrSMGkvaGETNQYFY--EPKGVAAVIAPWNFPL 656
Cdd:cd07113 81 AQLETLCSGKSIHLSRAfEVGQSANFLRYFAGwatkingETLAPSIP-SMQ---GERYTAFTrrEPVGVVAGIVPWNFSV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 657 AISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGrSGIMGDYLVDHPHVSLIAFTGSMEVGLR 736
Cdd:cd07113 157 MIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNG-KGAVGAQLISHPDVAKVSFTGSVATGKK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 737 IIERAAkvqpgqEMVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAE 816
Cdd:cd07113 236 IGRQAA------SDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 817 AVPVGPVEDPANLIGAVAEENAQKRIMNYIEVGRQEG-RLLYQGH-VPEVGFFVPLTIIGDIRPEHRLAQEEIFGPLLAV 894
Cdd:cd07113 310 SFQVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGdEIVRGGEaLAGEGYFVQPTLVLARSADSRLMREETFGPVVSF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 895 MRARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNRNCTgaLVGRQPFGGFRLSGAGtKAGGPDYLLH 974
Cdd:cd07113 390 VPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTF--LDPAVPFGGMKQSGIG-REFGSAFIDD 466
|
....*...
gi 221564986 975 FMDPRVVT 982
Cdd:cd07113 467 YTELKSVM 474
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
545-963 |
1.02e-64 |
|
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: 225.15 E-value: 1.02e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 545 EVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADVTEAIDFLEYYArEMIRLGS 624
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAA-SLITQII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 625 PRSMGKVAGETNQY-FYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFN 703
Cdd:cd07105 80 GGSIPSDKPGTLAMvVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 704 FV---PGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAKvqpgqeMVKKVICEMGGKNAIIIDDDADLDEAVPHVF 780
Cdd:cd07105 160 VVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK------HLKPVLLELGGKAPAIVLEDADLDAAANAAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 781 NSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPAnLIGAVAEENAQKRIMNYIEVGrqeGRLLYQGH 860
Cdd:cd07105 234 FGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVLGS-LVSAAAADRVKELVDDALSKG---AKLVVGGL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 861 VPEV--GFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEH-IAIAtKRFRVGN 937
Cdd:cd07105 310 ADESpsGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARaLAVA-KRIESGA 388
|
410 420
....*....|....*....|....*....
gi 221564986 938 LYLNrnctGALVGRQ---PFGGFRLSGAG 963
Cdd:cd07105 389 VHIN----GMTVHDEptlPHGGVKSSGYG 413
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
527-963 |
7.48e-64 |
|
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: 223.46 E-value: 7.48e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 527 NPSDpSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADVT 606
Cdd:cd07094 5 NPYD-GEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 607 EAIDFLEYYAREMIRL-GSPRSMGKVAGETNQYFY---EPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTS 682
Cdd:cd07094 84 RAIDTLRLAAEEAERIrGEEIPLDATQGSDNRLAWtirEPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 683 IIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAKvqpgqemvKKVICEMGGKN 762
Cdd:cd07094 164 LSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGG--------KRIALELGGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 763 AIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQKRI 842
Cdd:cd07094 236 PVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 843 MNYIEVGRQEGRLLYQGHVPEVGFFVPlTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRS 922
Cdd:cd07094 316 ERWVEEAVEAGARLLCGGERDGALFKP-TVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRD 394
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 221564986 923 PEHIAIATKRFRVGNLYLNrNCTGALVGRQPFGGFRLSGAG 963
Cdd:cd07094 395 LNVAFKAAEKLEVGGVMVN-DSSAFRTDWMPFGGVKESGVG 434
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
523-981 |
9.55e-63 |
|
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: 220.19 E-value: 9.55e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 523 LPSMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAY 602
Cdd:cd07147 1 LEVTNPYT-GEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 603 ADVTEAIDFLEYYAREMIRLG--------SPRSMGKVaGETNQYfyePKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVV 674
Cdd:cd07147 80 GEVARAIDTFRIAAEEATRIYgevlpldiSARGEGRQ-GLVRRF---PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 675 FKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMgDYLVDHPHVSLIAFTGSMEVGLRIIERAAKvqpgqemvKKV 754
Cdd:cd07147 156 LKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDDA-DLLVTDERIKLLSFTGSPAVGWDLKARAGK--------KKV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 755 ICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVA 834
Cdd:cd07147 227 VLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 835 EENAQKRIMNYIEVGRQEGRLLYQGHVPEVGFFVPlTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYAL 914
Cdd:cd07147 307 SESEAERVEGWVNEAVDAGAKLLTGGKRDGALLEP-TILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGL 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221564986 915 TGGLFSRSPEHIAIATKRFRVGNLYLN-----RnctgalVGRQPFGGFRLSGAGTKagGPDYLLHFM-DPRVV 981
Cdd:cd07147 386 QAGVFTRDLEKALRAWDELEVGGVVINdvptfR------VDHMPYGGVKDSGIGRE--GVRYAIEEMtEPRLL 450
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
527-967 |
8.74e-62 |
|
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: 217.61 E-value: 8.74e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 527 NPSDpSEIVGWVCQAGTDEVAQAIGAARKSFETwrdITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADVT 606
Cdd:cd07146 5 NPYT-GEVVGTVPAGTEEALREALALAASYRST---LTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 607 EAIDFLEYYAREMIRL-GSPRSMGKVAGETNQYFY---EPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTS 682
Cdd:cd07146 81 RAADVLRFAAAEALRDdGESFSCDLTANGKARKIFtlrEPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 683 IIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAkvqpgqemVKKVICEMGGKN 762
Cdd:cd07146 161 LSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--------YKRQLLELGGND 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 763 AIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQKRI 842
Cdd:cd07146 233 PLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 843 MNYIEVGRQEG-RLLYqGHVpEVGFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSR 921
Cdd:cd07146 313 ENRVEEAIAQGaRVLL-GNQ-RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTN 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 221564986 922 SPEHIAIATKRFRVGNLYLNrNCTGALVGRQPFGGFRLSGAGTKAG 967
Cdd:cd07146 391 DLDTIKRLVERLDVGTVNVN-EVPGFRSELSPFGGVKDSGLGGKEG 435
|
|
| ABALDH |
TIGR03374 |
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1. ... |
507-976 |
3.98e-61 |
|
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1.35), also called gamma-aminobutyraldehyde dehydrogenase. This enzyme can follow putrescine transaminase (EC 2.6.1.82) for a two-step conversion of putrescine to gamma-aminobutyric acid (GABA). The member from Escherichia coli is characterized as a homotetramer that binds one NADH per momomer. This enzyme belongs to the medium-chain aldehyde dehydrogenases, and is quite similar in sequence to the betaine aldehyde dehydrogenase (EC 1.2.1.8) family.
Pssm-ID: 132417 Cd Length: 472 Bit Score: 216.40 E-value: 3.98e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 507 KYPLFIGGQELETE-DLLPSMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYE 585
Cdd:TIGR03374 1 QHKLLINGELVSGEgEKQPVYNPAT-GEVILEIAEASAEQVDAAVRAADAAFAEWGQTTPKARAECLLKLADVIEENAQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 586 LSALQVLEIGKQWDQAYADVTEAI-DFLEYYAremirlGSPRSM-GKVAGE-----TNQYFYEPKGVAAVIAPWNFPLAI 658
Cdd:TIGR03374 80 FAELESRNCGKPLHSVFNDEIPAIvDVFRFFA------GAARCLsGLAAGEyleghTSMIRRDPLGVVASIAPWNYPLMM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 659 SMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVgLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRII 738
Cdd:TIGR03374 154 AAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVVNILFGRGKTVGDPLTGHEKVRMVSLTGSIATGEHIL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 739 ERAAKVqpgqemVKKVICEMGGKNAIIIDDDADLDEAVPHVfnSAFGF--QGQKCSACSRVIVLDGIYDKFVQRLTALAE 816
Cdd:TIGR03374 233 SHTAPS------IKRTHMELGGKAPVIVFDDADIDAVVEGV--RTFGFynAGQDCTAACRIYAQRGIYDTLVEKLGAAVA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 817 AVPVGPVEDPANLIGAVAEENAQKRIMNYIEVGRQEG--RLLYQG-HVPEVGFFVPLTIIGDIRPEHRLAQEEIFGPLLA 893
Cdd:TIGR03374 305 TLKSGAPDDESTELGPLSSLAHLERVMKAVEEAKALGhiKVITGGeKRKGNGYYFAPTLLAGAKQDDAIVQKEVFGPVVS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 894 VMRARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNRNCTgaLVGRQPFGGFRLSGAGTKA---GGPD 970
Cdd:TIGR03374 385 ITSFDDEEQVVNWANDSQYGLASSVWTKDVGRAHRLSARLQYGCTWVNTHFM--LVSEMPHGGQKLSGYGKDMslyGLED 462
|
....*...
gi 221564986 971 YLL--HFM 976
Cdd:TIGR03374 463 YTVvrHIM 470
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
572-981 |
5.42e-61 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 213.83 E-value: 5.42e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 572 LLKACTVVRRRIYELSALQVLEIGKQWDQAYADVTEAIDFLEYYArEMIRlgspRSMGKV-----AGETNQYFYEPKGVA 646
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMA-EWAR----RYEGEIiqsdrPGENILLFKRALGVT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 647 AVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIA 726
Cdd:PRK10090 76 TGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 727 FTGSMEVGLRIIERAAKvqpgqeMVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDK 806
Cdd:PRK10090 156 MTGSVSAGEKIMAAAAK------NITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 807 FVQRLTALAEAVPVG-PVEDPANLIGAVAEENAQKRIMNYIEVGRQEGRLLYQG--HVPEVGFFVPLTIIGDIRPEHRLA 883
Cdd:PRK10090 230 FVNRLGEAMQAVQFGnPAERNDIAMGPLINAAALERVEQKVARAVEEGARVALGgkAVEGKGYYYPPTLLLDVRQEMSIM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 884 QEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNRNCTGALvgrQPF-GGFRLSGA 962
Cdd:PRK10090 310 HEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAM---QGFhAGWRKSGI 386
|
410
....*....|....*....
gi 221564986 963 GtKAGGPDYLLHFMDPRVV 981
Cdd:PRK10090 387 G-GADGKHGLHEYLQTQVV 404
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
546-963 |
1.21e-60 |
|
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: 213.48 E-value: 1.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 546 VAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADVTEAIDFLEYYAREMIRLGSP 625
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 626 RSMgKVAGETNQYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVF-NF 704
Cdd:cd07100 81 EPI-ETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFqNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 705 VPGRSGImgDYLVDHPHVSLIAFTGSMEVGLRIIERAAKvqpgqeMVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAF 784
Cdd:cd07100 160 LIDSDQV--EAIIADPRVRGVTLTGSERAGRAVAAEAGK------NLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 785 GFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQKRIMNYIEVGRQEG-RLLYQGHVPE 863
Cdd:cd07100 232 QNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGaTLLLGGKRPD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 864 -VGFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNr 942
Cdd:cd07100 312 gPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFIN- 390
|
410 420
....*....|....*....|....
gi 221564986 943 nctgALVG---RQPFGGFRLSGAG 963
Cdd:cd07100 391 ----GMVKsdpRLPFGGVKRSGYG 410
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
508-963 |
9.15e-60 |
|
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: 212.70 E-value: 9.15e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 508 YPLFIGGQELETedlLPSMNPSDPSEIVGWV-CQA---GTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRI 583
Cdd:cd07116 1 YDNFIGGEWVAP---VKGEYFDNITPVTGKVfCEVprsTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 584 YELSALQVLEIGKQWDQAY-ADVTEAIDFLEYYArEMIRlGSPRSMGKVAGETNQY-FYEPKGVAAVIAPWNFPLAISMG 661
Cdd:cd07116 78 EMLAVAETWDNGKPVRETLaADIPLAIDHFRYFA-GCIR-AQEGSISEIDENTVAYhFHEPLGVVGQIIPWNFPLLMATW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 662 MVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVgLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERA 741
Cdd:cd07116 156 KLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 742 AkvqpgqEMVKKVICEMGGKNaiiidddadldeavPHVF-------NSAF------GF------QGQKCSACSRVIVLDG 802
Cdd:cd07116 235 S------ENIIPVTLELGGKS--------------PNIFfadvmdaDDAFfdkaleGFvmfalnQGEVCTCPSRALIQES 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 803 IYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQKRIMNYIEVGRQEGRLLYQG-------HVPEVGFFVPLTIIGD 875
Cdd:cd07116 295 IYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGgernelgGLLGGGYYVPTTFKGG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 876 IRpeHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLnrNCTGALVGRQPFG 955
Cdd:cd07116 375 NK--MRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWT--NCYHLYPAHAAFG 450
|
....*...
gi 221564986 956 GFRLSGAG 963
Cdd:cd07116 451 GYKQSGIG 458
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
510-967 |
3.51e-59 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 212.36 E-value: 3.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 510 LFIGGQELE--TEDLLPSMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFET--WRDITPEIRAEFLLKACTVVRRRIYE 585
Cdd:PLN02466 60 LLINGQFVDaaSGKTFPTLDPRT-GEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 586 LSALQVLEIGKQWDQ-AYADVTEAIDFLEYYAremirlgsprsmG---KVAGETN--------QYFYEPKGVAAVIAPWN 653
Cdd:PLN02466 139 LAALETWDNGKPYEQsAKAELPMFARLFRYYA------------GwadKIHGLTVpadgphhvQTLHEPIGVAGQIIPWN 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 654 FPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEV 733
Cdd:PLN02466 207 FPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDT 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 734 GLRIIERAAKVQpgqemVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTA 813
Cdd:PLN02466 287 GKIVLELAAKSN-----LKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 814 LAEAVPVGpveDPanlIGAVAEENAQ------KRIMNYIEVGRQEGRLLYQG--HVPEVGFFVPLTIIGDIRPEHRLAQE 885
Cdd:PLN02466 362 RALKRVVG---DP---FKKGVEQGPQidseqfEKILRYIKSGVESGATLECGgdRFGSKGYYIQPTVFSNVQDDMLIAQD 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 886 EIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLnrNCTGALVGRQPFGGFRLSGAGTK 965
Cdd:PLN02466 436 EIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWV--NCFDVFDAAIPFGGYKMSGIGRE 513
|
..
gi 221564986 966 AG 967
Cdd:PLN02466 514 KG 515
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
533-983 |
5.67e-59 |
|
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: 209.47 E-value: 5.67e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 533 EIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADVTEAIDFL 612
Cdd:cd07101 7 EPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 613 EYYAREMIRLGSPRsmgKVAG-----ETNQYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQ 687
Cdd:cd07101 87 RYYARRAERLLKPR---RRRGaipvlTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 688 LVDIFREVGLPDGVFNFVPGRSGIMGDYLVDhpHVSLIAFTGSMEVGLRIIERAAKVQPGQEMvkkvicEMGGKNAIIID 767
Cdd:cd07101 164 AVELLIEAGLPRDLWQVVTGPGSEVGGAIVD--NADYVMFTGSTATGRVVAERAGRRLIGCSL------ELGGKNPMIVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 768 DDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQKRIMNYIE 847
Cdd:cd07101 236 EDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 848 VGRQEG-RLLYQGH-VPEVG--FFVPlTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSP 923
Cdd:cd07101 316 DAVAKGaTVLAGGRaRPDLGpyFYEP-TVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDG 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221564986 924 EHIAIATKRFRVGNLYLNRNCTGALVGRQ-PFGGFRLSGAGTKAgGPDYLLHFMDPRVVTE 983
Cdd:cd07101 395 ARGRRIAARLRAGTVNVNEGYAAAWASIDaPMGGMKDSGLGRRH-GAEGLLKYTETQTVAV 454
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
510-963 |
2.82e-58 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 208.60 E-value: 2.82e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 510 LFIGGQELETED--LLPSMNPSDPSEIVGwVCQAGTDEVAQAIGAARKSFET--WRDITPEIRAEFLLKACTVVRRRIYE 585
Cdd:PRK09847 22 LFINGEYTAAAEneTFETVDPVTQAPLAK-IARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 586 LSALQVLEIGKQWDQAYAD-VTEAIDFLEYYAREMIRLgsprsMGKVA----GETNQYFYEPKGVAAVIAPWNFPLAISM 660
Cdd:PRK09847 101 LALLETLDTGKPIRHSLRDdIPGAARAIRWYAEAIDKV-----YGEVAttssHELAMIVREPVGVIAAIVPWNFPLLLTC 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 661 GMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIER 740
Cdd:PRK09847 176 WKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 741 AakvqpGQEMVKKVICEMGGKNAIIIDDD-ADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVP 819
Cdd:PRK09847 256 A-----GDSNMKRVWLEAGGKSANIVFADcPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 820 VGPVEDPANLIGAVAEENAQKRIMNYIEVGRQEGRLLY----QGHVPEVGffvPlTIIGDIRPEHRLAQEEIFGPLLAVM 895
Cdd:PRK09847 331 PGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLdgrnAGLAAAIG---P-TIFVDVDPNASLSREEIFGPVLVVT 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221564986 896 RARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNRNCTGALVgrQPFGGFRLSGAG 963
Cdd:PRK09847 407 RFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMT--VPFGGYKQSGNG 472
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
508-982 |
5.20e-58 |
|
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: 207.73 E-value: 5.20e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 508 YPLFIGGQELETED--LLPSMNPSDPSEIVGwVCQAGTDEVAQAIGAARKSFET--WRDITPEIRAEFLLKACTVVRRRI 583
Cdd:cd07140 6 HQLFINGEFVDAEGgkTYNTINPTDGSVICK-VSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 584 YELSALQVLEIGKQWDQAY-ADVTEAIDFLEYYAREMIRL-GSPRSMGKVAGETNQYFY--EPKGVAAVIAPWNFPLAIS 659
Cdd:cd07140 85 EELATIESLDSGAVYTLALkTHVGMSIQTFRYFAGWCDKIqGKTIPINQARPNRNLTLTkrEPIGVCGIVIPWNYPLMML 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 660 MGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIE 739
Cdd:cd07140 165 AWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 740 RAAKVQpgqemVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVP 819
Cdd:cd07140 245 SCAVSN-----LKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 820 VGpveDPANLIGAVAEENAQK---RIMNYIEVGRQEG-RLLYQG-HVPEVGFFVPLTIIGDIRPEHRLAQEEIFGPLLAV 894
Cdd:cd07140 320 IG---DPLDRSTDHGPQNHKAhldKLVEYCERGVKEGaTLVYGGkQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMII 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 895 MRAR--DFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNR-NCTGAlvgRQPFGGFRLSGAGtKAGGPDY 971
Cdd:cd07140 397 SKFDdgDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTyNKTDV---AAPFGGFKQSGFG-KDLGEEA 472
|
490
....*....|.
gi 221564986 972 LLHFMDPRVVT 982
Cdd:cd07140 473 LNEYLKTKTVT 483
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
510-961 |
1.16e-57 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 206.73 E-value: 1.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 510 LFIGGQELE-TEDLLPSMNPSDpSEIVgWVCQAGT-DEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELS 587
Cdd:PRK09457 3 LWINGDWIAgQGEAFESRNPVS-GEVL-WQGNDATaAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 588 ALQVLEIGK-QWDQAyadvTE--------AIDFLEYYARemirlgSPRSMGKVAGETNQYFYEPKGVAAVIAPWNFPLAI 658
Cdd:PRK09457 81 EVIARETGKpLWEAA----TEvtaminkiAISIQAYHER------TGEKRSEMADGAAVLRHRPHGVVAVFGPYNFPGHL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 659 SMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGiMGDYLVDHPHVSLIAFTGSMEVGLRII 738
Cdd:PRK09457 151 PNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRE-TGKALAAHPDIDGLLFTGSANTGYLLH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 739 ERAAKvQPGqemvKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIY-DKFVQRLTALAEA 817
Cdd:PRK09457 230 RQFAG-QPE----KILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 818 VPVG-PVEDPANLIGAVAEENAQKRIM----NYIEVGrqeGRLLYQGHVPEVGF-FVPLTIIgDIRPEHRLAQEEIFGPL 891
Cdd:PRK09457 305 LTVGrWDAEPQPFMGAVISEQAAQGLVaaqaQLLALG---GKSLLEMTQLQAGTgLLTPGII-DVTGVAELPDEEYFGPL 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 892 LAVMRARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNRNCTGAlVGRQPFGGFRLSG 961
Cdd:PRK09457 381 LQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGA-SSAAPFGGVGASG 449
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
511-972 |
5.43e-57 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 204.76 E-value: 5.43e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 511 FIGGQELETE--DLLPSMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSA 588
Cdd:PRK11241 14 LINGEWLDANngEVIDVTNPAN-GDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLAR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 589 LQVLEIGKQWDQAYADVTEAIDFLEYYAREMIRLGSPRSMGKVAGETNQYFYEPKGVAAVIAPWNFPLAISMGMVSAAIV 668
Cdd:PRK11241 93 LMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 669 TGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAKvqpgq 748
Cdd:PRK11241 173 AGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAK----- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 749 eMVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPAN 828
Cdd:PRK11241 248 -DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 829 LIGAVAEENAQKRIMNYIEVGRQEG-RLLYQGHVPEVG--FFVPlTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALV 905
Cdd:PRK11241 327 TIGPLIDEKAVAKVEEHIADALEKGaRVVCGGKAHELGgnFFQP-TILVDVPANAKVAKEETFGPLAPLFRFKDEADVIA 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221564986 906 WANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNrncTGALVGR-QPFGGFRLSG---AGTKAGGPDYL 972
Cdd:PRK11241 406 QANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGIN---TGIISNEvAPFGGIKASGlgrEGSKYGIEDYL 473
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
542-984 |
6.76e-54 |
|
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: 195.21 E-value: 6.76e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 542 GTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGK-QWDQAYADVTEAIDFLEYYAREMI 620
Cdd:cd07098 16 TPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKtMVDASLGEILVTCEKIRWTLKHGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 621 RLGSP--RSMGKVAG-ETNQYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREV-- 695
Cdd:cd07098 96 KALRPesRPGGLLMFyKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIRECla 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 696 --GLPDGVFNFVPGRSGImGDYLVDHPHVSLIAFTGSMEVGLRIIERAAkvqpgqEMVKKVICEMGGKNAIIIDDDADLD 773
Cdd:cd07098 176 acGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAA------ESLTPVVLELGGKDPAIVLDDADLD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 774 EAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQKRIMNYIEVGRQEG 853
Cdd:cd07098 249 QIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 854 -RLLYQGH------VPEVGFFVPlTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEHI 926
Cdd:cd07098 329 aRLLAGGKryphpeYPQGHYFPP-TLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRA 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 221564986 927 AIATKRFRVGNLYLNRNCTGALVGRQPFGGFRLSGAGtKAGGPDYLLHFMDPRVVTEN 984
Cdd:cd07098 408 RRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFG-RFAGEEGLRGLCNPKSVTED 464
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
521-926 |
1.58e-53 |
|
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: 194.35 E-value: 1.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 521 DLLPSMNPSDPSEIVGwVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQ 600
Cdd:cd07130 12 GVVTSISPANGEPIAR-VRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 601 AYADVTEAIDFLEYyaremiRLGSPRSM-GKV-AGE-TNQYFYE---PKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVV 674
Cdd:cd07130 91 GLGEVQEMIDICDF------AVGLSRQLyGLTiPSErPGHRMMEqwnPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 675 FKPS---GLTSIIGWQLV-DIFREVGLPDGVFNFVPGrSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAakvqpgQEM 750
Cdd:cd07130 165 WKPSpttPLTAIAVTKIVaRVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAV------AAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 751 VKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLI 830
Cdd:cd07130 238 FGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 831 GAVAEENAQKRIMNYIEVGR-QEGRLLYQGHVPEV-GFFVPLTIIgDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWAN 908
Cdd:cd07130 318 GPLHTKAAVDNYLAAIEEAKsQGGTVLFGGKVIDGpGNYVEPTIV-EGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNN 396
|
410
....*....|....*...
gi 221564986 909 STRYALTGGLFSRSPEHI 926
Cdd:cd07130 397 EVPQGLSSSIFTTDLRNA 414
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
541-942 |
6.44e-53 |
|
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: 192.08 E-value: 6.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 541 AGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAyadvTEAIDFLEYYAREMI 620
Cdd:cd07102 15 ASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQA----GGEIRGMLERARYMI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 621 RLgSPRSMGKVAGETNQYF-----YEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREV 695
Cdd:cd07102 91 SI-AEEALADIRVPEKDGFeryirREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 696 GLPDGVFNFVPGRSGIMGDyLVDHPHVSLIAFTGSMEVGLRiIERAAkvqpgQEMVKKVICEMGGKNAIIIDDDADLDEA 775
Cdd:cd07102 170 GLPEGVFQVLHLSHETSAA-LIADPRIDHVSFTGSVAGGRA-IQRAA-----AGRFIKVGLELGGKDPAYVRPDADLDAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 776 VPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQKRIMNYIEVGRQEG-R 854
Cdd:cd07102 243 AESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGaR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 855 LLYQGHV----PEVGFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEH-IAIA 929
Cdd:cd07102 323 ALIDGALfpedKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARaEALG 402
|
410
....*....|...
gi 221564986 930 TkRFRVGNLYLNR 942
Cdd:cd07102 403 E-QLETGTVFMNR 414
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
533-983 |
7.57e-52 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 190.86 E-value: 7.57e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 533 EIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADVTEAIDFL 612
Cdd:PRK09407 43 EPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLDVALTA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 613 EYYAREMIRLGSPR---SMGKVAGETNQYfYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLV 689
Cdd:PRK09407 123 RYYARRAPKLLAPRrraGALPVLTKTTEL-RQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAV 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 690 DIFREVGLPDGVFNFVPGRSGIMGDYLVDhpHVSLIAFTGSMEVGLRIIERAAKVQPGqemvkkviC--EMGGKNAIIID 767
Cdd:PRK09407 202 ELLYEAGLPRDLWQVVTGPGPVVGTALVD--NADYLMFTGSTATGRVLAEQAGRRLIG--------FslELGGKNPMIVL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 768 DDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQKRIMNYIE 847
Cdd:PRK09407 272 DDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVD 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 848 VGRQEG-RLLYQGHV-PEVG--FFVPlTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSP 923
Cdd:PRK09407 352 DAVAKGaTVLAGGKArPDLGplFYEP-TVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDT 430
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221564986 924 EH-IAIATkRFRVGNLYLNRNCTGALVGRQ-PFGGFRLSGAGTKAgGPDYLLHFMDPRVVTE 983
Cdd:PRK09407 431 ARgRAIAA-RIRAGTVNVNEGYAAAWGSVDaPMGGMKDSGLGRRH-GAEGLLKYTESQTIAT 490
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
540-965 |
3.24e-47 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 176.87 E-value: 3.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 540 QAGT-DEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADVTEAIDFLEYYARE 618
Cdd:PLN00412 48 QACTqEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 619 MIRLgspRSMGKV-------AGETNQYFYE---PKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQL 688
Cdd:PLN00412 128 GVRI---LGEGKFlvsdsfpGNERNKYCLTskiPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHM 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 689 VDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSmEVGLRIIERAAKVqPGQemvkkviCEMGGKNAIIIDD 768
Cdd:PLN00412 205 VHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIAISKKAGMV-PLQ-------MELGGKDACIVLE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 769 DADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANlIGAVAEENAQKRIMNYIEV 848
Cdd:PLN00412 276 DADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDDCD-ITPVVSESSANFIEGLVMD 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 849 GRQEGRLLYQGHVPEVGFFVPLtIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEHIAI 928
Cdd:PLN00412 355 AKEKGATFCQEWKREGNLIWPL-LLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAIL 433
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 221564986 929 ATKRFRVGNLYLNrnctgALVGRQ----PFGGFRLSGAGTK 965
Cdd:PLN00412 434 ISDAMETGTVQIN-----SAPARGpdhfPFQGLKDSGIGSQ 469
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
541-963 |
1.26e-45 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 171.07 E-value: 1.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 541 AGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADVTEAIDFLEYYAR--E 618
Cdd:PRK09406 20 LTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYYAEhaE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 619 MIRLGSPRSMGKVAGETNQYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLP 698
Cdd:PRK09406 100 ALLADEPADAAAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRAGFP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 699 DGVFNFVPGRSGIMGDYLVDhPHVSLIAFTGSMEVGlriieRAAKVQPGQEmVKKVICEMGGKNAIIIDDDADLDEAVPH 778
Cdd:PRK09406 180 DGCFQTLLVGSGAVEAILRD-PRVAAATLTGSEPAG-----RAVAAIAGDE-IKKTVLELGGSDPFIVMPSADLDRAAET 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 779 VFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQKRIMNYIEVGRQEG-RLLY 857
Cdd:PRK09406 253 AVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAAGaTILC 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 858 QGHVPE-VGFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVG 936
Cdd:PRK09406 333 GGKRPDgPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAG 412
|
410 420
....*....|....*....|....*....
gi 221564986 937 NLYLNRNCTG--ALvgrqPFGGFRLSGAG 963
Cdd:PRK09406 413 QVFINGMTVSypEL----PFGGVKRSGYG 437
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
507-935 |
1.48e-45 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 174.16 E-value: 1.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 507 KYPLFIGGQELETED--LLPSMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIY 584
Cdd:PLN02419 113 RVPNLIGGSFVESQSssFIDVINPAT-QEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMD 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 585 ELSALQVLEIGKQWDQAYADVTEAIDFLEYyAREMIRLGSPRSMGKVAGETNQY-FYEPKGVAAVIAPWNFPLAISMGMV 663
Cdd:PLN02419 192 KLAMNITTEQGKTLKDSHGDIFRGLEVVEH-ACGMATLQMGEYLPNVSNGVDTYsIREPLGVCAGICPFNFPAMIPLWMF 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 664 SAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMgDYLVDHPHVSLIAFTGSMEVGLRIIERAAK 743
Cdd:PLN02419 271 PVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAAA 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 744 VQpgqemvKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVL---DGIYDKFVQRltalAEAVPV 820
Cdd:PLN02419 350 KG------KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVgdaKSWEDKLVER----AKALKV 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 821 GPVEDPANLIGAVAEENAQKRIMNYIEVGRQEG-RLLYQGH---VP--EVGFFVPLTIIGDIRPEHRLAQEEIFGPLLAV 894
Cdd:PLN02419 420 TCGSEPDADLGPVISKQAKERICRLIQSGVDDGaKLLLDGRdivVPgyEKGNFIGPTILSGVTPDMECYKEEIFGPVLVC 499
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 221564986 895 MRARDFNEALVWANSTRYALTGGLFSRSpehiAIATKRFRV 935
Cdd:PLN02419 500 MQANSFDEAISIINKNKYGNGAAIFTSS----GAAARKFQM 536
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
525-963 |
5.56e-42 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 160.41 E-value: 5.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 525 SMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYAD 604
Cdd:PRK13968 11 SVNPAT-GEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 605 VTEAIDFLEYYAREMIRLGSPRSmgkVAGETNQYF--YEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPS---- 678
Cdd:PRK13968 90 VAKSANLCDWYAEHGPAMLKAEP---TLVENQQAVieYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHApnvm 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 679 GLTSIIGwqlvDIFREVGLPDGVFNFV----PGRSGIMGDylvdhPHVSLIAFTGSMEVGLRIIERAAKVqpgqemVKKV 754
Cdd:PRK13968 167 GCAQLIA----QVFKDAGIPQGVYGWLnadnDGVSQMIND-----SRIAAVTVTGSVRAGAAIGAQAGAA------LKKC 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 755 ICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVA 834
Cdd:PRK13968 232 VLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 835 EENAQKRIMNYIEVGRQEG-RLLYQGH-VPEVGFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRY 912
Cdd:PRK13968 312 RFDLRDELHHQVEATLAEGaRLLLGGEkIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEF 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 221564986 913 ALTGGLFSRSPEHIAIATKRFRVGNLYLNRNCtgALVGRQPFGGFRLSGAG 963
Cdd:PRK13968 392 GLSATIFTTDETQARQMAARLECGGVFINGYC--ASDARVAFGGVKKSGFG 440
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
484-967 |
1.08e-40 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 157.69 E-value: 1.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 484 FTREEQRqaFREHIGQVRSRFGrkypLFIGGQELETEDLLPSMNPSDpSEIVGWVCQAGTDEVAQAIGAARKSFETWRDI 563
Cdd:PLN02315 3 FARKEYE--FLSEIGLSSRNLG----CYVGGEWRANGPLVSSVNPAN-NQPIAEVVEASLEDYEEGLRACEEAAKIWMQV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 564 TPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYADVTEAIDFLEYyaremiRLGSPRSM-GKV--AGETNQYFY 640
Cdd:PLN02315 76 PAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDF------AVGLSRQLnGSIipSERPNHMMM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 641 E---PKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREV----GLPDGVFNFVPGRSGImG 713
Cdd:PLN02315 150 EvwnPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTSFCGGAEI-G 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 714 DYLVDHPHVSLIAFTGSMEVGLrIIERAAKVQPGqemvkKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSA 793
Cdd:PLN02315 229 EAIAKDTRIPLVSFTGSSKVGL-MVQQTVNARFG-----KCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 794 CSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQKRIMNYIEVGR-QEGRLLYQGHVPEV-GFFVPLT 871
Cdd:PLN02315 303 CRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKsQGGKILTGGSAIESeGNFVQPT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 872 IIgDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEHIA--IATKRFRVGNLYLNRNCTGALV 949
Cdd:PLN02315 383 IV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFkwIGPLGSDCGIVNVNIPTNGAEI 461
|
490
....*....|....*...
gi 221564986 950 GrQPFGGFRLSGAGTKAG 967
Cdd:PLN02315 462 G-GAFGGEKATGGGREAG 478
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
527-976 |
8.05e-39 |
|
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: 151.03 E-value: 8.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 527 NPSDPSEIvGWVCQAGTDEVAQAIGAARKSFET---WrdITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYA 603
Cdd:cd07148 5 NPFDLKPI-GEVPTVDWAAIDKALDTAHALFLDrnnW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 604 DVTEAIDFLEYYAREMIRL-GSPRSMGKVAGETNQYFY---EPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSG 679
Cdd:cd07148 82 EVTRAIDGVELAADELGQLgGREIPMGLTPASAGRIAFttrEPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 680 LTSIIGWQLVDIFREVGLPDGVFNFVPGRSGImGDYLVDHPHVSLIAFTGSMEVGLRIierAAKVQPGqemvKKVICEMG 759
Cdd:cd07148 162 ATPLSCLAFVDLLHEAGLPEGWCQAVPCENAV-AEKLVTDPRVAFFSFIGSARVGWML---RSKLAPG----TRCALEHG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 760 GKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQ 839
Cdd:cd07148 234 GAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 840 KRIMNYIEVGRQEG-RLLYQGHVPEVGFFVPlTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGL 918
Cdd:cd07148 314 DRVEEWVNEAVAAGaRLLCGGKRLSDTTYAP-TVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAV 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221564986 919 FSRSpehIAIATKRFRvgnlylNRNCTGALVGRQ--------PFGGFRLSGAGTkaGGPDYLLHFM 976
Cdd:cd07148 393 FTKD---LDVALKAVR------RLDATAVMVNDHtafrvdwmPFAGRRQSGYGT--GGIPYTMHDM 447
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
546-981 |
1.52e-36 |
|
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: 143.92 E-value: 1.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 546 VAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAYaDVTEAIDFLEYYAR----EMIR 621
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAE-NICGDQVQLRARAFviysYRIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 622 LGSPRSMGKVAGETNQYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVG-LPDG 700
Cdd:cd07084 80 HEPGNHLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 701 VFNFVPGrSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAKVQpgqemvkkVICEMGGKNAIIIDDDADLDEAVP-HV 779
Cdd:cd07084 160 DVTLING-DGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQAR--------IYLELAGFNWKVLGPDAQAVDYVAwQC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 780 FNSAFGFQGQKCSACSRVIVL-DGIYDKFVQRLTALAEAVP-----VGPVEDPANLIGAVAEENAQKRIMNY--IEVGRQ 851
Cdd:cd07084 231 VQDMTACSGQKCTAQSMLFVPeNWSKTPLVEKLKALLARRKledllLGPVQTFTTLAMIAHMENLLGSVLLFsgKELKNH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 852 EGRLLYQGHVPEvGFFVPltiIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRY--ALTGGLFSRSPEHI-AI 928
Cdd:cd07084 311 SIPSIYGACVAS-ALFVP---IDEILKTYELVTEEIFGPFAIVVEYKKDQLALVLELLERMhgSLTAAIYSNDPIFLqEL 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 221564986 929 ATKRFRVGNLY-LNRNCTGALVGRQPFGGFRLSGAGTKAGGPDYLLHFMDPRVV 981
Cdd:cd07084 387 IGNLWVAGRTYaILRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIKLVWRCHAE 440
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
641-963 |
5.72e-35 |
|
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: 139.28 E-value: 5.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 641 EPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREvGLPDGVFNFVPGRSGIMGdYLVDHp 720
Cdd:cd07135 107 EPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPK-YLDPDAFQVVQGGVPETT-ALLEQ- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 721 HVSLIAFTGSMEVGlRII-ERAAK-VQPgqemvkkVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSRVI 798
Cdd:cd07135 184 KFDKIFYTGSGRVG-RIIaEAAAKhLTP-------VTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 799 VLDGIYDKFVQRL-TALAEAVPVGPVEDPAnlIGAVAEENAQKRIMNYIEvgRQEGRLLYQGHVPEVGFFVPLTIIGDIR 877
Cdd:cd07135 256 VDPSVYDEFVEELkKVLDEFYPGGANASPD--YTRIVNPRHFNRLKSLLD--TTKGKVVIGGEMDEATRFIPPTIVSDVS 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 878 PEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNRNCTGALVGRQPFGGF 957
Cdd:cd07135 332 WDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNAPFGGV 411
|
....*.
gi 221564986 958 RLSGAG 963
Cdd:cd07135 412 GDSGYG 417
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
547-968 |
3.50e-34 |
|
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: 136.59 E-value: 3.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 547 AQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQwdQAYADVTE----------AIDFLEYYA 616
Cdd:cd07134 1 RRVFAAQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKP--AAEVDLTEilpvlseinhAIKHLKKWM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 617 REMiRLGSPRSMgkvAGETNQYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVG 696
Cdd:cd07134 79 KPK-RVRTPLLL---FGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 697 LPDGVFNFVpgrsgimGDYLV---------DHphvslIAFTGSMEVGLRIIERAAKvqpgqeMVKKVICEMGGKNAIIID 767
Cdd:cd07134 155 DEDEVAVFE-------GDAEVaqallelpfDH-----IFFTGSPAVGKIVMAAAAK------HLASVTLELGGKSPTIVD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 768 DDADLDEAVPHVFNSAFGFQGQKCSACSRVIVLDGIYDKFVQRLTALAEAV--PVGPVEDPANLIGAVAEENAQkRIMNY 845
Cdd:cd07134 217 ETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFygKDAARKASPDLARIVNDRHFD-RLKGL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 846 IEVGRQEGRLLYQG--HVPEVGFFVPlTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSP 923
Cdd:cd07134 296 LDDAVAKGAKVEFGgqFDAAQRYIAP-TVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDK 374
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 221564986 924 EHIAIATKRFRVGNLYLNRNCTGALVGRQPFGGFRLSGAGtKAGG 968
Cdd:cd07134 375 ANVNKVLARTSSGGVVVNDVVLHFLNPNLPFGGVNNSGIG-SYHG 418
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
640-963 |
1.03e-32 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 133.62 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 640 YEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGL---TSIIGWQLVDIFrevgLPDGVFNFVPGRSGIMGDyL 716
Cdd:PTZ00381 107 PEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELsphTSKLMAKLLTKY----LDPSYVRVIEGGVEVTTE-L 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 717 VDHPhVSLIAFTGSMEVGlRIIERAAkvqpGQEMVkKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGFQGQKCSACSR 796
Cdd:PTZ00381 182 LKEP-FDHIFFTGSPRVG-KLVMQAA----AENLT-PCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDY 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 797 VIVLDGIYDKFVQrltALAEAVPVGPVEDPANL--IGAVAEENAQKRIMNYIEvgRQEGRLLYQGHVPEVGFFVPLTIIG 874
Cdd:PTZ00381 255 VLVHRSIKDKFIE---ALKEAIKEFFGEDPKKSedYSRIVNEFHTKRLAELIK--DHGGKVVYGGEVDIENKYVAPTIIV 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 875 DIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNRNCTGALVGRQPF 954
Cdd:PTZ00381 330 NPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPF 409
|
....*....
gi 221564986 955 GGFRLSGAG 963
Cdd:PTZ00381 410 GGVGNSGMG 418
|
|
| PutA_N |
pfam18083 |
Proline utilization A N-terminal domain; This domain is found in Proline utilization A (PutA) ... |
8-117 |
9.91e-30 |
|
Proline utilization A N-terminal domain; This domain is found in Proline utilization A (PutA) proteins present in Geobacter sulfurreducens. PutA are bifunctional peripheral membrane flavoenzymes that catalyze the oxidation of l-proline to l-glutamate and couple the oxidation of imported proline imported to the reduction of membrane-associated quinones. This domain is located at the N-terminus and is referred to as the alpha domain. The hydrocarbon tail of Zwittergent 3-12 binds to an exposed hydrophobic patch of the alpha domain which contains aromatic and nonpolar residues. The domain may be involved in membrane association.
Pssm-ID: 436258 Cd Length: 113 Bit Score: 113.99 E-value: 9.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 8 RRIVSCGREMFAGIYGETPSLFDKGRWLGKLMAWSMSDEEFKTRLFRFVDVFPTLSTDRMVADHLEEYFDGAQPPVLALL 87
Cdd:pfam18083 2 ARTQRIGRELFAALSGERPSLFDRRWWDDKLMEWAMKDEQLKVQLFRFVDVLPALKTPAEVARHLREYLGDVQDELPQPL 81
|
90 100 110
....*....|....*....|....*....|....
gi 221564986 88 RQAAGVFGpfGNFIQRKAVSTAIRK----MAQQF 117
Cdd:pfam18083 82 RWALRAAD--GGSLGGRALAKAARKgaeqMARRF 113
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
640-963 |
1.59e-29 |
|
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: 122.63 E-value: 1.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 640 YEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGL---TSIIgwqLVDIFREVgLPDGVFNFVPGrsgimGDY- 715
Cdd:cd07087 98 PEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELapaTSAL---LAKLIPKY-FDPEAVAVVEG-----GVEv 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 716 ---LVDHP--HvslIAFTGSMEVGLRIIERAAK-VQPgqemvkkVICEMGGKNaiiidddadldeavP-HVFNSA----- 783
Cdd:cd07087 169 ataLLAEPfdH---IFFTGSPAVGKIVMEAAAKhLTP-------VTLELGGKS--------------PcIVDKDAnleva 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 784 --------FGFQGQKCSACSRVIVLDGIYDKFVQRLT-ALAEAVPvgpvEDPANL--IGAVAEENAQKRIMNYIEvgrqE 852
Cdd:cd07087 225 arriawgkFLNAGQTCIAPDYVLVHESIKDELIEELKkAIKEFYG----EDPKESpdYGRIINERHFDRLASLLD----D 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 853 GRLLYQGHVPEVGFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKR 932
Cdd:cd07087 297 GKVVIGGQVDKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAE 376
|
330 340 350
....*....|....*....|....*....|.
gi 221564986 933 FRVGNLYLNRNCTGALVGRQPFGGFRLSGAG 963
Cdd:cd07087 377 TSSGGVCVNDVLLHAAIPNLPFGGVGNSGMG 407
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
632-963 |
1.44e-24 |
|
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: 107.96 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 632 AGETNQYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVGLPDGVfnfvpgrSGI 711
Cdd:cd07133 91 LPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEV-------AVV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 712 MGDYLV---------DHphvsLIaFTGSMEVGlRIIERAA-------------K----VQPGQEMVKKVICEMGGKnaii 765
Cdd:cd07133 164 TGGADVaaafsslpfDH----LL-FTGSTAVG-RHVMRAAaenltpvtlelggKspaiIAPDADLAKAAERIAFGK---- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 766 idddadldeavphVFNSafgfqGQKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPAnlIGAVAEENAQKRIMNY 845
Cdd:cd07133 234 -------------LLNA-----GQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYPTLADNPD--YTSIINERHYARLQGL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 846 IEVGRQEG-RLLYQGHVPEV---GFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSR 921
Cdd:cd07133 294 LEDARAKGaRVIELNPAGEDfaaTRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGE 373
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 221564986 922 SPEHIAIATKRFRVGNLYLNRNCTGALVGRQPFGGFRLSGAG 963
Cdd:cd07133 374 DKAEQDRVLRRTHSGGVTINDTLLHVAQDDLPFGGVGASGMG 415
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
637-963 |
7.48e-24 |
|
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: 106.05 E-value: 7.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 637 QYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGL---TSIIgwqLVDIFREVgLPDGVFNFVPG---RSG 710
Cdd:cd07136 95 YIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELtpnTSKV---IAKIIEET-FDEEYVAVVEGgveENQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 711 IMGDYLVDHphvslIAFTGSMEVGLRIIERAAK-VQPgqemvkkVICEMGGKNaiiidddadldeavPHVFNS------- 782
Cdd:cd07136 171 ELLDQKFDY-----IFFTGSVRVGKIVMEAAAKhLTP-------VTLELGGKS--------------PCIVDEdanlkla 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 783 ----AFG-F--QGQKCSACSRVIVLDGIYDKFVQRL-TALAEAVPVGPVEDP--ANLIgavaeeNAQ--KRIMNYIEvgr 850
Cdd:cd07136 225 akriVWGkFlnAGQTCVAPDYVLVHESVKEKFIKELkEEIKKFYGEDPLESPdyGRII------NEKhfDRLAGLLD--- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 851 qEGRLLYQGHVPEVGFFVPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEHIAIAT 930
Cdd:cd07136 296 -NGKIVFGGNTDRETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVL 374
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 221564986 931 KRFRVG------------NLYLnrnctgalvgrqPFGGFRLSGAG 963
Cdd:cd07136 375 ENLSFGggcindtimhlaNPYL------------PFGGVGNSGMG 407
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
641-963 |
5.50e-20 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 94.21 E-value: 5.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 641 EPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIfrevgLPD-------GVFNFVPGRSGIMG 713
Cdd:cd07132 99 EPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL-----IPKyldkecyPVVLGGVEETTELL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 714 DYLVDHphvslIAFTGSMEVGlRIIERAAkvqpgQEMVKKVICEMGGKNAIIIDDDADLDEAVPHV-----FNSafgfqG 788
Cdd:cd07132 174 KQRFDY-----IFYTGSTSVG-KIVMQAA-----AKHLTPVTLELGGKSPCYVDKSCDIDVAARRIawgkfINA-----G 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 789 QKCSACSRVIVLDGIYDKFVQRL-TALAEAVPVGPVEDPaNLIGAVAEENAQkRIMNYIEvgrqEGRLLYQGHVPEVGFF 867
Cdd:cd07132 238 QTCIAPDYVLCTPEVQEKFVEALkKTLKEFYGEDPKESP-DYGRIINDRHFQ-RLKKLLS----GGKVAIGGQTDEKERY 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 868 VPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNRNCTGA 947
Cdd:cd07132 312 IAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHY 391
|
330
....*....|....*.
gi 221564986 948 LVGRQPFGGFRLSGAG 963
Cdd:cd07132 392 TLDSLPFGGVGNSGMG 407
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
103-424 |
9.17e-19 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 90.53 E-value: 9.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 103 RKAVSTAIRKMA-QQFIVGENTTEAISNIERLRHQGFAAVVDVLGEATLSEKEADAYVDQYLDLIGSIERAMGRWK---- 177
Cdd:PLN02681 73 RAIVLALVKATFySHFCAGEDAEEAARTVRRLWELGLGGILDYAAEDAGDNAACDRNLEKFLAAIRAAATLPPSSSsaav 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 178 ------PLG-AGRTSGSMDWGHA-PRINVSVKATA--LSCLASPM------------DYEGSVAAILRRLRLICRRVREV 235
Cdd:PLN02681 153 kitalcPPSlLERVSDLLRWQDRdPNGKLPWKQWSfpLFADSSPLyhatsepepltaEEERLLELAHERLQKLCERAAQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 236 NGFLCLDMETYRYKEIILEVYRRLKLE---NPDYHHLGLVLQSYLRDTDHDLDNLVTWARENCLGISIRLVKGAYWDYEM 312
Cdd:PLN02681 233 GVPLLIDAEYTSLQPAIDYITYDLAREfnkGKDRPIVYGTYQAYLKDARERLRLDLERSEREGVPLGAKLVRGAYLSLER 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 313 IRSRQSGLPEPVWTMKAETDAAFERQARRIME---NSDvCHFACASHNIRSISAVIELARELAVS--DDRYEFQVLYGMA 387
Cdd:PLN02681 313 RLAASLGVPSPVHDTIQDTHACYNRCAEFLLEkasNGD-GEVMLATHNVESGELAAAKMNELGLHkgDPRVQFAQLLGMS 391
|
330 340 350
....*....|....*....|....*....|....*..
gi 221564986 388 EPVRKAILNRTGRLRLYCPYGPMVPGMGYLVRRLLEN 424
Cdd:PLN02681 392 DNLSFGLGNAGFRVSKYLPYGPVEEVIPYLLRRAEEN 428
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
545-962 |
4.26e-18 |
|
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: 89.07 E-value: 4.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 545 EVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLEIGKQWDQAY-ADVTEAID----FLEYYAREM 619
Cdd:cd07127 85 DPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFMMAFqAGGPHAQDrgleAVAYAWREM 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 620 IRLGSPRSMGKVAGETNQYFYE------PKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFR 693
Cdd:cd07127 165 SRIPPTAEWEKPQGKHDPLAMEktftvvPRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPHPAAILPLAITVQVAR 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 694 EV----GL-PDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAKVQpgqemvkkVICEMGGKNAIIIDD 768
Cdd:cd07127 245 EVlaeaGFdPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQAQ--------VYTEKAGVNTVVVDS 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 769 DADLDEAVPHVFNSAFGFQGQKCSACSRVIV-LDGI--------YDKFVQrltALAEAVPvGPVEDPA---NLIGAVAEE 836
Cdd:cd07127 317 TDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVpRDGIqtddgrksFDEVAA---DLAAAID-GLLADPAraaALLGAIQSP 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 837 NAQKRimnyIEVGRQEGRLLYQGHV------PEVGFFVPLTIIGDIRPEHRLAQEEiFGPLLAVMRARDFNEALVWANS- 909
Cdd:cd07127 393 DTLAR----IAEARQLGEVLLASEAvahpefPDARVRTPLLLKLDASDEAAYAEER-FGPIAFVVATDSTDHSIELAREs 467
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 221564986 910 --TRYALTGGLFSRSPEHIAIATKRFRVGNLYLNRNCTGALVGRQP--FGGFRLSGA 962
Cdd:cd07127 468 vrEHGAMTVGVYSTDPEVVERVQEAALDAGVALSINLTGGVFVNQSaaFSDFHGTGA 524
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
546-916 |
7.26e-18 |
|
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: 87.60 E-value: 7.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 546 VAQAIGAARKSFETWRDITPEIRAEFLlkactvvrrriyelsalqvleigkqwdQAYADVTEAI--DFLEYYAREMiRLG 623
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFL---------------------------EAIADEIEALgdELVARAHAET-GLP 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 624 SPRSMGKVAGETNQ-----------YFYE-----------------------PKGVAAVIAPWNFPLAISM--GMVSAAI 667
Cdd:cd07129 53 EARLQGELGRTTGQlrlfadlvregSWLDaridpadpdrqplprpdlrrmlvPLGPVAVFGASNFPLAFSVagGDTASAL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 668 VTGNCVVFK--PS--GLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVGLRIIERAAK 743
Cdd:cd07129 133 AAGCPVVVKahPAhpGTSELVARAIRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 744 -VQPgqemvKKVICEMGGKNaiiidddadldeavPHVFNSAF----------GF-------QGQKCSACSRVIVLDGI-Y 804
Cdd:cd07129 213 rPEP-----IPFYAELGSVN--------------PVFILPGAlaergeaiaqGFvgsltlgAGQFCTNPGLVLVPAGPaG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 805 DKFVQRLTALAEAVPVGPVEDPAnliGAVAEENAQKRImnyieVGRQEGRLLYQGHVPEVGFFVP---LTIIGDIRPEHR 881
Cdd:cd07129 274 DAFIAALAEALAAAPAQTMLTPG---IAEAYRQGVEAL-----AAAPGVRVLAGGAAAEGGNQAAptlFKVDAAAFLADP 345
|
410 420 430
....*....|....*....|....*....|....*
gi 221564986 882 LAQEEIFGPLLAVMRARDFNEALVWANSTRYALTG 916
Cdd:cd07129 346 ALQEEVFGPASLVVRYDDAAELLAVAEALEGQLTA 380
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
637-967 |
2.10e-17 |
|
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: 85.93 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 637 QYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVgLPDGVFNFVPGrSGIMGDYL 716
Cdd:cd07137 96 EIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEG-GVPETTAL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 717 VDHpHVSLIAFTGSMEVGlRIIERAAKvqpgqEMVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGF-QGQKCSACS 795
Cdd:cd07137 174 LEQ-KWDKIFFTGSPRVG-RIIMAAAA-----KHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPD 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 796 RVIVLDGIYDKFVQRLTALAEAVpVGPVEDPANLIGAVAEENAQKRIMNYIEVGRQEGRLLYQGHVPEVGFFVPLTIIGD 875
Cdd:cd07137 247 YVLVEESFAPTLIDALKNTLEKF-FGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERDEKNLYIEPTILLD 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 876 IRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEhiaiATKRFR----VGNLYLNRNCTGALVGR 951
Cdd:cd07137 326 PPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKE----LKRRIVaetsSGGVTFNDTVVQYAIDT 401
|
330
....*....|....*.
gi 221564986 952 QPFGGFRLSGAGTKAG 967
Cdd:cd07137 402 LPFGGVGESGFGAYHG 417
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
604-927 |
2.35e-17 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 86.68 E-value: 2.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 604 DVTEAIDFLEYYAR--------EMIRLGSPRSMGKVAGETNQYFYEP-KGVAAVIAPWNFPlaiSMGM---VSAAIVTGN 671
Cdd:PRK11903 101 DIDGGIFTLGYYAKlgaalgdaRLLRDGEAVQLGKDPAFQGQHVLVPtRGVALFINAFNFP---AWGLwekAAPALLAGV 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 672 CVVFKPSGLTSIIGWQLVDIFREVG-LPDGVFNFVPGRSGIMGDYLVDHPHVSliaFTGSMEVGLRI------IERAAKV 744
Cdd:PRK11903 178 PVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSSAGLLDHLQPFDVVS---FTGSAETAAVLrshpavVQRSVRV 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 745 ----------------QPGQE----MVKKVICEMGGKNaiiidddadldeavphvfnsafgfqGQKCSACSRVIVLDGIY 804
Cdd:PRK11903 255 nveadslnsallgpdaAPGSEafdlFVKEVVREMTVKS-------------------------GQKCTAIRRIFVPEALY 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 805 DKFVQRLTALAEAVPVGpveDPAN---LIGAVAEENAQKRIMNYIEVGRQEGRLLYQGHV-------PEVGFFVPLTIIG 874
Cdd:PRK11903 310 DAVAEALAARLAKTTVG---NPRNdgvRMGPLVSRAQLAAVRAGLAALRAQAEVLFDGGGfalvdadPAVAACVGPTLLG 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 221564986 875 --DIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEHIA 927
Cdd:PRK11903 387 asDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLA 441
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
511-976 |
2.35e-17 |
|
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: 86.55 E-value: 2.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 511 FIGGQELE-TEDLLPSMNPSDpSEIVGWVCQAGTDeVAQAIGAAR-KSFETWRDITPEIRAEFLLKACTVVRRRIYELSA 588
Cdd:cd07128 4 YVAGQWHAgTGDGRTLHDAVT-GEVVARVSSEGLD-FAAAVAYAReKGGPALRALTFHERAAMLKALAKYLMERKEDLYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 589 LQVLEIGKQWDQAYaDVTEAIDFLEYYA----REM-----IRLGSPRSMGKVAGETNQYFYEPK-GVAAVIAPWNFPlai 658
Cdd:cd07128 82 LSAATGATRRDSWI-DIDGGIGTLFAYAslgrRELpnahfLVEGDVEPLSKDGTFVGQHILTPRrGVAVHINAFNFP--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 659 SMGMVSAAIVT---GNCVVFKPSGLTSIIGWQLVDIFREVG-LPDGVFNFVPGRSGIMGDYLVDHPHVsliAFTGSMEVG 734
Cdd:cd07128 158 VWGMLEKFAPAllaGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGSVGDLLDHLGEQDVV---AFTGSAATA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 735 LR------IIER----------------AAKVQPGQE----MVKKVICEMGGKnaiiidddadldeavphvfnsafgfQG 788
Cdd:cd07128 235 AKlrahpnIVARsirfnaeadslnaailGPDATPGTPefdlFVKEVAREMTVK-------------------------AG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 789 QKCSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQKRIMNYIEVGRQEGRLLY--------QGH 860
Cdd:cd07128 290 QKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFggpdrfevVGA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 861 VPEVGFFVPLTII--GDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEHIA-----IATKRF 933
Cdd:cd07128 370 DAEKGAFFPPTLLlcDDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARelvlgAAPYHG 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 221564986 934 RVgnLYLNRNCTGALVGR-QPF-----GGFRLSGAGTKAGGPDYLLHFM 976
Cdd:cd07128 450 RL--LVLNRDSAKESTGHgSPLpqlvhGGPGRAGGGEELGGLRGVKHYM 496
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
596-905 |
8.13e-16 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 81.39 E-value: 8.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 596 KQWDQAYADVTEAIDFLEYYAREMIRLGSpRSM---GKVAGETNQYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNC 672
Cdd:cd07126 94 KSDAQALGEVVVTRKFLENFAGDQVRFLA-RSFnvpGDHQGQQSSGYRWPYGPVAIITPFNFPLEIPALQLMGALFMGNK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 673 VVFKPSGLTSIIGWQLVDIFREVGLPDGVFNFVPGRSGIMGDYLVD-HPHVSLiaFTGSMevglRIIERAAKVQPGqemv 751
Cdd:cd07126 173 PLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEaNPRMTL--FTGSS----KVAERLALELHG---- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 752 kKVICEMGGKNAIIIDDDADLDEAVPHVFNS-AFGFQGQKCSACSRVIVLDGIYDK-FVQRLTALA-----EAVPVGPVE 824
Cdd:cd07126 243 -KVKLEDAGFDWKILGPDVSDVDYVAWQCDQdAYACSGQKCSAQSILFAHENWVQAgILDKLKALAeqrklEDLTIGPVL 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 825 DPANligavaeenaqKRIMNYIE--VGRQEGRLLYQG------HVPEV-------GFFVPLTIIGDirPEH-RLAQEEIF 888
Cdd:cd07126 322 TWTT-----------ERILDHVDklLAIPGAKVLFGGkpltnhSIPSIygayeptAVFVPLEEIAI--EENfELVTTEVF 388
|
330
....*....|....*..
gi 221564986 889 GPLLAVMRARDFNEALV 905
Cdd:cd07126 389 GPFQVVTEYKDEQLPLV 405
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
635-909 |
1.82e-12 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 70.91 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 635 TNQYFYEPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVgLPDGVFNFVPGRSGImGD 714
Cdd:PLN02203 101 TAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKY-LDSKAVKVIEGGPAV-GE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 715 YLVDHPHvSLIAFTGSMEVGLRIIERAAKvqpgqeMVKKVICEMGGKN---AIIIDDDADLDEAVPHVFNSAFGF-QGQK 790
Cdd:PLN02203 179 QLLQHKW-DKIFFTGSPRVGRIIMTAAAK------HLTPVALELGGKCpciVDSLSSSRDTKVAVNRIVGGKWGScAGQA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 791 CSACSRVIVLDGIYDKFVQRLTALAEAVPVGPVEDPANLIGAVAEENAQkRIMNYIEVGRQEGRLLYQGHVPEVGFFVPL 870
Cdd:PLN02203 252 CIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQ-RLSNLLKDPRVAASIVHGGSIDEKKLFIEP 330
|
250 260 270
....*....|....*....|....*....|....*....
gi 221564986 871 TIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWANS 909
Cdd:PLN02203 331 TILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINS 369
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
641-967 |
1.30e-11 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 68.15 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 641 EPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREVgLPDGVFNFVPGrsGIMGDYLVDHP 720
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEG--AVTETTALLEQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 721 HVSLIAFTGSMEVGLRIIERAAKvqpgqeMVKKVICEMGGKNAIIIDDDADLDEAVPHVFNSAFGF-QGQKCSACSRVIV 799
Cdd:PLN02174 188 KWDKIFYTGSSKIGRVIMAAAAK------HLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGCnNGQACISPDYILT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 800 LDGIYDKFVQRLT-ALAEAVPVGPVEdpANLIGAVAEENAQKRIMNYIEVGRQEGRLLYQGHVPEVGFFVPLTIIGDIRP 878
Cdd:PLN02174 262 TKEYAPKVIDAMKkELETFYGKNPME--SKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGEKDRENLKIAPTILLDVPL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 879 EHRLAQEEIFGPLLAVMRARDFNEALVWANSTRYALTGGLFSRSPEHIAIATKRFRVGNLYLNRNCTGALVGRQPFGGFR 958
Cdd:PLN02174 340 DSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVG 419
|
....*....
gi 221564986 959 LSGAGTKAG 967
Cdd:PLN02174 420 ESGMGAYHG 428
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
544-907 |
2.92e-06 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 50.70 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 544 DEVAQAIGAARKSFETWRDITPEIRAEFLLKACTVVRRRIYELSALQVLE--IGKQWDQ-----AYADVTEAIDFLEyya 616
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEEtgMGRVEDKiaknhLAAEKTPGTEDLT--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 617 remirlgsPRSMGKVAGETnQYFYEPKGVAAVIAPWNFPLAI----SMGMVSAaivtGNCVVFKP---SGLTSIIGWQLV 689
Cdd:cd07121 81 --------TTAWSGDNGLT-LVEYAPFGVIGAITPSTNPTETiinnSISMLAA----GNAVVFNPhpgAKKVSAYAVELI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 690 -DIFREVGLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGsmevGLRIIERAAKVQpgqemvKKVICEmGGKNAIIIDD 768
Cdd:cd07121 148 nKAIAEAGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTG----GPAVVKAALSSG------KKAIGA-GAGNPPVVVD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 769 DADLDEAVPH--VFNSAFGfQGQKCSACSRVIVLDGIYDKFVQRLTAlAEAVPVGPVEDPANLIGAVAEENAQkrIMNYI 846
Cdd:cd07121 217 ETADIEKAARdiVQGASFD-NNLPCIAEKEVIAVDSVADYLIAAMQR-NGAYVLNDEQAEQLLEVVLLTNKGA--TPNKK 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221564986 847 EVGRQEGRLLYQGHVpEVGFFVPLtIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWA 907
Cdd:cd07121 293 WVGKDASKILKAAGI-EVPADIRL-IIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELA 351
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
641-918 |
1.09e-05 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 49.19 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 641 EPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFKPSGLTSIIGWQLVDIFREV----GLPDGVFNFVPGRSGIMGDYL 716
Cdd:cd07081 94 EPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAavaaGAPENLIGWIDNPSIELAQRL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 717 VDHPHVSLIAFTGS---MEVGLRIIERAAKVQPGQEMVkkVICEMGgknaiiidddaDLDEAVPHVFNSAFGFQGQKCSA 793
Cdd:cd07081 174 MKFPGIGLLLATGGpavVKAAYSSGKPAIGVGAGNTPV--VIDETA-----------DIKRAVQSIVKSKTFDNGVICAS 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 794 CSRVIVLDGIYDKfVQRLTALAEAVPVgpvedPANLIGAVAEENAQKRIMNYIEVGRQEGRLlyqghVPEVGFFVPLT-- 871
Cdd:cd07081 241 EQSVIVVDSVYDE-VMRLFEGQGAYKL-----TAEELQQVQPVILKNGDVNRDIVGQDAYKI-----AAAAGLKVPQEtr 309
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 221564986 872 -IIGDIRP--EHRLAQEEIFGPLLAVMRARDFNEALvwANSTRYALTGGL 918
Cdd:cd07081 310 iLIGEVTSlaEHEPFAHEKLSPVLAMYRAANFADAD--AKALALKLEGGC 357
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
641-935 |
7.05e-05 |
|
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: 46.33 E-value: 7.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 641 EPKGVAAVIAPWNFPLAISMGMVSAAIVTGNCVVFK--PSGLTSIIgwQLVDIFRE----VGLPDGVFNFVPGRSGIMGD 714
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSphPRAKKCSI--EAAKIMREaavaAGAPEGLIQWIEEPSIELTQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 715 YLVDHPHVSLIAFTGSME--------------VGL----RIIERAAKVQpgqEMVKKVIcemggknaiiidddadldeav 776
Cdd:cd07122 172 ELMKHPDVDLILATGGPGmvkaayssgkpaigVGPgnvpAYIDETADIK---RAVKDII--------------------- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 777 phvFNSAFGFqGQKCSACSRVIVLDGIYDKFVQRLTALAeavpvgpvedpanliGAVAEENAQKRIMNYIE--------- 847
Cdd:cd07122 228 ---LSKTFDN-GTICASEQSVIVDDEIYDEVRAELKRRG---------------AYFLNEEEKEKLEKALFddggtlnpd 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 848 -VGRQEGRLLYQghvpeVGFFVPLTI------IGDIRPEHRLAQEEIFgPLLAVMRARDFNEALVWANS-TRYA---LTG 916
Cdd:cd07122 289 iVGKSAQKIAEL-----AGIEVPEDTkvlvaeETGVGPEEPLSREKLS-PVLAFYRAEDFEEALEKARElLEYGgagHTA 362
|
330 340
....*....|....*....|..
gi 221564986 917 GLFSRSPEHI---AIATKRFRV 935
Cdd:cd07122 363 VIHSNDEEVIeefALRMPVSRI 384
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
622-903 |
2.37e-04 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, 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. This group includes families ALDH18, ALDH19, and ALDH20 and represents 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: 143396 [Multi-domain] Cd Length: 397 Bit Score: 44.52 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 622 LGSPRSMGKVAGETNQYFYE------PKGVAAVIAPWNFPLAISMGMVSAaIVTGNCVVFKPSGLTSIIGWQLVDIFREV 695
Cdd:cd07077 74 RGITASVGHIQDVLLPDNGEtyvrafPIGVTMHILPSTNPLSGITSALRG-IATRNQCIFRPHPSAPFTNRALALLFQAA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 696 ---GLPDGVFNFVPGRSGIMGDYLVDHPHVSLIAFTGSMEVglriIERAAKVQPGqemvKKVICEMGGKNAIIIDDDADL 772
Cdd:cd07077 153 daaHGPKILVLYVPHPSDELAEELLSHPKIDLIVATGGRDA----VDAAVKHSPH----IPVIGFGAGNSPVVVDETADE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 773 DEAVPHVFNSAFgFQGQKCSACSRVIVLDGIYDKFVQRltalaeavpvgpvedpanligavaeenaqkrimnYIEVGRQE 852
Cdd:cd07077 225 ERASGSVHDSKF-FDQNACASEQNLYVVDDVLDPLYEE----------------------------------FKLKLVVE 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 221564986 853 GRLLYQGhvpevgffvPLTIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEA 903
Cdd:cd07077 270 GLKVPQE---------TKPLSKETTPSFDDEALESMTPLECQFRVLDVISA 311
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
791-907 |
1.07e-03 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 42.58 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221564986 791 CSACSRVIVLDGIYDKFVQRLTAlAEAVPVGPvEDPANLIGAVAEEN--AQKRImnyieVGRQEGRLLYQGHVpEVGFFV 868
Cdd:PRK15398 272 CIAEKEVIVVDSVADELMRLMEK-NGAVLLTA-EQAEKLQKVVLKNGgtVNKKW-----VGKDAAKILEAAGI-NVPKDT 343
|
90 100 110
....*....|....*....|....*....|....*....
gi 221564986 869 PLtIIGDIRPEHRLAQEEIFGPLLAVMRARDFNEALVWA 907
Cdd:PRK15398 344 RL-LIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALA 381
|
|
| |
