|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
435-959 |
0e+00 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 591.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 435 SPENFMSAVFelaenedlfereshrflasvdalDAEVPAPNRVQDRTAAPEpldvsngfvNTADSDPSLPaNQEWARRIR 514
Cdd:cd07125 1 ANSSFVNRIF-----------------------DLEVPLEALADALKAFDE---------KEWEAIPIIN-GEETETGEG 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 515 EAAKASTLGNDTIEANTVGTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSD 594
Cdd:cd07125 48 APVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADAD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 595 PEISEAIDFAHYYAELAVAL----------EQVDGAEYDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAA 664
Cdd:cd07125 128 AEVREAIDFCRYYAAQARELfsdpelpgptGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 665 RCGAVMVEALWAAGVPREALQYVQFSDRELGRALVADDAVDRVILTGGFETAELFRSFR-----PDLELLAETSGKNAII 739
Cdd:cd07125 208 LIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALaerdgPILPLIAETGGKNAMI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 740 VTPSADYDLAAKDVIASAFGHAGQKCSAASLVILVGQAArsKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLD 819
Cdd:cd07125 288 VDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIA--ERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 820 GLTKLGAGEQWVVQPRKLDEE-GRLWSPGVRSGVrrGSEYHRTEYFGPVLGIMTAA--TLEEAIEIANEVDYGLTAGLHS 896
Cdd:cd07125 366 AHTELMRGEAWLIAPAPLDDGnGYFVAPGIIEIV--GIFDLTTEVFGPILHVIRFKaeDLDEAIEDINATGYGLTLGIHS 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2066550363 897 LDAKEIATWVDSIEAGNLYVNRGITGAIVQRQPFGGWKKSVVGPttKAGGPNYLHALGDWHTA 959
Cdd:cd07125 444 RDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGP--KAGGPNYLLRFGNEKTV 504
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
30-999 |
1.70e-155 |
|
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: 489.94 E-value: 1.70e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 30 ALAPEAVQLVRRWLKAAEEIPVDASAAQLAGVLKDPKGLAFTVGFVDGVVRPEDLSVAGRNLDRIAGDAPGFLPLTMRSA 109
Cdd:COG0506 8 ALRARAVALARRLVEAIRAAPEGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLAKSPSFLVNASTWG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 110 IRAGGLAtKVAPQVVVPIARRVLRAMVGHLIIDATDSKLGGAIEKIRKPGIRLNMNLLGEAVLGKKEADRRLEGTKALLA 189
Cdd:COG0506 88 LMLTLVG-RLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAARKLRAKGYRVSLDLLGEAVLTEAEAERYLDAYLEALE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 190 RP-----DVDYVSIKVSATTAPHQPWAFEESVEEVIAKLLPLYQLAKNAPtpKFINLDMEEYRDLEMTMAVFTRILDRPE 264
Cdd:COG0506 167 AIgaagvDRPGVSVKLSALGPRYSPAQRERVVEELLERLRPLARAAREAG--IFVTIDMEEYDRLDLTLDVFERLLADPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 265 FLG-LEAGIVLQAYLPDALDAMIRLQEWSAarvaRGGAPIKIRLVKGANLPMERVEASLHGWPVATWGSKQDTDTNYKRC 343
Cdd:COG0506 245 LAGwPGVGIVLQAYLKRAEADLDRLAALAR----RGGRRIRVRLVKGAYWDPEIVRAQVHGWPYPVFTRKADTDANYLRC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 344 VDYALqpEHVKHVRIGVAGHNLFDVALSWLLAKQRGV-TEGIEYEMLLGMAQGQAE-VVKRDVGSLLLYTPVVHPSEFDV 421
Cdd:COG0506 321 ARKLL--EAGDAIYPQFATHNARTIAAALALAGERGRpPDRFEFQMLYGMGEDLQRaLAAVDGGRLLLYCPVVAPVGGDA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 422 AIAYLIRRLEEGASPENFMSAVFELAENEDLFERESHRFLASVDALDAEVPAPNRVQDRTAAPEPLDvSNGFVNTADSDP 501
Cdd:COG0506 399 ALAYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPRFLAALAAPTPPPPPPLRRQRRRRRRARGG-ALAAALAAAAAA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 502 SLPANQEWARRIREAAKASTLGNDTIEANTVGTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEV 581
Cdd:COG0506 478 AALAAAAAAAAALAAAAAGAAAAAAAAAVAVVPAAAAAVVAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 582 AASEAGKTLDQSDPEISEAIDFAHYYAELAVALEQVDGAEYDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPAR 661
Cdd:COG0506 558 AAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAARAAAPPPPPPGGLVALLPLGPLAAAAAAAAAAAA 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 662 QAARCGAVMVEALWAAGVPREALQYVQFSDRELGRALVADDAVDRVILTGGFETAELFRSFRPDLELLAETSGKNAIIVT 741
Cdd:COG0506 638 AAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAGGGVLVLGAGGGAGGAAALTLAAAAAAATAATAAAAA 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 742 PSADYDLAAKDVIASAFGHAGQKCSAASLVILVGQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLDGL 821
Cdd:COG0506 718 AAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVAASAAASASASASLLSLLALLLLDADLVILLLALAAAAAAL 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 822 TKLGAGEQWVVQPRKLDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKE 901
Cdd:COG0506 798 LVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLPGGGPLVPGLLTAPLLVALILGLIVLVLLEIVLVLALVLAL 877
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 902 IATWVDSIEAGNLYVNRGITGAIVQRQPFGGWKKSVVGPTTKAGGPNYLHALGDWHTAAATKGAEIADAHVKGLLDGARS 981
Cdd:COG0506 878 ALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGTLAL 957
|
970
....*....|....*...
gi 2066550363 982 CPDVSAEDAAALERAFRS 999
Cdd:COG0506 958 AAAAAAATALAAAAAAAA 975
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
533-952 |
2.94e-108 |
|
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: 347.88 E-value: 2.94e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 533 GTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELAV 612
Cdd:COG1012 40 ATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARGEVDRAADFLRYYAGEAR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 613 ALEqvdgAEYDPSRL--------------VVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAG 678
Cdd:COG1012 120 RLY----GETIPSDApgtrayvrreplgvVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 679 VPREALQYVQFSDRELGRALVADDAVDRVILTGGFETAELFRSFRPD--LELLAETSGKNAIIVTPSADYDLAAKDVIAS 756
Cdd:COG1012 196 LPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAEnlKRVTLELGGKNPAIVLDDADLDAAVEAAVRG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 757 AFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLDGLTKLG--AGEQWVVQP 834
Cdd:COG1012 276 AFGNAGQRCTAASRLLV--HESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEDAvaEGAELLTGG 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 835 RKLD-EEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGN 913
Cdd:COG1012 354 RRPDgEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGM 433
|
410 420 430
....*....|....*....|....*....|....*....
gi 2066550363 914 LYVNRGITGAiVQRQPFGGWKKSVVGpttKAGGPNYLHA 952
Cdd:COG1012 434 VWINDGTTGA-VPQAPFGGVKQSGIG---REGGREGLEE 468
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
533-950 |
3.16e-106 |
|
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: 343.82 E-value: 3.16e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 533 GTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELAV 612
Cdd:cd07124 66 ATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREML 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 613 AL-----EQVDGAE----YDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPREA 683
Cdd:cd07124 146 RLrgfpvEMVPGEDnryvYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGV 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 684 LQYVQFSDRELGRALVADDAVDRVILTGGFETA----ELFRSFRPDLE----LLAETSGKNAIIVTPSADYDLAAKDVIA 755
Cdd:cd07124 226 VNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGlriyERAAKVQPGQKwlkrVIAEMGGKNAIIVDEDADLDEAAEGIVR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 756 SAFGHAGQKCSAASLVILVGQAarSKRFRSQLLDGVRSIDVGYPTEATTQMGPII--------------GPAEGKLLDGL 821
Cdd:cd07124 306 SAFGFQGQKCSACSRVIVHESV--YDEFLERLVERTKALKVGDPEDPEVYMGPVIdkgardrirryieiGKSEGRLLLGG 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 822 TKLGageqwvvqprkLDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKE 901
Cdd:cd07124 384 EVLE-----------LAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEH 452
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2066550363 902 IATWVDSIEAGNLYVNRGITGAIVQRQPFGGWKKSvvGPTTKAGGPNYL 950
Cdd:cd07124 453 LERARREFEVGNLYANRKITGALVGRQPFGGFKMS--GTGSKAGGPDYL 499
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
533-952 |
8.49e-101 |
|
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: 327.18 E-value: 8.49e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 533 GTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELAv 612
Cdd:pfam00171 26 ATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGEVDRAIDVLRYYAGLA- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 613 alEQVDG--AEYDPSRLVVVT--P--------PWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVP 680
Cdd:pfam00171 105 --RRLDGetLPSDPGRLAYTRrePlgvvgaitPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAGLP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 681 REALQYVQFSDRELGRALVADDAVDRVILTGGFETAELF-----RSFRPdleLLAETSGKNAIIVTPSADYDLAAKDVIA 755
Cdd:pfam00171 183 AGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIaeaaaQNLKR---VTLELGGKNPLIVLEDADLDAAVEAAVF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 756 SAFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLDGLTKLG--AGEQWVVQ 833
Cdd:pfam00171 260 GAFGNAGQVCTATSRLLV--HESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDAkeEGAKLLTG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 834 PRKLDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGN 913
Cdd:pfam00171 338 GEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGM 417
|
410 420 430
....*....|....*....|....*....|....*....
gi 2066550363 914 LYVNRGITGAIVQRqPFGGWKKSVVGpttKAGGPNYLHA 952
Cdd:pfam00171 418 VWINDYTTGDADGL-PFGGFKQSGFG---REGGPYGLEE 452
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
113-951 |
5.13e-90 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 313.29 E-value: 5.13e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 113 GGLATKVAPQVVVPIARRVLRAMVGHLIidatdskLGGAIE-------KIRKPGIRLNMNLLGEAVLGKKEADR------ 179
Cdd:PRK11904 154 KRLVNRLGEPVIRKAMRQAMKIMGKQFV-------LGRTIEealkrarSARNKGYRYSFDMLGEAALTAADAERyfkaya 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 180 -------RLEGTKALLARPDVdyvSIKVSATTAPHQPWAFEESVEEVIAKLLPLYQLAKNAptpkFINL--DMEEYRDLE 250
Cdd:PRK11904 227 raieaigRAAGGADLPARPGI---SIKLSALHPRYEAAQRERVLAELVPRVLELARLAKEA----NIGLtiDAEEADRLE 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 251 MTMAVFTRILDRPEFLGLEA-GIVLQAYLPDALDAMirlqEWSAARVARGGAPIKIRLVKGANLPME---RVEASLHGWP 326
Cdd:PRK11904 300 LSLDLFEALFRDPSLKGWGGfGLAVQAYQKRALPVL----DWLADLARRQGRRIPVRLVKGAYWDSEikrAQELGLPGYP 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 327 VATwgSKQDTDTNYKRCVDYALqpEHVKHVRIGVAGHNLFDVALSWLLAKQRgvteGIEYEMLLGMAQG-QAEVVKRDVG 405
Cdd:PRK11904 376 VFT--RKAATDVSYLACARKLL--SARGAIYPQFATHNAHTVAAILEMAGHR----GFEFQRLHGMGEAlYDALLDAPGI 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 406 SLLLYTPVVHPSEFdvaIAYLIRRL-EEGASPenfmSAVfelaenedlferesHRFlasvdaLDAEVPAPNRVQD----- 479
Cdd:PRK11904 448 PCRIYAPVGSHKDL---LPYLVRRLlENGANS----SFV--------------HRL------VDPDVPIEELVADpvekl 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 480 RTAA-------PEPLDV-------SNGfVNTADSDPSLPANQEWARRIREAAKASTLGNDTIEANTV------------- 532
Cdd:PRK11904 501 RSFEtlpnpkiPLPRDIfgperknSKG-LNLNDRSELEPLAAAIAAFLEKQWQAGPIINGEGEARPVvspadrrrvvgev 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 533 --GTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAEL 610
Cdd:PRK11904 580 afADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQ 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 611 A-------VALEQVDGAE---YDPSRLVVVT-PPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGV 679
Cdd:PRK11904 660 ArrlfgapEKLPGPTGESnelRLHGRGVFVCiSPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGI 739
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 680 PREALQYVQFSDRELGRALVADDAVDRVILTGGFETAELF-RSF----RPDLELLAETSGKNAIIVTPSADYDLAAKDVI 754
Cdd:PRK11904 740 PKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIInRTLaardGPIVPLIAETGGQNAMIVDSTALPEQVVDDVV 819
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 755 ASAFGHAGQKCSAasLVILVGQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGpAEGKllDGLTKLGAgeqwvvqp 834
Cdd:PRK11904 820 TSAFRSAGQRCSA--LRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVID-AEAK--ANLDAHIE-------- 886
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 835 rKLDEEGRL-WSPGVRSGVRRGS------------EYHRTEYFGPVLGIMT--AATLEEAIEIANEVDYGLTAGLHSLDA 899
Cdd:PRK11904 887 -RMKREARLlAQLPLPAGTENGHfvaptafeidsiSQLEREVFGPILHVIRykASDLDKVIDAINATGYGLTLGIHSRIE 965
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|..
gi 2066550363 900 KEIATWVDSIEAGNLYVNRGITGAIVQRQPFGGWKKSVVGPttKAGGPNYLH 951
Cdd:PRK11904 966 ETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTGP--KAGGPHYLL 1015
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
196-1149 |
4.34e-88 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 310.26 E-value: 4.34e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 196 VSIKVSATtAPHQPWAFEESV-EEVIAKLLPLYQLAKNAPTPkfINLDMEEYRDLEMTMAVFTRILDRPEFLGLEA-GIV 273
Cdd:PRK11905 246 ISVKLSAL-HPRYERAQRERVmAELLPRLKALALLAKAYDIG--LNIDAEEADRLELSLDLLEALCSDPDLAGWNGiGFV 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 274 LQAYLPDA---LDAMIRLqewsaARvaRGGAPIKIRLVKGANLPME----RVEAsLHGWPVATwgSKQDTDTNYKRCVDY 346
Cdd:PRK11905 323 VQAYQKRCpfvIDYLIDL-----AR--RSGRRLMVRLVKGAYWDAEikraQVDG-LEGFPVFT--RKVHTDVSYIACARK 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 347 ALqpEHVKHVRIGVAGHNLFDVALSWLLAKQRGvteGIEYEMLLGMaqGQAevvkrdvgsllLYTPVVHPSEFDVA---- 422
Cdd:PRK11905 393 LL--AARDVIYPQFATHNAQTLAAIYELAGGKG---DFEFQCLHGM--GEP-----------LYDQVVGKEKLGRPcriy 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 423 ---------IAYLIRRL-EEGA-------------SPENFMSAVFELAEN------------EDLF--ERESHRFL---- 461
Cdd:PRK11905 455 apvgthetlLAYLVRRLlENGAnssfvnrivdenvPVEELIADPVEKVAAmgvaphpqiplpRDLYgpERRNSKGLdlsd 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 462 -ASVDALDAEVpAPNRVQDRTAAPEpldVSNGFVNTADSDPSLPANQewarrireaakastlgNDTIEANTVGTAEELAS 540
Cdd:PRK11905 535 eATLAALDEAL-NAFAAKTWHAAPL---LAGGDVDGGTRPVLNPADH----------------DDVVGTVTEASAEDVER 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 541 RIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELAVALEqvDGA 620
Cdd:PRK11905 595 ALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLL--NGP 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 621 EYDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPREALQYVQFSDRELGRALVA 700
Cdd:PRK11905 673 GHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVA 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 701 DDAVDRVILTGGFETAELFRS-----FRPDLELLAETSGKNAIIVTPSADYDLAAKDVIASAFGHAGQKCSAasLVILVG 775
Cdd:PRK11905 753 DPRIAGVMFTGSTEVARLIQRtlakrSGPPVPLIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSA--LRVLCL 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 776 QAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGP-AEGKLLDGLTKLGAGEQWV--VQPRKLDEEGRLWSPGVRSgV 852
Cdd:PRK11905 831 QEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAeAQANIEAHIEAMRAAGRLVhqLPLPAETEKGTFVAPTLIE-I 909
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 853 RRGSEYHRtEYFGPVLGIMT--AATLEEAIEIANEVDYGLTAGLHS-LDAKeIATWVDSIEAGNLYVNRGITGAIVQRQP 929
Cdd:PRK11905 910 DSISDLER-EVFGPVLHVVRfkADELDRVIDDINATGYGLTFGLHSrIDET-IAHVTSRIRAGNIYVNRNIIGAVVGVQP 987
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 930 FGGWKKSVVGPttKAGGPNYLHALgdwhtaAATKGAEIADAHVKGLLDGARSCPDVSAEDAAALERAFRSDELAWQEDFG 1009
Cdd:PRK11905 988 FGGEGLSGTGP--KAGGPLYLGRL------VREAPTPIPPAHESVDTDAAARDFLAWLDKEGKAALAAAARDARARSALG 1059
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 1010 VARDVQGLYAERNVFRYLPMPgtttVRLAEGERPADLVRVLGAGLRAGVKLRVSTGVELPSGL--RAAIVSAGIPI--DV 1085
Cdd:PRK11905 1060 LEQELPGPTGESNLLSLHPRG----RVLCVADTEEALLRQLAAALATGNVAVVAADSGLAAALadLPGLVAARIDWtqDW 1135
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 1086 QKDAEFLAragrfapgrlrLIGEGRAELAAAVKGR---CDLAIIdhEVVEAGRVEMLPFLR---EQAVSI 1149
Cdd:PRK11905 1136 EADDPFAG-----------ALLEGDAERARAVRQAlaaRPGAIV--PLIAAEPTDAYDLARlveERSVSI 1192
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
526-950 |
1.16e-85 |
|
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: 287.53 E-value: 1.16e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 526 TIEANTVGTAEElasRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAH 605
Cdd:TIGR01237 62 TVSKASQEHAEH---ALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFME 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 606 YYAELAVALE----------QVDGAEYDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALW 675
Cdd:TIGR01237 139 YYARQMIELAkgkpvnsregETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 676 AAGVPREALQYVQFSDRELGRALVADDAVDRVILTGG-------FETAELFRSFRPDLE-LLAETSGKNAIIVTPSADYD 747
Cdd:TIGR01237 219 EAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSrevgtriFERAAKVQPGQKHLKrVIAEMGGKDTVIVDEDADIE 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 748 LAAKDVIASAFGHAGQKCSAASLVILVGQAarSKRFRSQLLDGVRSIDVGYPTEATTQMGPII--------------GPA 813
Cdd:TIGR01237 299 LAAQSAFTSAFGFAGQKCSAGSRAVVHEKV--YDEVVERFVEITESLKVGPPDSADVYVGPVIdqksfnkimeyieiGKA 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 814 EGKLLDGltklGAGEqwvvqprklDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAG 893
Cdd:TIGR01237 377 EGRLVSG----GCGD---------DSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGG 443
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2066550363 894 LHSLDAKEIATWVDSIEAGNLYVNRGITGAIVQRQPFGGWKKSvvGPTTKAGGPNYL 950
Cdd:TIGR01237 444 VISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPFGGFKMS--GTDSKAGGPDYL 498
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
534-962 |
5.11e-84 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 283.36 E-value: 5.11e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 534 TAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELAVA 613
Cdd:PRK03137 71 TKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 614 L------EQVDGAE----YDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPREA 683
Cdd:PRK03137 151 LadgkpvESRPGEHnryfYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGV 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 684 LQYVQFSDRELGRALVaDDAVDRVI-LTGGFETA----ELFRSFRPDLELL----AETSGKNAIIVTPSADYDLAAKDVI 754
Cdd:PRK03137 231 VNFVPGSGSEVGDYLV-DHPKTRFItFTGSREVGlriyERAAKVQPGQIWLkrviAEMGGKDAIVVDEDADLDLAAESIV 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 755 ASAFGHAGQKCSAASLVILVgqAARSKRFRSQLLDGVRSIDVGYPTEAtTQMGPII--------------GPAEGKLLDG 820
Cdd:PRK03137 310 ASAFGFSGQKCSACSRAIVH--EDVYDEVLEKVVELTKELTVGNPEDN-AYMGPVInqasfdkimsyieiGKEEGRLVLG 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 821 ltklGAGEqwvvqprklDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAK 900
Cdd:PRK03137 387 ----GEGD---------DSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNRE 453
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2066550363 901 EIATWVDSIEAGNLYVNRGITGAIVQRQPFGGWKKSvvGPTTKAGGPNYLHalgdWHTAAAT 962
Cdd:PRK03137 454 HLEKARREFHVGNLYFNRGCTGAIVGYHPFGGFNMS--GTDSKAGGPDYLL----LFLQAKT 509
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
542-952 |
1.49e-83 |
|
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: 279.09 E-value: 1.49e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 542 IRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELAVALEQVDGAE 621
Cdd:cd07078 4 VAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVIPS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 622 YDPSRLVVVTP----------PWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPREALQYVQFSD 691
Cdd:cd07078 84 PDPGELAIVRReplgvvgaitPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 692 RELGRALVADDAVDRVILTGGFETAELF-----RSFRPdleLLAETSGKNAIIVTPSADYDLAAKDVIASAFGHAGQKCS 766
Cdd:cd07078 164 DEVGAALASHPRVDKISFTGSTAVGKAImraaaENLKR---VTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 767 AASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLDGLTKLGAGEQWVVQ---PRKLDEEGRL 843
Cdd:cd07078 241 AASRLLV--HESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLcggKRLEGGKGYF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 844 WSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGNLYVNRGITGA 923
Cdd:cd07078 319 VPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGA 398
|
410 420
....*....|....*....|....*....
gi 2066550363 924 IVQrQPFGGWKKSVVGpttKAGGPNYLHA 952
Cdd:cd07078 399 EPS-APFGGVKQSGIG---REGGPYGLEE 423
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
151-442 |
7.22e-82 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 269.36 E-value: 7.22e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 151 AIEKIRKPGIRLNMNLLGEAVLGKKEADRRLEGTKALLA----------RPDVDYVSIKVSATTAPHQPWAFEESVEEVI 220
Cdd:pfam01619 4 TIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDalgkaagpwpLGPRPGISVKLSALHPRYEPLERERVMAELL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 221 AKLLPLYQLAKNAPtpKFINLDMEEYRDLEMTMAVFTRILDRPEFLGLE-AGIVLQAYLPDALDAMIRLQEWsaARvaRG 299
Cdd:pfam01619 84 ERLRPLCRLAKELG--VRLNIDAEEADRLDLTLDLFERLLAEPELRGWNgVGITLQAYLKDALAVLDWLLEL--AR--RR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 300 GAPIKIRLVKGANLPMERVEASLHGWPVATWGSKQDTDTNYKRCVDYALqpEHVKHVRIGVAGHNLFDVALSWLLAKQRG 379
Cdd:pfam01619 158 GRPLGVRLVKGAYWDSEIKRAQQGGWPYPVFTRKEATDANYEACARFLL--ENHDRIYPQFATHNARSVAAALALAEELG 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2066550363 380 VTEG-IEYEMLLGMAQGQAEVVKRDVGSLLLYTPVVHPSEFdvaIAYLIRRLEEGASPENFMSA 442
Cdd:pfam01619 236 IPPRrFEFQQLYGMGDNLSFALVAAGYRVRKYAPVGPHEEL---LAYLVRRLLENTANSSFVRR 296
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
154-1028 |
2.01e-77 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 279.94 E-value: 2.01e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 154 KIRKPGIRLNMNLLGEAVLGKKEADRRLEG--------TKALLAR-----PDVdyvSIKVSATTAPHQPWAFEESVEEVI 220
Cdd:PRK11809 274 KLEEKGFRYSYDMLGEAALTEADAQAYLASyeqaihaiGKASNGRgiyegPGI---SIKLSALHPRYSRAQYDRVMEELY 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 221 AKLLPLYQLAKNAPTPkfINLDMEEYRDLEMTMAVFTRILDRPEFLGLEA-GIVLQAYL---PDALDAMIRLQEWSAARv 296
Cdd:PRK11809 351 PRLKSLTLLARQYDIG--INIDAEEADRLEISLDLLEKLCFEPELAGWNGiGFVIQAYQkrcPFVIDYLIDLARRSRRR- 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 297 arggapIKIRLVKGANLPMERVEAS---LHGWPVATwgSKQDTDTNYKRCVDYALQ-PEHVKHvriGVAGHNLFDVALSW 372
Cdd:PRK11809 428 ------LMIRLVKGAYWDSEIKRAQvdgLEGYPVYT--RKVYTDVSYLACARKLLAvPNLIYP---QFATHNAHTLAAIY 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 373 LLAKQRGVTEGIEYEMLLGMAQGQAEVVkrdVGSLL---------LYTPV-VHpsefDVAIAYLIRR-LEEGASpenfMS 441
Cdd:PRK11809 497 HLAGQNYYPGQYEFQCLHGMGEPLYEQV---VGKVAdgklnrpcrIYAPVgTH----ETLLAYLVRRlLENGAN----TS 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 442 AVFELAENEdlfereshrflASVDALDA----EVPAPNRVQDRTAAPEP------------------LDVSN-------- 491
Cdd:PRK11809 566 FVNRIADTS-----------LPLDELVAdpveAVEKLAQQEGQLGLPHPkiplprdlygkgransagLDLANehrlasls 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 492 -GFVNTAD----SDPSLPANQEWA--RRIREAAKASTLGNDTIEAntvgTAEELASRIRTALDANAIWRDLPAAERAAIL 564
Cdd:PRK11809 635 sALLASAHqkwqAAPMLEDPVAAGemSPVINPADPRDIVGYVREA----TPAEVEQALESAVNAAPIWFATPPAERAAIL 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 565 HKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAelAVALEQVDGAEYDPSRLVVVTPPWNFPVAIPAGS 644
Cdd:PRK11809 711 ERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYA--GQVRDDFDNDTHRPLGPVVCISPWNFPLAIFTGQ 788
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 645 TLAALASGASVIIKPARQAARCGAVMVEALWAAGVPREALQYVQFSDRELGRALVADDAVDRVILTGGFETAELF-RSF- 722
Cdd:PRK11809 789 VAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLqRNLa 868
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 723 -------RPdLELLAETSGKNAIIVTPSADYDLAAKDVIASAFGHAGQKCSAasLVILVGQAARSKRFRSQLLDGVRSID 795
Cdd:PRK11809 869 grldpqgRP-IPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSA--LRVLCLQDDVADRTLKMLRGAMAECR 945
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 796 VGYPTEATTQMGPIIGpAEGK--LLDGLTKLGAGEQWVVQPRKLDEEgrlwspgvrsGVRRG-------------SEYHR 860
Cdd:PRK11809 946 MGNPDRLSTDIGPVID-AEAKanIERHIQAMRAKGRPVFQAARENSE----------DWQSGtfvpptlieldsfDELKR 1014
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 861 tEYFGPVLGIM--TAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGNLYVNRGITGAIVQRQPFGGWKKSVV 938
Cdd:PRK11809 1015 -EVFGPVLHVVryNRNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGT 1093
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 939 GPttKAGGPNYLHAL-------GDWHTAAATKGAEIADAHVKGLLDGARSCP----DVSAEDAAALERAFRSDELAwqed 1007
Cdd:PRK11809 1094 GP--KAGGPLYLYRLlatrpedALAVTLARQDAEYPVDAQLRAALLAPLTALrewaAEREPELAALCDQYAELAQA---- 1167
|
970 980
....*....|....*....|.
gi 2066550363 1008 fGVARDVQGLYAERNVFRYLP 1028
Cdd:PRK11809 1168 -GTTRLLPGPTGERNTYTLLP 1187
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
524-940 |
1.17e-75 |
|
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: 258.33 E-value: 1.17e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 524 NDTIEANTVGTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDF 603
Cdd:cd07097 25 SDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARGEVTRAGQI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 604 AHYYAELAVALEqvdGAEYDPSR-------------LVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVM 670
Cdd:cd07097 105 FRYYAGEALRLS---GETLPSTRpgvevettreplgVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWAL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 671 VEALWAAGVPREALQYVQFSDRELGRALVADDAVDRVILTGGFET------AELFRSFRPDLELlaetSGKNAIIVTPSA 744
Cdd:cd07097 182 VEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVgrriaaAAAARGARVQLEM----GGKNPLVVLDDA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 745 DYDLAAKDVIASAFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPI--------------I 810
Cdd:cd07097 258 DLDLAVECAVQGAFFSTGQRCTASSRLIV--TEGIHDRFVEALVERTKALKVGDALDEGVDIGPVvserqlekdlryieI 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 811 GPAEG-KLLDGltklgaGEqwvvqPRKLDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYG 889
Cdd:cd07097 336 ARSEGaKLVYG------GE-----RLKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFG 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2066550363 890 LTAGLHSLDAKEIATWVDSIEAGNLYVNRGITGAIVQrQPFGGWKKSVVGP 940
Cdd:cd07097 405 LSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYH-VPFGGRKGSSYGP 454
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
107-981 |
3.18e-75 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 271.81 E-value: 3.18e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 107 RSAIRAGGLATKVAPqVVVPIARRVLRAMVGHLIIDATDSKLGGAIEKIRKPGIRLNMNLLGEAVLGKKEADRRLE---- 182
Cdd:COG4230 149 LASGLLRLLGRLGRP-GIRRAMRAAMMMMMGLFGVGFVTEEAAEAARKAARKREYYYYDMLGEAAAAAADAAAYAYayaa 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 183 ------GTKALLARPDVDYVSIKVSATTAPHQPWAFEESVEEVIAKLLPLYQLAKNAPtpKFINLDMEEYRDLEMTMAVF 256
Cdd:COG4230 228 aaaaaiAAAGGGSGGPGPSISSSLSVLLSARHPRYRRRREERLLLLLLPLLALLALAA--ININIDEEEDAEELLLLLLL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 257 TRILDRPEFLGLEAG-IVLQAYLPDALDAMIRLQEWSAARVARGGAPIKIRLVKGANLPMERVEASLHGWPVATwgskqD 335
Cdd:COG4230 306 LDLLAALLLDGGLGGgGGVGQAVQAYAKALLLVLDLLARRRRRRRRRLVVRLVKGAEWDREIQRAQVLGYVVYP-----V 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 336 TDTNYKRCVDYALQPEHVKHVRIGVAGHNLFDVALSWLLAKQRGVTEGIEYEMLLGMAQGQAEVVKRD-----------V 404
Cdd:COG4230 381 TTRKVLYDAAALALALLLLAAQPAFAPQFATHAAATAAAAAAAGGGGEFEFQCLHGMGEYLYDQVGRGklgrpcriyapV 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 405 GS---LLlytpvvhpsefdvaiAYLIRRL-EEGA-------------SPENFMSAVFELAEN------------EDLF-- 453
Cdd:COG4230 461 GShedLL---------------AYLVRRLlENGAnssfvnriadedvPVEELIADPVEKARAlggaphpriplpRDLYgp 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 454 ERESHRFL-----ASVDALDAEVpAPNRVQDRTAAPepldVSNGFVNTADSDPSL-PANQewARRIREAAKAstlgndti 527
Cdd:COG4230 526 ERRNSAGLdlsdeAVLAALSAAL-AAAAEKQWQAAP----LIAGEAASGEARPVRnPADH--SDVVGTVVEA-------- 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 528 eantvgTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYY 607
Cdd:COG4230 591 ------TAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAIAEVREAVDFCRYY 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 608 AELAVALEqvDGAEYDPSRLVVVT-PPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPREALQY 686
Cdd:COG4230 665 AAQARRLF--AAPTVLRGRGVFVCiSPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQL 742
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 687 VQFSDRELGRALVADDAVDRVILTGGFETA-----ELFRSFRPDLELLAETSGKNAIIVTPSADYDLAAKDVIASAFGHA 761
Cdd:COG4230 743 LPGDGETVGAALVADPRIAGVAFTGSTETArlinrTLAARDGPIVPLIAETGGQNAMIVDSSALPEQVVDDVLASAFDSA 822
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 762 GQKCSAasLVILVGQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGpAEGKllDGLtklgagEQWVvqpRKLDEEG 841
Cdd:COG4230 823 GQRCSA--LRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVID-AEAR--ANL------EAHI---ERMRAEG 888
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 842 RL-WSPGVRSGVRRG-------------SEYHRtEYFGPVLGIMT--AATLEEAIEIANEVDYGLTAGLHS-LDAKeIAT 904
Cdd:COG4230 889 RLvHQLPLPEECANGtfvaptlieidsiSDLER-EVFGPVLHVVRykADELDKVIDAINATGYGLTLGVHSrIDET-IDR 966
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2066550363 905 WVDSIEAGNLYVNRGITGAIVQRQPFGGWKKSVVGPttKAGGPNYLHALGDWHTAAATKGAEIADAHVKGLLDGARS 981
Cdd:COG4230 967 VAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGP--KAGGPHYLLRFATERTVTVNTTAAGGNASLLALGDWLAS 1041
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
533-936 |
5.12e-74 |
|
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: 254.19 E-value: 5.12e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 533 GTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELA- 611
Cdd:cd07131 34 STASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGr 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 612 ------VALEQVDGAEYD---PSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPRE 682
Cdd:cd07131 114 rlfgetVPSELPNKDAMTrrqPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 683 ALQYVQFSDRELGRALVADDAVDRVILTGGFETAELF-----RSFRPdleLLAETSGKNAIIVTPSADYDLAAKDVIASA 757
Cdd:cd07131 194 VVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIgetcaRPNKR---VALEMGGKNPIIVMDDADLDLALEGALWSA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 758 FGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAE----------GKlLDGLTKLGAG 827
Cdd:cd07131 271 FGTTGQRCTATSRLIV--HESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQlekvlnyneiGK-EEGATLLLGG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 828 EQwvvQPRKLDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVD 907
Cdd:cd07131 348 ER---LTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARR 424
|
410 420
....*....|....*....|....*....
gi 2066550363 908 SIEAGNLYVNRGITGAIVQrQPFGGWKKS 936
Cdd:cd07131 425 DLEAGITYVNAPTIGAEVH-LPFGGVKKS 452
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
537-950 |
1.02e-72 |
|
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: 250.96 E-value: 1.02e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 537 ELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELAVALE- 615
Cdd:cd07083 56 EAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRy 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 616 ----------QVDGAEYDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPREALQ 685
Cdd:cd07083 136 pavevvpypgEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQ 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 686 YVQFSDRELGRALVADDAVDRVILTGGFETAEL-----------FRSFRPdleLLAETSGKNAIIVTPSADYDLAAKDVI 754
Cdd:cd07083 216 FLPGVGEEVGAYLTEHERIRGINFTGSLETGKKiyeaaarlapgQTWFKR---LYVETGGKNAIIVDETADFELVVEGVV 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 755 ASAFGHAGQKCSAASLVILVGQAArsKRFRSQLLDGVRSIDVGYPTEATTQMGPII-GPAEGKLLDGLTKLGAGEQWVVQ 833
Cdd:cd07083 293 VSAFGFQGQKCSAASRLILTQGAY--EPVLERLLKRAERLSVGPPEENGTDLGPVIdAEQEAKVLSYIEHGKNEGQLVLG 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 834 PRKLDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMT--AATLEEAIEIANEVDYGLTAGLHSLDaKEIATWV-DSIE 910
Cdd:cd07083 371 GKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRykDDDFAEALEVANSTPYGLTGGVYSRK-REHLEEArREFH 449
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2066550363 911 AGNLYVNRGITGAIVQRQPFGGWKKSVVGPttKAGGPNYL 950
Cdd:cd07083 450 VGNLYINRKITGALVGVQPFGGFKLSGTNA--KTGGPHYL 487
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
535-953 |
5.90e-69 |
|
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: 240.58 E-value: 5.90e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 535 AEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAElaVAL 614
Cdd:TIGR01238 73 LAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAK--QVR 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 615 EQVDGAEYDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPREALQYVQFSDREL 694
Cdd:TIGR01238 151 DVLGEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADV 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 695 GRALVADDAVDRVILTGGFETAELF-----RSFRPDLELLAETSGKNAIIVTPSADYDLAAKDVIASAFGHAGQKCSAas 769
Cdd:TIGR01238 231 GAALTSDPRIAGVAFTGSTEVAQLInqtlaQREDAPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSA-- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 770 LVILVGQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPII-GPAEGKLLDGLTKLGAGEQWVVQPRKLDEEGRLWSPGV 848
Cdd:TIGR01238 309 LRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIdAEAKQNLLAHIEHMSQTQKKIAQLTLDDSRACQHGTFV 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 849 RSGVRRGSEYH--RTEYFGPVLGIM--TAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGNLYVNRGITGAI 924
Cdd:TIGR01238 389 APTLFELDDIAelSEEVFGPVLHVVryKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAV 468
|
410 420
....*....|....*....|....*....
gi 2066550363 925 VQRQPFGGWKKSVVGPttKAGGPNYLHAL 953
Cdd:TIGR01238 469 VGVQPFGGQGLSGTGP--KAGGPHYLYRL 495
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
548-952 |
3.28e-68 |
|
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: 234.05 E-value: 3.28e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 548 ANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELAVALEQVDGAEYDPSRL 627
Cdd:cd06534 6 AFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPGGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 628 VVVTP----------PWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPREALQYVQFSDRELGRA 697
Cdd:cd06534 86 AYVRReplgvvgvitPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 698 LVADDAVDRVILTGGFETAELFR-----SFRPdleLLAETSGKNAIIVTPSADYDLAAKDVIASAFGHAGQKCSAASLVI 772
Cdd:cd06534 166 LLSHPRVDKISFTGSTAVGKAIMkaaaeNLKP---VTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 773 LVGQAARskRFRSQLLdgvrsidvgypteattqmgpiigpaegklldgltklgageqwvvqprkldeegrlwspGVRSGV 852
Cdd:cd06534 243 VHESIYD--EFVEKLV----------------------------------------------------------TVLVDV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 853 RRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGNLYVNRGITGAIVQrQPFGG 932
Cdd:cd06534 263 DPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPE-APFGG 341
|
410 420
....*....|....*....|
gi 2066550363 933 WKKSVVGpttKAGGPNYLHA 952
Cdd:cd06534 342 VKNSGIG---REGGPYGLEE 358
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
524-936 |
9.69e-65 |
|
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: 227.83 E-value: 9.69e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 524 NDTIEANTVGTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDF 603
Cdd:cd07086 23 GEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLGEVQEMIDI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 604 AHYYAELA-------VALEQVDGAEYD---PSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCG----AV 669
Cdd:cd07086 103 CDYAVGLSrmlygltIPSERPGHRLMEqwnPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAiavtKI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 670 MVEALWAAGVPREALQYVQfSDRELGRALVADDAVDRVILTGGFET--------AELFRsfRPDLELlaetSGKNAIIVT 741
Cdd:cd07086 183 LAEVLEKNGLPPGVVNLVT-GGGDGGELLVHDPRVPLVSFTGSTEVgrrvgetvARRFG--RVLLEL----GGNNAIIVM 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 742 PSADYDLAAKDVIASAFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPA-------- 813
Cdd:cd07086 256 DDADLDLAVRAVLFAAVGTAGQRCTTTRRLIV--HESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAavekylna 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 814 --EGKlLDGLTKLGAGEqwvVQPRklDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLT 891
Cdd:cd07086 334 ieIAK-SQGGTVLTGGK---RIDG--GEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLS 407
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2066550363 892 AGLHSLDAKEIATWVD--SIEAGNLYVNRGITGAIVQrQPFGGWKKS 936
Cdd:cd07086 408 SSIFTEDLREAFRWLGpkGSDCGIVNVNIPTSGAEIG-GAFGGEKET 453
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
533-939 |
2.53e-60 |
|
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: 214.82 E-value: 2.53e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 533 GTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELAV 612
Cdd:cd07088 32 ATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARVEVEFTADYIDYMAEWAR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 613 ALE----QVDGAEYD------PSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPRE 682
Cdd:cd07088 112 RIEgeiiPSDRPNENififkvPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 683 ALQYVQFSDRELGRALVADDAVDRVILTGGFET-AELFRS-----FRPDLELlaetSGKNAIIVTPSADYDLAAKDVIAS 756
Cdd:cd07088 192 VLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAgQKIMEAaaeniTKVSLEL----GGKAPAIVMKDADLDLAVKAIVDS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 757 AFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLDGLTKLG--AGEQWVVQP 834
Cdd:cd07088 268 RIINCGQVCTCAERVYV--HEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMVERAveAGATLLTGG 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 835 RKLD-EEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGN 913
Cdd:cd07088 346 KRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGE 425
|
410 420
....*....|....*....|....*..
gi 2066550363 914 LYVNRGITGAIvqrQPF-GGWKKSVVG 939
Cdd:cd07088 426 TYINRENFEAM---QGFhAGWKKSGLG 449
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
552-936 |
1.50e-58 |
|
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: 208.28 E-value: 1.50e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 552 WRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPE-------ISEAIDFAHYYA-ELAVALEQVDGA-EY 622
Cdd:cd07095 16 WAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEvaamagkIDISIKAYHERTgERATPMAQGRAVlRH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 623 DPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPREALQYVQfSDRELGRALVADD 702
Cdd:cd07095 96 RPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQ-GGRETGEALAAHE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 703 AVDRVILTGGFETAELF-RSF--RPDLELLAETSGKNAIIVTPSADYDLAAKDVIASAFGHAGQKCSAASLVILVgQAAR 779
Cdd:cd07095 175 GIDGLLFTGSAATGLLLhRQFagRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIVP-DGAV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 780 SKRFRSQLLDGVRSIDVGYPTEATTQMGPII--GPAEGKLLDGLTKLGAGEQWVVQPRKLDEEGRLWSPGVRSgVRRGSE 857
Cdd:cd07095 254 GDAFLERLVEAAKRLRIGAPDAEPPFMGPLIiaAAAARYLLAQQDLLALGGEPLLAMERLVAGTAFLSPGIID-VTDAAD 332
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2066550363 858 YHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGNLYVNRGITGAiVQRQPFGGWKKS 936
Cdd:cd07095 333 VPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTTGA-SSTAPFGGVGLS 410
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
533-939 |
1.66e-58 |
|
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: 208.83 E-value: 1.66e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 533 GTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELAV 612
Cdd:cd07103 16 AGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVDYAASFLEWFAEEAR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 613 aleQVDGaEYDPS-----RLVVVT-P--------PWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAG 678
Cdd:cd07103 96 ---RIYG-RTIPSpapgkRILVIKqPvgvvaaitPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAEEAG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 679 VPREALQYVQFSDRELGRALVADDAVDRVILTGGFET--------AELFRsfRPDLELlaetsGKNA-IIVTPSADYDLA 749
Cdd:cd07103 172 LPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVgkllmaqaADTVK--RVSLEL-----GGNApFIVFDDADLDKA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 750 AKDVIASAFGHAGQKCSAASLvILVgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLDGLTK--LGAG 827
Cdd:cd07103 245 VDGAIASKFRNAGQTCVCANR-IYV-HESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEdaVAKG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 828 EQWVVQPRKLDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVD 907
Cdd:cd07103 323 AKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAE 402
|
410 420 430
....*....|....*....|....*....|..
gi 2066550363 908 SIEAGNLYVNRGITGAIVqrQPFGGWKKSVVG 939
Cdd:cd07103 403 ALEAGMVGINTGLISDAE--APFGGVKESGLG 432
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
538-939 |
2.56e-56 |
|
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: 201.92 E-value: 2.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 538 LASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELAVAL--- 614
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFlad 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 615 EQVDGA------EYDPSRLVVVTPPWNFP------VAIPAgstlaaLASGASVIIKPARQAARCGAVMVEALWAAGVPRE 682
Cdd:cd07100 81 EPIETDagkayvRYEPLGVVLGIMPWNFPfwqvfrFAAPN------LMAGNTVLLKHASNVPGCALAIEELFREAGFPEG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 683 ALQYVqFSDRELGRALVADDAVDRVILTGGfETAElfRSfrpdlelLAETSGKN------------AIIVTPSADYDLAA 750
Cdd:cd07100 155 VFQNL-LIDSDQVEAIIADPRVRGVTLTGS-ERAG--RA-------VAAEAGKNlkksvlelggsdPFIVLDDADLDKAV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 751 KDVIASAFGHAGQKCSAASLVILVGQAArsKRFRSQLLDGVRSIDVGYPTEATTQMGPIigpAEGKLLDGLTK-----LG 825
Cdd:cd07100 224 KTAVKGRLQNAGQSCIAAKRFIVHEDVY--DEFLEKFVEAMAALKVGDPMDEDTDLGPL---ARKDLRDELHEqveeaVA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 826 AGEQWVVQPRKLDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATW 905
Cdd:cd07100 299 AGATLLLGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERV 378
|
410 420 430
....*....|....*....|....*....|....
gi 2066550363 906 VDSIEAGNLYVNrGITGAiVQRQPFGGWKKSVVG 939
Cdd:cd07100 379 ARRLEAGMVFIN-GMVKS-DPRLPFGGVKRSGYG 410
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
534-939 |
2.63e-56 |
|
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: 202.66 E-value: 2.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 534 TAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELAVA 613
Cdd:cd07094 19 DRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRAIDTLRLAAEEAER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 614 L--EQVDGAEYDPS--RLVVVTP----------PWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGV 679
Cdd:cd07094 99 IrgEEIPLDATQGSdnRLAWTIRepvgvvlaitPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILVEAGV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 680 PREALQYVQFSDRELGRALVADDAVDRVILTGGFETAELFRSFRPDLELLAETSGKNAIIVTPSADYDLAAKDVIASAFG 759
Cdd:cd07094 179 PEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKRIALELGGNAPVIVDRDADLDAAIEALAKGGFY 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 760 HAGQKCSAASLVILVGQAArsKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLL---------DGLTKLGAGEQw 830
Cdd:cd07094 259 HAGQVCISVQRIYVHEELY--DEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVerwveeaveAGARLLCGGER- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 831 vvqprkldeEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIE 910
Cdd:cd07094 336 ---------DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLE 406
|
410 420
....*....|....*....|....*....
gi 2066550363 911 AGNLYVNRGiTGAIVQRQPFGGWKKSVVG 939
Cdd:cd07094 407 VGGVMVNDS-SAFRTDWMPFGGVKESGVG 434
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
534-939 |
5.52e-56 |
|
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: 202.03 E-value: 5.52e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 534 TAEELASRIRTALDA-NAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAElav 612
Cdd:cd07082 36 SALEILEAAETAYDAgRGWWPTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALKEVDRTIDYIRDTIE--- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 613 ALEQVDG--AEYD---------------PSRLVVVTPPWNFPVAIPAgSTLA-ALASGASVIIKPARQAARCGAVMVEAL 674
Cdd:cd07082 113 ELKRLDGdsLPGDwfpgtkgkiaqvrrePLGVVLAIGPFNYPLNLTV-SKLIpALIMGNTVVFKPATQGVLLGIPLAEAF 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 675 WAAGVPREALQYVQFSDRELGRALVADDAVDRVILTGGFETAELFRSFRPDLELLAETSGKNAIIVTPSADYDLAAKDVI 754
Cdd:cd07082 192 HDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHPMKRLVLELGGKDPAIVLPDADLELAAKEIV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 755 ASAFGHAGQKCSAASLVILVGQAARskRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPA-----EGKLLDGLTKlGAGeq 829
Cdd:cd07082 272 KGALSYSGQRCTAIKRVLVHESVAD--ELVELLKEEVAKLKVGMPWDNGVDITPLIDPKsadfvEGLIDDAVAK-GAT-- 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 830 wVVQPRKlDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSI 909
Cdd:cd07082 347 -VLNGGG-REGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADAL 424
|
410 420 430
....*....|....*....|....*....|....
gi 2066550363 910 EAGNLYVNRGitgaiVQRQ----PFGGWKKSVVG 939
Cdd:cd07082 425 EVGTVNINSK-----CQRGpdhfPFLGRKDSGIG 453
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
537-957 |
5.87e-56 |
|
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: 200.83 E-value: 5.87e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 537 ELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELAVALE- 615
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 616 -----QVDG----AEYDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMV-EALWAAGVPREALQ 685
Cdd:cd07104 81 eilpsDVPGkesmVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIaEIFEEAGLPKGVLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 686 YVQFSDRELGRALVADDAVDRVILTG----GFETAELF-RSF-RPDLELlaetSGKNAIIVTPSADYDLAAKDVIASAFG 759
Cdd:cd07104 161 VVPGGGSEIGDALVEHPRVRMISFTGstavGRHIGELAgRHLkKVALEL----GGNNPLIVLDDADLDLAVSAAAFGAFL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 760 HAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLDGL--------TKLGAGEQWv 831
Cdd:cd07104 237 HQGQICMAAGRILV--HESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIvedavaagARLLTGGTY- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 832 vqprkldeEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLD---AKEIAtwvDS 908
Cdd:cd07104 314 --------EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDlerAMAFA---ER 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2066550363 909 IEAGNLYVNrGIT---GAIVqrqPFGGWKKSVVGpttKAGGPNYLHALGDWH 957
Cdd:cd07104 383 LETGMVHIN-DQTvndEPHV---PFGGVKASGGG---RFGGPASLEEFTEWQ 427
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
532-936 |
4.06e-55 |
|
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: 198.98 E-value: 4.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 532 VGTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELA 611
Cdd:cd07099 14 VTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLALEAIDWAARNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 612 -------------VALEQVDGAEYDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAG 678
Cdd:cd07099 94 prvlaprkvptglLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 679 VPREALQYVQfSDRELGRALVaDDAVDRVILTGGFET-----AELFRSFRPdleLLAETSGKNAIIVTPSADYDLAAKDV 753
Cdd:cd07099 174 PPQGVLQVVT-GDGATGAALI-DAGVDKVAFTGSVATgrkvmAAAAERLIP---VVLELGGKDPMIVLADADLERAAAAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 754 IASAFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPA-----EGKLLDGLTKlgaGE 828
Cdd:cd07099 249 VWGAMVNAGQTCISVERVYV--HESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARqldivRRHVDDAVAK---GA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 829 QWVVQPRKLDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLD---AKEIATw 905
Cdd:cd07099 324 KALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDlarAEAIAR- 402
|
410 420 430
....*....|....*....|....*....|.
gi 2066550363 906 vdSIEAGNLYVNRGITGAIVQRQPFGGWKKS 936
Cdd:cd07099 403 --RLEAGAVSINDVLLTAGIPALPFGGVKDS 431
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
533-936 |
5.81e-54 |
|
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: 195.92 E-value: 5.81e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 533 GTAEELASRIRTALDA-NAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELA 611
Cdd:cd07109 16 GGAADVDRAVQAARRAfESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEAAARYFEYYGGAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 612 VALE---------QVDGAEYDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPRE 682
Cdd:cd07109 96 DKLHgetiplgpgYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAGLPAG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 683 ALQYVQFSDRELGRALVADDAVDRVILTGGFETAELF------RSFRPDLELlaetSGKNAIIVTPSADYDLAAKDVIAS 756
Cdd:cd07109 176 ALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVmraaaeNVVPVTLEL----GGKSPQIVFADADLEAALPVVVNA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 757 AFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGyPTEATTQMGPIIGPAEGKLLDGLTKLGA--GEQWVVQP 834
Cdd:cd07109 252 IIQNAGQTCSAGSRLLV--HRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRVEGFVARARarGARIVAGG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 835 RKLD---EEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEiATWV-DSIE 910
Cdd:cd07109 329 RIAEgapAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDR-ALRVaRRLR 407
|
410 420
....*....|....*....|....*.
gi 2066550363 911 AGNLYVNRGITGAIVQRqPFGGWKKS 936
Cdd:cd07109 408 AGQVFVNNYGAGGGIEL-PFGGVKKS 432
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
532-939 |
7.74e-54 |
|
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: 195.51 E-value: 7.74e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 532 VGTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELA 611
Cdd:cd07149 17 VASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDRAIETLRLSAEEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 612 -------VALEQVDGAE-------YDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAA 677
Cdd:cd07149 97 krlagetIPFDASPGGEgrigftiREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 678 GVPREALQYVQFSDRELGRALVADDAVDRVILTGGFETAELFRSFRPDLELLAETSGKNAIIVTPSADYDLAAKDVIASA 757
Cdd:cd07149 177 GLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLKKVTLELGSNAAVIVDADADLEKAVERCVSGA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 758 FGHAGQKCSAASLvILVgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEgklldgltkLGAGEQWVVQP--- 834
Cdd:cd07149 257 FANAGQVCISVQR-IFV-HEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAE---------AERIEEWVEEAveg 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 835 -----RKLDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSI 909
Cdd:cd07149 326 garllTGGKRDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAAREL 405
|
410 420 430
....*....|....*....|....*....|
gi 2066550363 910 EAGNLYVNrGITGAIVQRQPFGGWKKSVVG 939
Cdd:cd07149 406 EVGGVMIN-DSSTFRVDHMPYGGVKESGTG 434
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
534-941 |
8.05e-52 |
|
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: 189.38 E-value: 8.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 534 TAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELAV- 612
Cdd:cd07102 16 SLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMISIAEe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 613 ALEQVDGAEYD---------PSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPREA 683
Cdd:cd07102 96 ALADIRVPEKDgferyirrePLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 684 LQYVqFSDRELGRALVADDAVDRVILTGGFET-AELFRS----FRP-DLELlaetSGKNAIIVTPSADYDLAAKDVIASA 757
Cdd:cd07102 176 FQVL-HLSHETSAALIADPRIDHVSFTGSVAGgRAIQRAaagrFIKvGLEL----GGKDPAYVRPDADLDAAAESLVDGA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 758 FGHAGQKCSAASLvILVgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLDGLTK--LGAGEQWVVQPR 835
Cdd:cd07102 251 FFNSGQSCCSIER-IYV-HESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIAdaIAKGARALIDGA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 836 KL---DEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAG 912
Cdd:cd07102 329 LFpedKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETG 408
|
410 420
....*....|....*....|....*....
gi 2066550363 913 NLYVNRGItgAIVQRQPFGGWKKSVVGPT 941
Cdd:cd07102 409 TVFMNRCD--YLDPALAWTGVKDSGRGVT 435
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
533-939 |
1.26e-51 |
|
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: 189.65 E-value: 1.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 533 GTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAhyyaELAV 612
Cdd:cd07085 35 ATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADARGDVLRGLEVV----EFAC 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 613 ALEQVDGAEYdpsrLVVVTP------------------PWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEAL 674
Cdd:cd07085 111 SIPHLLKGEY----LENVARgidtysyrqplgvvagitPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 675 WAAGVPREALQYVQfSDRELGRALVADDAVDRVILTGGFETAELF--RSFRPDLELLAETSGKNAIIVTPSADYDLAAKD 752
Cdd:cd07085 187 QEAGLPDGVLNVVH-GGKEAVNALLDHPDIKAVSFVGSTPVGEYIyeRAAANGKRVQALGGAKNHAVVMPDADLEQTANA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 753 VIASAFGHAGQKCSAASLVILVGQAArsKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLDGLTKLG--AGEQW 830
Cdd:cd07085 266 LVGAAFGAAGQRCMALSVAVAVGDEA--DEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESGveEGAKL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 831 VVQPRKLD----EEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWV 906
Cdd:cd07085 344 VLDGRGVKvpgyENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQ 423
|
410 420 430
....*....|....*....|....*....|...
gi 2066550363 907 DSIEAGNLYVNRGITgAIVQRQPFGGWKKSVVG 939
Cdd:cd07085 424 REVDAGMVGINVPIP-VPLAFFSFGGWKGSFFG 455
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
536-939 |
5.94e-51 |
|
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: 187.17 E-value: 5.94e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 536 EELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAI----DFAHYYAELA 611
Cdd:cd07145 21 EEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVERTIrlfkLAAEEAKVLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 612 VALEQVDGAEYDPSRLVVVT--P--------PWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPR 681
Cdd:cd07145 101 GETIPVDAYEYNERRIAFTVrePigvvgaitPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAGLPP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 682 EALQYVQFSDRELGRALVADDAVDRVILTGGFETAELF--RSFRPDLELLAETSGKNAIIVTPSADYDLAAKDVIASAFG 759
Cdd:cd07145 181 GVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIasKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 760 HAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGP-----AEGKLLDGLTKLGageqwVVQP 834
Cdd:cd07145 261 NAGQVCNAVKRILV--EEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPeaverMENLVNDAVEKGG-----KILY 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 835 RKLDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGNL 914
Cdd:cd07145 334 GGKRDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGV 413
|
410 420
....*....|....*....|....*...
gi 2066550363 915 YVNRGITgaivQRQ---PFGGWKKSVVG 939
Cdd:cd07145 414 VINDSTR----FRWdnlPFGGFKKSGIG 437
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
533-939 |
6.29e-51 |
|
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: 187.00 E-value: 6.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 533 GTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDP-EISEAIDFAHYYAELA 611
Cdd:cd07093 16 GGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTrDIPRAAANFRFFADYI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 612 V-----ALEQVDGA----EYDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPRE 682
Cdd:cd07093 96 LqldgeSYPQDGGAlnyvLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEAGLPPG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 683 ALQYVQFSDRELGRALVADDAVDRVILTGGFETAELF-----RSFRPdleLLAETSGKNAIIVTPSADYDLAAKDVIASA 757
Cdd:cd07093 176 VVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTImraaaPNLKP---VSLELGGKNPNIVFADADLDRAVDAAVRSS 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 758 FGHAGQKCSAASLvILVgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPA---------EGKLLDGLTKLGAGE 828
Cdd:cd07093 253 FSNNGEVCLAGSR-ILV-QRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEhlekvlgyvELARAEGATILTGGG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 829 QWVVQPRkldEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDS 908
Cdd:cd07093 331 RPELPDL---EGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARR 407
|
410 420 430
....*....|....*....|....*....|....*
gi 2066550363 909 IEAGNLYVN----RGItgaivqRQPFGGWKKSVVG 939
Cdd:cd07093 408 LEAGTVWVNcwlvRDL------RTPFGGVKASGIG 436
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
533-939 |
1.50e-50 |
|
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: 185.62 E-value: 1.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 533 GTAEELASRIRTALDA--NAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAEL 610
Cdd:cd07118 16 GTVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 611 AVALEqvdGAEYD-------------PSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAA 677
Cdd:cd07118 96 ARTLH---GDSYNnlgddmlglvlrePIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 678 GVPREALQYVQFSDRELGRALVADDAVDRVILTG--GFETAELFRSFRPDLELLAETSGKNAIIVTPSADYDLAAKDVIA 755
Cdd:cd07118 173 GLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGstRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 756 SAFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLDGLTKLG--AGEQWVVQ 833
Cdd:cd07118 253 GVYFNAGECCNSGSRLLV--HESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGraEGATLLLG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 834 PRKLDE-EGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAG 912
Cdd:cd07118 331 GERLASaAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAG 410
|
410 420
....*....|....*....|....*..
gi 2066550363 913 NLYVNRGITGAivQRQPFGGWKKSVVG 939
Cdd:cd07118 411 TVWVNTFLDGS--PELPFGGFKQSGIG 435
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
532-956 |
3.78e-50 |
|
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: 184.42 E-value: 3.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 532 VGTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELA 611
Cdd:cd07152 9 VADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEAAGLP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 612 -----VALEQVDG----AEYDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMV-EALWAAGVPR 681
Cdd:cd07152 89 tqpqgEILPSAPGrlslARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIaRLFEEAGLPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 682 EALQyVQFSDRELGRALVADDAVDRVILTG----GFETAELF-RSF-RPDLELlaetSGKNAIIVTPSADYDLAAKDVIA 755
Cdd:cd07152 169 GVLH-VLPGGADAGEALVEDPNVAMISFTGstavGRKVGEAAgRHLkKVSLEL----GGKNALIVLDDADLDLAASNGAW 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 756 SAFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLDGLTK--LGAGEQWVVQ 833
Cdd:cd07152 244 GAFLHQGQICMAAGRHLV--HESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDdsVAAGARLEAG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 834 PRKldeEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGN 913
Cdd:cd07152 322 GTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGM 398
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2066550363 914 LYVNRGITGAIVQrQPFGGWKKSvvGPTTKAGGPNYLHALGDW 956
Cdd:cd07152 399 LHINDQTVNDEPH-NPFGGMGAS--GNGSRFGGPANWEEFTQW 438
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
533-939 |
1.01e-49 |
|
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: 183.52 E-value: 1.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 533 GTAEELASRIRTALDA--NAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAEL 610
Cdd:cd07114 16 ASAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVRYLAEWYRYYAGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 611 AVALEQ----VDGAEY------DPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVP 680
Cdd:cd07114 96 ADKIEGavipVDKGDYlnftrrEPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAGFP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 681 REALQYVQFSDRELGRALVADDAVDRVILTGGFETAELF-----RSFRP-DLELlaetSGKNAIIVTPSADYDLAAKDVI 754
Cdd:cd07114 176 PGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIaraaaENLAPvTLEL----GGKSPNIVFDDADLDAAVNGVV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 755 ASAFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLDGLTKLG--AGEQWVV 832
Cdd:cd07114 252 AGIFAAAGQTCVAGSRLLV--QRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAreEGARVLT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 833 QPRKLDEE----GRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDS 908
Cdd:cd07114 330 GGERPSGAdlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARA 409
|
410 420 430
....*....|....*....|....*....|...
gi 2066550363 909 IEAGNLYVN--RgitgAIVQRQPFGGWKKSVVG 939
Cdd:cd07114 410 IEAGTVWVNtyR----ALSPSSPFGGFKDSGIG 438
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
525-939 |
8.93e-49 |
|
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: 180.62 E-value: 8.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 525 DTIEANTVGTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFA 604
Cdd:cd07110 8 ATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDDVAGCF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 605 HYYAELAVALEQVDGAE-------------YDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMV 671
Cdd:cd07110 88 EYYADLAEQLDAKAERAvplpsedfkarvrREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 672 EALWAAGVPREALQYVQFSDRELGRALVADDAVDRVILTGGFETAELF-----RSFRP-DLELlaetSGKNAIIVTPSAD 745
Cdd:cd07110 168 EIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVmqaaaQDIKPvSLEL----GGKSPIIVFDDAD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 746 YDLAAKDVIASAFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLDGLTKLG 825
Cdd:cd07110 244 LEKAVEWAMFGCFWNNGQICSATSRLLV--HESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 826 --AGEQWVVQPRKLD--EEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKE 901
Cdd:cd07110 322 keEGARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAER 401
|
410 420 430
....*....|....*....|....*....|....*...
gi 2066550363 902 IATWVDSIEAGNLYVNrgITGAIVQRQPFGGWKKSVVG 939
Cdd:cd07110 402 CDRVAEALEAGIVWIN--CSQPCFPQAPWGGYKRSGIG 437
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
532-956 |
1.77e-48 |
|
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: 179.83 E-value: 1.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 532 VGTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELA 611
Cdd:cd07150 17 VGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTFTPELLRAAAGEC 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 612 VALE----------QVDGAEYDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPR 681
Cdd:cd07150 97 RRVRgetlpsdspgTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAGLPK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 682 EALQYVQFSDRELGRALVADDAVDRVILTG----GFETAELF-RSFRP-DLELlaetSGKNAIIVTPSADYDLAAKDVIA 755
Cdd:cd07150 177 GVFNVVTGGGAEVGDELVDDPRVRMVTFTGstavGREIAEKAgRHLKKiTLEL----GGKNPLIVLADADLDYAVRAAAF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 756 SAFGHAGQKCSAASLVILVGQAArsKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLDGL--------TKLGAG 827
Cdd:cd07150 253 GAFMHQGQICMSASRIIVEEPVY--DEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQvedavakgAKLLTG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 828 EQWvvqprkldeEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVD 907
Cdd:cd07150 331 GKY---------DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAE 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2066550363 908 SIEAGNLYVNrGITGAIVQRQPFGGWKKSVVGpttKAGGPNYLHALGDW 956
Cdd:cd07150 402 RLESGMVHIN-DPTILDEAHVPFGGVKASGFG---REGGEWSMEEFTEL 446
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
504-939 |
1.03e-47 |
|
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: 178.27 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 504 PANQEWARRIREAAKAstlgnDTIEAntVGTAeelasriRTALDAnAIWRDLPAAERAAILHKAGDELERRRGELMEVAA 583
Cdd:cd07119 20 PANGEVIATVPEGTAE-----DAKRA--IAAA-------RRAFDS-GEWPHLPAQERAALLFRIADKIREDAEELARLET 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 584 SEAGKTLDQSDPEISEAIDFAHYYAELAVAL--EQVDGAEYDPSRLV-------VVTPPWNFPVAIPAGSTLAALASGAS 654
Cdd:cd07119 85 LNTGKTLRESEIDIDDVANCFRYYAGLATKEtgEVYDVPPHVISRTVrepvgvcGLITPWNYPLLQAAWKLAPALAAGNT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 655 VIIKPARQAARCGAVMVEALWAAGVPREALQYVQFSDRELGRALVADDAVDRVILTGGFETAE-LFRSFRPDLELLA-ET 732
Cdd:cd07119 165 VVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRsIMRAAAGNVKKVAlEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 733 SGKNAIIVTPSADYDLAAKDVIASAFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGP 812
Cdd:cd07119 245 GGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLV--EESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 813 AEGKLLDGLTKLGAGE--QWVVQPRKLDE----EGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEV 886
Cdd:cd07119 323 EHREKVLSYIQLGKEEgaRLVCGGKRPTGdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDT 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2066550363 887 DYGLTAGLHSLDAKEIATWVDSIEAGNLYVNRgiTGAIVQRQPFGGWKKSVVG 939
Cdd:cd07119 403 PYGLAGAVWTKDIARANRVARRLRAGTVWIND--YHPYFAEAPWGGYKQSGIG 453
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
524-939 |
1.86e-47 |
|
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: 177.11 E-value: 1.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 524 NDTIEANTVGTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDF 603
Cdd:cd07151 20 GETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANIEWGAAMAI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 604 AHYYAELAVALE------QVDGAEY----DPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMV-E 672
Cdd:cd07151 100 TREAATFPLRMEgrilpsDVPGKENrvyrEPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGLLLaK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 673 ALWAAGVPREALQYVQFSDRELGRALVaDDAVDRVI-LTG----GFETAEL-FRSF-RPDLELlaetSGKNAIIVTPSAD 745
Cdd:cd07151 180 IFEEAGLPKGVLNVVVGAGSEIGDAFV-EHPVPRLIsFTGstpvGRHIGELaGRHLkKVALEL----GGNNPFVVLEDAD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 746 YDLAAKDVIASAFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIgpaEGKLLDGLTKL- 824
Cdd:cd07151 255 IDAAVNAAVFGKFLHQGQICMAINRIIV--HEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLI---NESQVDGLLDKi 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 825 -GAGEQWVVQPRKLDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIA 903
Cdd:cd07151 330 eQAVEEGATLLVGGEAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGV 409
|
410 420 430
....*....|....*....|....*....|....*....
gi 2066550363 904 TWVDSIEAGNLYVNRGitgaIVQRQP---FGGWKKSVVG 939
Cdd:cd07151 410 QFARRIDAGMTHINDQ----PVNDEPhvpFGGEKNSGLG 444
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
532-939 |
1.04e-46 |
|
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: 174.47 E-value: 1.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 532 VGTAEELASRIRTALDANAiwrDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELA 611
Cdd:cd07146 17 AGTEEALREALALAASYRS---TLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAADVLRFAAAEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 612 valEQVDGAEYD-----------------PSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEAL 674
Cdd:cd07146 94 ---LRDDGESFScdltangkarkiftlrePLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 675 WAAGVPREALQYVQFSDRELGRALVADDAVDRVILTGGFETAELFRSFRPDLELLAETSGKNAIIVTPSADYDLAAKDVI 754
Cdd:cd07146 171 YEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYKRQLLELGGNDPLIVMDDADLERAATLAV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 755 ASAFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLDGLTK--LGAGEQWVV 832
Cdd:cd07146 251 AGSYANSGQRCTAVKRILV--HESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEeaIAQGARVLL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 833 QPRKldeEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAG 912
Cdd:cd07146 329 GNQR---QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVG 405
|
410 420
....*....|....*....|....*..
gi 2066550363 913 NLYVNrGITGAIVQRQPFGGWKKSVVG 939
Cdd:cd07146 406 TVNVN-EVPGFRSELSPFGGVKDSGLG 431
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
534-932 |
1.37e-46 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 175.15 E-value: 1.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 534 TAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISE-----AIDFAHYYA 608
Cdd:PRK09457 35 TAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEVTAminkiAISIQAYHE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 609 ELAVALEQVDGA----EYDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPREAL 684
Cdd:PRK09457 115 RTGEKRSEMADGaavlRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 685 QYVQfSDRELGRALVADDAVDRVILTGGFETAE-LFRSF--RPDLELLAETSGKNAIIVTPSADYDLAAKDVIASAFGHA 761
Cdd:PRK09457 195 NLVQ-GGRETGKALAAHPDIDGLLFTGSANTGYlLHRQFagQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 762 GQKCSAASLvILVGQAARSKRFRSQLLDGVRSIDVGYPtEATTQ--MGPIIG-PAEGKLLDGLTKLGA-GEQWVVQPRKL 837
Cdd:PRK09457 274 GQRCTCARR-LLVPQGAQGDAFLARLVAVAKRLTVGRW-DAEPQpfMGAVISeQAAQGLVAAQAQLLAlGGKSLLEMTQL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 838 DEEGRLWSPGVRSgVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGNLYVN 917
Cdd:PRK09457 352 QAGTGLLTPGIID-VTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWN 430
|
410
....*....|....*
gi 2066550363 918 RGITGAiVQRQPFGG 932
Cdd:PRK09457 431 KPLTGA-SSAAPFGG 444
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
533-939 |
1.43e-46 |
|
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: 174.09 E-value: 1.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 533 GTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTL-DQSDPEISEAIDFAHYYAELA 611
Cdd:cd07108 16 SRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPEAAVLADLFRYFGGLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 612 VAL--EQVDGAE-------YDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALwAAGVPRE 682
Cdd:cd07108 96 GELkgETLPFGPdvltytvREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEIL-AQVLPAG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 683 ALQYVQFSDRELGRALVADDAVDRVILTGGFETAELFRSFRPD------LELlaetSGKNAIIVTPSADYDLAAKDVIAS 756
Cdd:cd07108 175 VLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADrlipvsLEL----GGKSPMIVFPDADLDDAVDGAIAG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 757 A-FGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGP----------AEGKLLDGLTKLG 825
Cdd:cd07108 251 MrFTRQGQSCTAGSRLFV--HEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEkqfakvcgyiDLGLSTSGATVLR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 826 AGEQWVVQPrklDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATW 905
Cdd:cd07108 329 GGPLPGEGP---LADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRA 405
|
410 420 430
....*....|....*....|....*....|....
gi 2066550363 906 VDSIEAGNLYVNRGitGAIVQRQPFGGWKKSVVG 939
Cdd:cd07108 406 AHALEAGWVQVNQG--GGQQPGQSYGGFKQSGLG 437
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
542-936 |
2.33e-46 |
|
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: 172.76 E-value: 2.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 542 IRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELAVAL--EQVDG 619
Cdd:cd07105 6 VEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIigGSIPS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 620 AEYDPSRLVVVTP--------PWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPREALQYVQFS- 690
Cdd:cd07105 86 DKPGTLAMVVKEPvgvvlgiaPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVTHSp 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 691 --DRELGRALVADDAVDRVILTG----GFETAELF-RSFRPdleLLAETSGKNAIIVTPSADYDLAAKDVIASAFGHAGQ 763
Cdd:cd07105 166 edAPEVVEALIAHPAVRKVNFTGstrvGRIIAETAaKHLKP---VLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 764 KCSAASLVILVGQAARskRFRSQLLDGVRSIDVGypteaTTQMGPIIGPAEGKLLDGLTK--LGAGEQWVV-QPRKLDEE 840
Cdd:cd07105 243 ICMSTERIIVHESIAD--EFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDdaLSKGAKLVVgGLADESPS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 841 GRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLD---AKEIAtwvDSIEAGNLYVN 917
Cdd:cd07105 316 GTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDlarALAVA---KRIESGAVHIN 392
|
410 420
....*....|....*....|..
gi 2066550363 918 rgitGAIVQRQ---PFGGWKKS 936
Cdd:cd07105 393 ----GMTVHDEptlPHGGVKSS 410
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
533-939 |
6.79e-46 |
|
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: 172.24 E-value: 6.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 533 GTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTL-DQSDPEISEAIDFAHYYAELA 611
Cdd:cd07115 16 ASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIrAARRLDVPRAADTFRYYAGWA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 612 VALE----QVDGAEYD-----PSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPRE 682
Cdd:cd07115 96 DKIEgeviPVRGPFLNytvrePVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAGFPAG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 683 ALQYVQFSDRELGRALVADDAVDRVILTGGFETAE-LFRSFRPDLELLA-ETSGKNAIIVTPSADYDLAAKDVIASAFGH 760
Cdd:cd07115 176 VLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRkIMQGAAGNLKRVSlELGGKSANIVFADADLDAAVRAAATGIFYN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 761 AGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLDGLTKLGA--GEQWVVQPRKLD 838
Cdd:cd07115 256 QGQMCTAGSRLLV--HESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGReeGARLLTGGKRPG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 839 EEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGNLYVNr 918
Cdd:cd07115 334 ARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWIN- 412
|
410 420
....*....|....*....|.
gi 2066550363 919 gITGAIVQRQPFGGWKKSVVG 939
Cdd:cd07115 413 -TYNRFDPGSPFGGYKQSGFG 432
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
531-939 |
8.32e-46 |
|
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: 172.04 E-value: 8.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 531 TVGTAEELASRI---RTALDANAiWRdLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDP-EISEAIDFAHY 606
Cdd:cd07089 14 PDAGAADVDAAIaaaRRAFDTGD-WS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAmQVDGPIGHLRY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 607 YAELAVALEQVDGAEYDP------SRLVVVTP--------PWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVE 672
Cdd:cd07089 92 FADLADSFPWEFDLPVPAlrggpgRRVVRREPvgvvaaitPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 673 ALWAAGVPREALQYVQFSDRELGRALVADDAVDRVILTGGFET--------AELFRsfRPDLELlaetSGKNAIIVTPSA 744
Cdd:cd07089 172 IIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVgrrimaqaAATLK--RVLLEL----GGKSANIVLDDA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 745 DYDLAAKDVIASAFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLDGLTKL 824
Cdd:cd07089 246 DLAAAAPAAVGVCMHNAGQGCALTTRLLV--PRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIAR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 825 G--AGEQWVVQ---PRKLDeEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLD- 898
Cdd:cd07089 324 GrdEGARLVTGggrPAGLD-KGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADv 402
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2066550363 899 --AKEIATwvdSIEAGNLYVNRGITGAIvqRQPFGGWKKSVVG 939
Cdd:cd07089 403 drAYRVAR---RIRTGSVGINGGGGYGP--DAPFGGYKQSGLG 440
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
532-939 |
1.05e-45 |
|
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: 171.72 E-value: 1.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 532 VGTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELA 611
Cdd:cd07101 14 QSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVARYYARRA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 612 VAL---EQVDGA---------EYDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGV 679
Cdd:cd07101 94 ERLlkpRRRRGAipvltrttvNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 680 PREALQYVQFSDRELGRALVadDAVDRVILTGGFETAELF--RSFRPDLELLAETSGKNAIIVTPSADYDLAAKDVIASA 757
Cdd:cd07101 174 PRDLWQVVTGPGSEVGGAIV--DNADYVMFTGSTATGRVVaeRAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRAC 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 758 FGHAGQKCSAASLVILVGQAArsKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEgklLDGLTK-----LGAGEQWVV 832
Cdd:cd07101 252 FSNAGQLCVSIERIYVHESVY--DEFVRRFVARTRALRLGAALDYGPDMGSLISQAQ---LDRVTAhvddaVAKGATVLA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 833 QPRKLDEEGRL-WSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEA 911
Cdd:cd07101 327 GGRARPDLGPYfYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRA 406
|
410 420
....*....|....*....|....*....
gi 2066550363 912 GNLYVNRGITGAIVQRQ-PFGGWKKSVVG 939
Cdd:cd07101 407 GTVNVNEGYAAAWASIDaPMGGMKDSGLG 435
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
534-939 |
1.10e-45 |
|
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: 171.72 E-value: 1.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 534 TAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELAVA 613
Cdd:cd07090 17 GAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDSSADCLEYYAGLAPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 614 LE----QVDGAEY-----DPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPREAL 684
Cdd:cd07090 97 LSgehvPLPGGSFaytrrEPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAGLPDGVF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 685 QYVQfSDRELGRALVADDAVDRVILTGGFETAELFRSFRPD------LELlaetSGKNAIIVTPSADYDLAAKDVIASAF 758
Cdd:cd07090 177 NVVQ-GGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKgikhvtLEL----GGKSPLIIFDDADLENAVNGAMMANF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 759 GHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGP----------AEGKLlDGLTKLGAGE 828
Cdd:cd07090 252 LSQGQVCSNGTRVFV--QRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEehlekvlgyiESAKQ-EGAKVLCGGE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 829 QWVVQPrKLdEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDS 908
Cdd:cd07090 329 RVVPED-GL-ENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQ 406
|
410 420 430
....*....|....*....|....*....|..
gi 2066550363 909 IEAGNLYVNR-GITGAIVqrqPFGGWKKSVVG 939
Cdd:cd07090 407 LQAGTCWINTyNISPVEV---PFGGYKQSGFG 435
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
543-936 |
1.95e-45 |
|
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: 170.86 E-value: 1.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 543 RTALDANAiWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTL-DQSDPEISEAIDFAHYYAElavALEQVDG-- 619
Cdd:cd07112 34 RRAFESGV-WSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPIsDALAVDVPSAANTFRWYAE---AIDKVYGev 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 620 AEYDPSRLVVVT--P--------PWNFPVAIPAGSTLAALASGASVIIKPARQ----AARCGAVMVEAlwaaGVPREALQ 685
Cdd:cd07112 110 APTGPDALALITrePlgvvgavvPWNFPLLMAAWKIAPALAAGNSVVLKPAEQspltALRLAELALEA----GLPAGVLN 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 686 YVQFSDRELGRALVADDAVDRVILTGGFETAELF--RSFRPDL-ELLAETSGKNAIIVTPSA-DYDLAAKDVIASAFGHA 761
Cdd:cd07112 186 VVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFleYSGQSNLkRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQ 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 762 GQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLDGLTKLGAGEQWVV----QPRKL 837
Cdd:cd07112 266 GEVCSAGSRLLV--HESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESGKAEGARLvaggKRVLT 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 838 DEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGNLYVN 917
Cdd:cd07112 344 ETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVN 423
|
410
....*....|....*....
gi 2066550363 918 rgITGAIVQRQPFGGWKKS 936
Cdd:cd07112 424 --CFDEGDITTPFGGFKQS 440
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
533-939 |
2.68e-45 |
|
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: 170.20 E-value: 2.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 533 GTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLD-QSDPEISEAIDFAHYYAELA 611
Cdd:cd07092 16 ASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHlVRDDELPGAVDNFRFFAGAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 612 VALEQVDGAEY----------DPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAArCGAVMVEALWAAGVPR 681
Cdd:cd07092 96 RTLEGPAAGEYlpghtsmirrEPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTP-LTTLLLAELAAEVLPP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 682 EALQYVQFSDRELGRALVADDAVDRVILTGGFET-AELFRSFRPDLELL-AETSGKNAIIVTPSADYDLAAKDVIASAFG 759
Cdd:cd07092 175 GVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTgKKVARAAADTLKRVhLELGGKAPVIVFDDADLDAAVAGIATAGYY 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 760 HAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAE-GKLLDGLTKLGAGEQWVVQPRKLD 838
Cdd:cd07092 255 NAGQDCTAACRVYV--HESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQrERVAGFVERAPAHARVLTGGRRAE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 839 EEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGNLYVNR 918
Cdd:cd07092 333 GPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNT 412
|
410 420
....*....|....*....|.
gi 2066550363 919 GITgaIVQRQPFGGWKKSVVG 939
Cdd:cd07092 413 HIP--LAAEMPHGGFKQSGYG 431
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
523-939 |
3.26e-45 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 171.41 E-value: 3.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 523 GNDTIEANTVGTAEELAS-----------RIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLD 591
Cdd:PLN02278 38 DGKTFPVYNPATGEVIANvpcmgraetndAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 592 QSDPEISEAIDFAHYYAELAValeQVDGaEYDPS-----RLVVV---------TPPWNFPVAIPAGSTLAALASGASVII 657
Cdd:PLN02278 118 EAIGEVAYGASFLEYFAEEAK---RVYG-DIIPSpfpdrRLLVLkqpvgvvgaITPWNFPLAMITRKVGPALAAGCTVVV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 658 KPARQAARCGAVMVEALWAAGVPREALQYVQFSDRELGRALVADDAVDRVILTGGFETAELFRSF------RPDLELlae 731
Cdd:PLN02278 194 KPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGaaatvkRVSLEL--- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 732 tsGKNA-IIVTPSADYDLAAKDVIASAFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPII 810
Cdd:PLN02278 271 --GGNApFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILV--QEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 811 GPA-----EGKLLDGLTKlgaGEQWVVQPRKLDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANE 885
Cdd:PLN02278 347 NEAavqkvESHVQDAVSK---GAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIAND 423
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2066550363 886 VDYGLTAGLHSLDAKEIATWVDSIEAGNLYVNRGITGAIVqrQPFGGWKKSVVG 939
Cdd:PLN02278 424 TEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEV--APFGGVKQSGLG 475
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
533-939 |
4.25e-45 |
|
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: 169.99 E-value: 4.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 533 GTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDP-EISEAIDFAHYYAEla 611
Cdd:cd07138 33 GTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPITLARAaQVGLGIGHLRAAAD-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 612 vALEQVDGAEYDPSRLVVVTP--------PWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPREA 683
Cdd:cd07138 111 -ALKDFEFEERRGNSLVVREPigvcglitPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 684 LQYVQFSDRELGRALVADDAVDRVILTG----GFETAEL-FRSF-RPDLELlaetSGKNAIIVTPSADYDLAAKDVIASA 757
Cdd:cd07138 190 FNLVNGDGPVVGEALSAHPDVDMVSFTGstraGKRVAEAaADTVkRVALEL----GGKSANIILDDADLEKAVPRGVAAC 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 758 FGHAGQKCSAASLvILVgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPI--------------IGPAEG-KLLDGlt 822
Cdd:cd07138 266 FANSGQSCNAPTR-MLV-PRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLasaaqfdrvqgyiqKGIEEGaRLVAG-- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 823 klGAGeqwvvQPRKLdEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLD---A 899
Cdd:cd07138 342 --GPG-----RPEGL-ERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADperA 413
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2066550363 900 KEIATwvdSIEAGNLYVNRGITGAivqRQPFGGWKKSVVG 939
Cdd:cd07138 414 RAVAR---RLRAGQVHINGAAFNP---GAPFGGYKQSGNG 447
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
532-939 |
4.74e-45 |
|
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: 169.25 E-value: 4.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 532 VGTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELA 611
Cdd:cd07106 15 VASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGAVAWLRYTASLD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 612 VALEQVdgaEYDPSRLVVV--TP--------PWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEAL---WAAG 678
Cdd:cd07106 95 LPDEVI---EDDDTRRVELrrKPlgvvaaivPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAqevLPPG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 679 VpreaLQYVQFSDrELGRALVADDAVDRVILTGGFETAEL-FRSFRPDLELLA-ETSGKNAIIVTPSADYDLAAKDVIAS 756
Cdd:cd07106 172 V----LNVVSGGD-ELGPALTSHPDIRKISFTGSTATGKKvMASAAKTLKRVTlELGGNDAAIVLPDVDIDAVAPKLFWG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 757 AFGHAGQKCSAAslvilvgqaarsKR----------FRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLDGLTKLGA 826
Cdd:cd07106 247 AFINSGQVCAAI------------KRlyvhesiydeFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 827 GEQWVV----QPrkLDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLD---A 899
Cdd:cd07106 315 AKGAKVlaggEP--LDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDlerA 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2066550363 900 KEIAtwvDSIEAGNLYVNRgiTGAIVQRQPFGGWKKSVVG 939
Cdd:cd07106 393 EAVA---RRLEAGTVWINT--HGALDPDAPFGGHKQSGIG 427
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
532-939 |
6.09e-44 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 168.13 E-value: 6.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 532 VGTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELA 611
Cdd:PRK09407 50 VSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLDVALTARYYARRA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 612 VAL---EQVDGA---------EYDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGV 679
Cdd:PRK09407 130 PKLlapRRRAGAlpvltktteLRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 680 PREALQYVQFSDRELGRALVadDAVDRVILTGGFET----AElfRSFRPDLELLAETSGKNAIIVTPSADYDLAAKDVIA 755
Cdd:PRK09407 210 PRDLWQVVTGPGPVVGTALV--DNADYLMFTGSTATgrvlAE--QAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVR 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 756 SAFGHAGQKCSAASLVILVGQAArsKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEgklLD------------GLTK 823
Cdd:PRK09407 286 ACFSNAGQLCISIERIYVHESIY--DEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQ---LEtvsahvddavakGATV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 824 LGAGeqwvvqpRKLDEEGRL-WSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLD---A 899
Cdd:PRK09407 361 LAGG-------KARPDLGPLfYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDtarG 433
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2066550363 900 KEIAtwvDSIEAGNLYVNRGITGAIVQRQ-PFGGWKKSVVG 939
Cdd:PRK09407 434 RAIA---ARIRAGTVNVNEGYAAAWGSVDaPMGGMKDSGLG 471
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
532-939 |
7.12e-44 |
|
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: 166.27 E-value: 7.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 532 VGTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELA 611
Cdd:cd07147 17 LAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDTFRIAAEEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 612 VAL--EQVD------GAEYD------PSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAA 677
Cdd:cd07147 97 TRIygEVLPldisarGEGRQglvrrfPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAET 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 678 GVPREALQYVQFSdRELGRALVADDAVDRVILTGGFETAELFRSFRPDLELLAETSGKNAIIVTPSADYDLAAKDVIASA 757
Cdd:cd07147 177 GLPKGAFSVLPCS-RDDADLLVTDERIKLLSFTGSPAVGWDLKARAGKKKVVLELGGNAAVIVDSDADLDFAAQRIIFGA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 758 FGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLdgltklgagEQWVVQprKL 837
Cdd:cd07147 256 FYQAGQSCISVQRVLV--HRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERV---------EGWVNE--AV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 838 DEEGRLWSPGVRSG----------VRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVD 907
Cdd:cd07147 323 DAGAKLLTGGKRDGalleptiledVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWD 402
|
410 420 430
....*....|....*....|....*....|..
gi 2066550363 908 SIEAGNLYVNRgITGAIVQRQPFGGWKKSVVG 939
Cdd:cd07147 403 ELEVGGVVIND-VPTFRVDHMPYGGVKDSGIG 433
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
543-952 |
8.48e-43 |
|
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: 163.51 E-value: 8.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 543 RTALDANAiWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDP-EISEAIDFAHYYAELAVAL---EQVD 618
Cdd:cd07139 46 RRAFDNGP-WPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISWSRRaQGPGPAALLRYYAALARDFpfeERRP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 619 GAEYDPSRLV-----VV--TPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPREALQYVQfSD 691
Cdd:cd07139 125 GSGGGHVLVRrepvgVVaaIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVP-AD 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 692 RELGRALVADDAVDRVILTG--------GFETAELFRsfRPDLELlaetSGKNAIIVTPSADYDLAAKDVIASAFGHAGQ 763
Cdd:cd07139 204 REVGEYLVRHPGVDKVSFTGstaagrriAAVCGERLA--RVTLEL----GGKSAAIVLDDADLDAAVPGLVPASLMNNGQ 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 764 KCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLDGLTKLGAGEQWVV-----QPRKLD 838
Cdd:cd07139 278 VCVALTRILV--PRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYIAKGRAEGARLvtgggRPAGLD 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 839 EeGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLD---AKEIAtwvDSIEAGNLY 915
Cdd:cd07139 356 R-GWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADverGLAVA---RRIRTGTVG 431
|
410 420 430
....*....|....*....|....*....|....*..
gi 2066550363 916 VNrGITGAIVqrQPFGGWKKSVVGpttKAGGPNYLHA 952
Cdd:cd07139 432 VN-GFRLDFG--APFGGFKQSGIG---REGGPEGLDA 462
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
532-939 |
2.02e-42 |
|
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: 161.77 E-value: 2.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 532 VGTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELA 611
Cdd:cd07107 15 AASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMVAAALLDYFAGLV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 612 VAL---------EQVDGAEYDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAA----RCGAVMVEALwaag 678
Cdd:cd07107 95 TELkgetipvggRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPlsalRLAELAREVL---- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 679 vPREALQYVQFSDRELGRALVADDAVDRVILTGGFETAELF-RSFRPDLE-LLAETSGKNAIIVTPSADYDLAAKDVIAS 756
Cdd:cd07107 171 -PPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAImRAAAEGIKhVTLELGGKNALIVFPDADPEAAADAAVAG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 757 A-FGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPII--------------GPAEG-KLLDG 820
Cdd:cd07107 250 MnFTWCGQSCGSTSRLFV--HESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVsrqqydrvmhyidsAKREGaRLVTG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 821 ----LTKLGAGEQWVvqprkldeegrlwSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHS 896
Cdd:cd07107 328 ggrpEGPALEGGFYV-------------EPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWT 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2066550363 897 LDAKEIATWVDSIEAGNLYVN---RGITGAivqrqPFGGWKKSVVG 939
Cdd:cd07107 395 NDISQAHRTARRVEAGYVWINgssRHFLGA-----PFGGVKNSGIG 435
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
533-950 |
6.69e-42 |
|
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: 161.99 E-value: 6.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 533 GTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELE-RRRGELMEVAASEAGKTLDQSdpEI---SEAIDFAHYYA 608
Cdd:cd07123 66 ADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSgKYRYELNAATMLGQGKNVWQA--EIdaaCELIDFLRFNV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 609 ELAVALEQ---VDGAEYDPSRL--------VVVTPPWNFpVAIpaGSTLAALAS--GASVIIKPARQAARCGAVMVEALW 675
Cdd:cd07123 144 KYAEELYAqqpLSSPAGVWNRLeyrplegfVYAVSPFNF-TAI--GGNLAGAPAlmGNVVLWKPSDTAVLSNYLVYKILE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 676 AAGVPREALQYVQFSDRELGRALVADDAVDRVILTGGFET-----------AELFRSFrPdlELLAETSGKNAIIVTPSA 744
Cdd:cd07123 221 EAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTfkslwkqigenLDRYRTY-P--RIVGETGGKNFHLVHPSA 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 745 DYDLAAKDVIASAFGHAGQKCSAASLVILvgqaARS--KRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPA--------- 813
Cdd:cd07123 298 DVDSLVTATVRGAFEYQGQKCSAASRAYV----PESlwPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKafdrikgyi 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 814 -EGKLLDGLTKLGAG-----EQWVVQPrkldeegrlwspgvrSGVRRGSEYHRT---EYFGPVLGIMT--AATLEEAIEI 882
Cdd:cd07123 374 dHAKSDPEAEIIAGGkcddsVGYFVEP---------------TVIETTDPKHKLmteEIFGPVLTVYVypDSDFEETLEL 438
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2066550363 883 ANEV-DYGLTAGLHSLDAKEIATWVDSIE--AGNLYVNRGITGAIVQRQPFGGWKKSvvGPTTKAGGPNYL 950
Cdd:cd07123 439 VDTTsPYALTGAIFAQDRKAIREATDALRnaAGNFYINDKPTGAVVGQQPFGGARAS--GTNDKAGSPLNL 507
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
533-939 |
7.79e-41 |
|
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: 157.12 E-value: 7.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 533 GTAEELASRIRTALDA--NAIWRDLPAAeRAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAEL 610
Cdd:cd07120 16 GGVAEAEAAIAAARRAfdETDWAHDPRL-RARVLLELADAFEANAERLARLLALENGKILGEARFEISGAISELRYYAGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 611 AVAL---------EQVDGAEYDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAA-GVP 680
Cdd:cd07120 95 ARTEagrmiepepGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEIpSLP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 681 REALQYVQFSDRELGRALVADDAVDRVILTGGFET-AELFRSFRPDLELLA-ETSGKNAIIVTPSADYDLAAKDVIASAF 758
Cdd:cd07120 175 AGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATgRAIMAAAAPTLKRLGlELGGKTPCIVFDDADLDAALPKLERALT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 759 GHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLDGLTK--LGAGEQWVVQPRK 836
Cdd:cd07120 255 IFAGQFCMAGSRVLV--QRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVEraIAAGAEVVLRGGP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 837 LDEE---GRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGN 913
Cdd:cd07120 333 VTEGlakGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGT 412
|
410 420
....*....|....*....|....*.
gi 2066550363 914 LYVNRgiTGAIVQRQPFGGWKKSVVG 939
Cdd:cd07120 413 VWIND--WNKLFAEAEEGGYRQSGLG 436
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
524-951 |
4.12e-40 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 156.05 E-value: 4.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 524 NDTIEANTVGTAEELASRIRTALDA-----NAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEIS 598
Cdd:PLN02467 33 EETIGDIPAATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAWDMD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 599 EAIDFAHYYAELAvalEQVDGAEYDPSRL----------------VVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQ 662
Cdd:PLN02467 113 DVAGCFEYYADLA---EALDAKQKAPVSLpmetfkgyvlkeplgvVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 663 AARCGAVMVEALWAAGVPREALQYVQFSDRELGRALVADDAVDRVILTGGFETAELFRS-----FRP-DLELlaetSGKN 736
Cdd:PLN02467 190 ASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTaaaqmVKPvSLEL----GGKS 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 737 AIIVTPSADYDLAAKDVIASAFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIgpAEG- 815
Cdd:PLN02467 266 PIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLV--HERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVV--SEGq 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 816 --KLL--------DGLTKLGAGeqwvVQPRKLdEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANE 885
Cdd:PLN02467 342 yeKVLkfistaksEGATILCGG----KRPEHL-KKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELAND 416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2066550363 886 VDYGLTAGLHSLDAKEIATWVDSIEAGNLYVNrgITGAIVQRQPFGGWKKSVVGPTTKAGG-PNYLH 951
Cdd:PLN02467 417 SHYGLAGAVISNDLERCERVSEAFQAGIVWIN--CSQPCFCQAPWGGIKRSGFGRELGEWGlENYLS 481
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
524-906 |
4.11e-39 |
|
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: 152.75 E-value: 4.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 524 NDTIEANTVGTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDF 603
Cdd:cd07130 22 GEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLGEVQEMIDI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 604 AHYyaelAVAL-EQVDGA-------------EYDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQ----AAR 665
Cdd:cd07130 102 CDF----AVGLsRQLYGLtipserpghrmmeQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTtpltAIA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 666 CGAVMVEALWAAGVPrEALQYVQFSDRELGRALVADDAVDRVILTG--------GFETAELF-RSFrpdLELlaetSGKN 736
Cdd:cd07130 178 VTKIVARVLEKNGLP-GAIASLVCGGADVGEALVKDPRVPLVSFTGstavgrqvGQAVAARFgRSL---LEL----GGNN 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 737 AIIVTPSADYDLAAKDVIASAFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGP-AEG 815
Cdd:cd07130 250 AIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIV--HESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKaAVD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 816 KLLDGLTKLGA-GEQWVVQPRKLDEEGRLWSPGVRSGvRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGL 894
Cdd:cd07130 328 NYLAAIEEAKSqGGTVLFGGKVIDGPGNYVEPTIVEG-LSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSI 406
|
410
....*....|..
gi 2066550363 895 HSLDAKEIATWV 906
Cdd:cd07130 407 FTTDLRNAFRWL 418
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
552-939 |
1.13e-38 |
|
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: 151.44 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 552 WRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDP-EISEAIDFAHYYA---------ELAVALEQVDGAE 621
Cdd:cd07113 54 WAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHLSRAfEVGQSANFLRYFAgwatkingeTLAPSIPSMQGER 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 622 Y------DPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPREALQYVQfSDRELG 695
Cdd:cd07113 134 YtaftrrEPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVN-GKGAVG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 696 RALVADDAVDRVILTGGFETAELFRSF------RPDLELlaetSGKNAIIVTPSADYDLAAKDVIASAFGHAGQKCSAAS 769
Cdd:cd07113 213 AQLISHPDVAKVSFTGSVATGKKIGRQaasdltRVTLEL----GGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPE 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 770 LVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIG-PAEGKLLDGLTKL-GAGEQWVVQPRKLDEEGRLWSPG 847
Cdd:cd07113 289 RFYV--HRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANqPHFDKVCSYLDDArAEGDEIVRGGEALAGEGYFVQPT 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 848 VRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGNLYVN-RGITGAIVq 926
Cdd:cd07113 367 LVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNmHTFLDPAV- 445
|
410
....*....|...
gi 2066550363 927 rqPFGGWKKSVVG 939
Cdd:cd07113 446 --PFGGMKQSGIG 456
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
543-939 |
1.51e-38 |
|
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: 150.82 E-value: 1.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 543 RTALDaNAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQS-DPEISEAIDFAHYYAELAvalEQVDGA- 620
Cdd:cd07091 51 RAAFE-TGWWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEESaKGDVALSIKCLRYYAGWA---DKIQGKt 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 621 -EYDPSRLVVVTP----------PWNFPVAIPAGSTLAALASGASVIIKPARQ----AARCGAVMVEALWAAGVpreaLQ 685
Cdd:cd07091 127 iPIDGNFLAYTRRepigvcgqiiPWNFPLLMLAWKLAPALAAGNTVVLKPAEQtplsALYLAELIKEAGFPPGV----VN 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 686 YVQFSDRELGRALVADDAVDRVILTGGFETAELFrsfrpdLELLAETS---------GKNAIIVTPSADYDLAAKDVIAS 756
Cdd:cd07091 203 IVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTI------MEAAAKSNlkkvtlelgGKSPNIVFDDADLDKAVEWAAFG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 757 AFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAE-GKLLD--------GLTKLGAG 827
Cdd:cd07091 277 IFFNQGQCCCAGSRIFV--QESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQfDKILSyiesgkkeGATLLTGG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 828 EQWvvqprklDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVD 907
Cdd:cd07091 355 ERH-------GSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSR 427
|
410 420 430
....*....|....*....|....*....|...
gi 2066550363 908 SIEAGNLYVNrgiTGAIVQRQ-PFGGWKKSVVG 939
Cdd:cd07091 428 ALKAGTVWVN---TYNVFDAAvPFGGFKQSGFG 457
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
525-939 |
5.69e-37 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 146.04 E-value: 5.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 525 DTIEANTVGTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFA 604
Cdd:PRK09406 12 ETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 605 HYYAELAVAL---EQVDGAE---------YDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVE 672
Cdd:PRK09406 92 RYYAEHAEALladEPADAAAvgasrayvrYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 673 ALWAAGVPREALQYVqfsdrelgraLVADDAVDRVI---------LTGGFETAELFRSFRPD------LELlaetSGKNA 737
Cdd:PRK09406 172 LFRRAGFPDGCFQTL----------LVGSGAVEAILrdprvaaatLTGSEPAGRAVAAIAGDeikktvLEL----GGSDP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 738 IIVTPSADYDLAAKDVIASAFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPII---GPAE 814
Cdd:PRK09406 238 FIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIV--HADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLAteqGRDE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 815 -GKLLDGLTKLGAgeQWVVQPRKLDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAG 893
Cdd:PRK09406 316 vEKQVDDAVAAGA--TILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSN 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2066550363 894 LHSLDAKEIATWVDSIEAGNLYVNrGITGAIVQrQPFGGWKKSVVG 939
Cdd:PRK09406 394 AWTRDEAEQERFIDDLEAGQVFIN-GMTVSYPE-LPFGGVKRSGYG 437
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
543-952 |
2.22e-35 |
|
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: 141.76 E-value: 2.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 543 RTALDAnaiWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQS-DPEISEAIDFAHYYAELAVALEQvDGAE 621
Cdd:cd07111 69 RTAFES---WSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESrDCDIPLVARHFYHHAGWAQLLDT-ELAG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 622 YDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPREALQYVQfSDRELGRALVAD 701
Cdd:cd07111 145 WKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVT-GNGSFGSALANH 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 702 DAVDRVILTGGFETAELFRSFRP--DLELLAETSGKNAIIVTPSADYDLAAKDVIASAFGHAGQKCSAASLVILvgQAAR 779
Cdd:cd07111 224 PGVDKVAFTGSTEVGRALRRATAgtGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLV--QESV 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 780 SKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLDGLTKLGAGEQWVV-QPR-KLDEEGRLWSPGVRSGVRRGSE 857
Cdd:cd07111 302 AEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVfQPGaDLPSKGPFYPPTLFTNVPPASR 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 858 YHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGNLYVNRgiTGAIVQRQPFGGWKKSV 937
Cdd:cd07111 382 IAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWING--HNLFDAAAGFGGYRESG 459
|
410
....*....|....*
gi 2066550363 938 VGpttKAGGPNYLHA 952
Cdd:cd07111 460 FG---REGGKEGLYE 471
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
564-939 |
2.23e-35 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 139.87 E-value: 2.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 564 LHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELAVALE----QVDGAEYD----PSRLVVVTP--P 633
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEgeiiQSDRPGENillfKRALGVTTGilP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 634 WNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPREALQYVQFSDRELGRALVADDAVDRVILTGGF 713
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 714 ETAE--LFRSFRPDLELLAETSGKNAIIVTPSADYDLAAKDVIASAFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGV 791
Cdd:PRK10090 161 SAGEkiMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYV--QKGIYDQFVNRLGEAM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 792 RSIDVGYPTEATT-QMGPIIGPAEGKLLDGLTKLG--AGEQWVVQPRKLDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVL 868
Cdd:PRK10090 239 QAVQFGNPAERNDiAMGPLINAAALERVEQKVARAveEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVL 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2066550363 869 GIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGNLYVNRGITGAIvqrQPF-GGWKKSVVG 939
Cdd:PRK10090 319 PVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAM---QGFhAGWRKSGIG 387
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
534-953 |
5.97e-35 |
|
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: 140.13 E-value: 5.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 534 TAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTL-DQSDPEI---SEAIDFAHYYAE 609
Cdd:cd07098 16 TPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMvDASLGEIlvtCEKIRWTLKHGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 610 LAVALEQVDGA----------EYDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMV----EALW 675
Cdd:cd07098 96 KALRPESRPGGllmfykrarvEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLsiirECLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 676 AAGVPREALQYV-QFSdrELGRALVADDAVDRVILTGGFETAELF-----RSFRPdleLLAETSGKNAIIVTPSADYDLA 749
Cdd:cd07098 176 ACGHDPDLVQLVtCLP--ETAEALTSHPVIDHITFIGSPPVGKKVmaaaaESLTP---VVLELGGKDPAIVLDDADLDQI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 750 AKDVIASAFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPA-----EGKLLD----G 820
Cdd:cd07098 251 ASIIMRGTFQSSGQNCIGIERVIV--HEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPArfdrlEELVADavekG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 821 LTKLGAGEQWvvqPRKLDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAK 900
Cdd:cd07098 329 ARLLAGGKRY---PHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIK 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2066550363 901 EIATWVDSIEAGNLYVNRGITGAIVQRQPFGGWKKSVVGpttKAGGPNYLHAL 953
Cdd:cd07098 406 RARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFG---RFAGEEGLRGL 455
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
543-939 |
7.09e-35 |
|
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: 140.18 E-value: 7.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 543 RTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKT-LDQSDPEISEAIDFAHYYAELAVALE----QV 617
Cdd:cd07141 54 RAAFKLGSPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPfSKSYLVDLPGAIKVLRYYAGWADKIHgktiPM 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 618 DGAEY-----DPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQ----AARCGAVMVEALWAAGVpreaLQYVQ 688
Cdd:cd07141 134 DGDFFtytrhEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQtpltALYLASLIKEAGFPPGV----VNVVP 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 689 FSDRELGRALVADDAVDRVILTGGFETAELFRSF-------RPDLELlaetSGKNAIIVTPSADYDLAAKDVIASAFGHA 761
Cdd:cd07141 210 GYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAagksnlkRVTLEL----GGKSPNIVFADADLDYAVEQAHEALFFNM 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 762 GQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLDGLTKLGA--GEQWVVQPRKLDE 839
Cdd:cd07141 286 GQCCCAGSRTFV--QESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKkeGAKLECGGKRHGD 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 840 EGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGNLYVNrg 919
Cdd:cd07141 364 KGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVN-- 441
|
410 420
....*....|....*....|
gi 2066550363 920 ITGAIVQRQPFGGWKKSVVG 939
Cdd:cd07141 442 CYNVVSPQAPFGGYKMSGNG 461
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
523-950 |
8.13e-35 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 140.04 E-value: 8.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 523 GNDTIEANTVGTAEEL-------ASRIRTALDAN----AIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLD 591
Cdd:PRK11241 24 NGEVIDVTNPANGDKLgsvpkmgADETRAAIDAAnralPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 592 QSDPEISEAIDFAHYYAELA--VALEQVDGAEYDPSRLVVVTP--------PWNFPVAIPAGSTLAALASGASVIIKPAR 661
Cdd:PRK11241 104 EAKGEISYAASFIEWFAEEGkrIYGDTIPGHQADKRLIVIKQPigvtaaitPWNFPAAMITRKAGPALAAGCTMVLKPAS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 662 QAARCGAVMVEALWAAGVPREALQYVQFSDRELGRALVADDAVDRVILTGGFETA-ELFRSFRPDLELLAETSGKNA-II 739
Cdd:PRK11241 184 QTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGrQLMEQCAKDIKKVSLELGGNApFI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 740 VTPSADYDLAAKDVIASAFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPII-----GPAE 814
Cdd:PRK11241 264 VFDDADLDKAVEGALASKFRNAGQTCVCANRLYV--QDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIdekavAKVE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 815 GKLLDGLTKlgaGEQWVVQPRKLDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGL 894
Cdd:PRK11241 342 EHIADALEK---GARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYF 418
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2066550363 895 HSLDAKEIATWVDSIEAGNLYVNRGITGAIVqrQPFGGWKKSVVG-PTTKAGGPNYL 950
Cdd:PRK11241 419 YARDLSRVFRVGEALEYGIVGINTGIISNEV--APFGGIKASGLGrEGSKYGIEDYL 473
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
552-939 |
1.21e-34 |
|
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: 139.46 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 552 WRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQ-SDPEISEAIDFAHYYAELAvalEQVDGA--EYDPSRL- 627
Cdd:cd07144 62 WSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYHSnALGDLDEIIAVIRYYAGWA---DKIQGKtiPTSPNKLa 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 628 -VVVTP--------PWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPREALQYVQFSDRELGRAL 698
Cdd:cd07144 139 yTLHEPygvcgqiiPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSAL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 699 VADDAVDRVILTG----GFETAELFRSFRPDLELlaETSGKNAIIVTPSADYDLAAKDVIASAFGHAGQKCSAASLVILv 774
Cdd:cd07144 219 AEHPDVDKIAFTGstatGRLVMKAAAQNLKAVTL--ECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYV- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 775 gQAARSKRFRSQLLDGVRSI-DVGYPTEATTQMGPII--------------GPAEG-KLLDGLTKLGAGEqwvvqprkld 838
Cdd:cd07144 296 -QESIYDKFVEKFVEHVKQNyKVGSPFDDDTVVGPQVsktqydrvlsyiekGKKEGaKLVYGGEKAPEGL---------- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 839 EEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGNLYVNR 918
Cdd:cd07144 365 GKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINS 444
|
410 420
....*....|....*....|.
gi 2066550363 919 GITGAIvqRQPFGGWKKSVVG 939
Cdd:cd07144 445 SNDSDV--GVPFGGFKMSGIG 463
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
532-939 |
3.42e-34 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 138.09 E-value: 3.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 532 VGTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVaaseagKTLDQSDPeISEAI--------DF 603
Cdd:PRK13252 40 AATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAAL------ETLDTGKP-IQETSvvdivtgaDV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 604 AHYYAELAVALE----QVDGAEY-----DPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEAL 674
Cdd:PRK13252 113 LEYYAGLAPALEgeqiPLRGGSFvytrrEPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIY 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 675 WAAGVPREALQYVQfSDRELGRALVADDAVDRVILTGGFET-----AELFRSFRpdlELLAETSGKNAIIVTPSADYDLA 749
Cdd:PRK13252 193 TEAGLPDGVFNVVQ-GDGRVGAWLTEHPDIAKVSFTGGVPTgkkvmAAAAASLK---EVTMELGGKSPLIVFDDADLDRA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 750 AKDVIASAFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPII--------------GPAEG 815
Cdd:PRK13252 269 ADIAMLANFYSSGQVCTNGTRVFV--QKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVsfahrdkvlgyiekGKAEG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 816 -KLLDGLTKLGAGEQwvvqprkldEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGL 894
Cdd:PRK13252 347 aRLLCGGERLTEGGF---------ANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGV 417
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2066550363 895 HSLDAKEIATWVDSIEAGNLYVNR-GITGAivqRQPFGGWKKSVVG 939
Cdd:PRK13252 418 FTADLSRAHRVIHQLEAGICWINTwGESPA---EMPVGGYKQSGIG 460
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
525-936 |
8.94e-34 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 136.58 E-value: 8.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 525 DTIEANTVGTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQS-DPEISEAIDF 603
Cdd:PRK13473 28 EVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLAlNDEIPAIVDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 604 AHYYAELAVALEQVDGAEY----------DPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAArCGAVMVEA 673
Cdd:PRK13473 108 FRFFAGAARCLEGKAAGEYleghtsmirrDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITP-LTALKLAE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 674 LWAAGVPREALQYVQFSDRELGRALVADDAVDRVILTGGFETAELFRSF------RPDLELlaetSGKNAIIVTPSADYD 747
Cdd:PRK13473 187 LAADILPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAaadsvkRTHLEL----GGKAPVIVFDDADLD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 748 LAAKDVIASAFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLDGLTKLGAG 827
Cdd:PRK13473 263 AVVEGIRTFGYYNAGQDCTAACRIYA--QRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVERAKA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 828 EQW---VVQPRKLDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIAT 904
Cdd:PRK13473 341 LGHirvVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHR 420
|
410 420 430
....*....|....*....|....*....|..
gi 2066550363 905 WVDSIEAGNLYVNRGITgaIVQRQPFGGWKKS 936
Cdd:PRK13473 421 VSARLQYGCTWVNTHFM--LVSEMPHGGQKQS 450
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
534-942 |
9.95e-34 |
|
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: 136.70 E-value: 9.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 534 TAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRgELMEVAaseagKTLDQSDP-------EISEAIDFAHY 606
Cdd:cd07559 36 TAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENL-ELLAVA-----ETLDNGKPiretlaaDIPLAIDHFRY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 607 YAELAVALE----QVDGAE-----YDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEaLWAA 677
Cdd:cd07559 110 FAGVIRAQEgslsEIDEDTlsyhfHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLME-LIGD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 678 GVPREALQYVQFSDRELGRALVADDAVDRVILTGGFETAELFRSFRPD------LELlaetSGKNAIIVTPSA-----DY 746
Cdd:cd07559 189 LLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAEnlipvtLEL----GGKSPNIFFDDAmdaddDF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 747 DLAAKDVIASAFGHAGQKCSAASLvILVgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLDGLTKLG- 825
Cdd:cd07559 265 DDKAEEGQLGFAFNQGEVCTCPSR-ALV-QESIYDEFIERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGk 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 826 -AGEQWVVQPRKLDEEGRL----WSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAK 900
Cdd:cd07559 343 eEGAEVLTGGERLTLGGLDkgyfYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDIN 422
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2066550363 901 EIATWVDSIEAGNLYVNrgITGAIVQRQPFGGWKKSVVGPTT 942
Cdd:cd07559 423 RALRVARGIQTGRVWVN--CYHQYPAHAPFGGYKKSGIGRET 462
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
487-939 |
3.51e-33 |
|
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: 134.93 E-value: 3.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 487 LDVSNGFVNTADSD--PSL-PANQEWARRIREAAKAStlgndtieantVGTAEELAsriRTALDANAiWRDLPAAERAAI 563
Cdd:cd07142 6 LFINGQFVDAASGKtfPTIdPRNGEVIAHVAEGDAED-----------VDRAVKAA---RKAFDEGP-WPRMTGYERSRI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 564 LHKAGDELERRRGELMEVAASEAGKTLDQSD-PEISEAIDFAHYYAELAVALE----QVDGAE-----YDPSRLVVVTPP 633
Cdd:cd07142 71 LLRFADLLEKHADELAALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHgmtlPADGPHhvytlHEPIGVVGQIIP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 634 WNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPREALQYVQFSDRELGRALVADDAVDRVILTGGF 713
Cdd:cd07142 151 WNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGST 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 714 ETAELFRSFRPDLELLA---ETSGKNAIIVTPSADYDLAAKDVIASAFGHAGQKCSAASLVILvgQAARSKRFRSQLLDG 790
Cdd:cd07142 231 EVGKIIMQLAAKSNLKPvtlELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFV--HESIYDEFVEKAKAR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 791 VRSIDVGYPTEATTQMGPIIGPAEGKLLDGLTKLG--AGEQWVVQPRKLDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVL 868
Cdd:cd07142 309 ALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHGkeEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQ 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2066550363 869 GIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGNLYVN--RGITGAIvqrqPFGGWKKSVVG 939
Cdd:cd07142 389 SILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcyDVFDASI----PFGGYKMSGIG 457
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
525-939 |
3.56e-33 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 134.60 E-value: 3.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 525 DTIEANTVGTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFA 604
Cdd:PRK13968 18 EQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLC 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 605 HYYAELAVAL---------EQVDGAEYDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALW 675
Cdd:PRK13968 98 DWYAEHGPAMlkaeptlveNQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 676 AAGVPREALQYVQfSDRELGRALVADDAVDRVILTGGFET-----AELFRSFRpdlELLAETSGKNAIIVTPSADYDLAA 750
Cdd:PRK13968 178 DAGIPQGVYGWLN-ADNDGVSQMINDSRIAAVTVTGSVRAgaaigAQAGAALK---KCVLELGGSDPFIVLNDADLELAV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 751 KDVIASAFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIigpAEGKLLDGL-----TKLG 825
Cdd:PRK13968 254 KAAVAGRYQNTGQVCAAAKRFII--EEGIASAFTERFVAAAAALKMGDPRDEENALGPM---ARFDLRDELhhqveATLA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 826 AGEQWVVQPRKLDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATW 905
Cdd:PRK13968 329 EGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQM 408
|
410 420 430
....*....|....*....|....*....|....
gi 2066550363 906 VDSIEAGNLYVNrGITgAIVQRQPFGGWKKSVVG 939
Cdd:PRK13968 409 AARLECGGVFIN-GYC-ASDARVAFGGVKKSGFG 440
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
534-939 |
4.13e-32 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 132.19 E-value: 4.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 534 TAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELAVA 613
Cdd:PLN00412 51 TQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 614 L---------EQVDGAEYD--------PSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWA 676
Cdd:PLN00412 131 IlgegkflvsDSFPGNERNkycltskiPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 677 AGVPREALQYVQFSDRELGRALVADDAVDRVILTGGfETAELFRSFRPDLELLAETSGKNAIIVTPSADYDLAAKDVIAS 756
Cdd:PLN00412 211 AGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIAISKKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 757 AFGHAGQKCSAASLVILVGQAArsKRFRSQLLDGVRSIDVGYPtEATTQMGPIIGPAEGKLLDGLTKlGAGEQWVVQPRK 836
Cdd:PLN00412 290 GFSYSGQRCTAVKVVLVMESVA--DALVEKVNAKVAKLTVGPP-EDDCDITPVVSESSANFIEGLVM-DAKEKGATFCQE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 837 LDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGNLYV 916
Cdd:PLN00412 366 WKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQI 445
|
410 420
....*....|....*....|....*..
gi 2066550363 917 N----RGitgaiVQRQPFGGWKKSVVG 939
Cdd:PLN00412 446 NsapaRG-----PDHFPFQGLKDSGIG 467
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
534-942 |
5.20e-32 |
|
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: 131.42 E-value: 5.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 534 TAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDP-EISEAIDFAHYYAELAV 612
Cdd:cd07117 36 TDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRAvDIPLAADHFRYFAGVIR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 613 ALE-QVDGAEYDPSRLVVVTP--------PWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEaLWAAGVPREA 683
Cdd:cd07117 116 AEEgSANMIDEDTLSIVLREPigvvgqiiPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAK-IIQDVLPKGV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 684 LQYVQFSDRELGRALVADDAVDRVILTGGFETAELFRSFRPDLELLA--ETSGKNAIIVTPSADYDLAAKDVIASAFGHA 761
Cdd:cd07117 195 VNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIPAtlELGGKSANIIFDDANWDKALEGAQLGILFNQ 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 762 GQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLDGLTKLG--AGEQWVVQPRKLDE 839
Cdd:cd07117 275 GQVCCAGSRIFV--QEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAkeEGAKILTGGHRLTE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 840 E----GRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGNLY 915
Cdd:cd07117 353 NgldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVW 432
|
410 420
....*....|....*....|....*..
gi 2066550363 916 VNrgITGAIVQRQPFGGWKKSVVGPTT 942
Cdd:cd07117 433 VN--TYNQIPAGAPFGGYKKSGIGRET 457
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
534-917 |
1.07e-31 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 132.56 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 534 TAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAhyyaELAVA 613
Cdd:PLN02419 149 TNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVV----EHACG 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 614 LEQVDGAEY--------------DPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGV 679
Cdd:PLN02419 225 MATLQMGEYlpnvsngvdtysirEPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 680 PREALQYVQFSDRELGRalVADDAVDRVILTGGFETAELF---RSFRPDLELLAETSGKNAIIVTPSADYDLAAKDVIAS 756
Cdd:PLN02419 305 PDGVLNIVHGTNDTVNA--ICDDEDIRAVSFVGSNTAGMHiyaRAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAA 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 757 AFGHAGQKCSAASLVILVGQAarsKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLDGLTKLGA--GEQWVVQP 834
Cdd:PLN02419 383 GFGAAGQRCMALSTVVFVGDA---KSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVddGAKLLLDG 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 835 RKL----DEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIE 910
Cdd:PLN02419 460 RDIvvpgYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIE 539
|
....*..
gi 2066550363 911 AGNLYVN 917
Cdd:PLN02419 540 AGQIGIN 546
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
506-939 |
2.59e-31 |
|
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: 129.57 E-value: 2.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 506 NQEWARRIREAAKasTLGNDTIEANTVGTAEELASRIRTALDA-----NAIW-RDLPAAERAAILHKAGDELERRRGELM 579
Cdd:cd07143 12 NGEFVDSVHGGTV--KVYNPSTGKLITKIAEATEADVDIAVEVahaafETDWgLKVSGSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 580 EVAASEAGKTLDQSDP-EISEAIDFAHYYAELAvalEQVDGA--EYDPSRLVVV--TP--------PWNFPVAIPAGSTL 646
Cdd:cd07143 90 SIEALDNGKTFGTAKRvDVQASADTFRYYGGWA---DKIHGQviETDIKKLTYTrhEPigvcgqiiPWNFPLLMCAWKIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 647 AALASGASVIIKPARQAARCGAVMVEALWAAGVPREALQYVQFSDRELGRALVADDAVDRVILTGG-------FETAELF 719
Cdd:cd07143 167 PALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGStlvgrkvMEAAAKS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 720 RSFRPDLELlaetSGKNAIIVTPSADYDLAAKDVIASAFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYP 799
Cdd:cd07143 247 NLKKVTLEL----GGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYV--QEGIYDKFVKRFKEKAKKLKVGDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 800 TEATTQMGPIIGPAEGKLLDGLTKLG--AGEQWVVQPRKLDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLE 877
Cdd:cd07143 321 FAEDTFQGPQVSQIQYERIMSYIESGkaEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2066550363 878 EAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGNLYVNrgITGAIVQRQPFGGWKKSVVG 939
Cdd:cd07143 401 EAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVN--CYNLLHHQVPFGGYKQSGIG 460
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
533-939 |
8.89e-31 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 128.01 E-value: 8.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 533 GTAEELASRIRTALDA--NAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDP-EISEAIDFAHYYAE 609
Cdd:PLN02766 55 GDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGKAvDIPAAAGLLRYYAG 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 610 LAvalEQVDG------AEY------DPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAA 677
Cdd:PLN02766 135 AA---DKIHGetlkmsRQLqgytlkEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 678 GVPREALQYVQFSDRELGRALVADDAVDRVILTGGFETAELF--RSFRPDLELLA-ETSGKNAIIVTPSADYDLAAKDVI 754
Cdd:PLN02766 212 GVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKImqAAATSNLKQVSlELGGKSPLLIFDDADVDMAVDLAL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 755 ASAFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAE-GKLL--------DGLTKLG 825
Cdd:PLN02766 292 LGIFYNKGEICVASSRVYV--QEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQfEKILsyiehgkrEGATLLT 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 826 AGeqwvvqpRKLDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATW 905
Cdd:PLN02766 370 GG-------KPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTV 442
|
410 420 430
....*....|....*....|....*....|....
gi 2066550363 906 VDSIEAGNLYVNrgITGAIVQRQPFGGWKKSVVG 939
Cdd:PLN02766 443 SRSIRAGTIWVN--CYFAFDPDCPFGGYKMSGFG 474
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
539-939 |
6.10e-30 |
|
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: 124.84 E-value: 6.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 539 ASRIRTALD-ANAIWRD----LPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAElavA 613
Cdd:cd07148 20 WAAIDKALDtAHALFLDrnnwLPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVELAAD---E 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 614 LEQVDGAEY-----------------DPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWA 676
Cdd:cd07148 97 LGQLGGREIpmgltpasagriafttrEPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 677 AGVPREALQYVqFSDRELGRALVADDAVDRVILTGGFETAELFRS-FRPDLELLAETSGKNAIIVTPSADYDLAAKDVIA 755
Cdd:cd07148 177 AGLPEGWCQAV-PCENAVAEKLVTDPRVAFFSFIGSARVGWMLRSkLAPGTRCALEHGGAAPVIVDRSADLDAMIPPLVK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 756 SAFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLDGLTK--LGAGEQWVVQ 833
Cdd:cd07148 256 GGFYHAGQVCVSVQRVFV--PAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNeaVAAGARLLCG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 834 PRKLDEEgrLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGN 913
Cdd:cd07148 334 GKRLSDT--TYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATA 411
|
410 420
....*....|....*....|....*.
gi 2066550363 914 LYVNRGiTGAIVQRQPFGGWKKSVVG 939
Cdd:cd07148 412 VMVNDH-TAFRVDWMPFAGRRQSGYG 436
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
505-906 |
7.67e-29 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 122.25 E-value: 7.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 505 ANQEWARRIREAAKASTLGNDTIEANTVGTAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAAS 584
Cdd:PLN02315 25 VGGEWRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 585 EAGKTLDQSDPEISEAIDFAHYyaelAVAL-EQVDGA-------------EYDPSRLVVVTPPWNFPVAIPAGSTLAALA 650
Cdd:PLN02315 105 EMGKILAEGIGEVQEIIDMCDF----AVGLsRQLNGSiipserpnhmmmeVWNPLGIVGVITAFNFPCAVLGWNACIALV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 651 SGASVIIKPARQAARCGAVMVEaLWAAGVPREALQYVQFS----DRELGRALVADDAVDRVILTGGFETAELFRSF---R 723
Cdd:PLN02315 181 CGNCVVWKGAPTTPLITIAMTK-LVAEVLEKNNLPGAIFTsfcgGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTvnaR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 724 PDLELLaETSGKNAIIVTPSADYDLAAKDVIASAFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEAT 803
Cdd:PLN02315 260 FGKCLL-ELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLL--HESIYDDVLEQLLTVYKQVKIGDPLEKG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 804 TQMGPIIGPAEGK-LLDGLTKLGA-GEQWVVQPRKLDEEGRLWSPGVRSgVRRGSEYHRTEYFGPVLGIMTAATLEEAIE 881
Cdd:PLN02315 337 TLLGPLHTPESKKnFEKGIEIIKSqGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLEEAIE 415
|
410 420
....*....|....*....|....*
gi 2066550363 882 IANEVDYGLTAGLHSLDAKEIATWV 906
Cdd:PLN02315 416 INNSVPQGLSSSIFTRNPETIFKWI 440
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
628-932 |
9.88e-27 |
|
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: 114.62 E-value: 9.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 628 VVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEaLWAAGVPREALQYVQFSDRELGRALvaDDAVDRV 707
Cdd:cd07135 112 VLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAE-LVPKYLDPDAFQVVQGGVPETTALL--EQKFDKI 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 708 ILTGGFETAELF-----RSFRP-DLELlaetSGKNAIIVTPSADYDLAAKDVIASAFGHAGQKCSAASLVIlvgqAARSK 781
Cdd:cd07135 189 FYTGSGRVGRIIaeaaaKHLTPvTLEL----GGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVL----VDPSV 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 782 R--FRSQLldgVRSIDVGYPTEAT--TQMGPIIGPAEGKLLDGLTKLGAGEqwVVQPRKLDEEGRLWSPGVRSGVRRGSE 857
Cdd:cd07135 261 YdeFVEEL---KKVLDEFYPGGANasPDYTRIVNPRHFNRLKSLLDTTKGK--VVIGGEMDEATRFIPPTIVSDVSWDDS 335
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2066550363 858 YHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGNLYVNRGITGAIVQRQPFGG 932
Cdd:cd07135 336 LMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNAPFGG 410
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
534-939 |
1.51e-25 |
|
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: 111.78 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 534 TAEELASRIRTALDANAIWRDLPAAERAAILHKAGDELERRRgELMEVAAS-EAGKTL-DQSDPEISEAIDFAHYYAELA 611
Cdd:cd07116 36 TAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANL-EMLAVAETwDNGKPVrETLAADIPLAIDHFRYFAGCI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 612 VALE----QVDGAE-----YDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEaLWAAGVPRE 682
Cdd:cd07116 115 RAQEgsisEIDENTvayhfHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLME-LIGDLLPPG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 683 ALQYVQFSDRELGRALVADDAVDRVILTGGFETAELFRSFRPD--LELLAETSGKNAIIVTPS------ADYDLAAKDVI 754
Cdd:cd07116 194 VVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASEniIPVTLELGGKSPNIFFADvmdaddAFFDKALEGFV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 755 ASAFgHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGP--------------IIGPAEGKLLdg 820
Cdd:cd07116 274 MFAL-NQGEVCTCPSRALI--QESIYDRFMERALERVKAIKQGNPLDTETMIGAqasleqlekilsyiDIGKEEGAEV-- 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 821 ltkLGAGEQWVvqpRKLDEEGRLWSPGVRSGVRRGSEYhRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAK 900
Cdd:cd07116 349 ---LTGGERNE---LGGLLGGGYYVPTTFKGGNKMRIF-QEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGN 421
|
410 420 430
....*....|....*....|....*....|....*....
gi 2066550363 901 EIATWVDSIEAGNLYVNrgITGAIVQRQPFGGWKKSVVG 939
Cdd:cd07116 422 TAYRMGRGIQAGRVWTN--CYHLYPAHAAFGGYKQSGIG 458
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
549-953 |
5.36e-25 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 110.37 E-value: 5.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 549 NAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQS-DPEISEAIDFAHYYAElavALEQVDGA------- 620
Cdd:PRK09847 72 RGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSlRDDIPGAARAIRWYAE---AIDKVYGEvattssh 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 621 -----EYDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPREALQYVQFSDRELG 695
Cdd:PRK09847 149 elamiVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAG 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 696 RALVADDAVDRVILTGGFETAELFRSFRPDLEL---LAETSGKNA-IIVTPSADYDLAAKDVIASAFGHAGQKCSAASLV 771
Cdd:PRK09847 229 QALSRHNDIDAIAFTGSTRTGKQLLKDAGDSNMkrvWLEAGGKSAnIVFADCPDLQQAASATAAGIFYNQGQVCIAGTRL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 772 ILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAEGKLLDGLTKLGAGE-QWVVQPRKLDEEGRLwSPGVRS 850
Cdd:PRK09847 309 LL--EESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKgQLLLDGRNAGLAAAI-GPTIFV 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 851 GVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGNLYVNRGITGAIVqrQPF 930
Cdd:PRK09847 386 DVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMT--VPF 463
|
410 420
....*....|....*....|...
gi 2066550363 931 GGWKKSvvgpttKAGGPNYLHAL 953
Cdd:PRK09847 464 GGYKQS------GNGRDKSLHAL 480
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
533-939 |
1.26e-24 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 109.90 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 533 GTAEEL---ASRIRTALDANAiWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQS-DPEISEAIDFAHYYA 608
Cdd:PLN02466 92 GDAEDVnraVAAARKAFDEGP-WPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSaKAELPMFARLFRYYA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 609 ELAVALE----QVDGAEY-----DPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGV 679
Cdd:PLN02466 171 GWADKIHgltvPADGPHHvqtlhEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 680 PREALQYVQFSDRELGRALVADDAVDRVILTGGFETAELFrsfrpdLELLA---------ETSGKNAIIVTPSADYDLAA 750
Cdd:PLN02466 251 PPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIV------LELAAksnlkpvtlELGGKSPFIVCEDADVDKAV 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 751 KDVIASAFGHAGQKCSAASLVILvgqaarSKRFRSQLLDGVRSID----VGYPTEATTQMGPIIGPAEGKLLDGLTKLG- 825
Cdd:PLN02466 325 ELAHFALFFNQGQCCCAGSRTFV------HERVYDEFVEKAKARAlkrvVGDPFKKGVEQGPQIDSEQFEKILRYIKSGv 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 826 -AGEQWVVQPRKLDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIAT 904
Cdd:PLN02466 399 eSGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANT 478
|
410 420 430
....*....|....*....|....*....|....*..
gi 2066550363 905 WVDSIEAGNLYVN--RGITGAIvqrqPFGGWKKSVVG 939
Cdd:PLN02466 479 LSRALRVGTVWVNcfDVFDAAI----PFGGYKMSGIG 511
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
552-951 |
2.02e-22 |
|
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: 101.93 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 552 WRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDpEISEAIDFAHYYAELAVALEQVDGAEYDPSR----- 626
Cdd:cd07084 15 ARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAE-NICGDQVQLRARAFVIYSYRIPHEPGNHLGQglkqq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 627 ---------LVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAG-VPREALQYVQFsDRELGR 696
Cdd:cd07084 94 shgyrwpygPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLING-DGKTMQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 697 ALVADDAVDRVILTGGFETAELFRSFRPDLELLAETSGKNAIIVTPSAD-YDLAAKDVIASAFGHAGQKCSAASlVILVG 775
Cdd:cd07084 173 ALLLHPNPKMVLFTGSSRVAEKLALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQS-MLFVP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 776 QAARSKRFRSQLLDGVRSIDVGypteaTTQMGPIIGPAegkLLDGLTKLGAGEQWVV----QPRKLDEEGRLWSPGVRSG 851
Cdd:cd07084 252 ENWSKTPLVEKLKALLARRKLE-----DLLLGPVQTFT---TLAMIAHMENLLGSVLlfsgKELKNHSIPSIYGACVASA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 852 V-------RRGSEYHRTEYFGPVLGIMTAATLEEA--IEIANEVDYGLTAGLHS-----LDAKEIATWVdsieAGNLY-V 916
Cdd:cd07084 324 LfvpideiLKTYELVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSndpifLQELIGNLWV----AGRTYaI 399
|
410 420 430
....*....|....*....|....*....|....*
gi 2066550363 917 NRGITGAIVQRQPFGGWKKSVVGptTKAGGPNYLH 951
Cdd:cd07084 400 LRGRTGVAPNQNHGGGPAADPRG--AGIGGPEAIK 432
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
534-939 |
5.84e-22 |
|
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: 101.03 E-value: 5.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 534 TAEELASRIRTALDA--NAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAG-------KTldqsdpEISEAIDFA 604
Cdd:cd07140 41 TVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGavytlalKT------HVGMSIQTF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 605 HYYAELAvalEQVDGA-----EYDPSRLVVVTP-----------PWNFPVAIPAGSTLAALASGASVIIKPARQAARCGA 668
Cdd:cd07140 115 RYFAGWC---DKIQGKtipinQARPNRNLTLTKrepigvcgiviPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTAL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 669 VMVEALWAAGVPREALQYVQFSDRELGRALVADDAVDRVILTGGFET-AELFRSF------RPDLELlaetSGKNAIIVT 741
Cdd:cd07140 192 KFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIgKHIMKSCavsnlkKVSLEL----GGKSPLIIF 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 742 PSADYDLAAKDVIASAFGHAGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAE-GKLLDG 820
Cdd:cd07140 268 ADCDMDKAVRMGMSSVFFNKGENCIAAGRLFV--EESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHlDKLVEY 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 821 LTK-LGAGEQWVVQPRKLDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGI--MTAATLEEAIEIANEVDYGLTAGLHSL 897
Cdd:cd07140 346 CERgVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIIskFDDGDVDGVLQRANDTEYGLASGVFTK 425
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2066550363 898 DAKEIATWVDSIEAGNLYVNRGITGAIVqrQPFGGWKKSVVG 939
Cdd:cd07140 426 DINKALYVSDKLEAGTVFVNTYNKTDVA--APFGGFKQSGFG 465
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
621-932 |
1.66e-18 |
|
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: 89.51 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 621 EYDPSRLVVVTPPWNFPVA---IPAgstLAALASGASVIIKPARQAARCGAVMVEaLWAAGVPREALQYVQfSDRELGRA 697
Cdd:cd07087 97 IPEPLGVVLIIGPWNYPLQlalAPL---IGAIAAGNTVVLKPSELAPATSALLAK-LIPKYFDPEAVAVVE-GGVEVATA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 698 LVADdAVDRVILTGGFETAELF-----RSFRP-DLELlaetSGKNAIIVTPSADYDLAAKDVIASAFGHAGQKCSAASLV 771
Cdd:cd07087 172 LLAE-PFDHIFFTGSPAVGKIVmeaaaKHLTPvTLEL----GGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 772 iLVgqaarSKRFRSQLLDG-VRSIDVGYPTEattqmgPIIGPAEGKL-----LDGLTKLGAGEQwVVQPRKLDEEGRLWS 845
Cdd:cd07087 247 -LV-----HESIKDELIEElKKAIKEFYGED------PKESPDYGRIinerhFDRLASLLDDGK-VVIGGQVDKEERYIA 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 846 PGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGNLYVNRGITGAIV 925
Cdd:cd07087 314 PTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAI 393
|
....*..
gi 2066550363 926 QRQPFGG 932
Cdd:cd07087 394 PNLPFGG 400
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
553-965 |
3.25e-18 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 89.38 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 553 RDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAHYYAELAVALEQV----DGaeyDPSRLV 628
Cdd:PRK11903 58 RALTYAQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAKLGAALGDArllrDG---EAVQLG 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 629 ---------VVTP---------PWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGV-PREALQYVQF 689
Cdd:PRK11903 135 kdpafqgqhVLVPtrgvalfinAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 690 SDRELGRALVADDAVDrviLTGGFETAELFRS----FRPDLELLAETSGKNAIIVTP-----SADYDLAAKDVIASAFGH 760
Cdd:PRK11903 215 SSAGLLDHLQPFDVVS---FTGSAETAAVLRShpavVQRSVRVNVEADSLNSALLGPdaapgSEAFDLFVKEVVREMTVK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 761 AGQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAE-GKLLDGLTKLGAGEQWV-----VQP 834
Cdd:PRK11903 292 SGQKCTAIRRIFV--PEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQlAAVRAGLAALRAQAEVLfdgggFAL 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 835 RKLDEEGRLWSPGVRSGVRRG---SEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEA 911
Cdd:PRK11903 370 VDADPAVAACVGPTLLGASDPdaaTAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALELAD 449
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2066550363 912 --GNLYVnrgITGAIVQRQPFGGwkksVVGPTTKAGGPNY---------LHALGDWHTAAATKGA 965
Cdd:PRK11903 450 shGRVHV---ISPDVAALHTGHG----NVMPQSLHGGPGRagggeelggLRALAFYHRRSAVQAS 507
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
622-932 |
2.66e-17 |
|
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: 86.13 E-value: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 622 YDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPREaLQYVQfSDRELGRALVA- 700
Cdd:cd07134 98 YEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDE-VAVFE-GDAEVAQALLEl 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 701 ---------DDAVDRVILTGGfetAELFRSFrpDLELlaetSGKNAIIVTPSADYDLAAKDVIASAFGHAGQKCSAASLV 771
Cdd:cd07134 176 pfdhifftgSPAVGKIVMAAA---AKHLASV--TLEL----GGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 772 iLVgQAARSKRFRSQLldgVRSIDVGYPTEATTQMGP----IIGPAEGKLLDGLTK--LGAGEQwVVQPRKLDEEGRLWS 845
Cdd:cd07134 247 -FV-HESVKDAFVEHL---KAEIEKFYGKDAARKASPdlarIVNDRHFDRLKGLLDdaVAKGAK-VEFGGQFDAAQRYIA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 846 PGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGNLYVNRGITGAIV 925
Cdd:cd07134 321 PTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLN 400
|
....*..
gi 2066550363 926 QRQPFGG 932
Cdd:cd07134 401 PNLPFGG 407
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
622-932 |
2.50e-16 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 83.54 E-value: 2.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 622 YDPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEaLWAAGVPREALQYVQfSDRELGRALVaD 701
Cdd:PTZ00381 107 PEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAK-LLTKYLDPSYVRVIE-GGVEVTTELL-K 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 702 DAVDRVILTGGFETAELF-----RSFRP-DLELlaetSGKNAIIVTPSADYDLAAKDVIASAFGHAGQKCSAASLVILvg 775
Cdd:PTZ00381 184 EPFDHIFFTGSPRVGKLVmqaaaENLTPcTLEL----GGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLV-- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 776 qaarSKRFRSQLLDGVRsidvgypTEATTQMGP----------IIGPAEGKLLDGLTKLGAGEqwVVQPRKLDEEGRLWS 845
Cdd:PTZ00381 258 ----HRSIKDKFIEALK-------EAIKEFFGEdpkksedysrIVNEFHTKRLAELIKDHGGK--VVYGGEVDIENKYVA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 846 PGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGNLYVNRGITGAIV 925
Cdd:PTZ00381 325 PTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLN 404
|
....*..
gi 2066550363 926 QRQPFGG 932
Cdd:PTZ00381 405 PNLPFGG 411
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
545-947 |
9.49e-16 |
|
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: 81.43 E-value: 9.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 545 ALDANAIWRDLPAAERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAID----FAHYYAELAVALEQVDGA 620
Cdd:cd07129 8 AAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGqlrlFADLVREGSWLDARIDPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 621 eyDPSRL----------------VVVTPPWNFPVA--IPAGSTLAALASGASVIIK--PA--RQAARCGAVMVEALWAAG 678
Cdd:cd07129 88 --DPDRQplprpdlrrmlvplgpVAVFGASNFPLAfsVAGGDTASALAAGCPVVVKahPAhpGTSELVARAIRAALRATG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 679 VPREALQYVQFSDRELGRALVADDAVDRVILTGGFE--TAeLFR--SFRPD-LELLAETSGKNAIIVTPSA---DYDLAA 750
Cdd:cd07129 166 LPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRggRA-LFDaaAARPEpIPFYAELGSVNPVFILPGAlaeRGEAIA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 751 KDVIASAFGHAGQKCSAASLVILVgQAARSKRFRSQLLDGVRSIDvgypteATTQMGPIIGPAEGKLLDGLTKLGAGEQW 830
Cdd:cd07129 245 QGFVGSLTLGAGQFCTNPGLVLVP-AGPAGDAFIAALAEALAAAP------AQTMLTPGIAEAYRQGVEALAAAPGVRVL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 831 VVQPRKLDEEGRLWSPGVRSGVR-RGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDA--KEIATWVD 907
Cdd:cd07129 318 AGGAAAEGGNQAAPTLFKVDAAAfLADPALQEEVFGPASLVVRYDDAAELLAVAEALEGQLTATIHGEEDdlALARELLP 397
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2066550363 908 SIEAgnlyvnrgITGAIVqrqpFGGWKKSV-VGPTTKAGGP 947
Cdd:cd07129 398 VLER--------KAGRLL----FNGWPTGVeVCPAMVHGGP 426
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
623-932 |
3.13e-14 |
|
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: 76.49 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 623 DPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALwaagvpreaLQYVqfsDRELGRalvadd 702
Cdd:cd07132 99 EPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELI---------PKYL---DKECYP------ 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 703 avdrVILTGGFETAELFRSfRPD--------------------------LELlaetSGKNAIIVTPSADYDLAAKDVIAS 756
Cdd:cd07132 161 ----VVLGGVEETTELLKQ-RFDyifytgstsvgkivmqaaakhltpvtLEL----GGKSPCYVDKSCDIDVAARRIAWG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 757 AFGHAGQKCSAASLVILvgqaarSKRFRSQLLDGVRSIDV---GYPTEATTQMGPIIGPAE----GKLLDGlTKLGAGEQ 829
Cdd:cd07132 232 KFINAGQTCIAPDYVLC------TPEVQEKFVEALKKTLKefyGEDPKESPDYGRIINDRHfqrlKKLLSG-GKVAIGGQ 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 830 WvvqprklDEEGRLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSI 909
Cdd:cd07132 305 T-------DEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNT 377
|
330 340
....*....|....*....|...
gi 2066550363 910 EAGNLYVNRGITGAIVQRQPFGG 932
Cdd:cd07132 378 SSGGVCVNDTIMHYTLDSLPFGG 400
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
630-917 |
2.24e-13 |
|
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: 73.68 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 630 VTPPWNfPVAIPAGSTLAALASGASVIIKPARQAARCGA----VMVEALWAAGVPREALQYVQFSDRELGRALVADDAVD 705
Cdd:cd07122 102 LIPSTN-PTSTAIFKALIALKTRNAIIFSPHPRAKKCSIeaakIMREAAVAAGAPEGLIQWIEEPSIELTQELMKHPDVD 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 706 RVILTGGfetAELFRSfrpdlellAETSGKNAIIVTP---------SADYDLAAKDVIAS-AFGHaGQKCSAASLVILV- 774
Cdd:cd07122 181 LILATGG---PGMVKA--------AYSSGKPAIGVGPgnvpayideTADIKRAVKDIILSkTFDN-GTICASEQSVIVDd 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 775 -------------G----QAARSKRFRSQLLDGVRSID---VGYPTEATTQMGPIIGPAEGKLLdgltklgAGEQwvvqp 834
Cdd:cd07122 249 eiydevraelkrrGayflNEEEKEKLEKALFDDGGTLNpdiVGKSAQKIAELAGIEVPEDTKVL-------VAEE----- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 835 rkldeegrlwspgvrSGVRRGSEYHRtEYFGPVLGIMTAATLEEAIEIANE-VDY---GLTAGLHSLDAKEIATWVDSIE 910
Cdd:cd07122 317 ---------------TGVGPEEPLSR-EKLSPVLAFYRAEDFEEALEKARElLEYggaGHTAVIHSNDEEVIEEFALRMP 380
|
....*..
gi 2066550363 911 AGNLYVN 917
Cdd:cd07122 381 VSRILVN 387
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
553-906 |
4.96e-13 |
|
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: 73.07 E-value: 4.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 553 RDLPAAERAAILHKAGDELERRRGELMEVAASeAGKTLDQSDPEISEAIDFAHYYAELAvALEQVDG---AEYDPSRLV- 628
Cdd:cd07128 54 RALTFHERAAMLKALAKYLMERKEDLYALSAA-TGATRRDSWIDIDGGIGTLFAYASLG-RRELPNAhflVEGDVEPLSk 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 629 --------VVTP---------PWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGV-PREALQYVQFS 690
Cdd:cd07128 132 dgtfvgqhILTPrrgvavhinAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 691 DRELGRALvadDAVDRVILTGGFETAELFRS----FRPDLELLAETSGKNAIIVTPSA-----DYDLAAKDVIASAFGHA 761
Cdd:cd07128 212 VGDLLDHL---GEQDVVAFTGSAATAAKLRAhpniVARSIRFNAEADSLNAAILGPDAtpgtpEFDLFVKEVAREMTVKA 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 762 GQKCSAASLVILvgQAARSKRFRSQLLDGVRSIDVGYPTEATTQMGPIIGPAE-GKLLDGLTKLGAGEQWV--------- 831
Cdd:cd07128 289 GQKCTAIRRAFV--PEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQrEDVRAAVATLLAEAEVVfggpdrfev 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 832 ----------VQPRKLDEEGRLWSPGVrsgvrrgseyHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKE 901
Cdd:cd07128 367 vgadaekgafFPPTLLLCDDPDAATAV----------HDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAF 436
|
....*
gi 2066550363 902 IATWV 906
Cdd:cd07128 437 ARELV 441
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
623-939 |
1.74e-12 |
|
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: 70.90 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 623 DPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEaLWAAGVPREALQYVQFSDRElGRALVaDD 702
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAK-LIPEYLDTKAIKVIEGGVPE-TTALL-EQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 703 AVDRVILTGGFETAELF-----RSFRP-DLELlaetSGKNAIIVTPSADYDLAAKDVIASAFG-HAGQKCSAASLVILvg 775
Cdd:cd07137 177 KWDKIFFTGSPRVGRIImaaaaKHLTPvTLEL----GGKCPVIVDSTVDLKVAVRRIAGGKWGcNNGQACIAPDYVLV-- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 776 qaarSKRFRSQLLDGVRSID---VGYPTEATTQMGPIIGPAEGKLLDGLTKLGAGEQWVVQPRKLDEEGRLWSPGVRSGV 852
Cdd:cd07137 251 ----EESFAPTLIDALKNTLekfFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERDEKNLYIEPTILLDP 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 853 RRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGNLYVNRGITGAIVQRQPFGG 932
Cdd:cd07137 327 PLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTLPFGG 406
|
....*..
gi 2066550363 933 WKKSVVG 939
Cdd:cd07137 407 VGESGFG 413
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
275-432 |
6.29e-12 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 69.34 E-value: 6.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 275 QAYLPDALDamiRLQEwSAARVARGGAPIKIRLVKGANLPMERVEASLHGWPVATWGSKQDTDTNYKRCVDYALQPEHVK 354
Cdd:PLN02681 274 QAYLKDARE---RLRL-DLERSEREGVPLGAKLVRGAYLSLERRLAASLGVPSPVHDTIQDTHACYNRCAEFLLEKASNG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 355 HVRIGVAGHNLFDVALSWLLAKQRGVTEG---IEYEMLLGMAQ------GQAE--VVKrdvgslllYTPVvhpSEFDVAI 423
Cdd:PLN02681 350 DGEVMLATHNVESGELAAAKMNELGLHKGdprVQFAQLLGMSDnlsfglGNAGfrVSK--------YLPY---GPVEEVI 418
|
....*....
gi 2066550363 424 AYLIRRLEE 432
Cdd:PLN02681 419 PYLLRRAEE 427
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
633-940 |
5.38e-11 |
|
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: 66.35 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 633 PWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALwAAGVPREALQYVQfsdrelGRALVADD----AVDRVI 708
Cdd:cd07133 110 PWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELL-AEYFDEDEVAVVT------GGADVAAAfsslPFDHLL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 709 LTGGFETAELF-----RSFRP-DLELlaetSGKNAIIVTPSADYDLAAKDVIASAFGHAGQKCSAASLVILvgQAARSKR 782
Cdd:cd07133 183 FTGSTAVGRHVmraaaENLTPvTLEL----GGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLV--PEDKLEE 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 783 FRSQLLDGVRSIdvgYPTEATTQ-MGPIIGPAEGKLLDGL-----------TKLGAGEQWVVQPRKLdeegrlwSPGVRS 850
Cdd:cd07133 257 FVAAAKAAVAKM---YPTLADNPdYTSIINERHYARLQGLledarakgarvIELNPAGEDFAATRKL-------PPTLVL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 851 GVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGNLYVNRGITGAIVQRQPF 930
Cdd:cd07133 327 NVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHVAQDDLPF 406
|
330
....*....|
gi 2066550363 931 GGwkksvVGP 940
Cdd:cd07133 407 GG-----VGA 411
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
558-809 |
1.20e-09 |
|
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: 61.86 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 558 AERAAILHKAGDELERRRGELMEVAASEAGKTLDQSDPEISEAIDFAH-YYAELAVALEQVDGAEY--------DPSRLV 628
Cdd:cd07077 16 EQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMGCSEsKLYKNIDTERGITASVGhiqdvllpDNGETY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 629 VVTPPWN-----FPVAIPAG---STLAALASGASVIIKPARQA---ARCGAVMVEALWAAGVPREALQYVQFSDRELGRA 697
Cdd:cd07077 96 VRAFPIGvtmhiLPSTNPLSgitSALRGIATRNQCIFRPHPSApftNRALALLFQAADAAHGPKILVLYVPHPSDELAEE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 698 LVADDAVDRVILTGGFETAELFRSFRPDLELLAETSGKNAIIVTPSADYDLAAKDVIASAFgHAGQKCSAASLVILVGQA 777
Cdd:cd07077 176 LLSHPKIDLIVATGGRDAVDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKF-FDQNACASEQNLYVVDDV 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2066550363 778 ARSKRFRSQLLDGVRSIDV-------------GYPTEATTQMGPI 809
Cdd:cd07077 255 LDPLYEEFKLKLVVEGLKVpqetkplskettpSFDDEALESMTPL 299
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
623-939 |
3.17e-08 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 57.75 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 623 DPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPrEALQYVQFSDRELGRALvaDD 702
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDS-SAVRVVEGAVTETTALL--EQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 703 AVDRVILTGGFETAELFRSFRPD--LELLAETSGKNAIIVTPSADYDLAAKDVIASAFG-HAGQKCSAASLVIlvgqaaR 779
Cdd:PLN02174 188 KWDKIFYTGSSKIGRVIMAAAAKhlTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYIL------T 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 780 SKRFRSQLLDGVR-SIDVGY---PTEaTTQMGPIIGPAEGKLLDGLTKLGAGEQWVVQPRKLDEEGRLWSPGVRSGVRRG 855
Cdd:PLN02174 262 TKEYAPKVIDAMKkELETFYgknPME-SKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGEKDRENLKIAPTILLDVPLD 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 856 SEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGNLYVNRGITGAIVQRQPFGGWKK 935
Cdd:PLN02174 341 SLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVGE 420
|
....
gi 2066550363 936 SVVG 939
Cdd:PLN02174 421 SGMG 424
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
623-939 |
4.06e-07 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 53.96 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 623 DPSRLVVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMvealwAAGVPR----EALQYVQfsdrelGRAL 698
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFL-----AANIPKyldsKAVKVIE------GGPA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 699 VADDAV----DRVILTGGFETAELFRS-----FRP-DLELlaetSGKNAIIV---TPSADYDLAAKDVIASAFGH-AGQK 764
Cdd:PLN02203 176 VGEQLLqhkwDKIFFTGSPRVGRIIMTaaakhLTPvALEL----GGKCPCIVdslSSSRDTKVAVNRIVGGKWGScAGQA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 765 CSAASLVILvgqaarSKRFRSQLLDGVRSID---VGYPTEATTQMGPIIGPAEGKLLDGLTKLGAGEQWVVQPRKLDEEG 841
Cdd:PLN02203 252 CIAIDYVLV------EERFAPILIELLKSTIkkfFGENPRESKSMARILNKKHFQRLSNLLKDPRVAASIVHGGSIDEKK 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 842 RLWSPGVRSGVRRGSEYHRTEYFGPVLGIMTAATLEEAIEIANEVDYGLTAGLHSLDAKEIATWVDSIEAGNLYVNRGIT 921
Cdd:PLN02203 326 LFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAII 405
|
330
....*....|....*...
gi 2066550363 922 GAIVQRQPFGGWKKSVVG 939
Cdd:PLN02203 406 QYACDSLPFGGVGESGFG 423
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
558-903 |
1.99e-06 |
|
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: 51.88 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 558 AERAAILHKAGDELERRRGELMEVAASEAGKTLDQsDPEISEAidFAHYYAELAVALEQVDG--AEYDPSRLVVVTPPWN 635
Cdd:cd07081 21 EMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVE-DKVIKNH--FAAEYIYNVYKDEKTCGvlTGDENGGTLIIAEPIG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 636 F-----PVAIPAGST----LAALASGASVIIKPARQAA----RCGAVMVEALWAAGVPREALQYVQFSDRELGRALVADD 702
Cdd:cd07081 98 VvasitPSTNPTSTVifksLISLKTRNSIIFSPHPRAKkvtqRAATLLLQAAVAAGAPENLIGWIDNPSIELAQRLMKFP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 703 AVDRVILTGGFETAELFRSFRPdlELLAETSGKNAIIVTPSADYDLAAKDVIASAFGHAGQKCSAASLVILVGQAARSKR 782
Cdd:cd07081 178 GIGLLLATGGPAVVKAAYSSGK--PAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVVDSVYDEVM 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 783 FRSQLLDGVRsidvgYPTEATTQMGPIIgpaegklldgLTKLGAGEQWVVQPR---------KLDEEGRLWSpgVRSGVR 853
Cdd:cd07081 256 RLFEGQGAYK-----LTAEELQQVQPVI----------LKNGDVNRDIVGQDAykiaaaaglKVPQETRILI--GEVTSL 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2066550363 854 RGSEYHRTEYFGPVLGIMTAATLEEAIEIA----NEVDYGLTAGLHSLDAKEIA 903
Cdd:cd07081 319 AEHEPFAHEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSDNIKAIE 372
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
632-924 |
1.42e-05 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 49.01 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 632 PPWNfpvAIPAgsTLAALASGASVIIKPARQAARCGAVMV----EALWAAGV-PREALQYVQFSDRELGRALVADDAVDR 706
Cdd:cd07127 206 PTWN---GYPG--LFASLATGNPVIVKPHPAAILPLAITVqvarEVLAEAGFdPNLVTLAADTPEEPIAQTLATRPEVRI 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 707 VILTGGFETAELFRSFRPDLELLAETSGKNAIIVTPSADYDLAAKDVIASAFGHAGQKCSAASLV------ILVGQAARS 780
Cdd:cd07127 281 IDFTGSNAFGDWLEANARQAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIyvprdgIQTDDGRKS 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 781 krFRSQLLDGVRSID--VGYPTEATTQMGPIIGPAegkLLDGLTKLGAGEQWVVQPRKLD----EEGRLWSPGVRSGVRR 854
Cdd:cd07127 361 --FDEVAADLAAAIDglLADPARAAALLGAIQSPD---TLARIAEARQLGEVLLASEAVAhpefPDARVRTPLLLKLDAS 435
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2066550363 855 GSEYHRTEYFGPVLGIMTAATLEEAIEIANEV--DYG-LTAGLHSLDAKEIATWVDSIEAGNLYVNRGITGAI 924
Cdd:cd07127 436 DEAAYAEERFGPIAFVVATDSTDHSIELARESvrEHGaMTVGVYSTDPEVVERVQEAALDAGVALSINLTGGV 508
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
628-771 |
1.23e-03 |
|
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: 42.87 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066550363 628 VVVTPPWNFPVAIPAGSTLAALASGASVIIKPARQAARCGAVMVEALWAAGVPREALQYVQFSDRELGRALVadDAVDRV 707
Cdd:cd07126 146 VAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILL--EANPRM 223
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2066550363 708 IL-TGGFETAE-LFRSFRPDLELlaETSGKNAIIVTPS-ADYDLAAKDVIASAFGHAGQKCSAASLV 771
Cdd:cd07126 224 TLfTGSSKVAErLALELHGKVKL--EDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSIL 288
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
647-712 |
3.54e-03 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 41.21 E-value: 3.54e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2066550363 647 AALA--SGASVIIKPARQAARC----GAVMVEALWAAGVPREALQYVQFSDRELGRALV-ADDAVDRVILTGG 712
Cdd:PRK00197 134 AALClkSGNAVILRGGSEAIHSnralVAVIQEALEEAGLPADAVQLVETTDRAAVGELLkLDGYVDVIIPRGG 206
|
|
| |
