|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
528-950 |
0e+00 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 569.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEE 607
Cdd:cd07125 67 DAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 608 L----------DELEGVRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEA 677
Cdd:cd07125 147 LfsdpelpgptGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDV 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 678 LRLVdihPDEMAEVGEALVTGS--DQVILTGSIETAKLFRSW-----EPDLAVFAETSGKNAIIVTPQADIDLAAKDLVQ 750
Cdd:cd07125 227 LQLV---PGDGEEIGEALVAHPriDGVIFTGSTETAKLINRAlaerdGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQ 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 751 SAFGHAGQKCSAASIAILVGAMgkSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAAGKLKRGLTELEPGQTWLLKPR 830
Cdd:cd07125 304 SAFGSAGQRCSALRLLYLQEEI--AERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAPA 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 831 QLDDS-GRLWSPGIRDGVtpGQDAHMTEYFGPVLGIMRAE--TLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEAG 907
Cdd:cd07125 382 PLDDGnGYFVAPGIIEIV--GIFDLTTEVFGPILHVIRFKaeDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAG 459
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2515445683 908 NVYVNRGTTGAIVRRQPFGGWKRSqvGTGSKAGGPNHLIGMSH 950
Cdd:cd07125 460 NLYINRNITGAIVGRQPFGGWGLS--GTGPKAGGPNYLLRFGN 500
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
11-947 |
1.21e-132 |
|
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: 428.70 E-value: 1.21e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 11 SQVAHAAIDQAKTWAKRSASFPEDRAGKLLSQVLKGEGGLDFTVQFVDGVIRPEDPKTRAANLNKLAKKPASFLPAYLSL 90
Cdd:COG0506 7 EALRARAVALARRLVEAIRAAPEGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLAKSPSFLVNASTW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 91 PAKVGGVlAPASPTFITEAAFRVFRMLVGNLVLDTTPKKLGPAVKKLRADGSRLNLNLLGEAVLGRKEAARRLAAVTELL 170
Cdd:COG0506 87 GLMLTLV-GRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAARKLRAKGYRVSLDLLGEAVLTEAEAERYLDAYLEAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 171 EYD-----FVDYVSIKVSSVLGVHNPWGYQKAVDQAIEALLPLYRVANKGGKFVNLDMEEYHDLHLTIDVFTGILDREEF 245
Cdd:COG0506 166 EAIgaagvDRPGVSVKLSALGPRYSPAQRERVVEELLERLRPLARAAREAGIFVTIDMEEYDRLDLTLDVFERLLADPEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 246 KN-LRAGIVLQAYLPDTLPAMERLQEWAAQrvadGGAPVKVRLVKGANLPMEQVDALMHGWPLAVQPSKAATDANYMRIL 324
Cdd:COG0506 246 AGwPGVGIVLQAYLKRAEADLDRLAALARR----GGRRIRVRLVKGAYWDPEIVRAQVHGWPYPVFTRKADTDANYLRCA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 325 EYALrpEHISNVNLGIAGQNLFTLGFGLNLAKARGV-TEGFEVEMLKGMATNQALAIR-EDVGRILYYVPVVDPANYDVA 402
Cdd:COG0506 322 RKLL--EAGDAIYPQFATHNARTIAAALALAGERGRpPDRFEFQMLYGMGEDLQRALAaVDGGRLLLYCPVVAPVGGDAA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 403 ISYLVRRLEESAAHENFMSGVFEIADNDSVFARERNRFATGVVAAFPEADLAEAMGPLNEVPTLSFGPNRHQNRLTDDVD 482
Cdd:COG0506 400 LAYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPRFLAALAAPTPPPPPPLRRQRRRRRRARGGALAAALAAAAAAAA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 483 LltsfRNTPDSDPSLPANIEWANQIFAKMGDSELGVQGADDARVRTVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAG 562
Cdd:COG0506 480 L----AAAAAAAAALAAAAAGAAAAAAAAAVAVVPAAAAAVVAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 563 QVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEELDELEGVRFSPAPVTAAIPPWNFPLAIPAGSALAP 642
Cdd:COG0506 556 AAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAARAAAPPPPPPGGLVALLPLGPLAAAAAAAAAA 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 643 LATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEALRLVDIHPDEMAEVGEALVTGSDQVILTGSietaklfrswepDLA 722
Cdd:COG0506 636 AAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAGGGVLVLGAGGGAGGAAALT------------LAA 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 723 VFAETSGKNAIIVTPQADIDLAAKDLVQSAFGHAGQKCSAASIAILVGAMGKSERFINQVVDAAESLVVDWPTNPSAEMG 802
Cdd:COG0506 704 AAAAATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVAASAAASASASASLLSLLALLLLDADL 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 803 PIIEPAAGKLKRGLTELEPGQTWLLKPRQLDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVE 882
Cdd:COG0506 784 VILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLPGGGPLVPGLLTAPLLVALILGLIVLV 863
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2515445683 883 FGLTAGLHSLDPDEIKLWLSKVEAGNVYVNRGTTGAIVRRQPFGGWKRSQVGTGSKAGGPNHLIG 947
Cdd:COG0506 864 LLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGGGGGGG 928
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
528-941 |
2.47e-115 |
|
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: 366.76 E-value: 2.47e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEE 607
Cdd:COG1012 41 TAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 608 LD------ELEG----VRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEA 677
Cdd:COG1012 121 LYgetipsDAPGtrayVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 678 LRLVdihPDEMAEVGEALVT--GSDQVILTGSIETAKLFRSWEPD--LAVFAETSGKNAIIVTPQADIDLAAKDLVQSAF 753
Cdd:COG1012 201 LNVV---TGDGSEVGAALVAhpDVDKISFTGSTAVGRRIAAAAAEnlKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAF 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 754 GHAGQKCSAASIAILVGamGKSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAAGKLKRGLTE--LEPGQTWLLKPRQ 831
Cdd:COG1012 278 GNAGQRCTAASRLLVHE--SIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEdaVAEGAELLTGGRR 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 832 LDDS-GRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEAGNVY 910
Cdd:COG1012 356 PDGEgGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVW 435
|
410 420 430
....*....|....*....|....*....|.
gi 2515445683 911 VNRGTTGAIVrRQPFGGWKRSqvGTGSKAGG 941
Cdd:COG1012 436 INDGTTGAVP-QAPFGGVKQS--GIGREGGR 463
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
487-945 |
1.85e-109 |
|
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: 352.30 E-value: 1.85e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 487 FRNTPDSDPSLPANIEWANQIFAKMGDsELG-----------VQGADDARVR---------------TVAEMEQIVAEAR 540
Cdd:cd07124 1 FRNEPFTDFADEENRAAFRAALARVRE-ELGreyplviggkeVRTEEKIESRnpadpsevlgtvqkaTKEEAEAAVQAAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 541 KAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEEL---------DEL 611
Cdd:cd07124 80 AAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLrgfpvemvpGED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 612 EGVRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEALRLVdihPDEMAEV 691
Cdd:cd07124 160 NRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFL---PGPGEEV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 692 GEALVTGSDQ--VILTGSIETA----KLFRSWEPDLA----VFAETSGKNAIIVTPQADIDLAAKDLVQSAFGHAGQKCS 761
Cdd:cd07124 237 GDYLVEHPDVrfIAFTGSREVGlriyERAAKVQPGQKwlkrVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 762 AASIAILVGAMgkSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAAGKLKRGLTELEPGQTWLL---KPRQLDDSGRL 838
Cdd:cd07124 317 ACSRVIVHESV--YDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEGRLLlggEVLELAAEGYF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 839 WSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEAGNVYVNRGTTGA 918
Cdd:cd07124 395 VQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGA 474
|
490 500
....*....|....*....|....*..
gi 2515445683 919 IVRRQPFGGWKRSqvGTGSKAGGPNHL 945
Cdd:cd07124 475 LVGRQPFGGFKMS--GTGSKAGGPDYL 499
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
528-940 |
7.49e-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: 7.49e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEE 607
Cdd:pfam00171 27 TAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGEVDRAIDVLRYYAGLARR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 608 LD----ELEGVRFS-----PAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEAL 678
Cdd:pfam00171 107 LDgetlPSDPGRLAytrrePLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAGLPAGVL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 679 RLVdihPDEMAEVGEALVT--GSDQVILTGSIETAKLF--RSWEPDLAVFAETSGKNAIIVTPQADIDLAAKDLVQSAFG 754
Cdd:pfam00171 187 NVV---TGSGAEVGEALVEhpDVRKVSFTGSTAVGRHIaeAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 755 HAGQKCSAASIAILVGAMgkSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAA-----GKLKRGLTElepGQTWLLKP 829
Cdd:pfam00171 264 NAGQVCTATSRLLVHESI--YDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQlervlKYVEDAKEE---GAKLLTGG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 830 RQLDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEAGNV 909
Cdd:pfam00171 339 EAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMV 418
|
410 420 430
....*....|....*....|....*....|.
gi 2515445683 910 YVNRGTTGAIVRRqPFGGWKRSqvGTGSKAG 940
Cdd:pfam00171 419 WINDYTTGDADGL-PFGGFKQS--GFGREGG 446
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
528-945 |
2.40e-92 |
|
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: 306.02 E-value: 2.40e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEE 607
Cdd:TIGR01237 67 SQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 608 LD----------ELEGVRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEA 677
Cdd:TIGR01237 147 LAkgkpvnsregETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGV 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 678 LRLVdihPDEMAEVGEALVTGSDQVIL--TGS-------IETAKLFRSWEPDLA-VFAETSGKNAIIVTPQADIDLAAKD 747
Cdd:TIGR01237 227 VQFV---PGSGSEVGDYLVDHPKTSLItfTGSrevgtriFERAAKVQPGQKHLKrVIAEMGGKDTVIVDEDADIELAAQS 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 748 LVQSAFGHAGQKCSAASIAILVGAMgkSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAAGKLKRGLTELEPGQTWLL 827
Cdd:TIGR01237 304 AFTSAFGFAGQKCSAGSRAVVHEKV--YDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEGRLV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 828 KPRQLDDS-GRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEA 906
Cdd:TIGR01237 382 SGGCGDDSkGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEV 461
|
410 420 430
....*....|....*....|....*....|....*....
gi 2515445683 907 GNVYVNRGTTGAIVRRQPFGGWKRSqvGTGSKAGGPNHL 945
Cdd:TIGR01237 462 GNLYFNRNITGAIVGYQPFGGFKMS--GTDSKAGGPDYL 498
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
533-942 |
4.32e-88 |
|
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: 291.42 E-value: 4.32e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 533 EQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEEL---- 608
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLhgev 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 609 ------DELEGVRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEALRLVd 682
Cdd:cd07078 81 ipspdpGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVV- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 683 ihPDEMAEVGEALVT--GSDQVILTGSIETAKLFRSwepDLA-----VFAETSGKNAIIVTPQADIDLAAKDLVQSAFGH 755
Cdd:cd07078 160 --TGDGDEVGAALAShpRVDKISFTGSTAVGKAIMR---AAAenlkrVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 756 AGQKCSAASiAILVGAmGKSERFINQVVDAAESLVVDWPTNPSAEMGPII-EPAAGKLKRGLTE-LEPGQTWLL-KPRQL 832
Cdd:cd07078 235 AGQVCTAAS-RLLVHE-SIYDEFVERLVERVKALKVGNPLDPDTDMGPLIsAAQLDRVLAYIEDaKAEGAKLLCgGKRLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 833 DDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEAGNVYVN 912
Cdd:cd07078 313 GGKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIN 392
|
410 420 430
....*....|....*....|....*....|
gi 2515445683 913 RGTTGAIVrRQPFGGWKRSqvGTGsKAGGP 942
Cdd:cd07078 393 DYSVGAEP-SAPFGGVKQS--GIG-REGGP 418
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
528-954 |
1.33e-85 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 287.60 E-value: 1.33e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEE 607
Cdd:PRK03137 71 TKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 608 L----------DELEGVRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEA 677
Cdd:PRK03137 151 LadgkpvesrpGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGV 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 678 LRLVdihPDEMAEVGEALVTGSDQ--VILTGSIET--------AK-------LFRswepdlaVFAETSGKNAIIVTPQAD 740
Cdd:PRK03137 231 VNFV---PGSGSEVGDYLVDHPKTrfITFTGSREVglriyeraAKvqpgqiwLKR-------VIAEMGGKDAIVVDEDAD 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 741 IDLAAKDLVQSAFGHAGQKCSAASIAILVGAMgkSERFINQVVDAAESLVVDWPTNPSAeMGPIIEPAAGKLKRGLTELE 820
Cdd:PRK03137 301 LDLAAESIVASAFGFSGQKCSACSRAIVHEDV--YDEVLEKVVELTKELTVGNPEDNAY-MGPVINQASFDKIMSYIEIG 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 821 PGQTWLLKPRQLDDS-GRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKL 899
Cdd:PRK03137 378 KEEGRLVLGGEGDDSkGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEK 457
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2515445683 900 WLSKVEAGNVYVNRGTTGAIVRRQPFGGWKRSqvGTGSKAGGPNHLIGMSHAEPV 954
Cdd:PRK03137 458 ARREFHVGNLYFNRGCTGAIVGYHPFGGFNMS--GTDSKAGGPDYLLLFLQAKTV 510
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
220-1107 |
6.68e-82 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 292.15 E-value: 6.68e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 220 NLDMEEYHDLHLTIDVFTGILDREEFKNLRA-GIVLQAYLPDTLPAMERLQEwAAQRVadgGAPVKVRLVKGANLPME-- 296
Cdd:PRK11905 288 NIDAEEADRLELSLDLLEALCSDPDLAGWNGiGFVVQAYQKRCPFVIDYLID-LARRS---GRRLMVRLVKGAYWDAEik 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 297 --QVDALmHGWPlaVQPSKAATDANYM----RILEYALR--PEhisnvnlgIAGQNLFTLGFGLNLAKARGvteGFEVEM 368
Cdd:PRK11905 364 raQVDGL-EGFP--VFTRKVHTDVSYIacarKLLAARDViyPQ--------FATHNAQTLAAIYELAGGKG---DFEFQC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 369 LKGMAT---NQALAIREDVGRILYYVPVvdpANYDVAISYLVRRLEESAAHENFmsgVFEIADnDSVFARErnrfatgvV 445
Cdd:PRK11905 430 LHGMGEplyDQVVGKEKLGRPCRIYAPV---GTHETLLAYLVRRLLENGANSSF---VNRIVD-ENVPVEE--------L 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 446 AAFPeADLAEAMGPL--NEVPTLS--FGPNRHQNR---LTDDVDL------LTSFRNTPdsdpslpanieW-ANQIFAKM 511
Cdd:PRK11905 495 IADP-VEKVAAMGVAphPQIPLPRdlYGPERRNSKgldLSDEATLaaldeaLNAFAAKT-----------WhAAPLLAGG 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 512 GDSELGVQ----GADDARVRTV-----AEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGK 582
Cdd:PRK11905 563 DVDGGTRPvlnpADHDDVVGTVteasaEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGK 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 583 IVGEADVEVSEAIDFANYYADLAEELdeLEGVRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQ----AR 658
Cdd:PRK11905 643 TLANAIAEVREAVDFLRYYAAQARRL--LNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQtpliAA 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 659 RcgAViaQALWDAGVSKEALRLVdihPDEMAEVGEALVtgSDQ----VILTGSIETAKLFRSW-----EPDLAVFAETSG 729
Cdd:PRK11905 721 R--AV--RLLHEAGVPKDALQLL---PGDGRTVGAALV--ADPriagVMFTGSTEVARLIQRTlakrsGPPVPLIAETGG 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 730 KNAIIVTPQADIDLAAKDLVQSAFGHAGQKCSA------------ASIAILVGAMgkserfinqvvdaaESLVVDWPTNP 797
Cdd:PRK11905 792 QNAMIVDSSALPEQVVADVIASAFDSAGQRCSAlrvlclqedvadRVLTMLKGAM--------------DELRIGDPWRL 857
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 798 SAEMGPIIEPAA-----------GKLKRGLTELEPGQTwllkprqlDDSGRLWSP------GIRDgvtpgqdahMT-EYF 859
Cdd:PRK11905 858 STDVGPVIDAEAqanieahieamRAAGRLVHQLPLPAE--------TEKGTFVAPtlieidSISD---------LErEVF 920
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 860 GPVLGIMR--AETLEEAIRLQNAVEFGLTAGLHS-LDpDEIKLWLSKVEAGNVYVNRGTTGAIVRRQPFGGWKRSqvGTG 936
Cdd:PRK11905 921 GPVLHVVRfkADELDRVIDDINATGYGLTFGLHSrID-ETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLS--GTG 997
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 937 SKAGGPNHLIGMSHAEPVEVAVPESFATLSyPTLGEFDALADKLPKDDAGQYRAALRSVEAALKEHYLSardvsalGV-- 1014
Cdd:PRK11905 998 PKAGGPLYLGRLVREAPTPIPPAHESVDTD-AAARDFLAWLDKEGKAALAAAARDARARSALGLEQELP-------GPtg 1069
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 1015 EKNVFRYRPTSVMVRLEDPEQwWKVAPMVAGALTGKTSVelsVGDDLRDTVAQAFRAAGATVSVASPAQWLSDLPKSGAh 1094
Cdd:PRK11905 1070 ESNLLSLHPRGRVLCVADTEE-ALLRQLAAALATGNVAV---VAADSGLAAALADLPGLVAARIDWTQDWEADDPFAGA- 1144
|
970
....*....|...
gi 2515445683 1095 kiRYVGDDARAVA 1107
Cdd:PRK11905 1145 --LLEGDAERARA 1155
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
135-946 |
4.30e-80 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 284.40 E-value: 4.30e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 135 KKLRADGSRLNLNLLGEAVLGRKEAARRLAAVTELLE--------YDFVDY--VSIKVSSVLGVHNPWGYQKAVDQAIEA 204
Cdd:PRK11904 194 RSARNKGYRYSFDMLGEAALTAADAERYFKAYARAIEaigraaggADLPARpgISIKLSALHPRYEAAQRERVLAELVPR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 205 LLPLYRVANKGGKFVNLDMEEYHDLHLTIDVFTGILDREEFKNLRA-GIVLQAYLPDTLPAMERLQEWAAQRvadgGAPV 283
Cdd:PRK11904 274 VLELARLAKEANIGLTIDAEEADRLELSLDLFEALFRDPSLKGWGGfGLAVQAYQKRALPVLDWLADLARRQ----GRRI 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 284 KVRLVKGANLPMEQVDALMHGWP-LAVQPSKAATDANYM----RILeyALRPeHISNVnlgIAGQNLFTLGFGLNLAKAR 358
Cdd:PRK11904 350 PVRLVKGAYWDSEIKRAQELGLPgYPVFTRKAATDVSYLacarKLL--SARG-AIYPQ---FATHNAHTVAAILEMAGHR 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 359 GvtegFEVEMLKGMAT---NQALAIREDVGRIlyYVPVvdpANYDVAISYLVRRLEESAAHENFmsgVFEIADNDsVFAR 435
Cdd:PRK11904 424 G----FEFQRLHGMGEalyDALLDAPGIPCRI--YAPV---GSHKDLLPYLVRRLLENGANSSF---VHRLVDPD-VPIE 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 436 ErnrfatgvVAAFPeADLAEAMGPLNE----VPTLSFGPNR------------HQNRLTDDVDlltSFRNTPDSDPSLPA 499
Cdd:PRK11904 491 E--------LVADP-VEKLRSFETLPNpkipLPRDIFGPERknskglnlndrsELEPLAAAIA---AFLEKQWQAGPIIN 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 500 NIEWANQIFAKM-GDSELG-VQGADDARVrtvaemEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAA 577
Cdd:PRK11904 559 GEGEARPVVSPAdRRRVVGeVAFADAEQV------EQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCV 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 578 SECGKIVGEADVEVSEAIDFANYYADLAEELD----ELEG-------VRFSPAPVTAAIPPWNFPLAIPAGSALAPLATG 646
Cdd:PRK11904 633 REAGKTLQDAIAEVREAVDFCRYYAAQARRLFgapeKLPGptgesneLRLHGRGVFVCISPWNFPLAIFLGQVAAALAAG 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 647 SVVVFKPAEQARRCGAVIAQALWDAGVSKEALRLVdihPDEMAEVGEALVT--GSDQVILTGSIETAKLF-RSwepdLA- 722
Cdd:PRK11904 713 NTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLL---PGDGATVGAALTAdpRIAGVAFTGSTETARIInRT----LAa 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 723 -------VFAETSGKNAIIVTPQADIDLAAKDLVQSAFGHAGQKCSAA-------SIAilvgamgksERFINQVVDAAES 788
Cdd:PRK11904 786 rdgpivpLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALrvlfvqeDIA---------DRVIEMLKGAMAE 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 789 LVVDWPTNPSAEMGPIIEPAA-GKLKRGLTELEPGQTwLLKPRQLDDSGrlwspgiRDG--VTP------GQDAHMTEYF 859
Cdd:PRK11904 857 LKVGDPRLLSTDVGPVIDAEAkANLDAHIERMKREAR-LLAQLPLPAGT-------ENGhfVAPtafeidSISQLEREVF 928
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 860 GPVLGIMR--AETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEAGNVYVNRGTTGAIVRRQPFGGWKRSqvGTGS 937
Cdd:PRK11904 929 GPILHVIRykASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLS--GTGP 1006
|
....*....
gi 2515445683 938 KAGGPNHLI 946
Cdd:PRK11904 1007 KAGGPHYLL 1015
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
528-942 |
3.26e-75 |
|
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: 257.28 E-value: 3.26e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEE 607
Cdd:cd07131 35 TASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 608 L----------DELEGVRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEA 677
Cdd:cd07131 115 LfgetvpselpNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 678 LRLVDIHPDemaEVGEALV--TGSDQVILTGSIET--------AKLFRSwepdlaVFAETSGKNAIIVTPQADIDLAAKD 747
Cdd:cd07131 195 VNVVHGRGE---EVGEALVehPDVDVVSFTGSTEVgerigetcARPNKR------VALEMGGKNPIIVMDDADLDLALEG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 748 LVQSAFGHAGQKCSAASIAILVGAMgkSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAAgkLKRGLTELEPGQ---- 823
Cdd:cd07131 266 ALWSAFGTTGQRCTATSRLIVHESV--YDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQ--LEKVLNYNEIGKeega 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 824 TWLLKPRQLD----DSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKL 899
Cdd:cd07131 342 TLLLGGERLTgggyEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFR 421
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2515445683 900 WLSKVEAGNVYVNRGTTGAIVrRQPFGGWKRSqvGTGSKAGGP 942
Cdd:cd07131 422 ARRDLEAGITYVNAPTIGAEV-HLPFGGVKKS--GNGHREAGT 461
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
133-421 |
4.60e-74 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 247.79 E-value: 4.60e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 133 AVKKLRADGSRLNLNLLGEAVLGRKEAARRLAAVTELLEY----------DFVDYVSIKVSSVLGVHNPWGYQKAVDQAI 202
Cdd:pfam01619 4 TIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDAlgkaagpwplGPRPGISVKLSALHPRYEPLERERVMAELL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 203 EALLPLYRVANKGGKFVNLDMEEYHDLHLTIDVFTGILDREEFKNL-RAGIVLQAYLPDTLPAMERLQEWAAQRvadgGA 281
Cdd:pfam01619 84 ERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWnGVGITLQAYLKDALAVLDWLLELARRR----GR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 282 PVKVRLVKGANLPMEQVDALMHGWPLAVQPSKAATDANYMRILEYALrpEHISNVNLGIAGQNLFTLGFGLNLAKARGVT 361
Cdd:pfam01619 160 PLGVRLVKGAYWDSEIKRAQQGGWPYPVFTRKEATDANYEACARFLL--ENHDRIYPQFATHNARSVAAALALAEELGIP 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2515445683 362 EG-FEVEMLKGMATNQALAIREDVGRILYYVPVVDPAnyDVaISYLVRRLEESAAHENFMS 421
Cdd:pfam01619 238 PRrFEFQQLYGMGDNLSFALVAAGYRVRKYAPVGPHE--EL-LAYLVRRLLENTANSSFVR 295
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
537-940 |
2.15e-71 |
|
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: 242.91 E-value: 2.15e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 537 AEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEELDELEG--- 613
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELpsp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 614 -------VRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEALRLVDiHPD 686
Cdd:cd06534 81 dpggeayVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVP-GGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 687 EmaEVGEALVT--GSDQVILTGSIETAKLFRSwepDLA-----VFAETSGKNAIIVTPQADIDLAAKDLVQSAFGHAGQK 759
Cdd:cd06534 160 D--EVGAALLShpRVDKISFTGSTAVGKAIMK---AAAenlkpVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 760 CSAASiAILVgamgkSERFINQVVDAAESLVVDwptnpsaemgpiiepaagklkrgltelepgqtwllkprqlddsgrlw 839
Cdd:cd06534 235 CTAAS-RLLV-----HESIYDEFVEKLVTVLVD----------------------------------------------- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 840 spgirdgVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEAGNVYVNRGTTGAI 919
Cdd:cd06534 262 -------VDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVG 334
|
410 420
....*....|....*....|.
gi 2515445683 920 VrRQPFGGWKRSqvGTGSKAG 940
Cdd:cd06534 335 P-EAPFGGVKNS--GIGREGG 352
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
530-945 |
5.10e-71 |
|
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: 246.34 E-value: 5.10e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 530 AEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEELD 609
Cdd:cd07083 55 AEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 610 -----------ELEGVRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEAL 678
Cdd:cd07083 135 ypavevvpypgEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVV 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 679 RLVdihPDEMAEVGEALVtgSDQVI----LTGSIETAKLF----------RSWEPDLAvfAETSGKNAIIVTPQADIDLA 744
Cdd:cd07083 215 QFL---PGVGEEVGAYLT--EHERIrginFTGSLETGKKIyeaaarlapgQTWFKRLY--VETGGKNAIIVDETADFELV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 745 AKDLVQSAFGHAGQKCSAASIAILvgAMGKSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAA-GKLKRGLTELEPGQ 823
Cdd:cd07083 288 VEGVVVSAFGFQGQKCSAASRLIL--TQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQeAKVLSYIEHGKNEG 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 824 TWLLKPRQLDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMR--AETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWL 901
Cdd:cd07083 366 QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRykDDDFAEALEVANSTPYGLTGGVYSRKREHLEEAR 445
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2515445683 902 SKVEAGNVYVNRGTTGAIVRRQPFGGWKRSqvGTGSKAGGPNHL 945
Cdd:cd07083 446 REFHVGNLYINRKITGALVGVQPFGGFKLS--GTNAKTGGPHYL 487
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
528-934 |
8.68e-71 |
|
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: 244.85 E-value: 8.68e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLA-- 605
Cdd:cd07097 35 SAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARGEVTRAGQIFRYYAGEAlr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 606 ---EELD------ELEGVRfSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKE 676
Cdd:cd07097 115 lsgETLPstrpgvEVETTR-EPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 677 ALRLVdihpdeM---AEVGEALVT--GSDQVILTGSIETAK-LFRSWEPDLA-VFAETSGKNAIIVTPQADIDLAAKDLV 749
Cdd:cd07097 194 VFNLV------MgsgSEVGQALVEhpDVDAVSFTGSTAVGRrIAAAAAARGArVQLEMGGKNPLVVLDDADLDLAVECAV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 750 QSAFGHAGQKCSAASIAILVGAMgkSERFINQVVDAAESLVVDWPTNPSAEMGPIIEpaAGKLKRGLTELEPGQT----- 824
Cdd:cd07097 268 QGAFFSTGQRCTASSRLIVTEGI--HDRFVEALVERTKALKVGDALDEGVDIGPVVS--ERQLEKDLRYIEIARSegakl 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 825 -WLLKPRQLDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSK 903
Cdd:cd07097 344 vYGGERLKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRR 423
|
410 420 430
....*....|....*....|....*....|..
gi 2515445683 904 VEAGNVYVNRGTTGaiVRRQ-PFGGWKRSQVG 934
Cdd:cd07097 424 VEAGVVMVNLPTAG--VDYHvPFGGRKGSSYG 453
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
531-931 |
2.81e-69 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 239.10 E-value: 2.81e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 531 EMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAI--------DFANYYA 602
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAgkidisikAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 603 DLAEELDELEGV-RFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEALRLV 681
Cdd:cd07095 81 ERATPMAQGRAVlRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 682 DihpdEMAEVGEALVT--GSDQVILTGSIETAKLFR---SWEPDLAVFAETSGKNAIIVTPQADIDLAAKDLVQSAFGHA 756
Cdd:cd07095 161 Q----GGRETGEALAAheGIDGLLFTGSAATGLLLHrqfAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 757 GQKCSAASIAILV-GAMGksERFINQVVDAAESLVVDWPTNPSAEMGPII--EPAAGKLKRGLTELEPGQTWLLKPRQLD 833
Cdd:cd07095 237 GQRCTCARRLIVPdGAVG--DAFLERLVEAAKRLRIGAPDAEPPFMGPLIiaAAAARYLLAQQDLLALGGEPLLAMERLV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 834 DSGRLWSPGIRDgVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEAGNVYVNR 913
Cdd:cd07095 315 AGTAFLSPGIID-VTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNR 393
|
410
....*....|....*...
gi 2515445683 914 GTTGAIVRRqPFGGWKRS 931
Cdd:cd07095 394 PTTGASSTA-PFGGVGLS 410
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
528-975 |
6.24e-68 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 249.85 E-value: 6.24e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEE 607
Cdd:COG4230 591 TAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARR 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 608 LDElEGVRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEALRLVdihPDE 687
Cdd:COG4230 671 LFA-APTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLL---PGD 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 688 MAEVGEALVtgSDQ----VILTGSIETAK-----LFRSWEPDLAVFAETSGKNAIIVTPQADIDLAAKDLVQSAFGHAGQ 758
Cdd:COG4230 747 GETVGAALV--ADPriagVAFTGSTETARlinrtLAARDGPIVPLIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQ 824
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 759 KCSA------------ASIAILVGAMgkserfinqvvdaAEsLVVDWPTNPSAEMGPIIEPAAgklKRGLTE-LEpgqtw 825
Cdd:COG4230 825 RCSAlrvlcvqediadRVLEMLKGAM-------------AE-LRVGDPADLSTDVGPVIDAEA---RANLEAhIE----- 882
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 826 llkprQLDDSGRLwspgIRDGVTPGQDAHMT-----------------EYFGPVLGIMR--AETLEEAIRLQNAVEFGLT 886
Cdd:COG4230 883 -----RMRAEGRL----VHQLPLPEECANGTfvaptlieidsisdlerEVFGPVLHVVRykADELDKVIDAINATGYGLT 953
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 887 AGLHSLDPDEIKLWLSKVEAGNVYVNRGTTGAIVRRQPFGGWKRSqvGTGSKAGGPNHLIGMSHAEPVEVAVPESFATLS 966
Cdd:COG4230 954 LGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLS--GTGPKAGGPHYLLRFATERTVTVNTTAAGGNAS 1031
|
....*....
gi 2515445683 967 YPTLGEFDA 975
Cdd:COG4230 1032 LLALGDWLA 1040
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
524-940 |
3.34e-67 |
|
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: 234.77 E-value: 3.34e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 524 ARVR--TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYY 601
Cdd:cd07086 27 ARVFpaSPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLGEVQEMIDICDYA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 602 ADLAEELD------ELEGVR----FSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQ----ARRCGAVIAQA 667
Cdd:cd07086 107 VGLSRMLYgltipsERPGHRlmeqWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETtpltAIAVTKILAEV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 668 LWDAGVSKEALRLVdiHPDemAEVGEALV--TGSDQVILTGSIET--------AKLFRSwepdlaVFAETSGKNAIIVTP 737
Cdd:cd07086 187 LEKNGLPPGVVNLV--TGG--GDGGELLVhdPRVPLVSFTGSTEVgrrvgetvARRFGR------VLLELGGNNAIIVMD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 738 QADIDLAAKDLVQSAFGHAGQKCSAASIAILVGAMgkSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAA-GKLKRGL 816
Cdd:cd07086 257 DADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESV--YDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAvEKYLNAI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 817 TEL-EPGQTWLLKPRQLD--DSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLD 893
Cdd:cd07086 335 EIAkSQGGTVLTGGKRIDggEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTED 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2515445683 894 PDEIKLWLSK--VEAGNVYVNRGTTGAIVrRQPFGGWKRSqvGTGSKAG 940
Cdd:cd07086 415 LREAFRWLGPkgSDCGIVNVNIPTSGAEI-GGAFGGEKET--GGGRESG 460
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
525-952 |
4.97e-67 |
|
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: 233.27 E-value: 4.97e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 525 RVRTVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADL 604
Cdd:cd07099 13 PVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLALEAIDWAARN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 605 AEELDELEGVRFS-------------PAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDA 671
Cdd:cd07099 93 APRVLAPRKVPTGllmpnkkatveyrPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 672 GVSKEALRLVdihpDEMAEVGEALV-TGSDQVILTGSIETAK--LFRSWEPDLAVFAETSGKNAIIVTPQADIDLAAKDL 748
Cdd:cd07099 173 GPPQGVLQVV----TGDGATGAALIdAGVDKVAFTGSVATGRkvMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 749 VQSAFGHAGQKCSA-------ASIAilvgamgksERFINQVVDAAESLVVDWPTNPSAEMGPIIEPA-AGKLKRGLTE-L 819
Cdd:cd07099 249 VWGAMVNAGQTCISvervyvhESVY---------DEFVARLVAKARALRPGADDIGDADIGPMTTARqLDIVRRHVDDaV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 820 EPGQTWLLKPRQLDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKL 899
Cdd:cd07099 320 AKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2515445683 900 WLSKVEAGNVYVNRGTTGAIVRRQPFGGWKRSqvGTGSKaGGPNHLIGMSHAE 952
Cdd:cd07099 400 IARRLEAGAVSINDVLLTAGIPALPFGGVKDS--GGGRR-HGAEGLREFCRPK 449
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
532-934 |
5.02e-62 |
|
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: 218.10 E-value: 5.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 532 MEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYAD-----LAE 606
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAEnaeafLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 607 ELDELEG----VRFSPAPVTAAIPPWNFPL------AIPAgsalapLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKE 676
Cdd:cd07100 81 EPIETDAgkayVRYEPLGVVLGIMPWNFPFwqvfrfAAPN------LMAGNTVLLKHASNVPGCALAIEELFREAGFPEG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 677 ALRLVDIHPDEMAEV-GEALVTGsdqVILTGSietaklfrswEPDLAVFAETSGKN------------AIIVTPQADIDL 743
Cdd:cd07100 155 VFQNLLIDSDQVEAIiADPRVRG---VTLTGS----------ERAGRAVAAEAGKNlkksvlelggsdPFIVLDDADLDK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 744 AAKDLVQSAFGHAGQKCSAASIAILVGAMgkSERFINQVVDAAESLVVDWPTNPSAEMGPIiepAAGKLKRGLTE----- 818
Cdd:cd07100 222 AVKTAVKGRLQNAGQSCIAAKRFIVHEDV--YDEFLEKFVEAMAALKVGDPMDEDTDLGPL---ARKDLRDELHEqveea 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 819 LEPGQTWLLKPRQLDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIK 898
Cdd:cd07100 297 VAAGATLLLGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAE 376
|
410 420 430
....*....|....*....|....*....|....*..
gi 2515445683 899 LWLSKVEAGNVYVNR-GTTGAivrRQPFGGWKRSQVG 934
Cdd:cd07100 377 RVARRLEAGMVFINGmVKSDP---RLPFGGVKRSGYG 410
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
528-931 |
3.03e-61 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 217.90 E-value: 3.03e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSE-----AIDFANYYA 602
Cdd:PRK09457 35 TAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEVTAminkiAISIQAYHE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 603 DLAEELDELEG----VRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEAL 678
Cdd:PRK09457 115 RTGEKRSEMADgaavLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 679 RLVDIHPDEmaevGEALVT--GSDQVILTGSIETAKLFR---SWEPDLAVFAETSGKNAIIVTPQADIDLAAKDLVQSAF 753
Cdd:PRK09457 195 NLVQGGRET----GKALAAhpDIDGLLFTGSANTGYLLHrqfAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAF 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 754 GHAGQKCSAAS-IAILVGAMGksERFINQVVDAAESLVVD-WPTNPSAEMGPIIEPAAGKlkrGLTE-----LEPGQTWL 826
Cdd:PRK09457 271 ISAGQRCTCARrLLVPQGAQG--DAFLARLVAVAKRLTVGrWDAEPQPFMGAVISEQAAQ---GLVAaqaqlLALGGKSL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 827 LKPRQLDDSGRLWSPGIRDgVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEA 906
Cdd:PRK09457 346 LEMTQLQAGTGLLTPGIID-VTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRA 424
|
410 420
....*....|....*....|....*
gi 2515445683 907 GNVYVNRGTTGAiVRRQPFGGWKRS 931
Cdd:PRK09457 425 GIVNWNKPLTGA-SSAAPFGGVGAS 448
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
528-934 |
1.13e-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: 215.59 E-value: 1.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEE 607
Cdd:cd07088 33 TAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARVEVEFTADYIDYMAEWARR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 608 L----------DELEGVRFSPAPVTAAIPPWNFPLAIpAGSALAP-LATGSVVVFKPAEQARRCGAVIAQALWDAGVSKE 676
Cdd:cd07088 113 IegeiipsdrpNENIFIFKVPIGVVAGILPWNFPFFL-IARKLAPaLVTGNTIVIKPSEETPLNALEFAELVDEAGLPAG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 677 ALRLVdihPDEMAEVGEALVT--GSDQVILTGSIET-AKLFRSWEPDLA-VFAETSGKNAIIVTPQADIDLAAKDLVQSA 752
Cdd:cd07088 192 VLNIV---TGRGSVVGDALVAhpKVGMISLTGSTEAgQKIMEAAAENITkVSLELGGKAPAIVMKDADLDLAVKAIVDSR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 753 FGHAGQKCSAA-------SIAilvgamgksERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAAGKLKRGLTE--LEPGQ 823
Cdd:cd07088 269 IINCGQVCTCAervyvheDIY---------DEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMVEraVEAGA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 824 TWLLKPRQLD-DSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLS 902
Cdd:cd07088 340 TLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATN 419
|
410 420 430
....*....|....*....|....*....|...
gi 2515445683 903 KVEAGNVYVNRGTTGAIvrrQPF-GGWKRSQVG 934
Cdd:cd07088 420 ELEFGETYINRENFEAM---QGFhAGWKKSGLG 449
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
528-940 |
2.03e-60 |
|
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: 214.22 E-value: 2.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEE 607
Cdd:cd07103 17 GAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVDYAASFLEWFAEEARR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 608 LD------ELEGVRFS----PAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEA 677
Cdd:cd07103 97 IYgrtipsPAPGKRILvikqPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAEEAGLPAGV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 678 LRLVdihPDEMAEVGEALVTgSDQV---ILTGSIETAKLFrswepdLAVFAETS-------GKNA-IIVTPQADIDLAAK 746
Cdd:cd07103 177 LNVV---TGSPAEIGEALCA-SPRVrkiSFTGSTAVGKLL------MAQAADTVkrvslelGGNApFIVFDDADLDKAVD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 747 DLVQSAFGHAGQKCSAASiAILVGAmGKSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAAGKLKRGLTE--LEPGQT 824
Cdd:cd07103 247 GAIASKFRNAGQTCVCAN-RIYVHE-SIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEdaVAKGAK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 825 WLLKPRQLDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKV 904
Cdd:cd07103 325 VLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEAL 404
|
410 420 430
....*....|....*....|....*....|....*..
gi 2515445683 905 EAGNVYVNRGTTGAIVrrQPFGGWKRSQVGT-GSKAG 940
Cdd:cd07103 405 EAGMVGINTGLISDAE--APFGGVKESGLGReGGKEG 439
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
530-953 |
6.90e-60 |
|
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: 214.39 E-value: 6.90e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 530 AEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEelD 609
Cdd:TIGR01238 74 AHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVR--D 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 610 ELEGVRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEALRLVdihPDEMA 689
Cdd:TIGR01238 152 VLGEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLL---PGRGA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 690 EVGEALVtgSDQ----VILTGSIETAKLF-----RSWEPDLAVFAETSGKNAIIVTPQADIDLAAKDLVQSAFGHAGQKC 760
Cdd:TIGR01238 229 DVGAALT--SDPriagVAFTGSTEVAQLInqtlaQREDAPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRC 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 761 SAasIAILVGAMGKSERFINQVVDAAESLVVDWPTNPSAEMGPII-EPAAGKLKRGLTELEPGQTWLLKPRQLDDsgRLW 839
Cdd:TIGR01238 307 SA--LRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIdAEAKQNLLAHIEHMSQTQKKIAQLTLDDS--RAC 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 840 SPGirDGVTP------GQDAHMTEYFGPVLGIMR--AETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEAGNVYV 911
Cdd:TIGR01238 383 QHG--TFVAPtlfeldDIAELSEEVFGPVLHVVRykARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYV 460
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2515445683 912 NRGTTGAIVRRQPFGGWKRSqvGTGSKAGGPNHLIGMSHAEP 953
Cdd:TIGR01238 461 NRNQVGAVVGVQPFGGQGLS--GTGPKAGGPHYLYRLTQVQY 500
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
524-936 |
1.37e-59 |
|
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: 212.76 E-value: 1.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 524 ARVR--TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVS---EAIDFA 598
Cdd:cd07085 30 ARVPlaTAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADARGDVLrglEVVEFA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 599 ---------NYYADLAEELDELegVRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALW 669
Cdd:cd07085 110 csiphllkgEYLENVARGIDTY--SYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 670 DAGVSKEALRLVdiHPDemAEVGEALVT----------GSDQV---ILTGSIETAKlfRswepdlaVFAETSGKNAIIVT 736
Cdd:cd07085 188 EAGLPDGVLNVV--HGG--KEAVNALLDhpdikavsfvGSTPVgeyIYERAAANGK--R-------VQALGGAKNHAVVM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 737 PQADIDLAAKDLVQSAFGHAGQKCSAASIAILVGamGKSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAAGKLKRGL 816
Cdd:cd07085 255 PDADLEQTANALVGAAFGAAGQRCMALSVAVAVG--DEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 817 TE--LEPGQTWLLKPRQLD----DSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLH 890
Cdd:cd07085 333 IEsgVEEGAKLVLDGRGVKvpgyENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIF 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2515445683 891 SLDPDEIKLWLSKVEAGNVYVNRGTTgAIVRRQPFGGWKRSQVGTG 936
Cdd:cd07085 413 TRSGAAARKFQREVDAGMVGINVPIP-VPLAFFSFGGWKGSFFGDL 457
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
135-1108 |
3.71e-57 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 216.76 E-value: 3.71e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 135 KKLRADGSRLNLNLLGEAVLGRKEAARRLAAvtelleydfvdY---------------------VSIKVSSVLGVHNPWG 193
Cdd:PRK11809 273 RKLEEKGFRYSYDMLGEAALTEADAQAYLAS-----------YeqaihaigkasngrgiyegpgISIKLSALHPRYSRAQ 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 194 YQKAVDQAIEALLPLYRVANKGGKFVNLDMEEYHDLHLTIDvftgILDREEFKNLRAG-----IVLQAYL---PDTLPAM 265
Cdd:PRK11809 342 YDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLD----LLEKLCFEPELAGwngigFVIQAYQkrcPFVIDYL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 266 ERLqewaAQRvadGGAPVKVRLVKGANLPME----QVDALmHGWPlaVQPSKAATDANYM---RILEYAlrPEHISNvnl 338
Cdd:PRK11809 418 IDL----ARR---SRRRLMIRLVKGAYWDSEikraQVDGL-EGYP--VYTRKVYTDVSYLacaRKLLAV--PNLIYP--- 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 339 GIAGQNLFTLGFGLNLAKARGVTEGFEVEMLKGMatnqalairedvGRILY------------------YVPVvdpANYD 400
Cdd:PRK11809 483 QFATHNAHTLAAIYHLAGQNYYPGQYEFQCLHGM------------GEPLYeqvvgkvadgklnrpcriYAPV---GTHE 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 401 VAISYLVRRLEESAAHENFmsgVFEIADN---------DSVFARERNRFATGVVAAfPEADLaeamgPLnevPTLSFGPN 471
Cdd:PRK11809 548 TLLAYLVRRLLENGANTSF---VNRIADTslpldelvaDPVEAVEKLAQQEGQLGL-PHPKI-----PL---PRDLYGKG 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 472 R---------HQNRLTD-DVDLLTSFRNTPDSDPSLPANIEWanqifakmgDSELGVQGADDAR-----VR--TVAEMEQ 534
Cdd:PRK11809 616 RansagldlaNEHRLASlSSALLASAHQKWQAAPMLEDPVAA---------GEMSPVINPADPRdivgyVReaTPAEVEQ 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 535 IVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEelDELEGV 614
Cdd:PRK11809 687 ALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVR--DDFDND 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 615 RFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEALRLVdihPDEMAEVGEA 694
Cdd:PRK11809 765 THRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLL---PGRGETVGAA 841
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 695 LVtGSDQ---VILTGSIETAKLFRSwepDLA-----------VFAETSGKNAIIVTPQADIDLAAKDLVQSAFGHAGQKC 760
Cdd:PRK11809 842 LV-ADARvrgVMFTGSTEVARLLQR---NLAgrldpqgrpipLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRC 917
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 761 SAasIAILVGAMGKSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAAgklKRGL----------------TELEPGQT 824
Cdd:PRK11809 918 SA--LRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEA---KANIerhiqamrakgrpvfqAARENSED 992
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 825 WLL----KPR--QLDDSGRLwspgirdgvtpgqdahMTEYFGPVLGIMR--AETLEEAIRLQNAVEFGLTAGLHSLDPDE 896
Cdd:PRK11809 993 WQSgtfvPPTliELDSFDEL----------------KREVFGPVLHVVRynRNQLDELIEQINASGYGLTLGVHTRIDET 1056
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 897 IKLWLSKVEAGNVYVNRGTTGAIVRRQPFGGWKRSqvGTGSKAGGPNHLIGMSHAEPvEVAVPESFATLSYPTLGEFDAL 976
Cdd:PRK11809 1057 IAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLS--GTGPKAGGPLYLYRLLATRP-EDALAVTLARQDAEYPVDAQLR 1133
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 977 ADKLPKDDAGQYRAALRSVE-AALKEHYLSArdvSALGV---------EKNVFRYRPTsvmvrledpEQWWKVAPMVAGA 1046
Cdd:PRK11809 1134 AALLAPLTALREWAAEREPElAALCDQYAEL---AQAGTtrllpgptgERNTYTLLPR---------ERVLCLADTEQDA 1201
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2515445683 1047 LTGKTSVeLSVGddlrdtvAQAFRAAGATVsvaspAQWLSDLPKSGAHKIRYVGDDARAVAE 1108
Cdd:PRK11809 1202 LTQLAAV-LAVG-------SQALWPDDALH-----RALVAALPAAVQARIQLAKDWQLADQP 1250
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
531-942 |
2.72e-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: 201.61 E-value: 2.72e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 531 EMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEELD- 609
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 610 -----ELEG----VRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAV-IAQALWDAGVSKEALR 679
Cdd:cd07104 81 eilpsDVPGkesmVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLlIAEIFEEAGLPKGVLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 680 LVdihPDEMAEVGEALV----------TGSDQV---IltGSIETAKLFRswepdlaVFAETSGKNAIIVTPQADIDLAAK 746
Cdd:cd07104 161 VV---PGGGSEIGDALVehprvrmisfTGSTAVgrhI--GELAGRHLKK-------VALELGGNNPLIVLDDADLDLAVS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 747 DLVQSAFGHAGQKCSAASiAILVGAmGKSERFINQVVDAAESLVVDWPTNPSAEMGPIIEP-AAGKLKRGLTE------- 818
Cdd:cd07104 229 AAAFGAFLHQGQICMAAG-RILVHE-SVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINErQVDRVHAIVEDavaagar 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 819 LEPGQTWllkprqlddSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIK 898
Cdd:cd07104 307 LLTGGTY---------EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAM 377
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2515445683 899 LWLSKVEAGNVYVNRGTT--GAIVrrqPFGGWKRSQVGtgsKAGGP 942
Cdd:cd07104 378 AFAERLETGMVHINDQTVndEPHV---PFGGVKASGGG---RFGGP 417
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
528-935 |
1.24e-55 |
|
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: 200.68 E-value: 1.24e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEE 607
Cdd:cd07107 17 SAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMVAAALLDYFAGLVTE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 608 LD------ELEGVRFS---PAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQAR----RCGAVIAQALwDAGVs 674
Cdd:cd07107 97 LKgetipvGGRNLHYTlrePYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPlsalRLAELAREVL-PPGV- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 675 kealrlVDIHPDEMAEVGEALVTGSD--QVILTGSIETA-KLFRSWEPDLA-VFAETSGKNAIIVTPQADIDLAAKDLVQ 750
Cdd:cd07107 175 ------FNILPGDGATAGAALVRHPDvkRIALIGSVPTGrAIMRAAAEGIKhVTLELGGKNALIVFPDADPEAAADAAVA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 751 SA-FGHAGQKCSAASIAILVGAMgkSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAAgkLKRGLTELEPGQT---WL 826
Cdd:cd07107 249 GMnFTWCGQSCGSTSRLFVHESI--YDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQ--YDRVMHYIDSAKRegaRL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 827 L----KPRQLDDSGRLW-SPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWL 901
Cdd:cd07107 325 VtgggRPEGPALEGGFYvEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTA 404
|
410 420 430
....*....|....*....|....*....|....*..
gi 2515445683 902 SKVEAGNVYVNRGTT---GAivrrqPFGGWKRSQVGT 935
Cdd:cd07107 405 RRVEAGYVWINGSSRhflGA-----PFGGVKNSGIGR 436
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
528-934 |
1.30e-55 |
|
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: 200.45 E-value: 1.30e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLA-- 605
Cdd:cd07106 17 SEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGAVAWLRYTASLDlp 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 606 -EELDELEG----VRFSPAPVTAAIPPWNFPLAIpAGSALAP-LATGSVVVFKPAE----QARRCGAVIAQALwDAGVsk 675
Cdd:cd07106 97 dEVIEDDDTrrveLRRKPLGVVAAIVPWNFPLLL-AAWKIAPaLLAGNTVVLKPSPftplCTLKLGELAQEVL-PPGV-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 676 ealrlVDIHPDEmAEVGEALVT--GSDQVILTGSIETAKL-FRSWEPDLA-VFAETSGKNAIIVTPQADIDLAAKDLVQS 751
Cdd:cd07106 173 -----LNVVSGG-DELGPALTShpDIRKISFTGSTATGKKvMASAAKTLKrVTLELGGNDAAIVLPDVDIDAVAPKLFWG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 752 AFGHAGQKCSAA-------SIailvgamgkSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAA-GKLKRGLTE-LEPG 822
Cdd:cd07106 247 AFINSGQVCAAIkrlyvheSI---------YDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQyDKVKELVEDaKAKG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 823 QTWLLKPRQLDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLS 902
Cdd:cd07106 318 AKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVAR 397
|
410 420 430
....*....|....*....|....*....|..
gi 2515445683 903 KVEAGNVYVNrgTTGAIVRRQPFGGWKRSQVG 934
Cdd:cd07106 398 RLEAGTVWIN--THGALDPDAPFGGHKQSGIG 427
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
533-940 |
5.52e-55 |
|
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: 198.18 E-value: 5.52e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 533 EQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEELDE-- 610
Cdd:cd07105 3 DQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGgs 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 611 --------LEGVRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEALRLVD 682
Cdd:cd07105 83 ipsdkpgtLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 683 IHPDEMAEVGEALV----------TGSDQViltGSIETAKLFRSWEPdlaVFAETSGKNAIIVTPQADIDLAAKDLVQSA 752
Cdd:cd07105 163 HSPEDAPEVVEALIahpavrkvnfTGSTRV---GRIIAETAAKHLKP---VLLELGGKAPAIVLEDADLDAAANAALFGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 753 FGHAGQKCSA-------ASIAilvgamgksERFINQVVDAAESLVVDwptnpSAEMGPIIEPAAGKLKRGLTE--LEPGQ 823
Cdd:cd07105 237 FLNSGQICMSteriivhESIA---------DEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDdaLSKGA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 824 TWLL-KPRQLDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSldPDEIK-LWL 901
Cdd:cd07105 303 KLVVgGLADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFT--RDLARaLAV 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2515445683 902 SK-VEAGNVYVNRGTtgaiVRRQ---PFGGWKRSQVGT-GSKAG 940
Cdd:cd07105 381 AKrIESGAVHINGMT----VHDEptlPHGGVKSSGYGRfNGKWG 420
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
530-934 |
1.88e-54 |
|
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: 197.28 E-value: 1.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 530 AEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEA-DVEVSEAIDFANYYADLAEEL 608
Cdd:cd07115 19 EDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRLDVPRAADTFRYYAGWADKI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 609 ---------DELEGVRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEALR 679
Cdd:cd07115 99 egevipvrgPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAGFPAGVLN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 680 LVdihPDEMAEVGEALVT--GSDQVILTGSIETA-KLFRSWEPDLA-VFAETSGKNAIIVTPQADIDLAAKDLVQSAFGH 755
Cdd:cd07115 179 VV---TGFGEVAGAALVEhpDVDKITFTGSTAVGrKIMQGAAGNLKrVSLELGGKSANIVFADADLDAAVRAAATGIFYN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 756 AGQKCSAASIAILVGAMgkSERFINQVVDAAESLVVDWPTNPSAEMGPIIepAAGKLKRGLTELEPGQ----TWLLKPRQ 831
Cdd:cd07115 256 QGQMCTAGSRLLVHESI--YDEFLERFTSLARSLRPGDPLDPKTQMGPLV--SQAQFDRVLDYVDVGReegaRLLTGGKR 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 832 LDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEAGNVYV 911
Cdd:cd07115 332 PGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWI 411
|
410 420
....*....|....*....|...
gi 2515445683 912 NrgTTGAIVRRQPFGGWKRSQVG 934
Cdd:cd07115 412 N--TYNRFDPGSPFGGYKQSGFG 432
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
528-934 |
2.08e-54 |
|
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: 197.19 E-value: 2.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEE 607
Cdd:cd07110 17 TAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDDVAGCFEYYADLAEQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 608 LD-------ELEGVRFS------PAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVS 674
Cdd:cd07110 97 LDakaeravPLPSEDFKarvrrePVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIAAEAGLP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 675 KEALRLVDIHPDemaEVGEALVT--GSDQVILTGSIETA-KLFRSWEPDL-AVFAETSGKNAIIVTPQADIDLAAKDLVQ 750
Cdd:cd07110 177 PGVLNVVTGTGD---EAGAPLAAhpGIDKISFTGSTATGsQVMQAAAQDIkPVSLELGGKSPIIVFDDADLEKAVEWAMF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 751 SAFGHAGQKCSAASiAILVgAMGKSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPA-----AGKLKRGLTElepGQTW 825
Cdd:cd07110 254 GCFWNNGQICSATS-RLLV-HESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAqyekvLSFIARGKEE---GARL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 826 LLKPRQLDDSGRLW--SPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSK 903
Cdd:cd07110 329 LCGGRRPAHLEKGYfiAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEA 408
|
410 420 430
....*....|....*....|....*....|.
gi 2515445683 904 VEAGNVYVNrgTTGAIVRRQPFGGWKRSQVG 934
Cdd:cd07110 409 LEAGIVWIN--CSQPCFPQAPWGGYKRSGIG 437
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
531-935 |
3.47e-54 |
|
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: 197.02 E-value: 3.47e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 531 EMEQIVAEARKAAPEWAG-LSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDfanYYADLAEELD 609
Cdd:cd07082 39 EILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALKEVDRTID---YIRDTIEELK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 610 ELEG-----------------VRFSPAPVTAAIPPWNFPLAIPAgSALAP-LATGSVVVFKPAEQARRCGAVIAQALWDA 671
Cdd:cd07082 116 RLDGdslpgdwfpgtkgkiaqVRREPLGVVLAIGPFNYPLNLTV-SKLIPaLIMGNTVVFKPATQGVLLGIPLAEAFHDA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 672 GVSKEALRLVDIhpdEMAEVGEALVT-GSDQVI-LTGSIETAKLFRSWEPDLAVFAETSGKNAIIVTPQADIDLAAKDLV 749
Cdd:cd07082 195 GFPKGVVNVVTG---RGREIGDPLVThGRIDVIsFTGSTEVGNRLKKQHPMKRLVLELGGKDPAIVLPDADLELAAKEIV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 750 QSAFGHAGQKCSAasIAILVGAMGKSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAAGKLKRGLTE--LEPGQTWLL 827
Cdd:cd07082 272 KGALSYSGQRCTA--IKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDdaVAKGATVLN 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 828 KPRQLDDSgrLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEAG 907
Cdd:cd07082 350 GGGREGGN--LIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVG 427
|
410 420 430
....*....|....*....|....*....|..
gi 2515445683 908 NVYVNRGTtgaivRRQ----PFGGWKRSQVGT 935
Cdd:cd07082 428 TVNINSKC-----QRGpdhfPFLGRKDSGIGT 454
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
530-934 |
5.27e-54 |
|
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: 195.73 E-value: 5.27e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 530 AEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEEL- 608
Cdd:cd07094 21 ADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRAIDTLRLAAEEAERIr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 609 -------------DELEGVRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSK 675
Cdd:cd07094 101 geeipldatqgsdNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILVEAGVPE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 676 EALRLVdihPDEMAEVGEALVTGSD--QVILTGSIETAKLFRSWEPDLAVFAETSGKNAIIVTPQADIDLAAKDLVQSAF 753
Cdd:cd07094 181 GVLQVV---TGEREVLGDAFAADERvaMLSFTGSAAVGEALRANAGGKRIALELGGNAPVIVDRDADLDAAIEALAKGGF 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 754 GHAGQKCSAASIAILVGAMgkSERFINQVVDAAESLVVDWPTNPSAEMGPIIEP-AAGKLKRGLTE-LEPGQTWLLKPRQ 831
Cdd:cd07094 258 YHAGQVCISVQRIYVHEEL--YDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEeAAERVERWVEEaVEAGARLLCGGER 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 832 lddSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEAGNVYV 911
Cdd:cd07094 336 ---DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMV 412
|
410 420
....*....|....*....|....*
gi 2515445683 912 NRGTtgaIVRR--QPFGGWKRSQVG 934
Cdd:cd07094 413 NDSS---AFRTdwMPFGGVKESGVG 434
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
528-934 |
5.84e-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: 195.53 E-value: 5.84e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAG-LSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAe 606
Cdd:cd07109 17 GAADVDRAVQAARRAFESGWLrLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEAAARYFEYYGGAA- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 607 elDELEG------------VRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVS 674
Cdd:cd07109 96 --DKLHGetiplgpgyfvyTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAGLP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 675 KEALRLVdihPDEMAEVGEALVT--GSDQVILTGSIETAKLFR--SWEPDLAVFAETSGKNAIIVTPQADIDLAAKDLVQ 750
Cdd:cd07109 174 AGALNVV---TGLGAEAGAALVAhpGVDHISFTGSVETGIAVMraAAENVVPVTLELGGKSPQIVFADADLEAALPVVVN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 751 SAFGHAGQKCSAASiAILVgamGKS--ERFINQVVDAAESLVVDwPTNPSAEMGPIIEPAAGKLKRGLTEL--EPGQTWL 826
Cdd:cd07109 251 AIIQNAGQTCSAGS-RLLV---HRSiyDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRVEGFVARarARGARIV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 827 LKPRQLDD---SGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSK 903
Cdd:cd07109 326 AGGRIAEGapaGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARR 405
|
410 420 430
....*....|....*....|....*....|.
gi 2515445683 904 VEAGNVYVNRGTTGAIVRRqPFGGWKRSQVG 934
Cdd:cd07109 406 LRAGQVFVNNYGAGGGIEL-PFGGVKKSGHG 435
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
526-943 |
5.94e-53 |
|
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: 192.51 E-value: 5.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 526 VRTVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLA 605
Cdd:cd07152 9 VADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEAAGLP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 606 EE-----LDELEG----VRFSPAPVTAAIPPWNFPLaIPAGSALAP-LATGSVVVFKPAEQARRC-GAVIAQALWDAGVS 674
Cdd:cd07152 89 TQpqgeiLPSAPGrlslARRVPLGVVGVISPFNFPL-ILAMRSVAPaLALGNAVVLKPDPRTPVSgGVVIARLFEEAGLP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 675 KEALRLVdihPDEmAEVGEALVTGS--DQVILTGSIETAKLFRSWEPDL--AVFAETSGKNAIIVTPQADIDLAAKDLVQ 750
Cdd:cd07152 168 AGVLHVL---PGG-ADAGEALVEDPnvAMISFTGSTAVGRKVGEAAGRHlkKVSLELGGKNALIVLDDADLDLAASNGAW 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 751 SAFGHAGQKCSAASiAILVGAmGKSERFINQVVDAAESLVVDWPTNPSAEMGPIIEpaAGKLKRGL----------TELE 820
Cdd:cd07152 244 GAFLHQGQICMAAG-RHLVHE-SVADAYTAKLAAKAKHLPVGDPATGQVALGPLIN--ARQLDRVHaivddsvaagARLE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 821 PGQTWllkprqlddSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLW 900
Cdd:cd07152 320 AGGTY---------DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMAL 390
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2515445683 901 LSKVEAGNVYVNRGTTGAIVrRQPFGGWKRSqvGTGSKAGGPN 943
Cdd:cd07152 391 ADRLRTGMLHINDQTVNDEP-HNPFGGMGAS--GNGSRFGGPA 430
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
524-934 |
1.64e-52 |
|
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: 191.95 E-value: 1.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 524 ARVR--TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEA-DVEVSEAIDFANY 600
Cdd:cd07138 28 GTVPlgTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPITLArAAQVGLGIGHLRA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 601 YADLAEELD--ELEG---VRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSK 675
Cdd:cd07138 108 AADALKDFEfeERRGnslVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 676 EALRLVDIHPdemAEVGEALVT--GSDQVILTGSIETAKLF-RSWEPDLAVFA-ETSGKNAIIVTPQADIDLAAKDLVQS 751
Cdd:cd07138 188 GVFNLVNGDG---PVVGEALSAhpDVDMVSFTGSTRAGKRVaEAAADTVKRVAlELGGKSANIILDDADLEKAVPRGVAA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 752 AFGHAGQKCSAASiAILVGAmGKSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPA-----AGKLKRGLTElepGQTwL 826
Cdd:cd07138 265 CFANSGQSCNAPT-RMLVPR-SRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAqfdrvQGYIQKGIEE---GAR-L 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 827 L-----KPRQLdDSGRLWSPGIRDGVTPgqdaHMT----EYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEI 897
Cdd:cd07138 339 VaggpgRPEGL-ERGYFVKPTVFADVTP----DMTiareEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERA 413
|
410 420 430
....*....|....*....|....*....|....*..
gi 2515445683 898 KLWLSKVEAGNVYVNRGTTGAivrRQPFGGWKRSQVG 934
Cdd:cd07138 414 RAVARRLRAGQVHINGAAFNP---GAPFGGYKQSGNG 447
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
528-934 |
3.20e-52 |
|
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: 190.63 E-value: 3.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKA--APEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLA 605
Cdd:cd07118 17 TVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASLA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 606 EEL----------DELEGVRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSK 675
Cdd:cd07118 97 RTLhgdsynnlgdDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 676 EAlrlVDIHPDEMAEVGEALVT--GSDQVILTGSIETAK-LFRSWEPDLA-VFAETSGKNAIIVTPQADIDLAAKDLVQS 751
Cdd:cd07118 177 GV---VNIVTGYGATVGQAMTEhpDVDMVSFTGSTRVGKaIAAAAARNLKkVSLELGGKNPQIVFADADLDAAADAVVFG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 752 AFGHAGQKCSAASIAILVGAMgkSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPA-AGKLKRGLTE-LEPGQTWLLKP 829
Cdd:cd07118 254 VYFNAGECCNSGSRLLVHESI--ADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAqLAKITDYVDAgRAEGATLLLGG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 830 RQLDD-SGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEAGN 908
Cdd:cd07118 332 ERLASaAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGT 411
|
410 420
....*....|....*....|....*.
gi 2515445683 909 VYVNRGTTGAIvrRQPFGGWKRSQVG 934
Cdd:cd07118 412 VWVNTFLDGSP--ELPFGGFKQSGIG 435
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
528-934 |
4.76e-52 |
|
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: 190.07 E-value: 4.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKA--APEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLA 605
Cdd:cd07114 17 SAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVRYLAEWYRYYAGLA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 606 eelDELEG-------------VRFSPAPVTAAIPPWNFPLAIPAGSaLAP-LATGSVVVFKPAEQARRCGAVIAQALWDA 671
Cdd:cd07114 97 ---DKIEGavipvdkgdylnfTRREPLGVVAAITPWNSPLLLLAKK-LAPaLAAGNTVVLKPSEHTPASTLELAKLAEEA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 672 GVSKEALRLVdihPDEMAEVGEALVT--GSDQVILTGSIETAK-LFRSWEPDLAVF-AETSGKNAIIVTPQADIDLAAKD 747
Cdd:cd07114 173 GFPPGVVNVV---TGFGPETGEALVEhpLVAKIAFTGGTETGRhIARAAAENLAPVtLELGGKSPNIVFDDADLDAAVNG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 748 LVQSAFGHAGQKCSAASiAILVGAmGKSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAA-----GKLKRGLTElepG 822
Cdd:cd07114 250 VVAGIFAAAGQTCVAGS-RLLVQR-SIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQlekveRYVARAREE---G 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 823 QTWLLKPRQLD----DSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIK 898
Cdd:cd07114 325 ARVLTGGERPSgadlGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAH 404
|
410 420 430
....*....|....*....|....*....|....*.
gi 2515445683 899 LWLSKVEAGNVYVNrgTTGAIVRRQPFGGWKRSQVG 934
Cdd:cd07114 405 RVARAIEAGTVWVN--TYRALSPSSPFGGFKDSGIG 438
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
528-934 |
9.92e-52 |
|
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: 189.06 E-value: 9.92e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEE 607
Cdd:cd07101 16 TPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVARYYARRAER 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 608 LDELEGVR------------FSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSK 675
Cdd:cd07101 96 LLKPRRRRgaipvltrttvnRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 676 EALRLVdihPDEMAEVGEALVTGSDQVILTGSIETAKLF--RSWEPDLAVFAETSGKNAIIVTPQADIDLAAKDLVQSAF 753
Cdd:cd07101 176 DLWQVV---TGPGSEVGGAIVDNADYVMFTGSTATGRVVaeRAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 754 GHAGQKCSAASIAILVGAMgkSERFINQVVDAAESLVV----DWptnpSAEMGPIIEPAagKLKRGLTELE----PGQTW 825
Cdd:cd07101 253 SNAGQLCVSIERIYVHESV--YDEFVRRFVARTRALRLgaalDY----GPDMGSLISQA--QLDRVTAHVDdavaKGATV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 826 LLKPRQLDDSGRL-WSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKV 904
Cdd:cd07101 325 LAGGRARPDLGPYfYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARL 404
|
410 420 430
....*....|....*....|....*....|.
gi 2515445683 905 EAGNVYVNRGTTGAIVRRQ-PFGGWKRSQVG 934
Cdd:cd07101 405 RAGTVNVNEGYAAAWASIDaPMGGMKDSGLG 435
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
528-936 |
2.61e-51 |
|
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: 187.80 E-value: 2.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYAD---- 603
Cdd:cd07149 19 SEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDRAIETLRLSAEeakr 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 604 LAEELDELEGVRFS----------PAPVTAAIPPWNFPLAIPAgSALAP-LATGSVVVFKPAEQARRCGAVIAQALWDAG 672
Cdd:cd07149 99 LAGETIPFDASPGGegrigftirePIGVVAAITPFNFPLNLVA-HKVGPaIAAGNAVVLKPASQTPLSALKLAELLLEAG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 673 VSKEALRLVDIHPDemaEVGEALVTGSD--QVILTGSIETAKLFRSWEPDLAVFAETSGKNAIIVTPQADIDLAAKDLVQ 750
Cdd:cd07149 178 LPKGALNVVTGSGE---TVGDALVTDPRvrMISFTGSPAVGEAIARKAGLKKVTLELGSNAAVIVDADADLEKAVERCVS 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 751 SAFGHAGQKCSAASiAILVGAMGKSErFINQVVDAAESLVVDWPTNPSAEMGPIIEP-AAGKLKRGLTE-LEPGQTWLLK 828
Cdd:cd07149 255 GAFANAGQVCISVQ-RIFVHEDIYDE-FLERFVAATKKLVVGDPLDEDTDVGPMISEaEAERIEEWVEEaVEGGARLLTG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 829 PRQlddSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEAGN 908
Cdd:cd07149 333 GKR---DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGG 409
|
410 420
....*....|....*....|....*...
gi 2515445683 909 VYVNRGTTgAIVRRQPFGGWKRSqvGTG 936
Cdd:cd07149 410 VMINDSST-FRVDHMPYGGVKES--GTG 434
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
528-934 |
6.90e-51 |
|
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: 187.06 E-value: 6.90e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWA-GLSGAERAKILRRAGQVLGERREELIEVAASECGKIVG-EADVEVSEAIDFANYYADLA 605
Cdd:cd07089 17 GAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMtARAMQVDGPIGHLRYFADLA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 606 EELDELEG--------------VRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQ----ARRCGAVIAQA 667
Cdd:cd07089 97 DSFPWEFDlpvpalrggpgrrvVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDtplsALLLGEIIAET 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 668 LWDAGVskealrlVDIHPDEMAEVGEALVT--GSDQVILTGSIET-AKLFRSWEPDLA-VFAETSGKNAIIVTPQADIDL 743
Cdd:cd07089 177 DLPAGV-------VNVVTGSDNAVGEALTTdpRVDMVSFTGSTAVgRRIMAQAAATLKrVLLELGGKSANIVLDDADLAA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 744 AAKDLVQSAFGHAGQKCSAASiAILVGAmGKSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAA-----GKLKRGLTE 818
Cdd:cd07089 250 AAPAAVGVCMHNAGQGCALTT-RLLVPR-SRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQrdrveGYIARGRDE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 819 lepGQTWLL---KPRQLDdSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPD 895
Cdd:cd07089 328 ---GARLVTgggRPAGLD-KGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVD 403
|
410 420 430
....*....|....*....|....*....|....*....
gi 2515445683 896 EIKLWLSKVEAGNVYVNRGTTGAIvrRQPFGGWKRSQVG 934
Cdd:cd07089 404 RAYRVARRIRTGSVGINGGGGYGP--DAPFGGYKQSGLG 440
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
522-940 |
9.86e-50 |
|
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: 183.33 E-value: 9.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 522 DDARVRTV-AEMEQIVAEARK-AAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFAN 599
Cdd:cd07146 8 TGEVVGTVpAGTEEALREALAlAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAADVLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 600 YyadLAEELDELEGVRFS-----------------PAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGA 662
Cdd:cd07146 88 F---AAAEALRDDGESFScdltangkarkiftlrePLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 663 VIAQALWDAGVSKEALRLVDIHPdemAEVGEALVTGSD--QVILTGSIETAKLFRSWEPDLAVFAETSGKNAIIVTPQAD 740
Cdd:cd07146 165 YLADLLYEAGLPPDMLSVVTGEP---GEIGDELITHPDvdLVTFTGGVAVGKAIAATAGYKRQLLELGGNDPLIVMDDAD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 741 IDLAAKDLVQSAFGHAGQKCSAASiAILVGAmGKSERFINQVVDAAESLVVDWPTNPSAEMGPII-EPAAGKLKRGLTE- 818
Cdd:cd07146 242 LERAATLAVAGSYANSGQRCTAVK-RILVHE-SVADEFVDLLVEKSAALVVGDPMDPATDMGTVIdEEAAIQIENRVEEa 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 819 LEPGQTWLLKPRQlddSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIK 898
Cdd:cd07146 320 IAQGARVLLGNQR---QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIK 396
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2515445683 899 LWLSKVEAGNVYVNRGtTGAIVRRQPFGGWKRSqvGTGSKAG 940
Cdd:cd07146 397 RLVERLDVGTVNVNEV-PGFRSELSPFGGVKDS--GLGGKEG 435
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
530-931 |
1.07e-49 |
|
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: 183.57 E-value: 1.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 530 AEMEQIVAEARKAAPE--WAGLSGAERAKILRRAGQVLGERREELievAASEC---GKIVGEA-DVEVSEAIDFANYYAD 603
Cdd:cd07112 24 ADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDEL---ALLETldmGKPISDAlAVDVPSAANTFRWYAE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 604 LAEEL---------DELEGVRFSPAPVTAAIPPWNFPLAIPAGSaLAP-LATGSVVVFKPAEQARRCGAVIAQALWDAGV 673
Cdd:cd07112 101 AIDKVygevaptgpDALALITREPLGVVGAVVPWNFPLLMAAWK-IAPaLAAGNSVVLKPAEQSPLTALRLAELALEAGL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 674 SKEALRLVdihPDEMAEVGEALV--TGSDQVILTGSIETAKLF--RSWEPDLA-VFAETSGKNAIIVTPQA-DIDLAAKD 747
Cdd:cd07112 180 PAGVLNVV---PGFGHTAGEALGlhMDVDALAFTGSTEVGRRFleYSGQSNLKrVWLECGGKSPNIVFADApDLDAAAEA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 748 LVQSAFGHAGQKCSAASiAILVGAMGKsERFINQVVDAAESLVVDWPTNPSAEMGPIIEPA-----AGKLKRGLTElepG 822
Cdd:cd07112 257 AAAGIFWNQGEVCSAGS-RLLVHESIK-DEFLEKVVAAAREWKPGDPLDPATRMGALVSEAhfdkvLGYIESGKAE---G 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 823 QTWLL--KPRQLDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLW 900
Cdd:cd07112 332 ARLVAggKRVLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRV 411
|
410 420 430
....*....|....*....|....*....|.
gi 2515445683 901 LSKVEAGNVYVNrgTTGAIVRRQPFGGWKRS 931
Cdd:cd07112 412 ARRLRAGTVWVN--CFDEGDITTPFGGFKQS 440
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
528-934 |
2.70e-49 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 183.93 E-value: 2.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEE 607
Cdd:PRK09407 52 TAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLDVALTARYYARRAPK 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 608 L---DELEG---------VRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSK 675
Cdd:PRK09407 132 LlapRRRAGalpvltkttELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPR 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 676 EALRLVdihPDEMAEVGEALVTGSDQVILTGSIETAKLfrswepdLA---------VFAETSGKNAIIVTPQADIDLAAK 746
Cdd:PRK09407 212 DLWQVV---TGPGPVVGTALVDNADYLMFTGSTATGRV-------LAeqagrrligFSLELGGKNPMIVLDDADLDKAAA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 747 DLVQSAFGHAGQKCsaASIAILVGAMGKSERFINQVVDAAESLVV----DWptnpSAEMGPIIEPA---------AGKLK 813
Cdd:PRK09407 282 GAVRACFSNAGQLC--ISIERIYVHESIYDEFVRAFVAAVRAMRLgagyDY----SADMGSLISEAqletvsahvDDAVA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 814 RGLTELEPGqtwllKPRQldDSGRL-WSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSL 892
Cdd:PRK09407 356 KGATVLAGG-----KARP--DLGPLfYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTG 428
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2515445683 893 DPDEIKLWLSKVEAGNVYVNRG------TTGAivrrqPFGGWKRSQVG 934
Cdd:PRK09407 429 DTARGRAIAARIRAGTVNVNEGyaaawgSVDA-----PMGGMKDSGLG 471
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
528-934 |
2.95e-49 |
|
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: 182.12 E-value: 2.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEE 607
Cdd:cd07090 17 GAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDSSADCLEYYAGLAPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 608 LD----ELEGVRFS-----PAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEAL 678
Cdd:cd07090 97 LSgehvPLPGGSFAytrrePLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAGLPDGVF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 679 RLVdihpDEMAEVGEALVTGSD--QVILTGSIETA-KLFRSWEPDLA-VFAETSGKNAIIVTPQADIDLAAKDLVQSAFG 754
Cdd:cd07090 177 NVV----QGGGETGQLLCEHPDvaKVSFTGSVPTGkKVMSAAAKGIKhVTLELGGKSPLIIFDDADLENAVNGAMMANFL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 755 HAGQKCSAASiAILVgAMGKSERFINQVVDAAESLVVDWPTNPSAEMGPII-----EPAAGKLKRGLTElepGQTWL--- 826
Cdd:cd07090 253 SQGQVCSNGT-RVFV-QRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALIseehlEKVLGYIESAKQE---GAKVLcgg 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 827 --LKPRQLDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKV 904
Cdd:cd07090 328 erVVPEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQL 407
|
410 420 430
....*....|....*....|....*....|.
gi 2515445683 905 EAGNVYVNR-GTTGAIVrrqPFGGWKRSQVG 934
Cdd:cd07090 408 QAGTCWINTyNISPVEV---PFGGYKQSGFG 435
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
528-936 |
4.63e-49 |
|
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: 181.29 E-value: 4.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEE 607
Cdd:cd07102 16 SLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMISIAEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 608 ------LDELEG----VRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEA 677
Cdd:cd07102 96 aladirVPEKDGferyIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 678 LrlVDIHPDEmaEVGEALVT--GSDQVILTGSIET-AKLFRSWEPDL-AVFAETSGKNAIIVTPQADIDLAAKDLVQSAF 753
Cdd:cd07102 176 F--QVLHLSH--ETSAALIAdpRIDHVSFTGSVAGgRAIQRAAAGRFiKVGLELGGKDPAYVRPDADLDAAAESLVDGAF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 754 GHAGQKCSA-------ASIailvgamgkSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAAGKLKRGLTE--LEPGQT 824
Cdd:cd07102 252 FNSGQSCCSieriyvhESI---------YDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIAdaIAKGAR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 825 WLLKP---RQLDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWL 901
Cdd:cd07102 323 ALIDGalfPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALG 402
|
410 420 430
....*....|....*....|....*....|....*
gi 2515445683 902 SKVEAGNVYVNRGTtgAIVRRQPFGGWKRSQVGTG 936
Cdd:cd07102 403 EQLETGTVFMNRCD--YLDPALAWTGVKDSGRGVT 435
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
528-934 |
1.93e-48 |
|
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: 179.68 E-value: 1.93e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEA-DVEVSEAIDFANYYADLA- 605
Cdd:cd07093 17 GAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLArTRDIPRAAANFRFFADYIl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 606 ----EELDELEG----VRFSPAPVTAAIPPWNFPLAIpAGSALAP-LATGSVVVFKPAEQARRCGAVIAQALWDAGVSKE 676
Cdd:cd07093 97 qldgESYPQDGGalnyVLRQPVGVAGLITPWNLPLML-LTWKIAPaLAFGNTVVLKPSEWTPLTAWLLAELANEAGLPPG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 677 ALRLVDihpDEMAEVGEALVT--GSDQVILTGSIETAKLF-RSWEPDL-AVFAETSGKNAIIVTPQADIDLAAKDLVQSA 752
Cdd:cd07093 176 VVNVVH---GFGPEAGAALVAhpDVDLISFTGETATGRTImRAAAPNLkPVSLELGGKNPNIVFADADLDRAVDAAVRSS 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 753 FGHAGQKCSAASiAILVgAMGKSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAAGKLKRGLTEL--EPGQTWLLkpr 830
Cdd:cd07093 253 FSNNGEVCLAGS-RILV-QRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELarAEGATILT--- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 831 qlddSGRLWSPGIRDG---VTP----GQDAHMT----EYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKL 899
Cdd:cd07093 328 ----GGGRPELPDLEGgyfVEPtvitGLDNDSRvaqeEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHR 403
|
410 420 430
....*....|....*....|....*....|....*..
gi 2515445683 900 WLSKVEAGNVYVNrgttGAIVR--RQPFGGWKRSQVG 934
Cdd:cd07093 404 VARRLEAGTVWVN----CWLVRdlRTPFGGVKASGIG 436
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
528-944 |
1.99e-48 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 180.01 E-value: 1.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADV-EVSEAIDFANYYADLAE 606
Cdd:TIGR01804 33 TPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKLETLDTGKTLQETIVaDMDSGADVFEFFAGLAP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 607 ELD----ELEGVRFS-----PAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEA 677
Cdd:TIGR01804 113 ALNgeiiPLGGPSFAytirePLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 678 LRLVdihPDEMAEVGEALVT--GSDQVILTGSIETAK-LFRSWEPDLA-VFAETSGKNAIIVTPQADIDLAAKDLVQSAF 753
Cdd:TIGR01804 193 FNVV---QGDGAEVGPLLVNhpDVAKVSFTGGVPTGKkIMAAAAGHLKhVTMELGGKSPLIVFDDADLESAVDGAMLGNF 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 754 GHAGQKCSAASiAILVGAMGKsERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAAGK-----LKRGLTELEPGQTWLLK 828
Cdd:TIGR01804 270 FSAGQVCSNGT-RVFVHKKIK-ERFLARLVERTERIKLGDPFDEATEMGPLISAAHRDkvlsyIEKGKAEGATLATGGGR 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 829 PRQLD-DSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEAG 907
Cdd:TIGR01804 348 PENVGlQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAG 427
|
410 420 430
....*....|....*....|....*....|....*..
gi 2515445683 908 NVYVNrgTTGAIVRRQPFGGWKRSQVGTGSKAGGPNH 944
Cdd:TIGR01804 428 TVWIN--TYNLYPAEAPFGGYKQSGIGRENGKAALAH 462
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
538-934 |
2.73e-48 |
|
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: 179.08 E-value: 2.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 538 EARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFanyYADLAEELDELEG---- 613
Cdd:cd07145 29 VAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVERTIRL---FKLAAEEAKVLRGetip 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 614 -------------VRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEALRL 680
Cdd:cd07145 106 vdayeynerriafTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAGLPPGVINV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 681 VDIHPDemaEVGEALVTGSD--QVILTGSIETAKLFRSWEPDLA--VFAETSGKNAIIVTPQADIDLAAKDLVQSAFGHA 756
Cdd:cd07145 186 VTGYGS---EVGDEIVTNPKvnMISFTGSTAVGLLIASKAGGTGkkVALELGGSDPMIVLKDADLERAVSIAVRGRFENA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 757 GQKCSAASiAILVgamGKS--ERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAAGKLKRGLTE--LEPGQTWLLKPRQl 832
Cdd:cd07145 263 GQVCNAVK-RILV---EEEvyDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVNdaVEKGGKILYGGKR- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 833 dDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDpdeIKLWL---SKVEAGNV 909
Cdd:cd07145 338 -DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTND---INRALkvaRELEAGGV 413
|
410 420
....*....|....*....|....*..
gi 2515445683 910 YVNRGTTgaiVRRQ--PFGGWKRSQVG 934
Cdd:cd07145 414 VINDSTR---FRWDnlPFGGFKKSGIG 437
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
524-942 |
1.86e-47 |
|
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: 176.75 E-value: 1.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 524 ARVR--TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYY 601
Cdd:cd07150 13 ARVAvgSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTFTPELLRAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 602 ADLA-----EELDELEGVRFS-----PAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDA 671
Cdd:cd07150 93 AGECrrvrgETLPSDSPGTVSmsvrrPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 672 GVSKEALRLVdihPDEMAEVGEALVTGS--DQVILTGSIETAKlfrswepDLAVFA---------ETSGKNAIIVTPQAD 740
Cdd:cd07150 173 GLPKGVFNVV---TGGGAEVGDELVDDPrvRMVTFTGSTAVGR-------EIAEKAgrhlkkitlELGGKNPLIVLADAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 741 IDLAAKDLVQSAFGHAGQKCSAASiAILVGAMGKSErFINQVVDAAESLVVDWPTNPSAEMGPIIEPAAGKLKRGLTE-- 818
Cdd:cd07150 243 LDYAVRAAAFGAFMHQGQICMSAS-RIIVEEPVYDE-FVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEda 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 819 ------LEPGQTWllkprqlddSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSL 892
Cdd:cd07150 321 vakgakLLTGGKY---------DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTN 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2515445683 893 DPDEIKLWLSKVEAGNVYVNRGT--TGAIVrrqPFGGWKRSQVGtgsKAGGP 942
Cdd:cd07150 392 DLQRAFKLAERLESGMVHINDPTilDEAHV---PFGGVKASGFG---REGGE 437
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
530-934 |
3.93e-47 |
|
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: 176.01 E-value: 3.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 530 AEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGK-IVGEADVEVSEAIDFANYYADLAEEL 608
Cdd:cd07108 19 ADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNaLRTQARPEAAVLADLFRYFGGLAGEL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 609 ---------DELEGVRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCG---AVIAQALWDAGVske 676
Cdd:cd07108 99 kgetlpfgpDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVlllAEILAQVLPAGV--- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 677 alrlVDIHPDEMAEVGEALVT--GSDQVILTGSIETAK-LFRSWEPDLA-VFAETSGKNAIIVTPQADIDLAAKDLVQSA 752
Cdd:cd07108 176 ----LNVITGYGEECGAALVDhpDVDKVTFTGSTEVGKiIYRAAADRLIpVSLELGGKSPMIVFPDADLDDAVDGAIAGM 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 753 -FGHAGQKCSAASIAILVGAMgkSERFINQVVDAAESLVVDWPTNPSAEMGPIIEP----------AAGKLKRGLTELEP 821
Cdd:cd07108 252 rFTRQGQSCTAGSRLFVHEDI--YDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEkqfakvcgyiDLGLSTSGATVLRG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 822 GqtwLLKPRQLDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWL 901
Cdd:cd07108 330 G---PLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAA 406
|
410 420 430
....*....|....*....|....*....|...
gi 2515445683 902 SKVEAGNVYVNRGttGAIVRRQPFGGWKRSQVG 934
Cdd:cd07108 407 HALEAGWVQVNQG--GGQQPGQSYGGFKQSGLG 437
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
530-940 |
1.55e-46 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 175.26 E-value: 1.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 530 AEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADlaeeld 609
Cdd:PLN02278 62 AETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAE------ 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 610 elEGVRFS----PAP--------------VTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDA 671
Cdd:PLN02278 136 --EAKRVYgdiiPSPfpdrrllvlkqpvgVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 672 GVSKEALRLVDIHPDemaEVGEALVTgSDQV---ILTGSIETAKLFrswepdLAVFAETS-------GKNA-IIVTPQAD 740
Cdd:PLN02278 214 GIPPGVLNVVMGDAP---EIGDALLA-SPKVrkiTFTGSTAVGKKL------MAGAAATVkrvslelGGNApFIVFDDAD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 741 IDLAAKDLVQSAFGHAGQKCSAASiAILVGAmGKSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAA-GKLKRGLTE- 818
Cdd:PLN02278 284 LDVAVKGALASKFRNSGQTCVCAN-RILVQE-GIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAvQKVESHVQDa 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 819 LEPGQTWLLKPRQLDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIK 898
Cdd:PLN02278 362 VSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAW 441
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2515445683 899 LWLSKVEAGNVYVNRGTTGAIVrrQPFGGWKRSQVG-TGSKAG 940
Cdd:PLN02278 442 RVSEALEYGIVGVNEGLISTEV--APFGGVKQSGLGrEGSKYG 482
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
528-942 |
9.67e-46 |
|
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: 171.99 E-value: 9.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKA--APEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVG-EADVEVSEAIDFANYYADL 604
Cdd:cd07139 34 TPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISwSRRAQGPGPAALLRYYAAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 605 AEEL---DELEG-------VRFSPAPVTAAIPPWNFPLAIPAgSALAP-LATGSVVVFKPAEQARRCGAVIAQALWDAGV 673
Cdd:cd07139 114 ARDFpfeERRPGsggghvlVRREPVGVVAAIVPWNAPLFLAA-LKIAPaLAAGCTVVLKPSPETPLDAYLLAEAAEEAGL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 674 SKEALRLVDIHpdemAEVGEALVT--GSDQVILTGSIETAK-LFRSWEPDLA-VFAETSGKNAIIVTPQADIDLAAKDLV 749
Cdd:cd07139 193 PPGVVNVVPAD----REVGEYLVRhpGVDKVSFTGSTAAGRrIAAVCGERLArVTLELGGKSAAIVLDDADLDAAVPGLV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 750 QSAFGHAGQKCSAASiAILVGAmGKSERFINQVVDAAESLVVDWPTNPSAEMGPII-----EPAAGKLKRGLTElepGQT 824
Cdd:cd07139 269 PASLMNNGQVCVALT-RILVPR-SRYDEVVEALAAAVAALKVGDPLDPATQIGPLAsarqrERVEGYIAKGRAE---GAR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 825 WLLKPRQLDDSGRLW--SPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLS 902
Cdd:cd07139 344 LVTGGGRPAGLDRGWfvEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVAR 423
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2515445683 903 KVEAGNVYVNrGTTGAIVrrQPFGGWKRSQVGtgsKAGGP 942
Cdd:cd07139 424 RIRTGTVGVN-GFRLDFG--APFGGFKQSGIG---REGGP 457
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
528-934 |
3.63e-45 |
|
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: 170.18 E-value: 3.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEE 607
Cdd:cd07151 30 SKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANIEWGAAMAITREAATFPLR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 608 LD------ELEG----VRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAV-IAQALWDAGVSKE 676
Cdd:cd07151 110 MEgrilpsDVPGkenrVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGLlLAKIFEEAGLPKG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 677 ALRLVDIHpdeMAEVGEALV----------TGSDQV---IltGSIETAKLFRswepdlaVFAETSGKNAIIVTPQADIDL 743
Cdd:cd07151 190 VLNVVVGA---GSEIGDAFVehpvprlisfTGSTPVgrhI--GELAGRHLKK-------VALELGGNNPFVVLEDADIDA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 744 AAKDLVQSAFGHAGQKCSAASiAILVGAmGKSERFINQVVDAAESLVVDWPTNPSAEMGPII-----EPAAGKLKRGLTE 818
Cdd:cd07151 258 AVNAAVFGKFLHQGQICMAIN-RIIVHE-DVYDEFVEKFVERVKALPYGDPSDPDTVVGPLInesqvDGLLDKIEQAVEE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 819 lepGQTWLLKPrqlDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIK 898
Cdd:cd07151 336 ---GATLLVGG---EAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGV 409
|
410 420 430
....*....|....*....|....*....|....*...
gi 2515445683 899 LWLSKVEAGNVYVNRGTTG--AIVrrqPFGGWKRSQVG 934
Cdd:cd07151 410 QFARRIDAGMTHINDQPVNdePHV---PFGGEKNSGLG 444
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
528-934 |
4.68e-44 |
|
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: 166.75 E-value: 4.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKA--APEWAGlSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLA 605
Cdd:cd07120 17 GVAEAEAAIAAARRAfdETDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEARFEISGAISELRYYAGLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 606 EELD----ELEGVRFS-----PAPVTAAIPPWNFPlAIPAGSALAP-LATGSVVVFKPAEQARRCGAVIAQALWD----- 670
Cdd:cd07120 96 RTEAgrmiEPEPGSFSlvlrePMGVAGIIVPWNSP-VVLLVRSLAPaLAAGCTVVVKPAGQTAQINAAIIRILAEipslp 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 671 AGVskealrlVDIHPDEMAEVGEALVTGSD-QVI-LTGSIETAK-LFRSWEPDLAVFA-ETSGKNAIIVTPQADIDLAAK 746
Cdd:cd07120 175 AGV-------VNLFTESGSEGAAHLVASPDvDVIsFTGSTATGRaIMAAAAPTLKRLGlELGGKTPCIVFDDADLDAALP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 747 DLVQSAFGHAGQKCSAASiAILVGAmGKSERFINQVVDAAESLVVDWPTNPSAEMGPII------------EPAAGKLKR 814
Cdd:cd07120 248 KLERALTIFAGQFCMAGS-RVLVQR-SIADEVRDRLAARLAAVKVGPGLDPASDMGPLIdranvdrvdrmvERAIAAGAE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 815 GLTELEPGQTWLLKprqlddsGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDP 894
Cdd:cd07120 326 VVLRGGPVTEGLAK-------GAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDL 398
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2515445683 895 DEIKLWLSKVEAGNVYVNrgTTGAIVRRQPFGGWKRSQVG 934
Cdd:cd07120 399 ARAMRVARAIRAGTVWIN--DWNKLFAEAEEGGYRQSGLG 436
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
536-934 |
1.08e-43 |
|
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: 166.23 E-value: 1.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 536 VAEARKAAPE--WAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGE-ADVEVSEAIDFANYYADLAEELD--- 609
Cdd:cd07091 47 VKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEEsAKGDVALSIKCLRYYAGWADKIQgkt 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 610 -ELEGVRFS-----PAPVTAAIPPWNFPLAIPAGSaLAP-LATGSVVVFKPAEQ----ARRCGAVIAQALWDAGVskeal 678
Cdd:cd07091 127 iPIDGNFLAytrrePIGVCGQIIPWNFPLLMLAWK-LAPaLAAGNTVVLKPAEQtplsALYLAELIKEAGFPPGV----- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 679 rlVDIHPDEMAEVGEALVT--GSDQVILTGSIETAKLFR--SWEPDL-AVFAETSGKNAIIVTPQADIDLAAKDLVQSAF 753
Cdd:cd07091 201 --VNIVPGFGPTAGAAISShmDVDKIAFTGSTAVGRTIMeaAAKSNLkKVTLELGGKSPNIVFDDADLDKAVEWAAFGIF 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 754 GHAGQKCSAASiAILVGAmGKSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAagKLKRGLTELEPGQ----TWLLKP 829
Cdd:cd07091 279 FNQGQCCCAGS-RIFVQE-SIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKA--QFDKILSYIESGKkegaTLLTGG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 830 RQLDDSGRLWSPGIRDGVTPgqdaHMT----EYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVE 905
Cdd:cd07091 355 ERHGSKGYFIQPTVFTDVKD----DMKiakeEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALK 430
|
410 420
....*....|....*....|....*....
gi 2515445683 906 AGNVYVNrgTTGAIVRRQPFGGWKRSQVG 934
Cdd:cd07091 431 AGTVWVN--TYNVFDAAVPFGGFKQSGFG 457
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
528-935 |
4.81e-43 |
|
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: 163.65 E-value: 4.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGE-ADVEVSEAIDFANYYADLAE 606
Cdd:cd07092 17 SAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLvRDDELPGAVDNFRFFAGAAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 607 EL------DELEG----VRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWD---AGV 673
Cdd:cd07092 97 TLegpaagEYLPGhtsmIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEvlpPGV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 674 skealrlVDIHPDEMAEVGEALVTGS--DQVILTGSIETAK-LFRSWEPDLA-VFAETSGKNAIIVTPQADIDLAAKDLV 749
Cdd:cd07092 177 -------VNVVCGGGASAGDALVAHPrvRMVSLTGSVRTGKkVARAAADTLKrVHLELGGKAPVIVFDDADLDAAVAGIA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 750 QSAFGHAGQKCSAASiAILVGAmGKSERFINQVVDAAESLVVDWPTNPSAEMGPIIepAAGKLKR---GLTELEPGQTWL 826
Cdd:cd07092 250 TAGYYNAGQDCTAAC-RVYVHE-SVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLN--SAAQRERvagFVERAPAHARVL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 827 LKPRQLDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEA 906
Cdd:cd07092 326 TGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDF 405
|
410 420
....*....|....*....|....*....
gi 2515445683 907 GNVYVNrgTTGAIVRRQPFGGWKRSQVGT 935
Cdd:cd07092 406 GTVWVN--THIPLAAEMPHGGFKQSGYGK 432
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
524-941 |
3.69e-42 |
|
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: 161.61 E-value: 3.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 524 ARVR--TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYY 601
Cdd:cd07130 26 ARVRqaTPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLGEVQEMIDICDFA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 602 ADLAEELD------ELEGVR----FSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQ----ARRCGAVIAQA 667
Cdd:cd07130 106 VGLSRQLYgltipsERPGHRmmeqWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTtpltAIAVTKIVARV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 668 LWDAGVSKEALRLVdIHPdemAEVGEALV----------TGSDQVILTGSIETAKLF-RSwepdlavFAETSGKNAIIVT 736
Cdd:cd07130 186 LEKNGLPGAIASLV-CGG---ADVGEALVkdprvplvsfTGSTAVGRQVGQAVAARFgRS-------LLELGGNNAIIVM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 737 PQADIDLAAKDLVQSAFGHAGQKCSAA-------SIAilvgamgksERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAA 809
Cdd:cd07130 255 EDADLDLAVRAVLFAAVGTAGQRCTTTrrlivheSIY---------DEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 810 -GKLKRGLTEL-EPGQTWLLKPRQLDDSGRLWSPGIrdgVTPGQDAH--MTEYFGPVLGIMRAETLEEAIRLQNAVEFGL 885
Cdd:cd07130 326 vDNYLAAIEEAkSQGGTVLFGGKVIDGPGNYVEPTI---VEGLSDAPivKEETFAPILYVLKFDTLEEAIAWNNEVPQGL 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2515445683 886 TAGLHSLDPDEIKLWLSKV--EAGNVYVNRGTTGAIVrRQPFGGWKrsQVGTGSKAGG 941
Cdd:cd07130 403 SSSIFTTDLRNAFRWLGPKgsDCGIVNVNIGTSGAEI-GGAFGGEK--ETGGGRESGS 457
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
530-946 |
6.51e-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: 6.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 530 AEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVL-GERREELIEVAASECGKIVGEADVEVS-EAIDFANYYADLAEE 607
Cdd:cd07123 69 ALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLsGKYRYELNAATMLGQGKNVWQAEIDAAcELIDFLRFNVKYAEE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 608 LDELEGVrfSPAPVT-------------AAIPPWNFPlAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVS 674
Cdd:cd07123 149 LYAQQPL--SSPAGVwnrleyrplegfvYAVSPFNFT-AIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLP 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 675 KEALRLVdihPDEMAEVGEAlVTGSDQ---VILTGSIETaklFRS-WE------------PDLAvfAETSGKNAIIVTPQ 738
Cdd:cd07123 226 PGVINFV---PGDGPVVGDT-VLASPHlagLHFTGSTPT---FKSlWKqigenldryrtyPRIV--GETGGKNFHLVHPS 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 739 ADIDLAAKDLVQSAFGHAGQKCSAASIAIlvgaMGKS--ERFINQVVDAAESLVVDWPTNPSAEMGPII-EPAAGKLKR- 814
Cdd:cd07123 297 ADVDSLVTATVRGAFEYQGQKCSAASRAY----VPESlwPEVKERLLEELKEIKMGDPDDFSNFMGAVIdEKAFDRIKGy 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 815 --------GLTELEPGQTwllkprqlDDS-GRLWSPGIRDgVTPGQDAHMT-EYFGPVLGIM--RAETLEEAIRL-QNAV 881
Cdd:cd07123 373 idhaksdpEAEIIAGGKC--------DDSvGYFVEPTVIE-TTDPKHKLMTeEIFGPVLTVYvyPDSDFEETLELvDTTS 443
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2515445683 882 EFGLTAGLHSLDPDEIKLWLSKVE--AGNVYVNRGTTGAIVRRQPFGGWKRSqvGTGSKAGGPNHLI 946
Cdd:cd07123 444 PYALTGAIFAQDRKAIREATDALRnaAGNFYINDKPTGAVVGQQPFGGARAS--GTNDKAGSPLNLL 508
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
526-954 |
7.12e-42 |
|
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: 160.54 E-value: 7.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 526 VRTVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADV-EVSEAIDFANYYADL 604
Cdd:cd07098 14 ADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLgEILVTCEKIRWTLKH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 605 AEELDELEG-------------VRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQarrcgaVIAQALWDA 671
Cdd:cd07098 94 GEKALRPESrpggllmfykrarVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQ------VAWSSGFFL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 672 GVSKEALRLVDIHPD------EMAEVGEALVTGS--DQVILTGSIETAKLF-----RSWEPdlaVFAETSGKNAIIVTPQ 738
Cdd:cd07098 168 SIIRECLAACGHDPDlvqlvtCLPETAEALTSHPviDHITFIGSPPVGKKVmaaaaESLTP---VVLELGGKDPAIVLDD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 739 ADIDLAAKDLVQSAFGHAGQKCsaASIAILVGAMGKSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAAGKLKRGLTE 818
Cdd:cd07098 245 ADLDQIASIIMRGTFQSSGQNC--IGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 819 --LEPGQTWL----LKPRQLDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSL 892
Cdd:cd07098 323 daVEKGARLLaggkRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGK 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2515445683 893 DPDEIKLWLSKVEAGNVYVNRGTTGAIVRRQPFGGWKRSQVGtgsKAGGPNHLIGMSHAEPV 954
Cdd:cd07098 403 DIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFG---RFAGEEGLRGLCNPKSV 461
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
530-945 |
9.40e-42 |
|
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: 160.64 E-value: 9.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 530 AEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEA-DVEVSEAIDFANYYADLAEEL 608
Cdd:cd07111 59 EDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESrDCDIPLVARHFYHHAGWAQLL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 609 DElEGVRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEALRLVDihpdEM 688
Cdd:cd07111 139 DT-ELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVT----GN 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 689 AEVGEALVT--GSDQVILTGSIETAKLFRS----WEPDLAVfaETSGKNAIIVTPQADIDLAAKDLVQSAFGHAGQKCSA 762
Cdd:cd07111 214 GSFGSALANhpGVDKVAFTGSTEVGRALRRatagTGKKLSL--ELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 763 ASiAILVGAmGKSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAAGKLKRGLTEL---EPGQTWlLKPRQLDDSGRLW 839
Cdd:cd07111 292 GS-RLLVQE-SVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEgraEGADVF-QPGADLPSKGPFY 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 840 SPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSldpDEIKLWLS---KVEAGNVYVNrgTT 916
Cdd:cd07111 369 PPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWS---ENLSLALEvalSLKAGVVWIN--GH 443
|
410 420
....*....|....*....|....*....
gi 2515445683 917 GAIVRRQPFGGWKRSQVGtgsKAGGPNHL 945
Cdd:cd07111 444 NLFDAAAGFGGYRESGFG---REGGKEGL 469
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
521-934 |
3.61e-41 |
|
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: 159.01 E-value: 3.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 521 ADDARVRTVAE-----MEQIVAEARKA--APEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSE 593
Cdd:cd07119 21 ANGEVIATVPEgtaedAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEIDIDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 594 AIDFANYYADLAEEL---------DELEGVRFSPAPVTAAIPPWNFPLAIpAGSALAP-LATGSVVVFKPAEQARRCGAV 663
Cdd:cd07119 101 VANCFRYYAGLATKEtgevydvppHVISRTVREPVGVCGLITPWNYPLLQ-AAWKLAPaLAAGNTVVIKPSEVTPLTTIA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 664 IAQALWDAGVSKEALRLVdihPDEMAEVGEALVTGS--DQVILTGSIET-AKLFRSWEPDLA-VFAETSGKNAIIVTPQA 739
Cdd:cd07119 180 LFELIEEAGLPAGVVNLV---TGSGATVGAELAESPdvDLVSFTGGTATgRSIMRAAAGNVKkVALELGGKNPNIVFADA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 740 DIDLAAKDLVQSAFGHAGQKCSAASiAILVGAMGKsERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAAGKLKRGLTEL 819
Cdd:cd07119 257 DFETAVDQALNGVFFNAGQVCSAGS-RLLVEESIH-DKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 820 --EPGQTWLLKPRQLDDS----GRLWSPGIRDGVtpgqDAHMT----EYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGL 889
Cdd:cd07119 335 gkEEGARLVCGGKRPTGDelakGYFVEPTIFDDV----DRTMRivqeEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAV 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2515445683 890 HSLDPDEIKLWLSKVEAGNVYVNrgTTGAIVRRQPFGGWKRSQVG 934
Cdd:cd07119 411 WTKDIARANRVARRLRAGTVWIN--DYHPYFAEAPWGGYKQSGIG 453
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
528-934 |
1.24e-39 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 154.89 E-value: 1.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKA-----APEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYA 602
Cdd:PLN02467 43 TAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 603 DLAEELDELEG-------------VRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALW 669
Cdd:PLN02467 123 DLAEALDAKQKapvslpmetfkgyVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 670 DAGVSKEALRLVDihpDEMAEVGEALVT--GSDQVILTGSIETA-KLFRSWEPDL-AVFAETSGKNAIIVTPQADIDLAA 745
Cdd:PLN02467 203 EVGLPPGVLNVVT---GLGTEAGAPLAShpGVDKIAFTGSTATGrKIMTAAAQMVkPVSLELGGKSPIIVFDDVDLDKAV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 746 KDLVQSAFGHAGQKCSAASIAILVGAMgkSERFINQVVDAAESLVVDWPTNPSAEMGPIIepAAGKLKRGL----TELEP 821
Cdd:PLN02467 280 EWAMFGCFWTNGQICSATSRLLVHERI--ASEFLEKLVKWAKNIKISDPLEEGCRLGPVV--SEGQYEKVLkfisTAKSE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 822 GQTWLL---KPRQLDdSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIK 898
Cdd:PLN02467 356 GATILCggkRPEHLK-KGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCE 434
|
410 420 430
....*....|....*....|....*....|....*.
gi 2515445683 899 LWLSKVEAGNVYVNrgTTGAIVRRQPFGGWKRSQVG 934
Cdd:PLN02467 435 RVSEAFQAGIVWIN--CSQPCFCQAPWGGIKRSGFG 468
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
528-934 |
1.30e-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: 151.05 E-value: 1.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKA-APEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADV-EVSEAIDFANYYADLA 605
Cdd:cd07113 35 TEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHLSRAfEVGQSANFLRYFAGWA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 606 -----EELD----ELEGVRFS------PAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWD 670
Cdd:cd07113 115 tkingETLApsipSMQGERYTaftrrePVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 671 AGVSKEALRLVDihpdEMAEVGEALVTGSD--QVILTGSIETAK-LFRSWEPDLAVFA-ETSGKNAIIVTPQADIDLAAK 746
Cdd:cd07113 195 AGIPDGVLNVVN----GKGAVGAQLISHPDvaKVSFTGSVATGKkIGRQAASDLTRVTlELGGKNAAAFLKDADIDWVVE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 747 DLVQSAFGHAGQKCSAAsiailvgamgksERF------INQVVD----AAESLVVDWPTNPSAEMGPII-EPAAGKLKRG 815
Cdd:cd07113 271 GLLTAGFLHQGQVCAAP------------ERFyvhrskFDELVTklkqALSSFQVGSPMDESVMFGPLAnQPHFDKVCSY 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 816 LTEL-EPGQTWLLKPRQLDDSGRLWSPGIRdgVTPGQDAHMT--EYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSL 892
Cdd:cd07113 339 LDDArAEGDEIVRGGEALAGEGYFVQPTLV--LARSADSRLMreETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTN 416
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2515445683 893 DPDEIKLWLSKVEAGNVYVNRGTTgaIVRRQPFGGWKRSQVG 934
Cdd:cd07113 417 NLSKALRYIPRIEAGTVWVNMHTF--LDPAVPFGGMKQSGIG 456
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
530-935 |
4.31e-38 |
|
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: 148.93 E-value: 4.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 530 AEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEE-- 607
Cdd:cd07147 21 DDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDTFRIAAEEATRiy 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 608 -----LDELEG-------VRFSPAPVTAAIPPWNFPLAIPAgSALAP-LATGSVVVFKPAEQARRCGAVIAQALWDAGVS 674
Cdd:cd07147 101 gevlpLDISARgegrqglVRRFPIGPVSAITPFNFPLNLVA-HKVAPaIAAGCPFVLKPASRTPLSALILGEVLAETGLP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 675 KEALRLVDIHPDEMaevgEALVTgsDQVI----LTGSIETAKLFRSWEPDLAVFAETSGKNAIIVTPQADIDLAAKDLVQ 750
Cdd:cd07147 180 KGAFSVLPCSRDDA----DLLVT--DERIkllsFTGSPAVGWDLKARAGKKKVVLELGGNAAVIVDSDADLDFAAQRIIF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 751 SAFGHAGQKCsaasIA---ILVGAMGKsERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAagklkrgltELEPGQTWLl 827
Cdd:cd07147 254 GAFYQAGQSC----ISvqrVLVHRSVY-DEFKSRLVARVKALKTGDPKDDATDVGPMISES---------EAERVEGWV- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 828 kPRQLDDSGRLWSPGIRDG----------VTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEI 897
Cdd:cd07147 319 -NEAVDAGAKLLTGGKRDGalleptiledVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKA 397
|
410 420 430
....*....|....*....|....*....|....*...
gi 2515445683 898 KLWLSKVEAGNVYVNRGTTGAiVRRQPFGGWKRSQVGT 935
Cdd:cd07147 398 LRAWDELEVGGVVINDVPTFR-VDHMPYGGVKDSGIGR 434
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
558-934 |
4.35e-38 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 147.96 E-value: 4.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 558 LRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEELdelEG-------------VRFSPAPVTAA 624
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRY---EGeiiqsdrpgenilLFKRALGVTTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 625 IPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEALRLVDihpDEMAEVGEALVTGSD--QV 702
Cdd:PRK10090 78 ILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVL---GRGETVGQELAGNPKvaMV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 703 ILTGSIET-AKLFRSWEPDLA-VFAETSGKNAIIVTPQADIDLAAKDLVQSAFGHAGQKCSAASIAILvgAMGKSERFIN 780
Cdd:PRK10090 155 SMTGSVSAgEKIMAAAAKNITkVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYV--QKGIYDQFVN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 781 QVVDAAESLVVDWP-TNPSAEMGPIIEPAA-----GKLKRGLTElepGQTWLLKPRQLDDSGRLWSPGIRDGVTPGQDAH 854
Cdd:PRK10090 233 RLGEAMQAVQFGNPaERNDIAMGPLINAAAlerveQKVARAVEE---GARVALGGKAVEGKGYYYPPTLLLDVRQEMSIM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 855 MTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEAGNVYVNRGTTGAIvrrQPF-GGWKRSQV 933
Cdd:PRK10090 310 HEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAM---QGFhAGWRKSGI 386
|
.
gi 2515445683 934 G 934
Cdd:PRK10090 387 G 387
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
528-934 |
7.07e-38 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 148.47 E-value: 7.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYAD---- 603
Cdd:PRK13968 27 GADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYAEhgpa 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 604 -LAEELDELEG----VRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEAL 678
Cdd:PRK13968 107 mLKAEPTLVENqqavIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVY 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 679 RLVDIHPDEMAE-VGEALVTGsdqVILTGSIETAKLFRSwEPDLAV---FAETSGKNAIIVTPQADIDLAAKDLVQSAFG 754
Cdd:PRK13968 187 GWLNADNDGVSQmINDSRIAA---VTVTGSVRAGAAIGA-QAGAALkkcVLELGGSDPFIVLNDADLELAVKAAVAGRYQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 755 HAGQKCSAASIAILvgAMGKSERFINQVVDAAESLVVDWPTNPSAEMGPIiepAAGKLKRGLTE-----LEPGQTWLLKP 829
Cdd:PRK13968 263 NTGQVCAAAKRFII--EEGIASAFTERFVAAAAALKMGDPRDEENALGPM---ARFDLRDELHHqveatLAEGARLLLGG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 830 RQLDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEAGNV 909
Cdd:PRK13968 338 EKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGV 417
|
410 420
....*....|....*....|....*
gi 2515445683 910 YVNrgTTGAIVRRQPFGGWKRSQVG 934
Cdd:PRK13968 418 FIN--GYCASDARVAFGGVKKSGFG 440
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
529-940 |
8.00e-38 |
|
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: 148.80 E-value: 8.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 529 VAEMEQIVAEARKAAPE--WAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEAD-VEVSEAIDFANYYADLA 605
Cdd:cd07142 40 AEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQARyAEVPLAARLFRYYAGWA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 606 EELDEL----EGVRF-----SPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKE 676
Cdd:cd07142 120 DKIHGMtlpaDGPHHvytlhEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 677 ALRLVDIHPDemaEVGEALVTGS--DQVILTGSIETAKLFR--SWEPDL-AVFAETSGKNAIIVTPQADIDLAAKDLVQS 751
Cdd:cd07142 200 VLNIVTGFGP---TAGAAIASHMdvDKVAFTGSTEVGKIIMqlAAKSNLkPVTLELGGKSPFIVCEDADVDKAVELAHFA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 752 AFGHAGQKCSAASIAILvgAMGKSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAA-----GKLKRGLTElepGQTWL 826
Cdd:cd07142 277 LFFNQGQCCCAGSRTFV--HESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQfekilSYIEHGKEE---GATLI 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 827 LKPRQLDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEA 906
Cdd:cd07142 352 TGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKA 431
|
410 420 430
....*....|....*....|....*....|....
gi 2515445683 907 GNVYVNrgTTGAIVRRQPFGGWKRSqvGTGSKAG 940
Cdd:cd07142 432 GTVWVN--CYDVFDASIPFGGYKMS--GIGREKG 461
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
530-934 |
1.63e-37 |
|
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: 147.88 E-value: 1.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 530 AEMEQIVAEARKA---APEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEA-DVEVSEAIDFANYYADLA 605
Cdd:cd07141 44 ADVDKAVKAARAAfklGSPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSyLVDLPGAIKVLRYYAGWA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 606 EEL---------DELEGVRFSPAPVTAAIPPWNFPLAIpAGSALAP-LATGSVVVFKPAEQ----ARRCGAVIAQALWDA 671
Cdd:cd07141 124 DKIhgktipmdgDFFTYTRHEPVGVCGQIIPWNFPLLM-AAWKLAPaLACGNTVVLKPAEQtpltALYLASLIKEAGFPP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 672 GVskealrlVDIHPDEMAEVGEALVT--GSDQVILTGSIETAKLFR--SWEPDLA-VFAETSGKNAIIVTPQADIDLAAK 746
Cdd:cd07141 203 GV-------VNVVPGYGPTAGAAISShpDIDKVAFTGSTEVGKLIQqaAGKSNLKrVTLELGGKSPNIVFADADLDYAVE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 747 DLVQSAFGHAGQKCSAASiAILVGAmGKSERFINQVVDAAESLVVDWPTNPSAEMGPIIEpaAGKLKRGLTELEPGQTWL 826
Cdd:cd07141 276 QAHEALFFNMGQCCCAGS-RTFVQE-SIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQID--EEQFKKILELIESGKKEG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 827 LK----PRQLDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLS 902
Cdd:cd07141 352 AKlecgGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSN 431
|
410 420 430
....*....|....*....|....*....|..
gi 2515445683 903 KVEAGNVYVNrgTTGAIVRRQPFGGWKRSQVG 934
Cdd:cd07141 432 ALRAGTVWVN--CYNVVSPQAPFGGYKMSGNG 461
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
530-934 |
1.33e-35 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 141.80 E-value: 1.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 530 AEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEEL- 608
Cdd:PRK09406 23 DEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYYAEHAEALl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 609 -DELEG----------VRFSPAPVTAAIPPWNFPL------AIPAgsalapLATGSVVVFKPAEQARRCGAVIAQALWDA 671
Cdd:PRK09406 103 aDEPADaaavgasrayVRYQPLGVVLAVMPWNFPLwqvvrfAAPA------LMAGNVGLLKHASNVPQTALYLADLFRRA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 672 GVSKEALRLVDIHPDEM------AEVGEALVTGSD----QVILTGSIETAKlfrswepdlaVFAETSGKNAIIVTPQADI 741
Cdd:PRK09406 177 GFPDGCFQTLLVGSGAVeailrdPRVAAATLTGSEpagrAVAAIAGDEIKK----------TVLELGGSDPFIVMPSADL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 742 DLAAKDLVQSAFGHAGQKCSAASIAILVGAMgkSERFINQVVDAAESLVVDWPTNPSAEMGPIIEpaagklKRGLTELEP 821
Cdd:PRK09406 247 DRAAETAVTARVQNNGQSCIAAKRFIVHADV--YDAFAEKFVARMAALRVGDPTDPDTDVGPLAT------EQGRDEVEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 822 --------GQTWLLKPRQLDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLD 893
Cdd:PRK09406 319 qvddavaaGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRD 398
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2515445683 894 PDEIKLWLSKVEAGNVYVNRGTTGaiVRRQPFGGWKRSQVG 934
Cdd:PRK09406 399 EAEQERFIDDLEAGQVFINGMTVS--YPELPFGGVKRSGYG 437
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
530-934 |
2.19e-35 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 141.59 E-value: 2.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 530 AEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEA-DVEVSEAIDFANYYADLAEEL 608
Cdd:PRK13473 39 AQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLAlNDEIPAIVDVFRFFAGAARCL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 609 ------DELEG----VRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQ----ARRCGAVIAQALWDaGVs 674
Cdd:PRK13473 119 egkaagEYLEGhtsmIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEItpltALKLAELAADILPP-GV- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 675 kealrlVDIHPDEMAEVGEALVT--GSDQVILTGSIET-AKLFRSWEPDLA-VFAETSGKNAIIVTPQADIDLAAKDLVQ 750
Cdd:PRK13473 197 ------LNVVTGRGATVGDALVGhpKVRMVSLTGSIATgKHVLSAAADSVKrTHLELGGKAPVIVFDDADLDAVVEGIRT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 751 SAFGHAGQKCSAASiAILVGAmGKSERFINQVVDAAESLVVDWPTNPSAEMGPIIepAAGKLKR--GLTELEPGQTW--- 825
Cdd:PRK13473 271 FGYYNAGQDCTAAC-RIYAQR-GIYDDLVAKLAAAVATLKVGDPDDEDTELGPLI--SAAHRDRvaGFVERAKALGHirv 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 826 LLKPRQLDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVE 905
Cdd:PRK13473 347 VTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQ 426
|
410 420
....*....|....*....|....*....
gi 2515445683 906 AGNVYVNrgTTGAIVRRQPFGGWKRSQVG 934
Cdd:PRK13473 427 YGCTWVN--THFMLVSEMPHGGQKQSGYG 453
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
524-934 |
2.83e-35 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 141.56 E-value: 2.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 524 ARVR--TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEAD-VEVSEAIDFANY 600
Cdd:PRK13252 36 ATVQaaTPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQETSvVDIVTGADVLEY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 601 YADLAEELD----ELEGVRF-----SPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDA 671
Cdd:PRK13252 116 YAGLAPALEgeqiPLRGGSFvytrrEPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 672 GVSKEALRLVdihpDEMAEVGEALVTGSD--QVILTGSIETAKlfrswepdlAVFA-----------ETSGKNAIIVTPQ 738
Cdd:PRK13252 196 GLPDGVFNVV----QGDGRVGAWLTEHPDiaKVSFTGGVPTGK---------KVMAaaaaslkevtmELGGKSPLIVFDD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 739 ADIDLAAKDLVQSAFGHAGQKCSAASiAILVGAMGKsERFINQVVDAAESLVVDWPTNPSAEMGPIIEPA-----AGKLK 813
Cdd:PRK13252 263 ADLDRAADIAMLANFYSSGQVCTNGT-RVFVQKSIK-AAFEARLLERVERIRIGDPMDPATNFGPLVSFAhrdkvLGYIE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 814 RGLTElepGQTWLLKPRQLD----DSGRLWSPGIRDGVTPGqdahMT----EYFGPVLGIMRAETLEEAIRLQNAVEFGL 885
Cdd:PRK13252 341 KGKAE---GARLLCGGERLTeggfANGAFVAPTVFTDCTDD----MTivreEIFGPVMSVLTFDDEDEVIARANDTEYGL 413
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2515445683 886 TAGLHSLDPDEIKLWLSKVEAGNVYVNrgTTGAIVRRQPFGGWKRSQVG 934
Cdd:PRK13252 414 AAGVFTADLSRAHRVIHQLEAGICWIN--TWGESPAEMPVGGYKQSGIG 460
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
530-945 |
2.95e-34 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 138.12 E-value: 2.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 530 AEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEEL- 608
Cdd:PRK11241 48 DETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIy 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 609 -DELEG--------VRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEALR 679
Cdd:PRK11241 128 gDTIPGhqadkrliVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFN 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 680 LVDihpDEMAEVGEALVTGS--DQVILTGSIETAK-LFRSWEPDL-AVFAETSGKNAIIVTPQADIDLAAKDLVQSAFGH 755
Cdd:PRK11241 208 VVT---GSAGAVGGELTSNPlvRKLSFTGSTEIGRqLMEQCAKDIkKVSLELGGNAPFIVFDDADLDKAVEGALASKFRN 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 756 AGQKCSAASiaILVGAMGKSERFINQVVDAAESLVVDWPTNPSAEMGPII-EPAAGKLKRGLTE-LEPGQTWLLKPRQLD 833
Cdd:PRK11241 285 AGQTCVCAN--RLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIdEKAVAKVEEHIADaLEKGARVVCGGKAHE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 834 DSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEAGNVYVNR 913
Cdd:PRK11241 363 LGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINT 442
|
410 420 430
....*....|....*....|....*....|...
gi 2515445683 914 GTTGAIVrrQPFGGWKRSQVG-TGSKAGGPNHL 945
Cdd:PRK11241 443 GIISNEV--APFGGIKASGLGrEGSKYGIEDYL 473
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
530-934 |
3.46e-34 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 138.42 E-value: 3.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 530 AEMEQIVAEARKAAP--EWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIV--GEAdVEVSEAIDFANYYADLA 605
Cdd:PLN02766 58 EDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFalGKA-VDIPAAAGLLRYYAGAA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 606 EELD--------ELEGVRF-SPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKE 676
Cdd:PLN02766 137 DKIHgetlkmsrQLQGYTLkEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDG 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 677 ALRLVdihPDEMAEVGEALVT--GSDQVILTGSIETAKLF--RSWEPDLA-VFAETSGKNAIIVTPQADIDLAAKDLVQS 751
Cdd:PLN02766 217 VINVV---TGFGPTAGAAIAShmDVDKVSFTGSTEVGRKImqAAATSNLKqVSLELGGKSPLLIFDDADVDMAVDLALLG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 752 AFGHAGQKCSAASiAILVGAmGKSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAagKLKRGLTELEPGQ----TWLL 827
Cdd:PLN02766 294 IFYNKGEICVASS-RVYVQE-GIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQ--QFEKILSYIEHGKregaTLLT 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 828 KPRQLDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEAG 907
Cdd:PLN02766 370 GGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAG 449
|
410 420
....*....|....*....|....*..
gi 2515445683 908 NVYVNrgTTGAIVRRQPFGGWKRSQVG 934
Cdd:PLN02766 450 TIWVN--CYFAFDPDCPFGGYKMSGFG 474
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
528-934 |
8.46e-33 |
|
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: 133.81 E-value: 8.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGL--SGAERAKILRRAGQVLGERREELIEVAASECGKIVGE-ADVEVSEAIDFANYYADL 604
Cdd:cd07143 42 TEADVDIAVEVAHAAFETDWGLkvSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTFGTaKRVDVQASADTFRYYGGW 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 605 AE-------ELDE--LEGVRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQ----ARRCGAVIAQALWDA 671
Cdd:cd07143 122 ADkihgqviETDIkkLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELtplsALYMTKLIPEAGFPP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 672 GVskealrlVDIHPDEMAEVGEALVT--GSDQVILTGSIETAK--LFRSWEPDLA-VFAETSGKNAIIVTPQADIDLAAK 746
Cdd:cd07143 202 GV-------INVVSGYGRTCGNAISShmDIDKVAFTGSTLVGRkvMEAAAKSNLKkVTLELGGKSPNIVFDDADLESAVV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 747 DLVQSAFGHAGQKCSAASiAILVGAmGKSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAagKLKRGLTELEPGQ--- 823
Cdd:cd07143 275 WTAYGIFFNHGQVCCAGS-RIYVQE-GIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQI--QYERIMSYIESGKaeg 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 824 -TWLLKPRQLDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLS 902
Cdd:cd07143 351 aTVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVAN 430
|
410 420 430
....*....|....*....|....*....|..
gi 2515445683 903 KVEAGNVYVNRGTTgaIVRRQPFGGWKRSQVG 934
Cdd:cd07143 431 ALKAGTVWVNCYNL--LHHQVPFGGYKQSGIG 460
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
536-934 |
1.10e-32 |
|
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: 133.69 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 536 VAEARKA-APEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGK-IVGEADVEVSEAIDFANYYADLAeelDELEG 613
Cdd:cd07144 51 VKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKpYHSNALGDLDEIIAVIRYYAGWA---DKIQG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 614 VRFS------------PAPVTAAIPPWNFPLAIpAGSALAP-LATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEalrL 680
Cdd:cd07144 128 KTIPtspnklaytlhePYGVCGQIIPWNYPLAM-AAWKLAPaLAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPG---V 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 681 VDIHPDEMAEVGEALVT--GSDQVILTGSIETAKLFR--SWEPDLAVFAETSGKNAIIVTPQADIDLAAKDLVQSAFGHA 756
Cdd:cd07144 204 VNIIPGYGAVAGSALAEhpDVDKIAFTGSTATGRLVMkaAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNS 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 757 GQKCSAASiAILVGAmGKSERFINQVVDAA-ESLVVDWPTNPSAEMGPII-----EPAAGKLKRGLTE---LEPGQTwll 827
Cdd:cd07144 284 GQNCTATS-RIYVQE-SIYDKFVEKFVEHVkQNYKVGSPFDDDTVVGPQVsktqyDRVLSYIEKGKKEgakLVYGGE--- 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 828 KPRQLDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEAG 907
Cdd:cd07144 359 KAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAG 438
|
410 420
....*....|....*....|....*..
gi 2515445683 908 NVYVNRGTTGAIvrRQPFGGWKRSQVG 934
Cdd:cd07144 439 MVWINSSNDSDV--GVPFGGFKMSGIG 463
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
528-934 |
1.17e-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: 133.35 E-value: 1.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEA-DVEVSEAIDFANYYAD--L 604
Cdd:cd07117 36 TDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETrAVDIPLAADHFRYFAGviR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 605 AEE-----LDE--LEGVRFSPAPVTAAIPPWNFPLAIPAGSaLAP-LATGSVVVFKPAEQARRCGAVIAQALWD---AGV 673
Cdd:cd07117 116 AEEgsanmIDEdtLSIVLREPIGVVGQIIPWNFPFLMAAWK-LAPaLAAGNTVVIKPSSTTSLSLLELAKIIQDvlpKGV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 674 skealrlVDIHPDEMAEVGEALVT--GSDQVILTGSIETAKLFRSWEPDLAVFA--ETSGKNAIIVTPQADIDLAAKDLV 749
Cdd:cd07117 195 -------VNIVTGKGSKSGEYLLNhpGLDKLAFTGSTEVGRDVAIAAAKKLIPAtlELGGKSANIIFDDANWDKALEGAQ 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 750 QSAFGHAGQKCSAASiAILVGAmGKSERFINQVVDAAESLVVDWPTNPSAEMGPIIEpaAGKLKRGLT----ELEPGQTW 825
Cdd:cd07117 268 LGILFNQGQVCCAGS-RIFVQE-GIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVN--KDQLDKILSyvdiAKEEGAKI 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 826 LLKPRQLD----DSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWL 901
Cdd:cd07117 344 LTGGHRLTenglDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVA 423
|
410 420 430
....*....|....*....|....*....|...
gi 2515445683 902 SKVEAGNVYVNrgTTGAIVRRQPFGGWKRSQVG 934
Cdd:cd07117 424 RAVETGRVWVN--TYNQIPAGAPFGGYKKSGIG 454
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
528-934 |
1.63e-32 |
|
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: 132.85 E-value: 1.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEA-DVEVSEAIDFANYYAD--L 604
Cdd:cd07559 36 TAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRETlAADIPLAIDHFRYFAGviR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 605 AEE-----LDE--LEGVRFSPAPVTAAIPPWNFPLAIpAGSALAP-LATGSVVVFKPAEQARRCGAVIAQALWD---AGV 673
Cdd:cd07559 116 AQEgslseIDEdtLSYHFHEPLGVVGQIIPWNFPLLM-AAWKLAPaLAAGNTVVLKPASQTPLSILVLMELIGDllpKGV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 674 skealrlVDIHPDEMAEVGEALVT--GSDQVILTGSIETAKLFRSWEPDLAVFA--ETSGKNAIIVTPQA-----DIDLA 744
Cdd:cd07559 195 -------VNVVTGFGSEAGKPLAShpRIAKLAFTGSTTVGRLIMQYAAENLIPVtlELGGKSPNIFFDDAmdaddDFDDK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 745 AKDlVQSAFG-HAGQKCSAASiAILVGAmGKSERFINQVVDAAESLVVDWPTNPSAEMGPIIepAAGKLKRGLTEL---- 819
Cdd:cd07559 268 AEE-GQLGFAfNQGEVCTCPS-RALVQE-SIYDEFIERAVERFEAIKVGNPLDPETMMGAQV--SKDQLEKILSYVdigk 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 820 EPGQTWLLKPRQL----DDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPD 895
Cdd:cd07559 343 EEGAEVLTGGERLtlggLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDIN 422
|
410 420 430
....*....|....*....|....*....|....*....
gi 2515445683 896 EIKLWLSKVEAGNVYVNrgTTGAIVRRQPFGGWKRSQVG 934
Cdd:cd07559 423 RALRVARGIQTGRVWVN--CYHQYPAHAPFGGYKKSGIG 459
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
553-936 |
6.27e-31 |
|
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: 127.92 E-value: 6.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 553 ERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYyadLAEELDELEGVRF---------------- 616
Cdd:cd07148 45 ERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVEL---AADELGQLGGREIpmgltpasagriaftt 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 617 -SPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEALRLVdihPDEmAEVGEAL 695
Cdd:cd07148 122 rEPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAV---PCE-NAVAEKL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 696 VTGSDQVILT--GSIETAKLFRS-WEPDLAVFAETSGKNAIIVTPQADIDLAAKDLVQSAFGHAGQKCsaASIAILVGAM 772
Cdd:cd07148 198 VTDPRVAFFSfiGSARVGWMLRSkLAPGTRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVC--VSVQRVFVPA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 773 GKSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPA-AGKLKRGLTE-LEPGQTWLLKPRQLDDSgrLWSPGIRdgVTPG 850
Cdd:cd07148 276 EIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPReVDRVEEWVNEaVAAGARLLCGGKRLSDT--TYAPTVL--LDPP 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 851 QDAHMT--EYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEAGNVYVNRGTTGAiVRRQPFGGW 928
Cdd:cd07148 352 RDAKVStqEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFR-VDWMPFAGR 430
|
....*...
gi 2515445683 929 KRSQVGTG 936
Cdd:cd07148 431 RQSGYGTG 438
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
528-935 |
2.09e-30 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 126.79 E-value: 2.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADlaee 607
Cdd:PLN00412 51 TQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAE---- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 608 ldelEGVRF-------------------------SPAPVTAAIPPWNFPLAIpAGSALAP-LATGSVVVFKPAEQARRCG 661
Cdd:PLN00412 127 ----EGVRIlgegkflvsdsfpgnernkycltskIPLGVVLAIPPFNYPVNL-AVSKIAPaLIAGNAVVLKPPTQGAVAA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 662 AVIAQALWDAGVSKEalrLVDIHPDEMAEVGEALVT--GSDQVILTGS---IETAKLFRSwepdLAVFAETSGKNAIIVT 736
Cdd:PLN00412 202 LHMVHCFHLAGFPKG---LISCVTGKGSEIGDFLTMhpGVNCISFTGGdtgIAISKKAGM----VPLQMELGGKDACIVL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 737 PQADIDLAAKDLVQSAFGHAGQKCSAASIAILVGAMgkSERFINQVVDAAESLVVDWPTNpSAEMGPIIEPAAGKLKRGL 816
Cdd:PLN00412 275 EDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESV--ADALVEKVNAKVAKLTVGPPED-DCDITPVVSESSANFIEGL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 817 TE--LEPGQTWLLKPRQlddSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDP 894
Cdd:PLN00412 352 VMdaKEKGATFCQEWKR---EGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDI 428
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2515445683 895 DEIKLWLSKVEAGNVYVNrgttGAIVR---RQPFGGWKRSQVGT 935
Cdd:PLN00412 429 NKAILISDAMETGTVQIN----SAPARgpdHFPFQGLKDSGIGS 468
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
528-912 |
2.70e-28 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 121.78 E-value: 2.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEAD------VEVSE------AI 595
Cdd:PLN02419 149 TNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHgdifrgLEVVEhacgmaTL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 596 DFANYYADLAEELDELEgVRfSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSK 675
Cdd:PLN02419 229 QMGEYLPNVSNGVDTYS-IR-EPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 676 EALRLVDIHPDEMaevgEALVTGSD--QVILTGSiETAKLF---RSWEPDLAVFAETSGKNAIIVTPQADIDLAAKDLVQ 750
Cdd:PLN02419 307 GVLNIVHGTNDTV----NAICDDEDirAVSFVGS-NTAGMHiyaRAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLA 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 751 SAFGHAGQKCSAASIAILVGamgKSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAAGKLKRGLTE--LEPGQTWLLK 828
Cdd:PLN02419 382 AGFGAAGQRCMALSTVVFVG---DAKSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQsgVDDGAKLLLD 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 829 PRQL----DDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKV 904
Cdd:PLN02419 459 GRDIvvpgYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDI 538
|
....*...
gi 2515445683 905 EAGNVYVN 912
Cdd:PLN02419 539 EAGQIGIN 546
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
614-940 |
2.83e-28 |
|
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: 119.25 E-value: 2.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 614 VRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQaLWDAGVSKEALRLVDIHPDEMAEVGE 693
Cdd:cd07135 104 IRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAE-LVPKYLDPDAFQVVQGGVPETTALLE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 694 A-----LVTGSDQViltGSIETAKLFRSWEPdlaVFAETSGKNAIIVTPQADIDLAAKDLVQSAFGHAGQKCSAASIaIL 768
Cdd:cd07135 183 QkfdkiFYTGSGRV---GRIIAEAAAKHLTP---VTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDY-VL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 769 VgamgkSERFINQVVDAAESLVVD-WP--TNPSAEMGPIIEPAAGKLKRGLTELEPGQTWLlkPRQLDDSGRLWSPGIRD 845
Cdd:cd07135 256 V-----DPSVYDEFVEELKKVLDEfYPggANASPDYTRIVNPRHFNRLKSLLDTTKGKVVI--GGEMDEATRFIPPTIVS 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 846 GVTPGqDAHMT-EYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEAGNVYVNRGTTGAIVRRQP 924
Cdd:cd07135 329 DVSWD-DSLMSeELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNAP 407
|
330
....*....|....*.
gi 2515445683 925 FGGWKRSqvGTGSKAG 940
Cdd:cd07135 408 FGGVGDS--GYGAYHG 421
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
536-934 |
4.24e-27 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 117.22 E-value: 4.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 536 VAEARKAAPE--WAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGE-ADVEVSEAIDFANYYADLAEELDELE 612
Cdd:PLN02466 101 VAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQsAKAELPMFARLFRYYAGWADKIHGLT 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 613 G---------VRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEALRLVDI 683
Cdd:PLN02466 181 VpadgphhvqTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSG 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 684 HPdemAEVGEALVT--GSDQVILTGSIETAKLFR--SWEPDL-AVFAETSGKNAIIVTPQADIDLAAkDLVQSA-FGHAG 757
Cdd:PLN02466 261 FG---PTAGAALAShmDVDKLAFTGSTDTGKIVLelAAKSNLkPVTLELGGKSPFIVCEDADVDKAV-ELAHFAlFFNQG 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 758 QKCSAASIAILvgamgkSERFINQVVDAAESL----VVDWPTNPSAEMGPIIEPAA-----GKLKRGLtelEPGQTWLLK 828
Cdd:PLN02466 337 QCCCAGSRTFV------HERVYDEFVEKAKARalkrVVGDPFKKGVEQGPQIDSEQfekilRYIKSGV---ESGATLECG 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 829 PRQLDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEAGN 908
Cdd:PLN02466 408 GDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGT 487
|
410 420
....*....|....*....|....*...
gi 2515445683 909 VYVNRGTT--GAIvrrqPFGGWKRSQVG 934
Cdd:PLN02466 488 VWVNCFDVfdAAI----PFGGYKMSGIG 511
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
528-940 |
4.93e-27 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 116.86 E-value: 4.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEE 607
Cdd:PLN02315 54 SLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 608 L----------DELEGVRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRcgAVIAQALWDAGV-SKE 676
Cdd:PLN02315 134 LngsiipserpNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPL--ITIAMTKLVAEVlEKN 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 677 ALrlvdihPDEM-------AEVGEALVTGS--DQVILTGSIETAKLFRSwepdlAVFA-------ETSGKNAIIVTPQAD 740
Cdd:PLN02315 212 NL------PGAIftsfcggAEIGEAIAKDTriPLVSFTGSSKVGLMVQQ-----TVNArfgkcllELSGNNAIIVMDDAD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 741 IDLAAKDLVQSAFGHAGQKCSAASIAILVGAMgkSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAAGK-LKRGLTEL 819
Cdd:PLN02315 281 IQLAVRSVLFAAVGTAGQRCTTCRRLLLHESI--YDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKnFEKGIEII 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 820 EP-GQTWLLKPRQLDDSGRLWSPGIRDgVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIK 898
Cdd:PLN02315 359 KSqGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIF 437
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2515445683 899 LWLSKV--EAGNVYVNRGTTGAIVrRQPFGGWKRSqvGTGSKAG 940
Cdd:PLN02315 438 KWIGPLgsDCGIVNVNIPTNGAEI-GGAFGGEKAT--GGGREAG 478
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
530-934 |
1.71e-26 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 114.99 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 530 AEMEQIVAEARKA--APEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGK-IVGEADVEVSEAIDFANYYADLAE 606
Cdd:PRK09847 57 VDIDRAVSAARGVfeRGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKpIRHSLRDDIPGAARAIRWYAEAID 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 607 EL---------DELEGVRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEA 677
Cdd:PRK09847 137 KVygevattssHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 678 LRLVdihPDEMAEVGEALVTGSDQVIL--TGSIETAK--LFRSWEPDLA-VFAETSGKNA-IIVTPQADIDLAAKDLVQS 751
Cdd:PRK09847 217 LNVV---TGFGHEAGQALSRHNDIDAIafTGSTRTGKqlLKDAGDSNMKrVWLEAGGKSAnIVFADCPDLQQAASATAAG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 752 AFGHAGQKCSAASIAILVGAMgkSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPA-AGKLKRGLTELEPGQTWLLKPR 830
Cdd:PRK09847 294 IFYNQGQVCIAGTRLLLEESI--ADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAhADSVHSFIREGESKGQLLLDGR 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 831 QLDDSGRLwSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEAGNVY 910
Cdd:PRK09847 372 NAGLAAAI-GPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVF 450
|
410 420
....*....|....*....|....
gi 2515445683 911 VNRGTTGAIVrrQPFGGWKRSQVG 934
Cdd:PRK09847 451 VNNYNDGDMT--VPFGGYKQSGNG 472
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
528-934 |
1.96e-25 |
|
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: 111.43 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKA--APEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEA-DVEVSEAIDFANYYADL 604
Cdd:cd07140 41 TVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLAlKTHVGMSIQTFRYFAGW 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 605 AeelDELEG----------------VRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQAL 668
Cdd:cd07140 121 C---DKIQGktipinqarpnrnltlTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 669 WDAGVSKEalrLVDIHPDEMAEVGEALVTGSD--QVILTGSIETAK-LFRSW-EPDL-AVFAETSGKNAIIVTPQADIDL 743
Cdd:cd07140 198 VKAGFPKG---VINILPGSGSLVGQRLSDHPDvrKLGFTGSTPIGKhIMKSCaVSNLkKVSLELGGKSPLIIFADCDMDK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 744 AAKDLVQSAFGHAGQKCSAASIAILVGAMgkSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPA-AGKL----KRGLTE 818
Cdd:cd07140 275 AVRMGMSSVFFNKGENCIAAGRLFVEESI--HDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAhLDKLveycERGVKE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 819 lepGQTWLLKPRQLDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAET--LEEAIRLQNAVEFGLTAGLHSLDPDE 896
Cdd:cd07140 353 ---GATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDgdVDGVLQRANDTEYGLASGVFTKDINK 429
|
410 420 430
....*....|....*....|....*....|....*...
gi 2515445683 897 IKLWLSKVEAGNVYVNrgTTGAIVRRQPFGGWKRSQVG 934
Cdd:cd07140 430 ALYVSDKLEAGTVFVN--TYNKTDVAAPFGGFKQSGFG 465
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
533-940 |
5.08e-25 |
|
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: 109.54 E-value: 5.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 533 EQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELI------------EVAASECGKIVGEAD------------ 588
Cdd:cd07087 1 AELVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAaalyadlgkppaEAYLTEIAVVLGEIDhalkhlkkwmkp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 589 --VEVSEAIDFANYYadlaeeldelegVRFSPAPVTAAIPPWNFPLAIpagsALAPL----ATGSVVVFKPAEQARRCGA 662
Cdd:cd07087 81 rrVSVPLLLQPAKAY------------VIPEPLGVVLIIGPWNYPLQL----ALAPLigaiAAGNTVVLKPSELAPATSA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 663 VIAQaLWDAGVSKEALRLV--DihpdemAEVGEALVT-GSDQVILTGSIETAKL-FRSWEPDLA-VFAETSGKNAIIVTP 737
Cdd:cd07087 145 LLAK-LIPKYFDPEAVAVVegG------VEVATALLAePFDHIFFTGSPAVGKIvMEAAAKHLTpVTLELGGKSPCIVDK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 738 QADIDLAAKDLVQSAFGHAGQKCsaasIA---ILVGamgKS--ERFINQVVDAAESLvvdWPTNP--SAEMGPII-EPAA 809
Cdd:cd07087 218 DANLEVAARRIAWGKFLNAGQTC----IApdyVLVH---ESikDELIEELKKAIKEF---YGEDPkeSPDYGRIInERHF 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 810 GKLKrGLteLEPGQtwLLKPRQLDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGL 889
Cdd:cd07087 288 DRLA-SL--LDDGK--VVIGGQVDKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYL 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2515445683 890 HSLDPDEIKLWLSKVEAGNVYVNRGTTGAIVRRQPFGGWKRSqvGTGS---KAG 940
Cdd:cd07087 363 FSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGGVGNS--GMGAyhgKAG 414
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
528-950 |
2.58e-22 |
|
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: 101.76 E-value: 2.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 528 TVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGE---ADVEVseAIDFANYYADL 604
Cdd:cd07116 36 TAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVREtlaADIPL--AIDHFRYFAGC 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 605 --AEE--LDELEGVRFS-----PAPVTAAIPPWNFPLAIpAGSALAP-LATGSVVVFKPAEQARRCGAVIAQALWD---A 671
Cdd:cd07116 114 irAQEgsISEIDENTVAyhfhePLGVVGQIIPWNFPLLM-ATWKLAPaLAAGNCVVLKPAEQTPASILVLMELIGDllpP 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 672 GVskealrlVDIHPDEMAEVGEALVTGSD--QVILTGSIETAKLFRSWEPD--LAVFAETSGKNAII----VTPQAD--I 741
Cdd:cd07116 193 GV-------VNVVNGFGLEAGKPLASSKRiaKVAFTGETTTGRLIMQYASEniIPVTLELGGKSPNIffadVMDADDafF 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 742 DLAAKDLVQSAFgHAGQKCSAASIAILVGAMgkSERFINQVVDAAESLVVDWPTNPSAEMGPiiEPAAGKLKRGLTELEP 821
Cdd:cd07116 266 DKALEGFVMFAL-NQGEVCTCPSRALIQESI--YDRFMERALERVKAIKQGNPLDTETMIGA--QASLEQLEKILSYIDI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 822 GQTwlLKPRQLDDSGRLWSPGIRDG-------VTPGQDAHM--TEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSL 892
Cdd:cd07116 341 GKE--EGAEVLTGGERNELGGLLGGgyyvpttFKGGNKMRIfqEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTR 418
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2515445683 893 DPDEIKLWLSKVEAGNVYVNrgTTGAIVRRQPFGGWKRSQVGTgskaggPNHLIGMSH 950
Cdd:cd07116 419 DGNTAYRMGRGIQAGRVWTN--CYHLYPAHAAFGGYKQSGIGR------ENHKMMLDH 468
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
540-954 |
1.80e-20 |
|
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: 95.76 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 540 RKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVE----VSEAIDFAnyyadlAEELDE----- 610
Cdd:cd07134 8 QAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTeilpVLSEINHA------IKHLKKwmkpk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 611 -------LEG----VRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAgvskealr 679
Cdd:cd07134 82 rvrtpllLFGtkskIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 680 lvdIHPDEMA------EVGEALV---------TGSDQV---ILTGSietAKLFRSwepdlaVFAETSGKNAIIVTPQADI 741
Cdd:cd07134 154 ---FDEDEVAvfegdaEVAQALLelpfdhiffTGSPAVgkiVMAAA---AKHLAS------VTLELGGKSPTIVDETADL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 742 DLAAKDLVQSAFGHAGQKCsaasIA---ILVGAmGKSERFINQVVDA-AESLVVDWPTNPSAEMGPII-EPAAGKLKRGL 816
Cdd:cd07134 222 KKAAKKIAWGKFLNAGQTC----IApdyVFVHE-SVKDAFVEHLKAEiEKFYGKDAARKASPDLARIVnDRHFDRLKGLL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 817 TE-LEPGQTwLLKPRQLDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPD 895
Cdd:cd07134 297 DDaVAKGAK-VEFGGQFDAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKA 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2515445683 896 EIKLWLSKVEAGNVYVNRGTTGAIVRRQPFGGWKRSQVGtgsKAGGPNHLIGMSHAEPV 954
Cdd:cd07134 376 NVNKVLARTSSGGVVVNDVVLHFLNPNLPFGGVNNSGIG---SYHGVYGFKAFSHERAV 431
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
554-954 |
5.66e-19 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 91.63 E-value: 5.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 554 RAKILRRAGQVLGERREELIEVAASECGK-----IVGEADVEVSEaIDF--ANYYADLAEELDELEGV--------RFSP 618
Cdd:PTZ00381 31 RKQQLRNLLRMLEENKQEFSEAVHKDLGRhpfetKMTEVLLTVAE-IEHllKHLDEYLKPEKVDTVGVfgpgksyiIPEP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 619 APVTAAIPPWNFPL---AIPAGSAlapLATGSVVVFKPAEQARRCGAVIAQaLWDAGVSKEALRLVdihpDEMAEVGEAL 695
Cdd:PTZ00381 110 LGVVLVIGAWNYPLnltLIPLAGA---IAAGNTVVLKPSELSPHTSKLMAK-LLTKYLDPSYVRVI----EGGVEVTTEL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 696 VTGS-DQVILTGSIETAKLFR--SWEPDLAVFAETSGKNAIIVTPQADIDLAAKDLVQSAFGHAGQKCSAASIAILVGAM 772
Cdd:PTZ00381 182 LKEPfDHIFFTGSPRVGKLVMqaAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 773 gkSERFINQVVDAAESLVVDWPTNpSAEMGPIIEPAAGKLKRGLTELEPGQtwLLKPRQLDDSGRLWSPGIRDGVTPgQD 852
Cdd:PTZ00381 262 --KDKFIEALKEAIKEFFGEDPKK-SEDYSRIVNEFHTKRLAELIKDHGGK--VVYGGEVDIENKYVAPTIIVNPDL-DS 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 853 AHMT-EYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEAGNVYVNRGTTGAIVRRQPFGGWKRS 931
Cdd:PTZ00381 336 PLMQeEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPFGGVGNS 415
|
410 420
....*....|....*....|....
gi 2515445683 932 QVGT-GSKAGgpnhLIGMSHAEPV 954
Cdd:PTZ00381 416 GMGAyHGKYG----FDTFSHPKPV 435
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
533-896 |
2.43e-18 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 89.52 E-value: 2.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 533 EQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEELDELe 612
Cdd:cd07129 2 DAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVREGSWL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 613 GVRFSPAPVTAAIPPW-------------------NFPLA--IPAGSALAPLATGSVVVFK--PA--EQARRCGAVIAQA 667
Cdd:cd07129 81 DARIDPADPDRQPLPRpdlrrmlvplgpvavfgasNFPLAfsVAGGDTASALAAGCPVVVKahPAhpGTSELVARAIRAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 668 LWDAGVSKEALRLVDihpDEMAEVGEALVtgSDQVI----LTGSIETAK-LFrswepDLA--------VFAETSGKNAII 734
Cdd:cd07129 161 LRATGLPAGVFSLLQ---GGGREVGVALV--KHPAIkavgFTGSRRGGRaLF-----DAAaarpepipFYAELGSVNPVF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 735 VTPQA---DIDLAAKDLVQSAFGHAGQKCSAASIAILVGAMGkSERFINQVVDAAESLVvdwptnPSAEMGPIIepaAGK 811
Cdd:cd07129 231 ILPGAlaeRGEAIAQGFVGSLTLGAGQFCTNPGLVLVPAGPA-GDAFIAALAEALAAAP------AQTMLTPGI---AEA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 812 LKRGLTELE--PGQTWLLKPRQLDDSgrlWSPGIRDGVTPGQDAH-----MTEYFGPVLGIMRAETLEEAIRLQNAVEFG 884
Cdd:cd07129 301 YRQGVEALAaaPGVRVLAGGAAAEGG---NQAAPTLFKVDAAAFLadpalQEEVFGPASLVVRYDDAAELLAVAEALEGQ 377
|
410
....*....|..
gi 2515445683 885 LTAGLHSLDPDE 896
Cdd:cd07129 378 LTATIHGEEDDL 389
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
533-942 |
3.06e-18 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 88.83 E-value: 3.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 533 EQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGK---IVGEAD---VEVSEAIDFANYYADLAE 606
Cdd:cd07084 2 ERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKgwmFAENICgdqVQLRARAFVIYSYRIPHE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 607 ELDELEGVR-------FSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEALr 679
Cdd:cd07084 82 PGNHLGQGLkqqshgyRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLLPPED- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 680 LVDIHPDEMAEVGEALVTGSDQVILTGSIETAKLFRSWEPDLAVFAETSGKNAIIVTPQAD-IDLAAKDLVQSAFGHAGQ 758
Cdd:cd07084 161 VTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 759 KCSAASiAILVGAMGKSERFINQVVDAAESLVVDwptnpSAEMGPIIEPA--AGKLKRGlTELEPGQTWLLKPRQLDDSG 836
Cdd:cd07084 241 KCTAQS-MLFVPENWSKTPLVEKLKALLARRKLE-----DLLLGPVQTFTtlAMIAHME-NLLGSVLLFSGKELKNHSIP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 837 RLWSPGIR-------DGVTPGQDAHMTEYFGPVLGIMR------AETLEEAIRLQNAvefgLTAGLHSLDPDEI-KLWLS 902
Cdd:cd07084 314 SIYGACVAsalfvpiDEILKTYELVTEEIFGPFAIVVEykkdqlALVLELLERMHGS----LTAAIYSNDPIFLqELIGN 389
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2515445683 903 KVEAGNVY-VNRGTTGAIVRRQPFGGWKRSQVGTGSkaGGP 942
Cdd:cd07084 390 LWVAGRTYaILRGRTGVAPNQNHGGGPAADPRGAGI--GGP 428
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
614-954 |
2.31e-17 |
|
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: 86.00 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 614 VRFSPAPVTAAIPPWNFPLAIpagsALAPLAT----GSVVVFKPAEQARRCGAVIAQALWDAgvskealrlvdIHPDEMA 689
Cdd:cd07133 97 VEYQPLGVVGIIVPWNYPLYL----ALGPLIAalaaGNRVMIKPSEFTPRTSALLAELLAEY-----------FDEDEVA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 690 EV-GEALVtGS-------DQVILTGSIETAKL-FRSWEPDLA-VFAETSGKNAIIVTPQADIDLAAKDLVQSAFGHAGQK 759
Cdd:cd07133 162 VVtGGADV-AAafsslpfDHLLFTGSTAVGRHvMRAAAENLTpVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 760 CsaasIA---ILVGAmGKSERFINQVVDAAESLVVDWPTNPsaEMGPII------------EPAAGKLKRgLTELEPGQt 824
Cdd:cd07133 241 C----VApdyVLVPE-DKLEEFVAAAKAAVAKMYPTLADNP--DYTSIInerhyarlqgllEDARAKGAR-VIELNPAG- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 825 wllkprQLDDSGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKV 904
Cdd:cd07133 312 ------EDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRT 385
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2515445683 905 EAGNVYVNRGTTGAIVRRQPFGGWKRSqvGTGS---KAGgpnhLIGMSHAEPV 954
Cdd:cd07133 386 HSGGVTINDTLLHVAQDDLPFGGVGAS--GMGAyhgKEG----FLTFSHAKPV 432
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
554-927 |
2.34e-16 |
|
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: 83.04 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 554 RAKILRRAGQVLGERREELIEVAASECGK-----IVGEADV---EVSEAIDFANYYA-------DLAEELDELEgVRFSP 618
Cdd:cd07132 22 RIQQLEALLRMLEENEDEIVEALAKDLRKpkfeaVLSEILLvknEIKYAISNLPEWMkpepvkkNLATLLDDVY-IYKEP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 619 APVTAAIPPWNFPLAIpagsALAPL----ATGSVVVFKPAEQARRCGAVIAQALwDAGVSKEALRLVDIHPDEMAEVgea 694
Cdd:cd07132 101 LGVVLIIGAWNYPLQL----TLVPLvgaiAAGNCVVIKPSEVSPATAKLLAELI-PKYLDKECYPVVLGGVEETTEL--- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 695 LVTGSDQVILTGSIETAKLFRSwepdlA-------VFAETSGKNAIIVTPQADIDLAAKDLVQSAFGHAGQKCsaasIA- 766
Cdd:cd07132 173 LKQRFDYIFYTGSTSVGKIVMQ-----AaakhltpVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTC----IAp 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 767 --ILVgamgkSERFINQVVDAAESLVVDW-PTNP--SAEMGPIIEpaAGKLKRgLTELEPGQTwLLKPRQLDDSGRLWSP 841
Cdd:cd07132 244 dyVLC-----TPEVQEKFVEALKKTLKEFyGEDPkeSPDYGRIIN--DRHFQR-LKKLLSGGK-VAIGGQTDEKERYIAP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 842 GIRDGVTPgQDAHM-TEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEAGNVYVNRGTTGAIV 920
Cdd:cd07132 315 TVLTDVKP-SDPVMqEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTL 393
|
....*..
gi 2515445683 921 RRQPFGG 927
Cdd:cd07132 394 DSLPFGG 400
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
518-897 |
3.85e-14 |
|
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: 76.54 E-value: 3.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 518 VQGADDARVRTVA-EMEQIVAEAR-KAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASEcGKIVGEADVEVSEAI 595
Cdd:cd07128 23 VTGEVVARVSSEGlDFAAAVAYAReKGGPALRALTFHERAAMLKALAKYLMERKEDLYALSAAT-GATRRDSWIDIDGGI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 596 DFANYYADLAEELDELEGV-------------RF------SPAP-VTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAE 655
Cdd:cd07128 102 GTLFAYASLGRRELPNAHFlvegdveplskdgTFvgqhilTPRRgVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPAT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 656 QarrcGAVIAQAL----WDAGVSKE-ALRLVdihpdeMAEVGEAL--VTGSDQVILTGSIETAKLFRSwEPDLA-----V 723
Cdd:cd07128 182 A----TAYLTEAVvkdiVESGLLPEgALQLI------CGSVGDLLdhLGEQDVVAFTGSAATAAKLRA-HPNIVarsirF 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 724 FAETSGKNAIIVTPQA-----DIDLAAKDLVQSAFGHAGQKCSAASIAILvgamgkSERFINQVVDAA----ESLVVDWP 794
Cdd:cd07128 251 NAEADSLNAAILGPDAtpgtpEFDLFVKEVAREMTVKAGQKCTAIRRAFV------PEARVDAVIEALkarlAKVVVGDP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 795 TNPSAEMGPII-----EPAAGKLKRGLTELE---PGQTWLLKPRQLDDSGRLWSPGIRDGVTPGQDA--HMTEYFGPVLG 864
Cdd:cd07128 325 RLEGVRMGPLVsreqrEDVRAAVATLLAEAEvvfGGPDRFEVVGADAEKGAFFPPTLLLCDDPDAATavHDVEAFGPVAT 404
|
410 420 430
....*....|....*....|....*....|...
gi 2515445683 865 IMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEI 897
Cdd:cd07128 405 LMPYDSLAEAIELAARGRGSLVASVVTNDPAFA 437
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
549-895 |
1.67e-13 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 74.74 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 549 LSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVEVSEAIDFANYYADLAEELDEL------EGVRFSPAP-- 620
Cdd:PRK11903 60 LTYAQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAKLGAALGDArllrdgEAVQLGKDPaf 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 621 -----------VTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQArrcgAVIAQALW----DAGVSKE-ALRLVDIH 684
Cdd:PRK11903 140 qgqhvlvptrgVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATAT----AWLTQRMVkdvvAAGILPAgALSVVCGS 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 685 P-DEMAEVGealvtGSDQVILTGSIETAKLFRSwEPDLA-----VFAETSGKNAIIVTPQAD-----IDLAAKDLVQSAF 753
Cdd:PRK11903 216 SaGLLDHLQ-----PFDVVSFTGSAETAAVLRS-HPAVVqrsvrVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMT 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 754 GHAGQKCSAASiAILVGAmGKSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPA------AG--KLKRGLTELEPGQTw 825
Cdd:PRK11903 290 VKSGQKCTAIR-RIFVPE-ALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAqlaavrAGlaALRAQAEVLFDGGG- 366
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2515445683 826 lLKPRQLDDSGRLWSPGIRDGVTPGQDA---HMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPD 895
Cdd:PRK11903 367 -FALVDADPAVAACVGPTLLGASDPDAAtavHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAA 438
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
614-927 |
1.84e-13 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 74.08 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 614 VRFSPAPVTAAIPPWNFPLAIpagsALAPL----ATGSVVVFKPAEQARRCGAVIAQALWDAgVSKEALRLVDihPDemA 689
Cdd:cd07136 96 IYYEPYGVVLIIAPWNYPFQL----ALAPLigaiAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVE--GG--V 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 690 EVGEALVTGS-DQVILTGSIETAKLfrswepdlaVFA-----------ETSGKNAIIVTPQADIDLAAKDLVQSAFGHAG 757
Cdd:cd07136 167 EENQELLDQKfDYIFFTGSVRVGKI---------VMEaaakhltpvtlELGGKSPCIVDEDANLKLAAKRIVWGKFLNAG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 758 QKCsaasIA---ILVGAMGKsERFINQVVDAAESLVVDWPTNpSAEMGPIIEpaAGKLKRGLTELEPGQtwLLKPRQLDD 834
Cdd:cd07136 238 QTC----VApdyVLVHESVK-EKFIKELKEEIKKFYGEDPLE-SPDYGRIIN--EKHFDRLAGLLDNGK--IVFGGNTDR 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 835 SGRLWSPGIRDGVTPgQDAHM-TEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEAGNVYVNR 913
Cdd:cd07136 308 ETLYIEPTILDNVTW-DDPVMqEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCIND 386
|
330
....*....|....
gi 2515445683 914 GTTGAIVRRQPFGG 927
Cdd:cd07136 387 TIMHLANPYLPFGG 400
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
526-934 |
8.08e-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: 68.98 E-value: 8.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 526 VRTVAEMEQIVAEARKAAPEWaglsgaeRAKILRRAGQVLGERREELIEVAASECGKIVGEADV-EVSEAIDFANyyadL 604
Cdd:cd07137 2 PRLVRELRETFRSGRTRSAEW-------RKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRdEVSVLVSSCK----L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 605 A-EELDELEGVRFSPAPVTA----------------AIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQa 667
Cdd:cd07137 71 AiKELKKWMAPEKVKTPLTTfpakaeivseplgvvlVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAK- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 668 LWDAGVSKEALRLVDIHPDEmaevGEALVTGS-DQVILTGSIETAKLF-----RSWEPdlaVFAETSGKNAIIVTPQADI 741
Cdd:cd07137 150 LIPEYLDTKAIKVIEGGVPE----TTALLEQKwDKIFFTGSPRVGRIImaaaaKHLTP---VTLELGGKCPVIVDSTVDL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 742 DLAAKDLVQSAFG-HAGQKCSAASIaILVgamgkSERFINQVVDAAESLVVD-WPTNP--SAEMGPIIEPAAGKLKRGLT 817
Cdd:cd07137 223 KVAVRRIAGGKWGcNNGQACIAPDY-VLV-----EESFAPTLIDALKNTLEKfFGENPkeSKDLSRIVNSHHFQRLSRLL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 818 ELEPGQTWLLKPRQLDDSGRLWSPGIRDGVtPGQDAHMT-EYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDE 896
Cdd:cd07137 297 DDPSVADKIVHGGERDEKNLYIEPTILLDP-PLDSSIMTeEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKEL 375
|
410 420 430
....*....|....*....|....*....|....*...
gi 2515445683 897 IKLWLSKVEAGNVYVNRGTTGAIVRRQPFGGWKRSQVG 934
Cdd:cd07137 376 KRRIVAETSSGGVTFNDTVVQYAIDTLPFGGVGESGFG 413
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
532-919 |
3.17e-10 |
|
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: 63.66 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 532 MEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADVE----VSEAIdfANYYADL--- 604
Cdd:cd07122 1 VDELVERARKAQREFATFSQEQVDKIVEAVAWAAADAAEELAKMAVEETGMGVVEDKVIknhfASEYV--YNDIKDMktv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 605 -AEELDELEGVRFSPAP---VTAAIPPWNfPLAIPAGSALAPLATGSVVVFKPAEQARRCgaviaqalwdagvSKEALRL 680
Cdd:cd07122 79 gVIEEDEEKGIVEIAEPvgvIAALIPSTN-PTSTAIFKALIALKTRNAIIFSPHPRAKKC-------------SIEAAKI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 681 VDihpDEMAEVG--EALVtgsdQVILTGSIE-TAKLFRSwePDLAVF-----------AETSGKNAIIVTP--------- 737
Cdd:cd07122 145 MR---EAAVAAGapEGLI----QWIEEPSIElTQELMKH--PDVDLIlatggpgmvkaAYSSGKPAIGVGPgnvpayide 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 738 QADIDLAAKDLVQSafghagqkcsaasiailvgamgKSerFINQVVDAAE-SLVVDwptnpsaemgpiiEPAAGKLKRGL 816
Cdd:cd07122 216 TADIKRAVKDIILS----------------------KT--FDNGTICASEqSVIVD-------------DEIYDEVRAEL 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 817 TE-----LEPGQTWLLKPRQLDDSGRLwSPGI--------------------------RDGVTPgQDAHMTEYFGPVLGI 865
Cdd:cd07122 259 KRrgayfLNEEEKEKLEKALFDDGGTL-NPDIvgksaqkiaelagievpedtkvlvaeETGVGP-EEPLSREKLSPVLAF 336
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2515445683 866 MRAETLEEAIRLQNA-VEF---GLTAGLHSLDPDEIKLWLSKVEAGNVYVNR-GTTGAI 919
Cdd:cd07122 337 YRAEDFEEALEKARElLEYggaGHTAVIHSNDEEVIEEFALRMPVSRILVNTpSSLGGI 395
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
537-946 |
1.32e-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: 61.47 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 537 AEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECG-----------KIVGEADVEVSEAIDFANY-YADL 604
Cdd:cd07077 1 ESAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGayirslianwiAMMGCSESKLYKNIDTERGiTASV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 605 AEELDELEG------VRFSPAPVTAAIPPWNFPLAIPAGSALApLATGSVVVFKPAEQA---RRCGAVIAQALWDAGVSK 675
Cdd:cd07077 81 GHIQDVLLPdngetyVRAFPIGVTMHILPSTNPLSGITSALRG-IATRNQCIFRPHPSApftNRALALLFQAADAAHGPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 676 EALRLVDiHPDEmaEVGEALVT--GSDQVILTGSIETAKLFRSWEPDLAVFAETSGKNAIIVTPQADIDLAAKDLVQSAF 753
Cdd:cd07077 160 ILVLYVP-HPSD--ELAEELLShpKIDLIVATGGRDAVDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 754 gHAGQKCSAASIAILVG--AMGKSERFINQVVDAAESLvvdwptnpsaemgpiiePAAGKLKRGLTelepgqtwllkprq 831
Cdd:cd07077 237 -FDQNACASEQNLYVVDdvLDPLYEEFKLKLVVEGLKV-----------------PQETKPLSKET-------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 832 lddsgrlwspgirdgvTPGQDAHMTEYFGPVLGIMRAETLEEAIrlQNAVEF------GLTAGLHSLDPDEIKLWLSKVE 905
Cdd:cd07077 285 ----------------TPSFDDEALESMTPLECQFRVLDVISAV--ENAWMIiesgggPHTRCVYTHKINKVDDFVQYID 346
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2515445683 906 AGNVYVNRGTTGAIVRRQPFGGWKRSQVGTGS---KAGGPNHLI 946
Cdd:cd07077 347 TASFYPNESSKKGRGAFAGKGVERIVTSGMNNifgAGVGHDALR 390
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
532-946 |
3.77e-09 |
|
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: 60.36 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 532 MEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGKIVGEADV--EVSEAIDFANYYAD------ 603
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVikNHFAAEYIYNVYKDektcgv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 604 LAEELDELEGVRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQAR----RCGAVIAQALWDAGVSKEALR 679
Cdd:cd07081 81 LTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKkvtqRAATLLLQAAVAAGAPENLIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 680 LVDiHPD--------EMAEVGEALVTGSDQViltgsIETAklFRSWEPDLAVFAetsGKNAIIVTPQADIDLAAKDLVQS 751
Cdd:cd07081 161 WID-NPSielaqrlmKFPGIGLLLATGGPAV-----VKAA--YSSGKPAIGVGA---GNTPVVIDETADIKRAVQSIVKS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 752 AFGHAGQKCSAASIAILVGAMGKS--ERF---------INQVVDAAESLVVDWPTNPSaemgpIIEPAAGKLKRGLTELE 820
Cdd:cd07081 230 KTFDNGVICASEQSVIVVDSVYDEvmRLFegqgaykltAEELQQVQPVILKNGDVNRD-----IVGQDAYKIAAAAGLKV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 821 PGQTWLLKprqlddsgrlwspgirdGVTPGQDAH---MTEYFGPVLGIMRA----ETLEEAIRLQNAVEFGLTAGLHS-- 891
Cdd:cd07081 305 PQETRILI-----------------GEVTSLAEHepfAHEKLSPVLAMYRAanfaDADAKALALKLEGGCGHTSAMYSdn 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2515445683 892 -LDPDEIKLWLSKVEAGNVYVNRGTT-GAIVRRQPFGGWKRSQVGTGSKAG-------GPNHLI 946
Cdd:cd07081 368 iKAIENMNQFANAMKTSRFVKNGPCSqGGLGDLYNFRGWPSMTLGCGTWGGnsvsenvGPKHLV 431
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
225-412 |
1.04e-08 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 58.94 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 225 EYHDLHLTIDVFTGILDREEFKNLRAGIVL---QAYLPDtlpAMERLQEwAAQRVADGGAPVKVRLVKGANLPMEQVDAL 301
Cdd:PLN02681 241 EYTSLQPAIDYITYDLAREFNKGKDRPIVYgtyQAYLKD---ARERLRL-DLERSEREGVPLGAKLVRGAYLSLERRLAA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 302 MHGWPLAVQPSKAATDANYMRILEYALrpEHISN--VNLGIAGQNLFTlgfgLNLAKARGVTEGFEVE-------MLKGM 372
Cdd:PLN02681 317 SLGVPSPVHDTIQDTHACYNRCAEFLL--EKASNgdGEVMLATHNVES----GELAAAKMNELGLHKGdprvqfaQLLGM 390
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2515445683 373 ATNQALAIREDVGRILYYVPVvdpANYDVAISYLVRRLEE 412
Cdd:PLN02681 391 SDNLSFGLGNAGFRVSKYLPY---GPVEEVIPYLLRRAEE 427
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
506-891 |
1.36e-07 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 55.29 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 506 QIFAKMGDSELGVQGADDARVRTVAEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECG---- 581
Cdd:PRK15398 12 AVLAEMLSSQTVSPPAAVGEMGVFASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGmgrv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 582 --KIV-GEADVEVSEAIDfanyyaDLAEEL----DELEGVRFSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPA 654
Cdd:PRK15398 92 edKIAkNVAAAEKTPGVE------DLTTEAltgdNGLTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 655 EQARRCgaviaqalwdagvskeALRLVDIHPDEMAEVG--EALVTgsdqVILTGSIETAK-LFRswEPDLAVFAET---- 727
Cdd:PRK15398 166 PGAKKV----------------SLRAIELLNEAIVAAGgpENLVV----TVAEPTIETAQrLMK--HPGIALLVVTggpa 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 728 -------SGKNAI---------IVTPQADIDLAAKDLVQSAfghagqkcsaasiailvgamgkseRFINQVVDAAESLVV 791
Cdd:PRK15398 224 vvkaamkSGKKAIgagagnppvVVDETADIEKAARDIVKGA------------------------SFDNNLPCIAEKEVI 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 792 dwptnpsaemgpIIEPAAGKLKRgltELEPGQTWLLKPRQLDdsgRLWSPGIRDGVTP-----GQDAH------------ 854
Cdd:PRK15398 280 ------------VVDSVADELMR---LMEKNGAVLLTAEQAE---KLQKVVLKNGGTVnkkwvGKDAAkileaaginvpk 341
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2515445683 855 ----------------MTEYFGPVLGIMRAETLEEAIRLQNAVEFGL--TAGLHS 891
Cdd:PRK15398 342 dtrllivetdanhpfvVTELMMPVLPVVRVKDVDEAIALAVKLEHGNrhTAIMHS 396
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
618-934 |
4.02e-07 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 53.90 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 618 PAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALwDAGVSKEALRLVDihpDEMAEVGEALVT 697
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVE---GAVTETTALLEQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 698 GSDQVILTGSIETAKLFRSWEPD--LAVFAETSGKNAIIVTPQADIDLAAKDLVQSAFG-HAGQKCSAASIAIlvgamgK 774
Cdd:PLN02174 188 KWDKIFYTGSSKIGRVIMAAAAKhlTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYIL------T 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 775 SERFINQVVDAAE-SLVVDWPTNP--SAEMGPIIEPAA-GKLKRGLTELEPGQTwLLKPRQLDDSGRLWSPGIRDGVTPG 850
Cdd:PLN02174 262 TKEYAPKVIDAMKkELETFYGKNPmeSKDMSRIVNSTHfDRLSKLLDEKEVSDK-IVYGGEKDRENLKIAPTILLDVPLD 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 851 QDAHMTEYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEAGNVYVNRGTTGAIVRRQPFGGWKR 930
Cdd:PLN02174 341 SLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVGE 420
|
....
gi 2515445683 931 SQVG 934
Cdd:PLN02174 421 SGMG 424
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
623-912 |
2.09e-06 |
|
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: 51.71 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 623 AAIPPWNfplAIPAgsALAPLATGSVVVFKPAEQA--------RRCGAVIAQALWDAgvskeALRLVDIHPDEmAEVGEA 694
Cdd:cd07127 203 STFPTWN---GYPG--LFASLATGNPVIVKPHPAAilplaitvQVAREVLAEAGFDP-----NLVTLAADTPE-EPIAQT 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 695 LVTGSDQVIL--TGSieTAklFRSWEPDLA----VFAETSGKNAIIVTPQADIDLAAKDLVQSAFGHAGQKCSAASiAIL 768
Cdd:cd07127 272 LATRPEVRIIdfTGS--NA--FGDWLEANArqaqVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQ-NIY 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 769 VGAMGKSER--------FINQVVDAAESLVVDwPTNPSAEMGPIIEPA-------AGKLKRGLTELEPgqtwLLKPRQLD 833
Cdd:cd07127 347 VPRDGIQTDdgrksfdeVAADLAAAIDGLLAD-PARAAALLGAIQSPDtlariaeARQLGEVLLASEA----VAHPEFPD 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 834 dsGRLWSPGIRDGVTPGQDAHMTEYFGPVLGIMRAETLEEAIRL--QNAVEFG-LTAGLHSLDPDEIKLW---------- 900
Cdd:cd07127 422 --ARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELarESVREHGaMTVGVYSTDPEVVERVqeaaldagva 499
|
330
....*....|..
gi 2515445683 901 LSKVEAGNVYVN 912
Cdd:cd07127 500 LSINLTGGVFVN 511
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
530-891 |
4.62e-06 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 50.31 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 530 AEMEQIVAEARKAAPEWAGLSGAERAKILRRAGQVLGERREELIEVAASECGkiVGEADVEVSEAIDFANYYA---DLAE 606
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETG--MGRVEDKIAKNHLAAEKTPgteDLTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 607 E---------LDELegvrfSPAPVTAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRcgaviaqalwdagVSKEA 677
Cdd:cd07121 82 TawsgdngltLVEY-----APFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKK-------------VSAYA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 678 LRLVDihpDEMAEVG--EALVTgsdqVILTGSIETA-KLFRSwePDLAVFAET-----------SGKNAI---------I 734
Cdd:cd07121 144 VELIN---KAIAEAGgpDNLVV----TVEEPTIETTnELMAH--PDINLLVVTggpavvkaalsSGKKAIgagagnppvV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 735 VTPQADIDLAAKDLVQSA-FGH----AGQK--CSAASIA-ILVGAMGKSERFI---NQVVDAAESLVVDWPtnpsaemGP 803
Cdd:cd07121 215 VDETADIEKAARDIVQGAsFDNnlpcIAEKevIAVDSVAdYLIAAMQRNGAYVlndEQAEQLLEVVLLTNK-------GA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 804 IIEPA-----AGKLkrgltelepgqtwllkprqLDDSGRLWSPGIRDGVTPGQDAH---MTEYFGPVLGIMRAETLEEAI 875
Cdd:cd07121 288 TPNKKwvgkdASKI-------------------LKAAGIEVPADIRLIIVETDKDHpfvVEEQMMPILPVVRVKNFDEAI 348
|
410
....*....|....*...
gi 2515445683 876 RLQNAVEFGL--TAGLHS 891
Cdd:cd07121 349 ELAVELEHGNrhTAIIHS 366
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
613-765 |
6.68e-06 |
|
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: 50.19 E-value: 6.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 613 GVRFSPAPVtAAIPPWNFPLAIPAGSALAPLATGSVVVFKPAEQARRCGAVIAQALWDAGVSKEALRLvdIHPDEmAEVG 692
Cdd:cd07126 138 GYRWPYGPV-AIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDL--IHSDG-PTMN 213
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2515445683 693 EALVTGSDQVIL-TGSIETA-KLFRSWEPDlaVFAETSGKNAIIVTPQ-ADIDLAAKDLVQSAFGHAGQKCSAASI 765
Cdd:cd07126 214 KILLEANPRMTLfTGSSKVAeRLALELHGK--VKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSI 287
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
618-934 |
7.44e-05 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 46.64 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 618 PAPVTAAIPPWNFPLaipaGSALAPL----ATGSVVVFKPAEQARRCGAVIAQALwDAGVSKEALRLVDIHPDemaeVGE 693
Cdd:PLN02203 108 PLGVVLIFSSWNFPI----GLSLEPLigaiAAGNAVVLKPSELAPATSAFLAANI-PKYLDSKAVKVIEGGPA----VGE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 694 ALVTGS-DQVILTGS-----IETAKLFRSWEPdlaVFAETSGKNAIIV---TPQADIDLAAKDLVQSAFGH-AGQKCSAA 763
Cdd:PLN02203 179 QLLQHKwDKIFFTGSprvgrIIMTAAAKHLTP---VALELGGKCPCIVdslSSSRDTKVAVNRIVGGKWGScAGQACIAI 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 764 SIaILVgamgkSERFINQVVDAAESLVVDWPTNPSAEMGPIIEPAAGKLKRGLTElepgqtwLLKPRQLD---------D 834
Cdd:PLN02203 256 DY-VLV-----EERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSN-------LLKDPRVAasivhggsiD 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515445683 835 SGRLW-SPGIRdgVTPGQDAH-MT-EYFGPVLGIMRAETLEEAIRLQNAVEFGLTAGLHSLDPDEIKLWLSKVEAGNVYV 911
Cdd:PLN02203 323 EKKLFiEPTIL--LNPPLDSDiMTeEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTF 400
|
330 340
....*....|....*....|...
gi 2515445683 912 NRGTTGAIVRRQPFGGWKRSQVG 934
Cdd:PLN02203 401 NDAIIQYACDSLPFGGVGESGFG 423
|
|
| |
