|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
482-965 |
8.57e-164 |
|
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: 496.33 E-value: 8.57e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 482 DAGVPEETgtLEERSRRLFVSEPDSDPALAANRQwARDIAAAIPDSTRGlaEVEAGAARLATNAEVDTLVTATAEAAGVW 561
Cdd:cd07125 11 DLEVPLEA--LADALKAFDEKEWEAIPIINGEET-ETGEGAPVIDPADH--ERTIGEVSLADAEDVDAALAIAAAAFAGW 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 562 QSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESSLLLHDGGHMVG-------ARF 634
Cdd:cd07125 86 SATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPELPGptgelngLEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 635 IPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHK 714
Cdd:cd07125 166 HGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 715 DVDRVVLTGSYDTARLFRSWK-----PDMHLLGETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCSASSLLVLVSSA 789
Cdd:cd07125 246 RIDGVIFTGSTETAKLINRALaerdgPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 790 gtSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLGSGEHWVLKPRYLGDG---LWTPGIRAGVvpGS 866
Cdd:cd07125 326 --AERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDGngyFVAPGIIEIV--GI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 867 EFHLTEYFAPVIGVMR--VDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGNLYVNRGITGAIVRRQPFGGWK 944
Cdd:cd07125 402 FDLTTEVFGPILHVIRfkAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWG 481
|
490 500
....*....|....*....|.
gi 2219515474 945 RSAIGSttKAGGPSYLLGLGE 965
Cdd:cd07125 482 LSGTGP--KAGGPNYLLRFGN 500
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
27-982 |
9.83e-129 |
|
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: 419.07 E-value: 9.83e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 27 ALGEKAVARARRWADESASEPVPRSAKLLSRILADPDGLTFTTRFVDDVVRPTDLDVAGDALKRLSSGRTDFLPPALAGA 106
Cdd:COG0506 8 ALRARAVALARRLVEAIRAAPEGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLAKSPSFLVNASTWG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 107 MGLGSAAsRLAPRTVTAVARRVFREIVGDLVVDATDKSLGPALARLRKGGNRLNVNLLGEAVLGEKEAARRLAEVSRLVT 186
Cdd:COG0506 88 LMLTLVG-RLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAARKLRAKGYRVSLDLLGEAVLTEAEAERYLDAYLEALE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 187 R-----EDVDYVSVKVSAVTGPHNPWGFDEVVAHGVQALLPLYRLARDNGTFLNLDMEDYKDLDLTIAVFTAILDQEDMY 261
Cdd:COG0506 167 AigaagVDRPGVSVKLSALGPRYSPAQRERVVEELLERLRPLARAAREAGIFVTIDMEEYDRLDLTLDVFERLLADPELA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 262 GY-EAGIVLQAYLPDSLGAMQRLQEWASRrvaaGGSRIKVRVVKGANLSMEKVDAEIHGWELTTWPSKQATDTNYKRMLS 340
Cdd:COG0506 247 GWpGVGIVLQAYLKRAEADLDRLAALARR----GGRRIRVRLVKGAYWDPEIVRAQVHGWPYPVFTRKADTDANYLRCAR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 341 WAMtpERTRAIRLGVAGQNLFDIAFAYELRAARGV-EDGVEFEMLSGMATGLQE-VVRRDTGHLLLYVPVVDPHEFDVAI 418
Cdd:COG0506 323 KLL--EAGDAIYPQFATHNARTIAAALALAGERGRpPDRFEFQMLYGMGEDLQRaLAAVDGGRLLLYCPVVAPVGGDAAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 419 SYLVRRLEENAAPENFMSGVFDLAADEVVFGRERDRFLAALSDLDPDAPVPEPNRRQDRLAERDAGVPEETGTLEERSRR 498
Cdd:COG0506 401 AYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPRFLAALAAPTPPPPPPLRRQRRRRRRARGGALAAALAAAAAAAAL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 499 LFVSEPdSDPALAANRQWARDIAAAIPDSTRGLAEVEAGAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGD 578
Cdd:COG0506 481 AAAAAA-AAALAAAAAGAAAAAAAAAVAVVPAAAAAVVAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 579 VLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAEsslllhDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVA 658
Cdd:COG0506 560 AEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAA------AAAARAAAPPPPPPGGLVALLPLGPLAAAAAAAA 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 659 AALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRswkpdm 738
Cdd:COG0506 634 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAGGGVLVLGAGGGAGGAAALTLAAAAAA------ 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 739 hllgeTSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCSASSLLVLVSSAGTSERIARQLVDATASLRVRLPLSLDSQM 818
Cdd:COG0506 708 -----ATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVAASAAASASASASLLSLLALLLLDAD 782
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 819 GPVVVPDDEKAVRGLTTLGSGEHWVLKPR--YLGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAV 896
Cdd:COG0506 783 LVILLLALAAAAAALLVGGPGAAALALGIveDAAAAALLLALAALELGEEELLLPGGGPLVPGLLTAPLLVALILGLIVL 862
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 897 DYGLTSGIQTLDATELAIWLEGVQAGNLYVNRGITGAIVRRQPFGGWKRSAIGSTTKAGGPSYLLGLGEVEPARGQGGKV 976
Cdd:COG0506 863 VLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGGGGGGGGGGGGGGGGGGGGG 942
|
....*.
gi 2219515474 977 EQGTAA 982
Cdd:COG0506 943 GGGGGG 948
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
537-949 |
3.41e-91 |
|
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: 302.05 E-value: 3.41e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 537 GAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHY 616
Cdd:COG1012 35 ARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARGEVDRAADFLRYY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 617 AESSLLLH-------DGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDA 689
Cdd:COG1012 115 AGEARRLYgetipsdAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 690 GIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPD--MHLLGETSGKNAIIVTPSADPDIAVRDAVY 767
Cdd:COG1012 195 GLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAEnlKRVTLELGGKNPAIVLDDADLDAAVEAAVR 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 768 SAFAHAGQKCSASSLLVLVSSAgtSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLG--SGEHWVLK 845
Cdd:COG1012 275 GAFGNAGQRCTAASRLLVHESI--YDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEDAvaEGAELLTG 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 846 PRYLGDG---LWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAG 922
Cdd:COG1012 353 GRRPDGEggyFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAG 432
|
410 420
....*....|....*....|....*..
gi 2219515474 923 NLYVNRGITGAIVrRQPFGGWKRSAIG 949
Cdd:COG1012 433 MVWINDGTTGAVP-QAPFGGVKQSGIG 458
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
537-961 |
1.09e-88 |
|
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: 296.06 E-value: 1.09e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 537 GAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHY 616
Cdd:cd07124 61 GTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYY 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 617 AESSLLLHDGGH-MV-----GARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAG 690
Cdd:cd07124 141 AREMLRLRGFPVeMVpgednRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAG 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 691 IPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDT--------ARLFRSWKPDMHLLGETSGKNAIIVTPSADPDIAV 762
Cdd:cd07124 221 LPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVglriyeraAKVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 763 RDAVYSAFAHAGQKCSASSLLVLVSSAgtSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLGSGEHW 842
Cdd:cd07124 301 EGIVRSAFGFQGQKCSACSRVIVHESV--YDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEGR 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 843 VLKPRyLGDGLWT------PGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWL 916
Cdd:cd07124 379 LLLGG-EVLELAAegyfvqPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERAR 457
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2219515474 917 EGVQAGNLYVNRGITGAIVRRQPFGGWKRSaiGSTTKAGGPSYLL 961
Cdd:cd07124 458 REFEVGNLYANRKITGALVGRQPFGGFKMS--GTGSKAGGPDYLL 500
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
540-960 |
5.56e-85 |
|
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: 284.04 E-value: 5.56e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 540 RLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAES 619
Cdd:pfam00171 24 PAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGEVDRAIDVLRYYAGL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 620 SLLLH------DGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPE 693
Cdd:pfam00171 104 ARRLDgetlpsDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAGLPA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 694 DLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLF-----RSWKPdmhLLGETSGKNAIIVTPSADPDIAVRDAVYS 768
Cdd:pfam00171 184 GVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIaeaaaQNLKR---VTLELGGKNPLIVLEDADLDAAVEAAVFG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 769 AFAHAGQKCSASSLLVLVSSAgtSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLGSGEHWVLK--- 845
Cdd:pfam00171 261 AFGNAGQVCTATSRLLVHESI--YDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDAKEEGAKLLtgg 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 846 PRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGNL 924
Cdd:pfam00171 339 EAGLDNGYFvEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMV 418
|
410 420 430
....*....|....*....|....*....|....*.
gi 2219515474 925 YVNRGITGAIVRRqPFGGWKRSAIGsttKAGGPSYL 960
Cdd:pfam00171 419 WINDYTTGDADGL-PFGGFKQSGFG---REGGPYGL 450
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
148-436 |
4.44e-79 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 261.66 E-value: 4.44e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 148 ALARLRKGGNRLNVNLLGEAVLGEKEAARRLAEVSRLVT----------REDVDYVSVKVSAVTGPHNPWGFDEVVAHGV 217
Cdd:pfam01619 4 TIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDalgkaagpwpLGPRPGISVKLSALHPRYEPLERERVMAELL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 218 QALLPLYRLARDNGTFLNLDMEDYKDLDLTIAVFTAILDQEDMYGYE-AGIVLQAYLPDSLGAMQRLQEWASRRvaagGS 296
Cdd:pfam01619 84 ERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNgVGITLQAYLKDALAVLDWLLELARRR----GR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 297 RIKVRVVKGANLSMEKVDAEIHGWELTTWPSKQATDTNYKRMLSWAMtpERTRAIRLGVAGQNLFDIAFAYELRAARGVE 376
Cdd:pfam01619 160 PLGVRLVKGAYWDSEIKRAQQGGWPYPVFTRKEATDANYEACARFLL--ENHDRIYPQFATHNARSVAAALALAEELGIP 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2219515474 377 -DGVEFEMLSGMATGLQEVVRRDTGHLLLYVPVVDPHEFdvaISYLVRRLEENAAPENFMS 436
Cdd:pfam01619 238 pRRFEFQQLYGMGDNLSFALVAAGYRVRKYAPVGPHEEL---LAYLVRRLLENTANSSFVR 295
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
148-961 |
9.18e-77 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 275.15 E-value: 9.18e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 148 ALAR---LRKGGNRLNVNLLGEAVLGEKEAARRLAEVSRL---VTREDVDY-------VSVKVSAVTGPHNPWGFDEVVA 214
Cdd:PRK11904 189 ALKRarsARNKGYRYSFDMLGEAALTAADAERYFKAYARAieaIGRAAGGAdlparpgISIKLSALHPRYEAAQRERVLA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 215 HGVQALLPLYRLARDNGTFLNLDMEDYKDLDLTIAVFTAILDQEDMYGYEA-GIVLQAYLPDSLGAMQRLQEWASRRvaa 293
Cdd:PRK11904 269 ELVPRVLELARLAKEANIGLTIDAEEADRLELSLDLFEALFRDPSLKGWGGfGLAVQAYQKRALPVLDWLADLARRQ--- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 294 gGSRIKVRVVKGANLSMEKVDAEIHGweLTTWP---SKQATDTNY----KRMLSwamtpERTrAIRLGVAGQNLFDIAFA 366
Cdd:PRK11904 346 -GRRIPVRLVKGAYWDSEIKRAQELG--LPGYPvftRKAATDVSYlacaRKLLS-----ARG-AIYPQFATHNAHTVAAI 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 367 YELRAargvEDGVEFEMLSGMATGLQEVVRRDTG-HLLLYVPVvDPHEfDVaISYLVRRLEENAAPENFMSGVFD----- 440
Cdd:PRK11904 417 LEMAG----HRGFEFQRLHGMGEALYDALLDAPGiPCRIYAPV-GSHK-DL-LPYLVRRLLENGANSSFVHRLVDpdvpi 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 441 --LAADEVvfgrerdRFLAALSDL-DPDAPVPE----PNRRQDRlaerdaGVpeETGtlEERSRRLFVSEPDSdpalAAN 513
Cdd:PRK11904 490 eeLVADPV-------EKLRSFETLpNPKIPLPRdifgPERKNSK------GL--NLN--DRSELEPLAAAIAA----FLE 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 514 RQWArdiAAAIPDSTRGLAEV--------EAGAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRA 585
Cdd:PRK11904 549 KQWQ---AGPIINGEGEARPVvspadrrrVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRA 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 586 ELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYA-ESSLLLHDGGHMVG-------ARFIPVDVTVVASPWNFPLAIPTGGV 657
Cdd:PRK11904 626 ELIALCVREAGKTLQDAIAEVREAVDFCRYYAaQARRLFGAPEKLPGptgesneLRLHGRGVFVCISPWNFPLAIFLGQV 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 658 AAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLF-RS--W 734
Cdd:PRK11904 706 AAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIInRTlaA 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 735 K--PDMHLLGETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCSAssLLVLVSSAGTSERIARQLVDATASLRVRLPL 812
Cdd:PRK11904 786 RdgPIVPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSA--LRVLFVQEDIADRVIEMLKGAMAELKVGDPR 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 813 SLDSQMGPVVvpdDEKAVRGLTT---LGSGEHWVLKPRYLGDGlwtpGIRAGVVPGSEFHLT-------EYFAPVIGVMR 882
Cdd:PRK11904 864 LLSTDVGPVI---DAEAKANLDAhieRMKREARLLAQLPLPAG----TENGHFVAPTAFEIDsisqlerEVFGPILHVIR 936
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 883 VDT--LQEAIEAVNAVDYGLTSGIQT-LDATELAIwLEGVQAGNLYVNRGITGAIVRRQPFGGWKRSaiGSTTKAGGPSY 959
Cdd:PRK11904 937 YKAsdLDKVIDAINATGYGLTLGIHSrIEETADRI-ADRVRVGNVYVNRNQIGAVVGVQPFGGQGLS--GTGPKAGGPHY 1013
|
..
gi 2219515474 960 LL 961
Cdd:PRK11904 1014 LL 1015
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
148-1121 |
3.15e-76 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 275.59 E-value: 3.15e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 148 ALARLRKG---GNRLNVNLLGEAVLGEKEAAR-------RLAEVSRLVTREDV---DYVSVKVSAVtgpHNPWGF---DE 211
Cdd:PRK11905 188 ALKRARELearGYRYSYDMLGEAARTAADAERyyrdyerAIHAIGKAATGRGVydgPGISVKLSAL---HPRYERaqrER 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 212 VVAHGVQALLPLYRLARDNGTFLNLDMEDYKDLDLTIAVFTAILDQEDMYGYEA-GIVLQAYLPDSLGAMQRLQEWAsRR 290
Cdd:PRK11905 265 VMAELLPRLKALALLAKAYDIGLNIDAEEADRLELSLDLLEALCSDPDLAGWNGiGFVVQAYQKRCPFVIDYLIDLA-RR 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 291 VaagGSRIKVRVVKGANLsmekvDAEI--------HGWELTTwpSKQATDTNY----KRMLswamtpERTRAIRLGVAGQ 358
Cdd:PRK11905 344 S---GRRLMVRLVKGAYW-----DAEIkraqvdglEGFPVFT--RKVHTDVSYiacaRKLL------AARDVIYPQFATH 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 359 NLFDIAFAYELRAARgveDGVEFEMLSGMATGLQEVVRRDTGH---LLLYVPVvDPHEFDVAisYLVRRLEENAAPENFM 435
Cdd:PRK11905 408 NAQTLAAIYELAGGK---GDFEFQCLHGMGEPLYDQVVGKEKLgrpCRIYAPV-GTHETLLA--YLVRRLLENGANSSFV 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 436 SGVFD--LAADEVVfgreRDRFLAALSDLD---PDAPVPE----PNRRQDR---------LAERDAGVpEETGTLEERSR 497
Cdd:PRK11905 482 NRIVDenVPVEELI----ADPVEKVAAMGVaphPQIPLPRdlygPERRNSKgldlsdeatLAALDEAL-NAFAAKTWHAA 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 498 RLFVSEPDSDPALA----ANRqwaRDIAaaipdstrglaeveaGAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAAL 573
Cdd:PRK11905 557 PLLAGGDVDGGTRPvlnpADH---DDVV---------------GTVTEASAEDVERALAAAQAAFPEWSATPAAERAAIL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 574 HRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYA-ESSLLLHDGGHMvgarfiPVDVTVVASPWNFPLAI 652
Cdd:PRK11905 619 ERAADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAaQARRLLNGPGHK------PLGPVVCISPWNFPLAI 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 653 PTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFR 732
Cdd:PRK11905 693 FTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQ 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 733 SW-----KPDMHLLGETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCSAssLLVLVSSAGTSERIARQLVDATASLR 807
Cdd:PRK11905 773 RTlakrsGPPVPLIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSA--LRVLCLQEDVADRVLTMLKGAMDELR 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 808 VRLPLSLDSQMGPVVvpdDEKAVRGLTTlgsgehWVLKPRYLGDGLWTPGIRAGVVPGSEFHLT------------EYFA 875
Cdd:PRK11905 851 IGDPWRLSTDVGPVI---DAEAQANIEA------HIEAMRAAGRLVHQLPLPAETEKGTFVAPTlieidsisdlerEVFG 921
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 876 PVIGVMRV--DTLQEAIEAVNAVDYGLTSGIQT-LDATeLAIWLEGVQAGNLYVNRGITGAIVRRQPFGGWKRSaiGSTT 952
Cdd:PRK11905 922 PVLHVVRFkaDELDRVIDDINATGYGLTFGLHSrIDET-IAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLS--GTGP 998
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 953 KAGGPSYLLGLgeVEPARGQGGKvEQGTAALDPRVAnlcdAVSSQLDAADLAELRRALVADAAawRTAYGANRDVTGLAC 1032
Cdd:PRK11905 999 KAGGPLYLGRL--VREAPTPIPP-AHESVDTDAAAR----DFLAWLDKEGKAALAAAARDARA--RSALGLEQELPGPTG 1069
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 1033 ERNILRY--REVDVVVRAGQGTALADVVRVMAAG---VRAGGFISLSVADRLPqplqnALLAAGVQVA--VEDQGAWDAR 1105
Cdd:PRK11905 1070 ESNLLSLhpRGRVLCVADTEEALLRQLAAALATGnvaVVAADSGLAAALADLP-----GLVAARIDWTqdWEADDPFAGA 1144
|
1050
....*....|....*.
gi 2219515474 1106 LAELAASGGLGTRVRV 1121
Cdd:PRK11905 1145 LLEGDAERARAVRQAL 1160
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
537-961 |
7.92e-76 |
|
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: 260.57 E-value: 7.92e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 537 GAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHY 616
Cdd:TIGR01237 61 GTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYY 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 617 AESSLLLHDG-------GHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDA 689
Cdd:TIGR01237 141 ARQMIELAKGkpvnsreGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 690 GIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSY--------DTARLFRSWKPDMHLLGETSGKNAIIVTPSADPDIA 761
Cdd:TIGR01237 221 GLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSRevgtrifeRAAKVQPGQKHLKRVIAEMGGKDTVIVDEDADIELA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 762 VRDAVYSAFAHAGQKCSASSLLVLVSSagTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLGSGEH 841
Cdd:TIGR01237 301 AQSAFTSAFGFAGQKCSAGSRAVVHEK--VYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEG 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 842 WVL--------KPRYLGdglwtPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELA 913
Cdd:TIGR01237 379 RLVsggcgddsKGYFIG-----PTIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHIN 453
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2219515474 914 IWLEGVQAGNLYVNRGITGAIVRRQPFGGWKRSAIGSttKAGGPSYLL 961
Cdd:TIGR01237 454 RAKAEFEVGNLYFNRNITGAIVGYQPFGGFKMSGTDS--KAGGPDYLA 499
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
542-961 |
1.02e-74 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 257.17 E-value: 1.02e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 542 ATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESSL 621
Cdd:PRK03137 70 ATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQML 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 622 LLHDG-------GHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPED 694
Cdd:PRK03137 150 KLADGkpvesrpGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAG 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 695 LVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTA-RLF-RSWK--P-DMHL---LGETSGKNAIIVTPSADPDIAVRDAV 766
Cdd:PRK03137 230 VVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGlRIYeRAAKvqPgQIWLkrvIAEMGGKDAIVVDEDADLDLAAESIV 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 767 YSAFAHAGQKCSASSLLVLVSSAgtSERIARQLVDATASLRVRLPLSlDSQMGPVVVPDDEKAVRGLTTLGSGE-HWVLK 845
Cdd:PRK03137 310 ASAFGFSGQKCSACSRAIVHEDV--YDEVLEKVVELTKELTVGNPED-NAYMGPVINQASFDKIMSYIEIGKEEgRLVLG 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 846 prylGDGLWTPG------IRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGV 919
Cdd:PRK03137 387 ----GEGDDSKGyfiqptIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREF 462
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2219515474 920 QAGNLYVNRGITGAIVRRQPFGGWKRSaiGSTTKAGGPSYLL 961
Cdd:PRK03137 463 HVGNLYFNRGCTGAIVGYHPFGGFNMS--GTDSKAGGPDYLL 502
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
551-960 |
8.98e-70 |
|
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: 240.57 E-value: 8.98e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 551 VTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESSLLLH------ 624
Cdd:cd07078 4 VAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHgevips 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 625 -DGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVVLAPLED 703
Cdd:cd07078 84 pDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 704 GDVSRHLVTHKDVDRVVLTGSYDTARLF-----RSWKPdmhLLGETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCS 778
Cdd:cd07078 164 DEVGAALASHPRVDKISFTGSTAVGKAImraaaENLKR---VTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 779 ASS-LLVLVSSAgtsERIARQLVDATASLRVRLPLSLDSQMGPVVVP----------DDEKAVRGLTTLGSGEHWVLKPR 847
Cdd:cd07078 241 AASrLLVHESIY---DEFVERLVERVKALKVGNPLDPDTDMGPLISAaqldrvlayiEDAKAEGAKLLCGGKRLEGGKGY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 848 YLgdglwTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGNLYVN 927
Cdd:cd07078 318 FV-----PPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIN 392
|
410 420 430
....*....|....*....|....*....|...
gi 2219515474 928 RGITGAIVrRQPFGGWKRSAIGsttKAGGPSYL 960
Cdd:cd07078 393 DYSVGAEP-SAPFGGVKQSGIG---REGGPYGL 421
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
141-1084 |
1.14e-65 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 243.73 E-value: 1.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 141 TDKSLGPALARLRK---GGNRLNVNLLGEAVLGEKEAARRLAEvsrlvtredvdY---------------------VSVK 196
Cdd:PRK11809 261 TGETIAEALANARKleeKGFRYSYDMLGEAALTEADAQAYLAS-----------YeqaihaigkasngrgiyegpgISIK 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 197 VSAVTGPHNPWGFDEVVAHGVQALLPLYRLARDNGTFLNLDMEDYKDLDLTIAVFTAILDQEDMYGYEA-GIVLQAYLP- 274
Cdd:PRK11809 330 LSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGiGFVIQAYQKr 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 275 -----DSLGAMQRlqewASRRvaaggsRIKVRVVKGANLSMEKVDAEIHGWE-LTTWPSKQATDTNY----KRMLSwamT 344
Cdd:PRK11809 410 cpfviDYLIDLAR----RSRR------RLMIRLVKGAYWDSEIKRAQVDGLEgYPVYTRKVYTDVSYlacaRKLLA---V 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 345 PErtrAIRLGVAGQNLFDIAFAYELrAARGVEDG-VEFEMLSGMATGLQEVV--RRDTGHL----LLYVPVvDPHEFDVA 417
Cdd:PRK11809 477 PN---LIYPQFATHNAHTLAAIYHL-AGQNYYPGqYEFQCLHGMGEPLYEQVvgKVADGKLnrpcRIYAPV-GTHETLLA 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 418 isYLVRRLEENAAPENFMSGVfdlaADEVVfgrerdrflaALSDLDPDaPVPEpnrrqdrlAERDAGVPEETGTLEER-- 495
Cdd:PRK11809 552 --YLVRRLLENGANTSFVNRI----ADTSL----------PLDELVAD-PVEA--------VEKLAQQEGQLGLPHPKip 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 496 -SRRLFVSEPDSDPAL-AANRQWARDIAAAIPDSTRGL--------AEVEAGAA----------------RLATNAEVDT 549
Cdd:PRK11809 607 lPRDLYGKGRANSAGLdLANEHRLASLSSALLASAHQKwqaapmleDPVAAGEMspvinpadprdivgyvREATPAEVEQ 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 550 LVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAEsslllhdgghM 629
Cdd:PRK11809 687 ALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAG----------Q 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 630 VGARF-----IPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVVLAPLEDG 704
Cdd:PRK11809 757 VRDDFdndthRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGE 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 705 DVSRHLVTHKDVDRVVLTGSYDTARLF-----RSWKPDMH---LLGETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQK 776
Cdd:PRK11809 837 TVGAALVADARVRGVMFTGSTEVARLLqrnlaGRLDPQGRpipLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQR 916
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 777 CSAssLLVLVSSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVvpdDEKAVRGL----TTLGSGEHWVLKPRYLGDG 852
Cdd:PRK11809 917 CSA--LRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVI---DAEAKANIerhiQAMRAKGRPVFQAARENSE 991
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 853 LWTPGirAGVVP-----GSEFHLT-EYFAPVIGVMRV--DTLQEAIEAVNAVDYGLTSGIQT-LDATeLAIWLEGVQAGN 923
Cdd:PRK11809 992 DWQSG--TFVPPtlielDSFDELKrEVFGPVLHVVRYnrNQLDELIEQINASGYGLTLGVHTrIDET-IAQVTGSAHVGN 1068
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 924 LYVNRGITGAIVRRQPFGGWKRSaiGSTTKAGGPSYLLGLGEVEPARGQGGKVEQgTAALDPRVANLCDAVSSQLDAadL 1003
Cdd:PRK11809 1069 LYVNRNMVGAVVGVQPFGGEGLS--GTGPKAGGPLYLYRLLATRPEDALAVTLAR-QDAEYPVDAQLRAALLAPLTA--L 1143
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 1004 AELRRALVADAAAWRTAY------GANRDVTGLACERNilRY----REVDVVVRAGQGTALADVVRVMAAGVRA---GGF 1070
Cdd:PRK11809 1144 REWAAEREPELAALCDQYaelaqaGTTRLLPGPTGERN--TYtllpRERVLCLADTEQDALTQLAAVLAVGSQAlwpDDA 1221
|
1050
....*....|....
gi 2219515474 1071 ISLSVADRLPQPLQ 1084
Cdd:PRK11809 1222 LHRALVAALPAAVQ 1235
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
217-1114 |
1.13e-63 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 236.76 E-value: 1.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 217 VQALLPLYRLARDNGTFLNLDMEDYKDLDLTIAVFTAILDQEDMYGYEAGIVLQAYLPDslgAMQRLQEWASRRVAAGGS 296
Cdd:COG4230 275 LPLLALLALAAININIDEEEDAEELLLLLLLLDLLAALLLDGGLGGGGGVGQAVQAYAK---ALLLVLDLLARRRRRRRR 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 297 RIKVRVVKGANLSMEKVDAEIHGweLTTWPSKQATDTNYKRMLswAMTPERTRAIRLGVAGQNLFDIAFAYELRAARGVE 376
Cdd:COG4230 352 RLVVRLVKGAEWDREIQRAQVLG--YVVYPVTTRKVLYDAAAL--ALALLLLAAQPAFAPQFATHAAATAAAAAAAGGGG 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 377 DGvEFEMLSGMATGLQEVVRRDTGHLLL--YVPVvDPHEFDVAisYLVRRLEENAAPENFMSGVFD--LAADEVVfgreR 452
Cdd:COG4230 428 EF-EFQCLHGMGEYLYDQVGRGKLGRPCriYAPV-GSHEDLLA--YLVRRLLENGANSSFVNRIADedVPVEELI----A 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 453 D--RFLAALSDLdPDAPVPEPNR--RQDRLAER--DAGVPEETGTLEERSRRlfvsepdsdpalAANRQWArdiAAAIPD 526
Cdd:COG4230 500 DpvEKARALGGA-PHPRIPLPRDlyGPERRNSAglDLSDEAVLAALSAALAA------------AAEKQWQ---AAPLIA 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 527 STRGLAEVEA-----------GAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEA 595
Cdd:COG4230 564 GEAASGEARPvrnpadhsdvvGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREA 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 596 GKTIDQSDPEVSEAIDFCHHYAESSLLLHDGGHMVGARFipvdvTVVA-SPWNFPLAIPTGGVAAALAAGSAVILKPAPP 674
Cdd:COG4230 644 GKTLPDAIAEVREAVDFCRYYAAQARRLFAAPTVLRGRG-----VFVCiSPWNFPLAIFTGQVAAALAAGNTVLAKPAEQ 718
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 675 ARRCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTAR-----LFRSWKPDMHLLGETSGKNA 749
Cdd:COG4230 719 TPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARlinrtLAARDGPIVPLIAETGGQNA 798
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 750 IIVTPSADPDIAVRDAVYSAFAHAGQKCSAssLLVLVSSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVvpdDEKA 829
Cdd:COG4230 799 MIVDSSALPEQVVDDVLASAFDSAGQRCSA--LRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVI---DAEA 873
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 830 VRGLTTlgsgehWVLKPRYLGDGLWTPGIRAGVVPGSEF-----------HLT-EYFAPVIGVMRV--DTLQEAIEAVNA 895
Cdd:COG4230 874 RANLEA------HIERMRAEGRLVHQLPLPEECANGTFVaptlieidsisDLErEVFGPVLHVVRYkaDELDKVIDAINA 947
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 896 VDYGLTSGIQT-LDATELAIwLEGVQAGNLYVNRGITGAIVRRQPFGGWKRSaiGSTTKAGGPSYLLGLgevepARGQGG 974
Cdd:COG4230 948 TGYGLTLGVHSrIDETIDRV-AARARVGNVYVNRNIIGAVVGVQPFGGEGLS--GTGPKAGGPHYLLRF-----ATERTV 1019
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 975 KVEQGTAALDPRVANLCDAVSSQLDAADLAElrralvadaaawrtayganrdVTGlacERNILRY--REVDVVVRAGQGT 1052
Cdd:COG4230 1020 TVNTTAAGGNASLLALGDWLASLLGALTLPG---------------------PTG---ERNTLTLrpRGRVLCLADSLEA 1075
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2219515474 1053 ALADVVRVMAAGVRAggfisLSVADRLPQPLQNALLAAGVQVAVEdqGAWDARLAELAASGG 1114
Cdd:COG4230 1076 LLAQLAAALATGNRA-----VVAADLALAGLPAVLLPPFDAVLFE--GRLRALRQALAARDG 1130
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
536-950 |
1.35e-62 |
|
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: 221.45 E-value: 1.35e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 536 AGAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHH 615
Cdd:cd07131 28 VGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGDVQEAIDMAQY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 616 YAESSLLLHdgGHMVG---------ARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAF 686
Cdd:cd07131 108 AAGEGRRLF--GETVPselpnkdamTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 687 HDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFR--SWKPDMHLLGETSGKNAIIVTPSADPDIAVRD 764
Cdd:cd07131 186 AEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGetCARPNKRVALEMGGKNPIIVMDDADLDLALEG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 765 AVYSAFAHAGQKCSASSLLVLVSSagTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDD-EKAVR--------GLTT 835
Cdd:cd07131 266 ALWSAFGTTGQRCTATSRLIVHES--VYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQlEKVLNyneigkeeGATL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 836 LGSGEhwVLKPRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAI 914
Cdd:cd07131 344 LLGGE--RLTGGGYEKGYFvEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFR 421
|
410 420 430
....*....|....*....|....*....|....*.
gi 2219515474 915 WLEGVQAGNLYVNRGITGAIVrRQPFGGWKRSAIGS 950
Cdd:cd07131 422 ARRDLEAGITYVNAPTIGAEV-HLPFGGVKKSGNGH 456
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
537-950 |
2.86e-62 |
|
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: 220.58 E-value: 2.86e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 537 GAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHY 616
Cdd:cd07097 29 GKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARGEVTRAGQIFRYY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 617 AESSLLLH-------DGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDA 689
Cdd:cd07097 109 AGEALRLSgetlpstRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 690 GIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDT---------ARLFRswkpdMHLlgETSGKNAIIVTPSADPDI 760
Cdd:cd07097 189 GLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVgrriaaaaaARGAR-----VQL--EMGGKNPLVVLDDADLDL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 761 AVRDAVYSAFAHAGQKCSASSLLVLVssAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLGSGE 840
Cdd:cd07097 262 AVECAVQGAFFSTGQRCTASSRLIVT--EGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIEIARSE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 841 HWVL----KPRYLGDGLW--TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAI 914
Cdd:cd07097 340 GAKLvyggERLKRPDEGYylAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATH 419
|
410 420 430
....*....|....*....|....*....|....*..
gi 2219515474 915 WLEGVQAGNLYVNRGITGaiVRRQ-PFGGWKRSAIGS 950
Cdd:cd07097 420 FKRRVEAGVVMVNLPTAG--VDYHvPFGGRKGSSYGP 454
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
517-968 |
3.70e-62 |
|
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: 220.94 E-value: 3.70e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 517 ARDIAAAIPDSTRGLAEVEAGAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAG 596
Cdd:TIGR01238 46 YKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 597 KTIDQSDPEVSEAIDFCHHYAESslLLHDGGHMVGArfiPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPAR 676
Cdd:TIGR01238 126 KTIHNAIAEVREAVDFCRYYAKQ--VRDVLGEFSVE---SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 677 RCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLF-----RSWKPDMHLLGETSGKNAII 751
Cdd:TIGR01238 201 LIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLInqtlaQREDAPVPLIAETGGQNAMI 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 752 VTPSADPDIAVRDAVYSAFAHAGQKCSAssLLVLVSSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVvpdDEKAVR 831
Cdd:TIGR01238 281 VDSTALPEQVVRDVLRSAFDSAGQRCSA--LRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVI---DAEAKQ 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 832 GLttLGSGEHWVLKPRYL------GDGLWTPGIragVVPGSEFHLT-------EYFAPVIGVMR--VDTLQEAIEAVNAV 896
Cdd:TIGR01238 356 NL--LAHIEHMSQTQKKIaqltldDSRACQHGT---FVAPTLFELDdiaelseEVFGPVLHVVRykARELDQIVDQINQT 430
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2219515474 897 DYGLTSGIQTLDATELAiWLEG-VQAGNLYVNRGITGAIVRRQPFGGWKRSaiGSTTKAGGPSYLLGLGEVEP 968
Cdd:TIGR01238 431 GYGLTMGVHSRIETTYR-WIEKhARVGNCYVNRNQVGAVVGVQPFGGQGLS--GTGPKAGGPHYLYRLTQVQY 500
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
542-961 |
2.53e-60 |
|
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: 215.52 E-value: 2.53e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 542 ATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESSL 621
Cdd:cd07083 52 ADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAAL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 622 LLHDGGHMVGAR--------FIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPE 693
Cdd:cd07083 132 RLRYPAVEVVPYpgednesfYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 694 DLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFrsWK------PDMH----LLGETSGKNAIIVTPSADPDIAVR 763
Cdd:cd07083 212 GVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKI--YEaaarlaPGQTwfkrLYVETGGKNAIIVDETADFELVVE 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 764 DAVYSAFAHAGQKCSASSLLVLVSSAgtSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLGSGEHWV 843
Cdd:cd07083 290 GVVVSAFGFQGQKCSAASRLILTQGA--YEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQL 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 844 LKPRYLGDG---LWTPGIRAGVVPGSEFHLTEYFAPVIGVMRV--DTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEG 918
Cdd:cd07083 368 VLGGKRLEGegyFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYkdDDFAEALEVANSTPYGLTGGVYSRKREHLEEARRE 447
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2219515474 919 VQAGNLYVNRGITGAIVRRQPFGGWKRSaiGSTTKAGGPSYLL 961
Cdd:cd07083 448 FHVGNLYINRKITGALVGVQPFGGFKLS--GTNAKTGGPHYLR 488
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
552-960 |
2.31e-59 |
|
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: 208.62 E-value: 2.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 552 TATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESSLLLH------- 624
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGgpelpsp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 625 DGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVVLAPLEDG 704
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 705 DVSRHLVTHKDVDRVVLTGSYDTARLFR-----SWKPdmhLLGETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCSA 779
Cdd:cd06534 161 EVGAALLSHPRVDKISFTGSTAVGKAIMkaaaeNLKP---VTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 780 SSLLVLvssagtSERIARQLVDAtaslrvrlplsldsqMGPVVVPDDekavrglttlgsgehwvlkprylgdglwtpgir 859
Cdd:cd06534 238 ASRLLV------HESIYDEFVEK---------------LVTVLVDVD--------------------------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 860 agvvPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGNLYVNRGITGAIVrRQP 939
Cdd:cd06534 264 ----PDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGP-EAP 338
|
410 420
....*....|....*....|.
gi 2219515474 940 FGGWKRSAIGSttkAGGPSYL 960
Cdd:cd06534 339 FGGVKNSGIGR---EGGPYGL 356
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
535-946 |
1.49e-54 |
|
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: 198.17 E-value: 1.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 535 EAGAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCH 614
Cdd:cd07086 25 PIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLGEVQEMIDICD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 615 HYAESSLLLHdG--------GHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAF 686
Cdd:cd07086 105 YAVGLSRMLY-GltipserpGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKIL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 687 HDA----GIPEDLVVLApLEDGDVSRHLVTHKDVDRVVLTGSYDT--------ARLFRswkpdMHLLgETSGKNAIIVTP 754
Cdd:cd07086 184 AEVleknGLPPGVVNLV-TGGGDGGELLVHDPRVPLVSFTGSTEVgrrvgetvARRFG-----RVLL-ELGGNNAIIVMD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 755 SADPDIAVRDAVYSAFAHAGQKCSASSLLVLVSSagTSERIARQLVDATASLRVRLPLSLDSQMGPVV----VPDDEKAV 830
Cdd:cd07086 257 DADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHES--VYDEFLERLVKAYKQVRIGDPLDEGTLVGPLInqaaVEKYLNAI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 831 R-----GLTTLGSGEhwvlKPRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGI 904
Cdd:cd07086 335 EiaksqGGTVLTGGK----RIDGGEPGNYvEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSI 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2219515474 905 QTLDATELAIWLE--GVQAGNLYVNRGITGAIVrRQPFGGWKRS 946
Cdd:cd07086 411 FTEDLREAFRWLGpkGSDCGIVNVNIPTSGAEI-GGAFGGEKET 453
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
541-949 |
3.25e-47 |
|
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: 176.08 E-value: 3.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 541 LATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESS 620
Cdd:cd07094 17 ADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRAIDTLRLAAEEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 621 LLLH------DGGHMVGARFI-----PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDA 689
Cdd:cd07094 97 ERIRgeeiplDATQGSDNRLAwtirePVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILVEA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 690 GIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDMHLLGETSGKNAIIVTPSADPDIAVRDAVYSA 769
Cdd:cd07094 177 GVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKRIALELGGNAPVIVDRDADLDAAIEALAKGG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 770 FAHAGQKCSASSLLVLVSSagTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDD--------EKAVR-GLTTLGSGE 840
Cdd:cd07094 257 FYHAGQVCISVQRIYVHEE--LYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAaerverwvEEAVEaGARLLCGGE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 841 hwvlkpryLGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQ 920
Cdd:cd07094 335 --------RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLE 406
|
410 420
....*....|....*....|....*....
gi 2219515474 921 AGNLYVNRGiTGAIVRRQPFGGWKRSAIG 949
Cdd:cd07094 407 VGGVMVNDS-SAFRTDWMPFGGVKESGVG 434
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
542-949 |
3.74e-47 |
|
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: 175.83 E-value: 3.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 542 ATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDP-EVSEAIDFCHHYAESS 620
Cdd:cd07093 16 GGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTrDIPRAAANFRFFADYI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 621 LLL------HDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPED 694
Cdd:cd07093 96 LQLdgesypQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEAGLPPG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 695 LVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLF-----RSWKPdMHLlgETSGKNAIIVTPSADPDIAVRDAVYSA 769
Cdd:cd07093 176 VVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTImraaaPNLKP-VSL--ELGGKNPNIVFADADLDRAVDAAVRSS 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 770 FAHAGQKCSASSLLvLVSSAGTSERIARqLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLGSGE----HW--- 842
Cdd:cd07093 253 FSNNGEVCLAGSRI-LVQRSIYDEFLER-FVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAEgatiLTggg 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 843 VLKPRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQA 921
Cdd:cd07093 331 RPELPDLEGGYFvEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEA 410
|
410 420 430
....*....|....*....|....*....|
gi 2219515474 922 GNLYVNrgitGAIVR--RQPFGGWKRSAIG 949
Cdd:cd07093 411 GTVWVN----CWLVRdlRTPFGGVKASGIG 436
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
542-949 |
9.48e-47 |
|
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: 174.66 E-value: 9.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 542 ATNAEVDTLVTATAEA--AGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYA-- 617
Cdd:cd07114 16 ASAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVRYLAEWYRYYAgl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 618 ----ESSLL-LHDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIP 692
Cdd:cd07114 96 adkiEGAVIpVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAGFP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 693 EDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLF--RSWKPDMHLLGETSGKNAIIVTPSADPDIAVRDAVYSAF 770
Cdd:cd07114 176 PGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIarAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 771 AHAGQKCSASS-LLVlvsSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGL---------TTLGSGE 840
Cdd:cd07114 256 AAAGQTCVAGSrLLV---QRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYvarareegaRVLTGGE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 841 hwVLKPRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD---ATELAiwl 916
Cdd:cd07114 333 --RPSGADLGAGYFfEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDlarAHRVA--- 407
|
410 420 430
....*....|....*....|....*....|....*
gi 2219515474 917 EGVQAGNLYVN--RgitgAIVRRQPFGGWKRSAIG 949
Cdd:cd07114 408 RAIEAGTVWVNtyR----ALSPSSPFGGFKDSGIG 438
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
541-949 |
4.56e-46 |
|
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: 173.22 E-value: 4.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 541 LATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESS 620
Cdd:cd07088 31 AATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARVEVEFTADYIDYMAEWA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 621 LLLhDGGHMVGAR-----FI---PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIP 692
Cdd:cd07088 111 RRI-EGEIIPSDRpneniFIfkvPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAGLP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 693 EDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDT-ARLFRSWKPDM-HLLGETSGKNAIIVTPSADPDIAVRDAVYSAF 770
Cdd:cd07088 190 AGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAgQKIMEAAAENItKVSLELGGKAPAIVMKDADLDLAVKAIVDSRI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 771 AHAGQKCSASSLlVLVSSAGTSERIARqLVDATASLRVRLPLSLDSQMGPVV-----------VpddEKAVRGLTTLGSG 839
Cdd:cd07088 270 INCGQVCTCAER-VYVHEDIYDEFMEK-LVEKMKAVKVGDPFDAATDMGPLVneaaldkveemV---ERAVEAGATLLTG 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 840 EHwvlkPRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEG 918
Cdd:cd07088 345 GK----RPEGEKGYFyEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNE 420
|
410 420 430
....*....|....*....|....*....|..
gi 2219515474 919 VQAGNLYVNRGITGAIvrrQPF-GGWKRSAIG 949
Cdd:cd07088 421 LEFGETYINRENFEAM---QGFhAGWKKSGLG 449
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
546-957 |
2.73e-44 |
|
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: 166.94 E-value: 2.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 546 EVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAesSLLLHD 625
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAA--GLPRRP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 626 GGHMVG---------ARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELV-RAFHDAGIPEDL 695
Cdd:cd07104 79 EGEILPsdvpgkesmVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIaEIFEEAGLPKGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 696 VVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLF-----RSWKPdMHLlgETSGKNAIIVTPSADPDIAVRDAVYSAF 770
Cdd:cd07104 159 LNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIgelagRHLKK-VAL--ELGGNNPLIVLDDADLDLAVSAAAFGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 771 AHAGQKCSASSlLVLVSSAGTSERIARqLVDATASLRVRLPLSLDSQMGPVVVPDD--------EKAV-RGLTTLGSGEH 841
Cdd:cd07104 236 LHQGQICMAAG-RILVHESVYDEFVEK-LVAKAKALPVGDPRDPDTVIGPLINERQvdrvhaivEDAVaAGARLLTGGTY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 842 wvlkprylgDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD---ATELAiwlE 917
Cdd:cd07104 314 ---------EGLFyQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDlerAMAFA---E 381
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2219515474 918 GVQAGNLYVNrGIT---GAIVrrqPFGGWKRSAIGSttkAGGP 957
Cdd:cd07104 382 RLETGMVHIN-DQTvndEPHV---PFGGVKASGGGR---FGGP 417
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
546-946 |
7.20e-44 |
|
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: 165.52 E-value: 7.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 546 EVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSE-------AIDFCHHYAe 618
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAmagkidiSIKAYHERT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 619 SSLLLHDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVVL 698
Cdd:cd07095 80 GERATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 699 ApLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFR---SWKPDMHLLGETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQ 775
Cdd:cd07095 160 V-QGGRETGEALAAHEGIDGLLFTGSAATGLLLHrqfAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 776 KCSASSLLVLVSSAGTSERIARqLVDATASLRVRLPLSLDSQMGPVVvpDDEKAVRGLTT----LGSGEHWVLKPRYL-- 849
Cdd:cd07095 239 RCTCARRLIVPDGAVGDAFLER-LVEAAKRLRIGAPDAEPPFMGPLI--IAAAAARYLLAqqdlLALGGEPLLAMERLva 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 850 GDGLWTPGI----RAGVVPGSEfhlteYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGNLY 925
Cdd:cd07095 316 GTAFLSPGIidvtDAADVPDEE-----IFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVN 390
|
410 420
....*....|....*....|.
gi 2219515474 926 VNRGITGAIVRRqPFGGWKRS 946
Cdd:cd07095 391 WNRPTTGASSTA-PFGGVGLS 410
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
542-950 |
1.31e-43 |
|
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: 165.30 E-value: 1.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 542 ATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESSL 621
Cdd:cd07103 16 AGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVDYAASFLEWFAEEAR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 622 LLHD---GGHMVGARFI----PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAP--PArrCAAELVRAFHDAGIP 692
Cdd:cd07103 96 RIYGrtiPSPAPGKRILvikqPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEetPL--SALALAELAEEAGLP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 693 EDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFrswkpdMHLLGETS-------GKNA-IIVTPSADPDIAVRD 764
Cdd:cd07103 174 AGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLL------MAQAADTVkrvslelGGNApFIVFDDADLDKAVDG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 765 AVYSAFAHAGQKC-SASSLLVLVSSAgtsERIARQLVDATASLRVRLPLSLDSQMGPVVvpdDEKAV------------R 831
Cdd:cd07103 248 AIASKFRNAGQTCvCANRIYVHESIY---DEFVEKLVERVKKLKVGNGLDEGTDMGPLI---NERAVekvealvedavaK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 832 GLTTLGSGEHWVLKPRYlgdglWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATE 911
Cdd:cd07103 322 GAKVLTGGKRLGLGGYF-----YEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLAR 396
|
410 420 430
....*....|....*....|....*....|....*....
gi 2219515474 912 LAIWLEGVQAGNLYVNRGITGAIVrrQPFGGWKRSAIGS 950
Cdd:cd07103 397 AWRVAEALEAGMVGINTGLISDAE--APFGGVKESGLGR 433
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
525-951 |
3.26e-43 |
|
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: 165.00 E-value: 3.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 525 PDSTRGLAEVEagaarLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDP 604
Cdd:cd07085 23 PATGEVIARVP-----LATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADARG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 605 EVSEAIDFCHHyAESSLLLHDGGHMVGAR--------FIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPAR 676
Cdd:cd07085 98 DVLRGLEVVEF-ACSIPHLLKGEYLENVArgidtysyRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 677 RCAAELVRAFHDAGIPeDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGS-------YDTARlfRSWKPDMHLLGetsGKNA 749
Cdd:cd07085 177 GAAMRLAELLQEAGLP-DGVLNVVHGGKEAVNALLDHPDIKAVSFVGStpvgeyiYERAA--ANGKRVQALGG---AKNH 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 750 IIVTPSADPDIAVRDAVYSAFAHAGQKCSASSLLVLVssAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKA 829
Cdd:cd07085 251 AVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAV--GDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKER 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 830 VRGLTTLG--SGEHWVL-----KPRYLGDGLWT-PGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLT 901
Cdd:cd07085 329 IEGLIESGveEGAKLVLdgrgvKVPGYENGNFVgPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNG 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2219515474 902 SGIQTLDATELAIWLEGVQAGNLYVNRGITgAIVRRQPFGGWKRSAIGST 951
Cdd:cd07085 409 AAIFTRSGAAARKFQREVDAGMVGINVPIP-VPLAFFSFGGWKGSFFGDL 457
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
531-957 |
6.25e-43 |
|
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: 163.27 E-value: 6.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 531 LAEVEAGAARLATNAevdtlVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAI 610
Cdd:cd07150 12 YARVAVGSRQDAERA-----IAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTFTP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 611 DF-------CHHYAESSLLLHDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELV 683
Cdd:cd07150 87 ELlraaageCRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 684 RAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLF-----RSWKPDMHLLGetsGKNAIIVTPSADP 758
Cdd:cd07150 167 EIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIaekagRHLKKITLELG---GKNPLIVLADADL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 759 DIAVRDAVYSAFAHAGQKCSASSlLVLVSSAGTSERIARqLVDATASLRVRLPLSLDSQMGPVVVPDD--------EKAV 830
Cdd:cd07150 244 DYAVRAAAFGAFMHQGQICMSAS-RIIVEEPVYDEFVKK-FVARASKLKVGDPRDPDTVIGPLISPRQverikrqvEDAV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 831 -RGLTTLGSGEHwvlkprylgDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD 908
Cdd:cd07150 322 aKGAKLLTGGKY---------DGNFyQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTND 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2219515474 909 ---ATELAIWLEgvqAGNLYVNrgitGAIVRRQ---PFGGWKRSAIGsttKAGGP 957
Cdd:cd07150 393 lqrAFKLAERLE---SGMVHIN----DPTILDEahvPFGGVKASGFG---REGGE 437
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
542-949 |
6.53e-43 |
|
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: 163.28 E-value: 6.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 542 ATNAEVDTLVTATAEA--AGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAES 619
Cdd:cd07118 16 GTVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 620 SLLLHDGGH-MVGARFI------PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIP 692
Cdd:cd07118 96 ARTLHGDSYnNLGDDMLglvlrePIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 693 EDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTAR-LFRSWKPDMHLLG-ETSGKNAIIVTPSADPDIAVRDAVYSAF 770
Cdd:cd07118 176 AGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKaIAAAAARNLKKVSlELGGKNPQIVFADADLDAAADAVVFGVY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 771 AHAGQKCSASSLLVLVSSagTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLG--SGEHWVLKPRY 848
Cdd:cd07118 256 FNAGECCNSGSRLLVHES--IADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGraEGATLLLGGER 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 849 L--GDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGNLY 925
Cdd:cd07118 334 LasAAGLFyQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVW 413
|
410 420
....*....|....*....|....
gi 2219515474 926 VNRGITGAIvrRQPFGGWKRSAIG 949
Cdd:cd07118 414 VNTFLDGSP--ELPFGGFKQSGIG 435
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
525-949 |
7.41e-43 |
|
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: 163.38 E-value: 7.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 525 PDSTRGLAEVEAGAArlatnAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTI-DQSD 603
Cdd:cd07115 4 PATGELIARVAQASA-----EDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIrAARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 604 PEVSEAIDFCHHYA------ESSLLLHDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARR 677
Cdd:cd07115 79 LDVPRAADTFRYYAgwadkiEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 678 CAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTAR-LFRSWKPDMHLLG-ETSGKNAIIVTPS 755
Cdd:cd07115 159 SALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRkIMQGAAGNLKRVSlELGGKSANIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 756 ADPDIAVRDAVYSAFAHAGQKCSASSLLVLVSSAgtSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTT 835
Cdd:cd07115 239 ADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESI--YDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 836 LGSGEHWVLKPRYLGDG----LWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATE 911
Cdd:cd07115 317 VGREEGARLLTGGKRPGargfFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430
....*....|....*....|....*....|....*...
gi 2219515474 912 LAIWLEGVQAGNLYVNrgITGAIVRRQPFGGWKRSAIG 949
Cdd:cd07115 397 AHRVAAALKAGTVWIN--TYNRFDPGSPFGGYKQSGFG 432
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
537-956 |
1.13e-42 |
|
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: 162.78 E-value: 1.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 537 GAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHY 616
Cdd:cd07099 10 GEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLALEAIDWA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 617 AE------------SSLLLHDGGHMVgaRFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVR 684
Cdd:cd07099 90 ARnaprvlaprkvpTGLLMPNKKATV--EYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 685 AFHDAGIPEDLVVLApLEDGDVSRHLVTHKdVDRVVLTGSYDTARLF-----RSWKPDMHLLGetsGKNAIIVTPSADPD 759
Cdd:cd07099 168 AWAAAGPPQGVLQVV-TGDGATGAALIDAG-VDKVAFTGSVATGRKVmaaaaERLIPVVLELG---GKDPMIVLADADLE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 760 IAVRDAVYSAFAHAGQKCSASSLLVLVSSAgtSERIARQLVDATASLRVRLPLSLDSQMGPVVVP----------DDEKA 829
Cdd:cd07099 243 RAAAAAVWGAMVNAGQTCISVERVYVHESV--YDEFVARLVAKARALRPGADDIGDADIGPMTTArqldivrrhvDDAVA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 830 vRGLTTLGSGEHWVLKPRYLGdglwtPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD- 908
Cdd:cd07099 321 -KGAKALTGGARSNGGGPFYE-----PTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDl 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2219515474 909 --ATELAIWLEgvqAGNLYVNRGITGAIVRRQPFGGWKRSAIGSTTKAGG 956
Cdd:cd07099 395 arAEAIARRLE---AGAVSINDVLLTAGIPALPFGGVKDSGGGRRHGAEG 441
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
547-949 |
1.50e-42 |
|
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: 161.47 E-value: 1.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 547 VDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAE--SSLL-- 622
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAEnaEAFLad 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 623 ---LHDGGH-MVgaRFIPVDVTVVASPWNFPL------AIPTggvaaaLAAGSAVILKPAPPARRCAAELVRAFHDAGIP 692
Cdd:cd07100 81 epiETDAGKaYV--RYEPLGVVLGIMPWNFPFwqvfrfAAPN------LMAGNTVLLKHASNVPGCALAIEELFREAGFP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 693 EDLVVLAPLeDGDVSRHLVTHKDVDRVVLTGSydtARLFRSwkpdmhlLGETSGKN------------AIIVTPSADPDI 760
Cdd:cd07100 153 EGVFQNLLI-DSDQVEAIIADPRVRGVTLTGS---ERAGRA-------VAAEAGKNlkksvlelggsdPFIVLDDADLDK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 761 AVRDAVYSAFAHAGQKCSASSLLVLVSSAgtSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDD--------EKAV-R 831
Cdd:cd07100 222 AVKTAVKGRLQNAGQSCIAAKRFIVHEDV--YDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLrdelheqvEEAVaA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 832 GLTTLGSGEhwvlkpRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD-- 908
Cdd:cd07100 300 GATLLLGGK------RPDGPGAFyPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDle 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2219515474 909 -ATELAiwlEGVQAGNLYVNrgitgAIVR---RQPFGGWKRSAIG 949
Cdd:cd07100 374 rAERVA---RRLEAGMVFIN-----GMVKsdpRLPFGGVKRSGYG 410
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
537-958 |
7.04e-42 |
|
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: 160.15 E-value: 7.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 537 GAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHY 616
Cdd:cd07152 5 GEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 617 AEssLLLHDGGHMVG--------ARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELV-RAFH 687
Cdd:cd07152 85 AG--LPTQPQGEILPsapgrlslARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIaRLFE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 688 DAGIPEDLVVLAPlEDGDVSRHLVTHKDVDRVVLTGSYDTARLF-----RSWKpDMHLlgETSGKNAIIVTPSADPDIAV 762
Cdd:cd07152 163 EAGLPAGVLHVLP-GGADAGEALVEDPNVAMISFTGSTAVGRKVgeaagRHLK-KVSL--ELGGKNALIVLDDADLDLAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 763 RDAVYSAFAHAGQKCSASSL-LVLVSSAgtsERIARQLVDATASLRVRLPLSLDSQMGPVVvpDDEKAVR---------- 831
Cdd:cd07152 239 SNGAWGAFLHQGQICMAAGRhLVHESVA---DAYTAKLAAKAKHLPVGDPATGQVALGPLI--NARQLDRvhaivddsva 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 832 -GLTTLGSGEHwvlkprylgDGL-WTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD- 908
Cdd:cd07152 314 aGARLEAGGTY---------DGLfYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDv 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2219515474 909 --ATELAiwlEGVQAGNLYVNRG--ITGAIVrrqPFGGWKRSaiGSTTKAGGPS 958
Cdd:cd07152 385 grAMALA---DRLRTGMLHINDQtvNDEPHN---PFGGMGAS--GNGSRFGGPA 430
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
533-949 |
9.73e-42 |
|
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: 159.62 E-value: 9.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 533 EVEAGAARlATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDF 612
Cdd:cd07106 8 EVFASAPV-ASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGAVAW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 613 CHHYAESSL---LLHDG-GHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHD 688
Cdd:cd07106 87 LRYTASLDLpdeVIEDDdTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 689 AgIPEDlVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARL-FRSWKPDM-HLLGETSGKNAIIVTPSADPDIAVRDAV 766
Cdd:cd07106 167 V-LPPG-VLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKvMASAAKTLkRVTLELGGNDAAIVLPDVDIDAVAPKLF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 767 YSAFAHAGQKCSASSLLVLVSSAGtsERIARQLVDATASLRVRLPLSLDSQMGPV-------VVPD--DEKAVRGLTTLG 837
Cdd:cd07106 245 WGAFINSGQVCAAIKRLYVHESIY--DEFCEALVALAKAAVVGDGLDPGTTLGPVqnkmqydKVKElvEDAKAKGAKVLA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 838 SGEhwVLKprylGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD---ATELA 913
Cdd:cd07106 323 GGE--PLD----GPGYFiPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDlerAEAVA 396
|
410 420 430
....*....|....*....|....*....|....*.
gi 2219515474 914 IWLEgvqAGNLYVNRgiTGAIVRRQPFGGWKRSAIG 949
Cdd:cd07106 397 RRLE---AGTVWINT--HGALDPDAPFGGHKQSGIG 427
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
548-950 |
1.11e-41 |
|
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: 160.04 E-value: 1.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 548 DTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESSLLLhDGG 627
Cdd:cd07082 42 EAAETAYDAGRGWWPTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRL-DGD 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 628 HMVGARF------------IPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDL 695
Cdd:cd07082 121 SLPGDWFpgtkgkiaqvrrEPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 696 VVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDMHLLGETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQ 775
Cdd:cd07082 201 VNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQ 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 776 KCSASSlLVLVssagtSERIARQLVD----ATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLT--TLGSGEHWVLKPRYL 849
Cdd:cd07082 281 RCTAIK-RVLV-----HESVADELVEllkeEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLIddAVAKGATVLNGGGRE 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 850 GDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGNLYVN-- 927
Cdd:cd07082 355 GGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINsk 434
|
410 420
....*....|....*....|....*
gi 2219515474 928 --RGITgaivrRQPFGGWKRSAIGS 950
Cdd:cd07082 435 cqRGPD-----HFPFLGRKDSGIGT 454
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
535-949 |
1.70e-41 |
|
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: 159.30 E-value: 1.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 535 EAGAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCH 614
Cdd:cd07149 11 VIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDRAIETLR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 615 HYAESSLLLHdgGHMV--------GARF-----IPVDVTVVASPWNFPL---------AIptggvaaalAAGSAVILKPA 672
Cdd:cd07149 91 LSAEEAKRLA--GETIpfdaspggEGRIgftirEPIGVVAAITPFNFPLnlvahkvgpAI---------AAGNAVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 673 PPARRCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDMHLLGETSGKNAIIV 752
Cdd:cd07149 160 SQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLKKVTLELGSNAAVIV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 753 TPSADPDIAVRDAVYSAFAHAGQKCsASSLLVLVSSAGTSERIARqLVDATASLRVRLPLSLDSQMGPVVvpdDEKAVRG 832
Cdd:cd07149 240 DADADLEKAVERCVSGAFANAGQVC-ISVQRIFVHEDIYDEFLER-FVAATKKLVVGDPLDEDTDVGPMI---SEAEAER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 833 LttlgsgEHWVLKPRYLGDGLWTPGIRAG----------VVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTS 902
Cdd:cd07149 315 I------EEWVEEAVEGGARLLTGGKRDGaileptvltdVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQA 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2219515474 903 GIQT--LDATELAIwlEGVQAGNLYVNrGITGAIVRRQPFGGWKRSAIG 949
Cdd:cd07149 389 GVFTndLQKALKAA--RELEVGGVMIN-DSSTFRVDHMPYGGVKESGTG 434
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
525-949 |
3.31e-41 |
|
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: 158.28 E-value: 3.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 525 PDSTRGLAEVEAgaarlATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDP 604
Cdd:cd07110 4 PATEATIGEIPA-----ATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 605 EVSEAIDFCHHYA----------ESSLLLHDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPP 674
Cdd:cd07110 79 DVDDVAGCFEYYAdlaeqldakaERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 675 ARRCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTAR-LFRSWKPDMHLLG-ETSGKNAIIV 752
Cdd:cd07110 159 TSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSqVMQAAAQDIKPVSlELGGKSPIIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 753 TPSADPDIAVRDAVYSAFAHAGQKCSASSLLvLVSSAGTSERIARqLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVR- 831
Cdd:cd07110 239 FDDADLEKAVEWAMFGCFWNNGQICSATSRL-LVHESIADAFLER-LATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLs 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 832 --------GLTTLGSGEHwvlkPRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTS 902
Cdd:cd07110 317 fiargkeeGARLLCGGRR----PAHLEKGYFiAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAA 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2219515474 903 GIQTLDATELAIWLEGVQAGNLYVNrgITGAIVRRQPFGGWKRSAIG 949
Cdd:cd07110 393 AVISRDAERCDRVAEALEAGIVWIN--CSQPCFPQAPWGGYKRSGIG 437
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
540-951 |
5.75e-40 |
|
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: 154.71 E-value: 5.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 540 RLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHY--- 616
Cdd:cd07102 13 PLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMisi 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 617 AESSLLLHDGGHMVGA-RFI---PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIP 692
Cdd:cd07102 93 AEEALADIRVPEKDGFeRYIrrePLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 693 EDLVVLAPLeDGDVSRHLVTHKDVDRVVLTGSYDT-ARLFRSWKPDMHLLG-ETSGKNAIIVTPSADPDIAVRDAVYSAF 770
Cdd:cd07102 173 EGVFQVLHL-SHETSAALIADPRIDHVSFTGSVAGgRAIQRAAAGRFIKVGlELGGKDPAYVRPDADLDAAAESLVDGAF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 771 AHAGQKCSAssllvlvssagtSERI----------ARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLT------ 834
Cdd:cd07102 252 FNSGQSCCS------------IERIyvhesiydafVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIadaiak 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 835 --TLGSGEHwvLKPRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATE 911
Cdd:cd07102 320 gaRALIDGA--LFPEDKAGGAYlAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIAR 397
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2219515474 912 LAIWLEGVQAGNLYVNRGItgAIVRRQPFGGWKRSAIGST 951
Cdd:cd07102 398 AEALGEQLETGTVFMNRCD--YLDPALAWTGVKDSGRGVT 435
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
531-950 |
4.99e-39 |
|
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: 151.74 E-value: 4.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 531 LAEVEAGAArlatnaevDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAI 610
Cdd:cd07146 12 VGTVPAGTE--------EALREALALAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 611 D---FCHHYA---ESSLLLHDGGHMVGARFI-----PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCA 679
Cdd:cd07146 84 DvlrFAAAEAlrdDGESFSCDLTANGKARKIftlrePLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 680 AELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDMHLLGETSGKNAIIVTPSADPD 759
Cdd:cd07146 164 IYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYKRQLLELGGNDPLIVMDDADLE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 760 IAVRDAVYSAFAHAGQKCSA-SSLLVLVSSAgtsERIARQLVDATASLRVRLPLSLDSQMGPVVvpDDEKAV----RGLT 834
Cdd:cd07146 244 RAATLAVAGSYANSGQRCTAvKRILVHESVA---DEFVDLLVEKSAALVVGDPMDPATDMGTVI--DEEAAIqienRVEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 835 TLGSGEHWVLKPRYLGDGLWtPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD---ATE 911
Cdd:cd07146 319 AIAQGARVLLGNQRQGALYA-PTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDldtIKR 397
|
410 420 430
....*....|....*....|....*....|....*....
gi 2219515474 912 LAiwlEGVQAGNLYVNrGITGAIVRRQPFGGWKRSAIGS 950
Cdd:cd07146 398 LV---ERLDVGTVNVN-EVPGFRSELSPFGGVKDSGLGG 432
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
525-949 |
1.31e-38 |
|
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: 150.46 E-value: 1.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 525 PDSTRGLAEVEAGAArlatnAEVDTLVTATAEA-AGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSD 603
Cdd:cd07109 4 PSTGEVFARIARGGA-----ADVDRAVQAARRAfESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 604 PEVSEAIDFCHHYAESSLLLH------DGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARR 677
Cdd:cd07109 79 ADVEAAARYFEYYGGAADKLHgetiplGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 678 CAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDMH--LLGETSGKNAIIVTPS 755
Cdd:cd07109 159 TALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVvpVTLELGGKSPQIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 756 ADPDIAVRDAVYSAFAHAGQKCSASSLLVLVSSAgtSERIARQLVDATASLRVRLPLSlDSQMGPVVVPDDEKAVRGLT- 834
Cdd:cd07109 239 ADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSI--YDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVa 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 835 --------TLGSGEhwVLKPRYLGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQT 906
Cdd:cd07109 316 rarargarIVAGGR--IAEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWT 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2219515474 907 LDaTELAIWL-EGVQAGNLYVNRGITGAIVRRqPFGGWKRSAIG 949
Cdd:cd07109 394 RD-GDRALRVaRRLRAGQVFVNNYGAGGGIEL-PFGGVKKSGHG 435
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
525-950 |
2.72e-38 |
|
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: 149.83 E-value: 2.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 525 PDSTRGLAEVEAGAArlatnAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDP 604
Cdd:cd07107 4 PATGQVLARVPAASA-----ADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 605 EVSEAIDFCHHYAESSLLLH------DGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKP---APPA 675
Cdd:cd07107 79 DVMVAAALLDYFAGLVTELKgetipvGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPpeqAPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 676 RRCAAELVRAFhdagIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDM--HLLGETSGKNAIIVT 753
Cdd:cd07107 159 ALRLAELAREV----LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGikHVTLELGGKNALIVF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 754 PSADPDIAVRDAVYSA-FAHAGQKCSASSLLvLVSSAGTSERIARqLVDATASLRVRLPLSLDSQMGPVV-------VPD 825
Cdd:cd07107 235 PDADPEAAADAAVAGMnFTWCGQSCGSTSRL-FVHESIYDEVLAR-VVERVAAIKVGDPTDPATTMGPLVsrqqydrVMH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 826 --DEKAVRGLTTLGSGEHwvLKPRYLGDGLWT-PGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTS 902
Cdd:cd07107 313 yiDSAKREGARLVTGGGR--PEGPALEGGFYVePTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTA 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2219515474 903 GIQTLDATELAIWLEGVQAGNLYVN---RGITGAivrrqPFGGWKRSAIGS 950
Cdd:cd07107 391 AIWTNDISQAHRTARRVEAGYVWINgssRHFLGA-----PFGGVKNSGIGR 436
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
537-957 |
3.71e-38 |
|
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: 149.65 E-value: 3.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 537 GAARLATNAEVDTLVTATAEA--AGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQS-DPEVSEAIDFC 613
Cdd:cd07139 28 GRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISWSrRAQGPGPAALL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 614 HHYAE-----------SSLllhDGGHMVGARfIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAEL 682
Cdd:cd07139 108 RYYAAlardfpfeerrPGS---GGGHVLVRR-EPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 683 VRAFHDAGIPEDLVVLAPlEDGDVSRHLVTHKDVDRVVLTGSYDTARLFrswkpdMHLLG--------ETSGKNAIIVTP 754
Cdd:cd07139 184 AEAAEEAGLPPGVVNVVP-ADREVGEYLVRHPGVDKVSFTGSTAAGRRI------AAVCGerlarvtlELGGKSAAIVLD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 755 SADPDIAVRDAVYSAFAHAGQKCSASSlLVLVSSAGTSERIARqLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLT 834
Cdd:cd07139 257 DADLDAAVPGLVPASLMNNGQVCVALT-RILVPRSRYDEVVEA-LAAAVAALKVGDPLDPATQIGPLASARQRERVEGYI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 835 TLGSGEHWVL-----KPRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD 908
Cdd:cd07139 335 AKGRAEGARLvtgggRPAGLDRGWFvEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTAD 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2219515474 909 ---ATELAiwlEGVQAGNLYVNrGITGAIVrrQPFGGWKRSAIGsttKAGGP 957
Cdd:cd07139 415 verGLAVA---RRIRTGTVGVN-GFRLDFG--APFGGFKQSGIG---REGGP 457
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
543-949 |
5.50e-38 |
|
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: 149.00 E-value: 5.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 543 TNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESSLL 622
Cdd:cd07101 16 TPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVARYYARRAER 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 623 L-----HDGGHMVGARFI----PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPE 693
Cdd:cd07101 96 LlkprrRRGAIPVLTRTTvnrrPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 694 DLVVLAPLEDGDVSRHLVTHkdVDRVVLTGSYDTARLFRSWKPDmHLLG---ETSGKNAIIVTPSADPDIAVRDAVYSAF 770
Cdd:cd07101 176 DLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGR-RLIGcslELGGKNPMIVLEDADLDKAAAGAVRACF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 771 AHAGQKC-SASSLLVLVSSAgtsERIARQLVDATASLRVRLPLSLDSQMGPVVVPD---------DEKAVRGLTTLGSGe 840
Cdd:cd07101 253 SNAGQLCvSIERIYVHESVY---DEFVRRFVARTRALRLGAALDYGPDMGSLISQAqldrvtahvDDAVAKGATVLAGG- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 841 hwvlKPRY-LGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGV 919
Cdd:cd07101 329 ----RARPdLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARL 404
|
410 420 430
....*....|....*....|....*....|.
gi 2219515474 920 QAGNLYVNRGITGAIVRRQ-PFGGWKRSAIG 949
Cdd:cd07101 405 RAGTVNVNEGYAAAWASIDaPMGGMKDSGLG 435
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
531-949 |
6.15e-38 |
|
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: 148.90 E-value: 6.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 531 LAEVEAGAArlatnAEVDTLVTATAEA--AGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTI-DQSDPEVS 607
Cdd:cd07112 15 LAEVAACDA-----ADVDRAVAAARRAfeSGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPIsDALAVDVP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 608 EAIDFCHHYAESSLLLHDGGHMVGARFI------PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAE 681
Cdd:cd07112 90 SAANTFRWYAEAIDKVYGEVAPTGPDALalitrePLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 682 LVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDMHLLG---ETSGKNAIIVTPSA-D 757
Cdd:cd07112 170 LAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRvwlECGGKSPNIVFADApD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 758 PDIAVRDAVYSAFAHAGQKCSASS-LLVlvsSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVvpDDEKAVRGLTTL 836
Cdd:cd07112 250 LDAAAEAAAAGIFWNQGEVCSAGSrLLV---HESIKDEFLEKVVAAAREWKPGDPLDPATRMGALV--SEAHFDKVLGYI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 837 GSGEHWVLKPRYLGDGLWT--------PGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD 908
Cdd:cd07112 325 ESGKAEGARLVAGGKRVLTetggffvePTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSD 404
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2219515474 909 ATELAIWLEGVQAGNLYVNRGITGAIvrRQPFGGWKRSAIG 949
Cdd:cd07112 405 LSRAHRVARRLRAGTVWVNCFDEGDI--TTPFGGFKQSGNG 443
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
533-949 |
7.23e-38 |
|
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: 148.54 E-value: 7.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 533 EVEAGAARLATNAEVDTLVTATAEA--AGVWqSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTI----DQSDPEV 606
Cdd:cd07089 7 EEVIGTAPDAGAADVDAAIAAARRAfdTGDW-STDAEERARCLRQLHEALEARKEELRALLVAEVGAPVmtarAMQVDGP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 607 SEAIDFCHHYAESSLLLHDGG-----HMVGARFI---PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRC 678
Cdd:cd07089 86 IGHLRYFADLADSFPWEFDLPvpalrGGPGRRVVrrePVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 679 AAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDM--HLLGETSGKNAIIVTPSA 756
Cdd:cd07089 166 ALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATlkRVLLELGGKSANIVLDDA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 757 DPDIAVRDAVYSAFAHAGQKCSASSLLVLVSSagTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTL 836
Cdd:cd07089 246 DLAAAAPAAVGVCMHNAGQGCALTTRLLVPRS--RYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIAR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 837 GSGEHWVL-----KPRYLGDGLWT-PGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDAT 910
Cdd:cd07089 324 GRDEGARLvtgggRPAGLDKGFYVePTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVD 403
|
410 420 430
....*....|....*....|....*....|....*....
gi 2219515474 911 ELAIWLEGVQAGNLYVNRGITGAIvrRQPFGGWKRSAIG 949
Cdd:cd07089 404 RAYRVARRIRTGSVGINGGGGYGP--DAPFGGYKQSGLG 440
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
546-949 |
8.72e-38 |
|
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: 147.72 E-value: 8.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 546 EVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAeSSLLLHD 625
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAA-SLITQII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 626 GGHM------VGARFI--PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPED--- 694
Cdd:cd07105 80 GGSIpsdkpgTLAMVVkePVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGvln 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 695 LVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSW-----KPdmhLLGETSGKNAIIVTPSADPDIAVRDAVYSA 769
Cdd:cd07105 160 VVTHSPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETaakhlKP---VLLELGGKAPAIVLEDADLDAAANAALFGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 770 FAHAGQKCSASSLLVLVSSagtserIARQLVDATASLRVRLPLSlDSQMGPVVVPDDEKAVRGLTT--LGSGEHWVL--K 845
Cdd:cd07105 237 FLNSGQICMSTERIIVHES------IADEFVEKLKAAAEKLFAG-PVVLGSLVSAAAADRVKELVDdaLSKGAKLVVggL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 846 PRYLGDGL-WTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD---ATELAiwlEGVQA 921
Cdd:cd07105 310 ADESPSGTsMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDlarALAVA---KRIES 386
|
410 420 430
....*....|....*....|....*....|.
gi 2219515474 922 GNLYVNrgitGAIVRRQ---PFGGWKRSAIG 949
Cdd:cd07105 387 GAVHIN----GMTVHDEptlPHGGVKSSGYG 413
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
531-949 |
1.07e-37 |
|
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: 148.61 E-value: 1.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 531 LAEVEAGAARLATNAevdtlVTATAEA--AGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSE 608
Cdd:cd07119 26 IATVPEGTAEDAKRA-----IAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEIDIDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 609 AIDFCHHYAESSLLLHDGGHMVGARFI------PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAEL 682
Cdd:cd07119 101 VANCFRYYAGLATKETGEVYDVPPHVIsrtvrePVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIAL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 683 VRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTAR-LFRSWKPDMHLLG-ETSGKNAIIVTPSADPDI 760
Cdd:cd07119 181 FELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRsIMRAAAGNVKKVAlELGGKNPNIVFADADFET 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 761 AVRDAVYSAFAHAGQKCSASSLLVLVSSagTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLGSGE 840
Cdd:cd07119 261 AVDQALNGVFFNAGQVCSAGSRLLVEES--IHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQLGKEE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 841 HWVLK-------PRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATEL 912
Cdd:cd07119 339 GARLVcggkrptGDELAKGYFvEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARA 418
|
410 420 430
....*....|....*....|....*....|....*...
gi 2219515474 913 AIWLEGVQAGNLYVNR-GITGAivrRQPFGGWKRSAIG 949
Cdd:cd07119 419 NRVARRLRAGTVWINDyHPYFA---EAPWGGYKQSGIG 453
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
537-949 |
4.94e-37 |
|
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: 145.93 E-value: 4.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 537 GAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTID-QSDPEVSEAIDFCHH 615
Cdd:cd07092 11 ATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHlVRDDELPGAVDNFRF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 616 YAESSLLLHDG-------GHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHD 688
Cdd:cd07092 91 FAGAARTLEGPaageylpGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 689 aGIPeDLVVLAPLEDGD-VSRHLVTHKDVDRVVLTGSYDTARLF-----RSWKpDMHLlgETSGKNAIIVTPSADPDIAV 762
Cdd:cd07092 171 -VLP-PGVVNVVCGGGAsAGDALVAHPRVRMVSLTGSVRTGKKVaraaaDTLK-RVHL--ELGGKAPVIVFDDADLDAAV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 763 RDAVYSAFAHAGQKCSASSlLVLVsSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDD--------EKAVRGLT 834
Cdd:cd07092 246 AGIATAGYYNAGQDCTAAC-RVYV-HESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQrervagfvERAPAHAR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 835 TLGSGEhwvlkpRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD---AT 910
Cdd:cd07092 324 VLTGGR------RAEGPGYFyEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDvgrAM 397
|
410 420 430
....*....|....*....|....*....|....*....
gi 2219515474 911 ELAIWLegvQAGNLYVNRGITgaIVRRQPFGGWKRSAIG 949
Cdd:cd07092 398 RLSARL---DFGTVWVNTHIP--LAAEMPHGGFKQSGYG 431
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
542-946 |
1.26e-36 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 145.49 E-value: 1.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 542 ATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSE-----AIDFcHHY 616
Cdd:PRK09457 34 ATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEVTAminkiAISI-QAY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 617 AESSLllHDGGHMVGA----RFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIP 692
Cdd:PRK09457 113 HERTG--EKRSEMADGaavlRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 693 EDLVVLAPLEDgDVSRHLVTHKDVDRVVLTGSYDTARLFR---SWKPDMHLLGETSGKNAIIVTPSADPDIAVRDAVYSA 769
Cdd:PRK09457 191 AGVLNLVQGGR-ETGKALAAHPDIDGLLFTGSANTGYLLHrqfAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 770 FAHAGQKCS-ASSLLVLVSSAGtsERIARQLVDATASLRVRLPlslDSQ----MGPVVvpdDEKAVRGLTT-----LGSG 839
Cdd:PRK09457 270 FISAGQRCTcARRLLVPQGAQG--DAFLARLVAVAKRLTVGRW---DAEpqpfMGAVI---SEQAAQGLVAaqaqlLALG 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 840 EHWVLKPRYL--GDGLWTPGIrAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLE 917
Cdd:PRK09457 342 GKSLLEMTQLqaGTGLLTPGI-IDVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLL 420
|
410 420
....*....|....*....|....*....
gi 2219515474 918 GVQAGNLYVNRGITGAiVRRQPFGGWKRS 946
Cdd:PRK09457 421 EIRAGIVNWNKPLTGA-SSAAPFGGVGAS 448
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
502-949 |
2.44e-36 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 145.41 E-value: 2.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 502 SEPDSDPALAANRQWARDIAAAIPDSTRGLAEVEA-------GAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALH 574
Cdd:PRK09407 4 TALPMPAPSALTFERLRRLTARVDGAAGPTREVTApftgeplATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 575 RVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESSL-LLHD---GGHMVGA-----RFIPVDVTVVASP 645
Cdd:PRK09407 84 RFHDLVLENREELLDLVQLETGKARRHAFEEVLDVALTARYYARRAPkLLAPrrrAGALPVLtktteLRQPKGVVGVISP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 646 WNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHkdVDRVVLTGSY 725
Cdd:PRK09407 164 WNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGST 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 726 DTARLFRSwKPDMHLLG---ETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKC-SASSLLVLVSSAgtsERIARQLVD 801
Cdd:PRK09407 242 ATGRVLAE-QAGRRLIGfslELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCiSIERIYVHESIY---DEFVRAFVA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 802 ATASLRVRLPLSLDSQMGPVVVPDDEKAV---------RGLTTLGSGehwvlKPRY-LGDGLWTPGIRAGVVPGSEFHLT 871
Cdd:PRK09407 318 AVRAMRLGAGYDYSADMGSLISEAQLETVsahvddavaKGATVLAGG-----KARPdLGPLFYEPTVLTGVTPDMELARE 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2219515474 872 EYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGNLYVNRGITGAIVRRQ-PFGGWKRSAIG 949
Cdd:PRK09407 393 ETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSVDaPMGGMKDSGLG 471
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
533-949 |
4.50e-36 |
|
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: 143.41 E-value: 4.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 533 EVEAGAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDP-------- 604
Cdd:cd07138 24 EEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPITLARAaqvglgig 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 605 ------EVSEAIDFCHHyAESSLLLHDgghmvgarfiPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRC 678
Cdd:cd07138 104 hlraaaDALKDFEFEER-RGNSLVVRE----------PIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 679 AAELVRAFHDAGIPE---DLVvlapleDGD---VSRHLVTHKDVDRVVLTGSYDTARLFrswkpdMHLLGET-------- 744
Cdd:cd07138 173 AIILAEILDEAGLPAgvfNLV------NGDgpvVGEALSAHPDVDMVSFTGSTRAGKRV------AEAAADTvkrvalel 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 745 SGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCSA-SSLLVLVSSAGTSERIARQLVDATaslRVRLPLSLDSQMGPVVV 823
Cdd:cd07138 241 GGKSANIILDDADLEKAVPRGVAACFANSGQSCNApTRMLVPRSRYAEAEEIAAAAAEAY---VVGDPRDPATTLGPLAS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 824 PDDEKAVRGLTTLGSGEHWVL------KPRYLGDGLWT-PGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAV 896
Cdd:cd07138 318 AAQFDRVQGYIQKGIEEGARLvaggpgRPEGLERGYFVkPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDT 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2219515474 897 DYGLTSGIQTLDATELAIWLEGVQAGNLYVNRGITGAivrRQPFGGWKRSAIG 949
Cdd:cd07138 398 PYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNP---GAPFGGYKQSGNG 447
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
525-949 |
7.70e-36 |
|
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: 142.44 E-value: 7.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 525 PDSTRGLAEVEAgaarlATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDP 604
Cdd:cd07090 4 PATGEVLATVHC-----AGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 605 EVSEAIDFCHHYAESSLLLH------DGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRC 678
Cdd:cd07090 79 DIDSSADCLEYYAGLAPTLSgehvplPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 679 AAELVRAFHDAGIPEDL--VVLApleDGDVSRHLVTHKDVDRVVLTGSYDTAR-LFRSWKPDM-HLLGETSGKNAIIVTP 754
Cdd:cd07090 159 ALLLAEILTEAGLPDGVfnVVQG---GGETGQLLCEHPDVAKVSFTGSVPTGKkVMSAAAKGIkHVTLELGGKSPLIIFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 755 SADPDIAVRDAVYSAFAHAGQKCSASSlLVLVSSaGTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVR--- 831
Cdd:cd07090 236 DADLENAVNGAMMANFLSQGQVCSNGT-RVFVQR-SIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLgyi 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 832 ------GLTTLGSGEHWVLKPRYLGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQ 905
Cdd:cd07090 314 esakqeGAKVLCGGERVVPEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVF 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2219515474 906 TLDATELAIWLEGVQAGNLYVNR-GITGAIVrrqPFGGWKRSAIG 949
Cdd:cd07090 394 TRDLQRAHRVIAQLQAGTCWINTyNISPVEV---PFGGYKQSGFG 435
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
542-961 |
1.05e-35 |
|
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: 143.50 E-value: 1.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 542 ATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAAR-RAELIEVAGSEAGKTIDQSDPEVS-EAIDFCH---HY 616
Cdd:cd07123 66 ADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKyRYELNAATMLGQGKNVWQAEIDAAcELIDFLRfnvKY 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 617 AESslLLHD-----GGHMVGA-RFIPVDVTVVA-SPWNFPlAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDA 689
Cdd:cd07123 146 AEE--LYAQqplssPAGVWNRlEYRPLEGFVYAvSPFNFT-AIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 690 GIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTarlFRS-WK------------PdmHLLGETSGKNAIIVTPSA 756
Cdd:cd07123 223 GLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPT---FKSlWKqigenldryrtyP--RIVGETGGKNFHLVHPSA 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 757 DPDIAVRDAVYSAFAHAGQKCSASSLLVLVSSAgtSERIARQLVDATASLRVRLPLSLDSQMGPVVvpdDEKAVRGLTTL 836
Cdd:cd07123 298 DVDSLVTATVRGAFEYQGQKCSAASRAYVPESL--WPEVKERLLEELKEIKMGDPDDFSNFMGAVI---DEKAFDRIKGY 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 837 -----GSGEHWVLkprYLGDGLWTPG--IRAGVV----PGSEFHLTEYFAPVIGVMRVD--TLQEAIEAVNAV-DYGLTS 902
Cdd:cd07123 373 idhakSDPEAEII---AGGKCDDSVGyfVEPTVIettdPKHKLMTEEIFGPVLTVYVYPdsDFEETLELVDTTsPYALTG 449
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2219515474 903 GI--QTLDATELAiwLEGVQ--AGNLYVNRGITGAIVRRQPFGGWKRSaiGSTTKAGGPSYLL 961
Cdd:cd07123 450 AIfaQDRKAIREA--TDALRnaAGNFYINDKPTGAVVGQQPFGGARAS--GTNDKAGSPLNLL 508
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
525-949 |
1.41e-35 |
|
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: 141.73 E-value: 1.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 525 PDSTRGLAEVEAGAArlatnAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTI-DQSD 603
Cdd:cd07108 4 PATGQVIGEVPRSRA-----ADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 604 PEVSEAIDFCHHYA------ESSLLLHDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARR 677
Cdd:cd07108 79 PEAAVLADLFRYFGglagelKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 678 CAAELVRAFHDAgIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPD--MHLLGETSGKNAIIVTPS 755
Cdd:cd07108 159 AVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADrlIPVSLELGGKSPMIVFPD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 756 ADPDIAVRDAVYSA-FAHAGQKCSASSLLVLVSSagTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLT 834
Cdd:cd07108 238 ADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHED--IYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 835 TLG---SGEHWVL-----KPRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQ 905
Cdd:cd07108 316 DLGlstSGATVLRggplpGEGPLADGFFvQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVW 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2219515474 906 TLDATELAIWLEGVQAGNLYVNRGitGAIVRRQPFGGWKRSAIG 949
Cdd:cd07108 396 TRDLGRALRAAHALEAGWVQVNQG--GGQQPGQSYGGFKQSGLG 437
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
542-956 |
3.50e-35 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 140.64 E-value: 3.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 542 ATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAE-SS 620
Cdd:PRK09406 20 LTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYYAEhAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 621 LLLHD--------GGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIP 692
Cdd:PRK09406 100 ALLADepadaaavGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRAGFP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 693 EDLVVLAPLEDGDVSRHLvthKDvDRVV---LTGSYDTARLFRSWKPDM--HLLGETSGKNAIIVTPSADPDIAVRDAVY 767
Cdd:PRK09406 180 DGCFQTLLVGSGAVEAIL---RD-PRVAaatLTGSEPAGRAVAAIAGDEikKTVLELGGSDPFIVMPSADLDRAAETAVT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 768 SAFAHAGQKCSASSLLVLvsSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPD---------DEKAVRGLTTLGS 838
Cdd:PRK09406 256 ARVQNNGQSCIAAKRFIV--HADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQgrdevekqvDDAVAAGATILCG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 839 GEhwvlkpRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLE 917
Cdd:PRK09406 334 GK------RPDGPGWFyPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFID 407
|
410 420 430
....*....|....*....|....*....|....*....
gi 2219515474 918 GVQAGNLYVNrGITgAIVRRQPFGGWKRSAIGSTTKAGG 956
Cdd:PRK09406 408 DLEAGQVFIN-GMT-VSYPELPFGGVKRSGYGRELSAHG 444
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
546-949 |
1.04e-33 |
|
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: 135.94 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 546 EVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESSLLLH- 624
Cdd:cd07145 22 EVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVERTIRLFKLAAEEAKVLRg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 625 -----DGGHMVGARFI-----PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPED 694
Cdd:cd07145 102 etipvDAYEYNERRIAftvrePIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAGLPPG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 695 LVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRS-----WKPDMHLLGetsGKNAIIVTPSADPDIAVRDAVYSA 769
Cdd:cd07145 182 VINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASkaggtGKKVALELG---GSDPMIVLKDADLERAVSIAVRGR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 770 FAHAGQKCSASSlLVLVSSAGTSERIARqLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLT--TLGSGEHWVLKPR 847
Cdd:cd07145 259 FENAGQVCNAVK-RILVEEEVYDKFLKL-LVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVndAVEKGGKILYGGK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 848 YLGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD---ATELAIWLEgvqAGNL 924
Cdd:cd07145 337 RDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDinrALKVARELE---AGGV 413
|
410 420
....*....|....*....|....*..
gi 2219515474 925 YVNRGITgaiVRRQ--PFGGWKRSAIG 949
Cdd:cd07145 414 VINDSTR---FRWDnlPFGGFKKSGIG 437
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
542-949 |
6.08e-33 |
|
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: 134.26 E-value: 6.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 542 ATNAEVDTLVTAtAEAA---GVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQS-DPEVSEAIDFCHHYA 617
Cdd:cd07091 38 ADEEDVDAAVKA-ARAAfetGWWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEESaKGDVALSIKCLRYYA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 618 ------ESSLLLHDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGI 691
Cdd:cd07091 117 gwadkiQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 692 PEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDMHL------LGetsGKNAIIVTPSADPDIAVRDA 765
Cdd:cd07091 197 PPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSNLkkvtleLG---GKSPNIVFDDADLDKAVEWA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 766 VYSAFAHAGQKCSASS-LLVlvsSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDD--------EKAVR-GLTT 835
Cdd:cd07091 274 AFGIFFNQGQCCCAGSrIFV---QESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQfdkilsyiESGKKeGATL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 836 LGSGEHWVLKPRYLgdglwTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIW 915
Cdd:cd07091 351 LTGGERHGSKGYFI-----QPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRV 425
|
410 420 430
....*....|....*....|....*....|....*
gi 2219515474 916 LEGVQAGNLYVNrgiTGAIVRRQ-PFGGWKRSAIG 949
Cdd:cd07091 426 SRALKAGTVWVN---TYNVFDAAvPFGGFKQSGFG 457
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
540-933 |
6.37e-33 |
|
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: 134.26 E-value: 6.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 540 RLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAES 619
Cdd:cd07130 29 RQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLGEVQEMIDICDFAVGL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 620 SLLLHdG--------GHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAE----LVRAFH 687
Cdd:cd07130 109 SRQLY-GltipserpGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPLTAIAvtkiVARVLE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 688 DAGIPEDLVVLApLEDGDVSRHLVTHKDVDRVVLTGSYDT---------ARLFRSwkpdmhLLgETSGKNAIIVTPSADP 758
Cdd:cd07130 188 KNGLPGAIASLV-CGGADVGEALVKDPRVPLVSFTGSTAVgrqvgqavaARFGRS------LL-ELGGNNAIIVMEDADL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 759 DIAVRDAVYSAFAHAGQKCSASSLLVLVSSagTSERIARQLVDATASLRVRLPLSLDSQMGPVV----VPDDEKAVR--- 831
Cdd:cd07130 260 DLAVRAVLFAAVGTAGQRCTTTRRLIVHES--IYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHtkaaVDNYLAAIEeak 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 832 --GLTTLGSGEhwvlkpRYLGDGLW-TPGIRAGVVPGSEFHlTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD 908
Cdd:cd07130 338 sqGGTVLFGGK------VIDGPGNYvEPTIVEGLSDAPIVK-EETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTD 410
|
410 420
....*....|....*....|....*..
gi 2219515474 909 ATELAIWL--EGVQAGNLYVNRGITGA 933
Cdd:cd07130 411 LRNAFRWLgpKGSDCGIVNVNIGTSGA 437
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
542-952 |
1.66e-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: 132.96 E-value: 1.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 542 ATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDP-EVSEAIDFCHHYA--- 617
Cdd:cd07117 35 ATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRAvDIPLAADHFRYFAgvi 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 618 ---ESSLLLHDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAgIPED 694
Cdd:cd07117 115 raeEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 695 LVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDmHLLGET---SGKNAIIVTPSADPDIAVRDAVYSAFA 771
Cdd:cd07117 194 VVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK-KLIPATlelGGKSANIIFDDANWDKALEGAQLGILF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 772 HAGQKCSASSLLVLVSsaGTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLGSGEHWVL---KPRY 848
Cdd:cd07117 273 NQGQVCCAGSRIFVQE--GIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGAKIltgGHRL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 849 LGDGL-----WTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGN 923
Cdd:cd07117 351 TENGLdkgffIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGR 430
|
410 420
....*....|....*....|....*....
gi 2219515474 924 LYVNrgITGAIVRRQPFGGWKRSAIGSTT 952
Cdd:cd07117 431 VWVN--TYNQIPAGAPFGGYKKSGIGRET 457
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
541-949 |
2.35e-32 |
|
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: 131.98 E-value: 2.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 541 LATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESS 620
Cdd:cd07147 17 LAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDTFRIAAEEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 621 LLLHD-----------GGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDA 689
Cdd:cd07147 97 TRIYGevlpldisargEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAET 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 690 GIPEDLVVLAPLeDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDMHLLGETSGKNAIIVTPSADPDIAVRDAVYSA 769
Cdd:cd07147 177 GLPKGAFSVLPC-SRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGKKKVVLELGGNAAVIVDSDADLDFAAQRIIFGA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 770 FAHAGQKC-SASSLLVlvsSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVrglttlgsgEHWVLKPRY 848
Cdd:cd07147 256 FYQAGQSCiSVQRVLV---HRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERV---------EGWVNEAVD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 849 LGDGLWTPGIRAG----------VVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEG 918
Cdd:cd07147 324 AGAKLLTGGKRDGalleptiledVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDE 403
|
410 420 430
....*....|....*....|....*....|.
gi 2219515474 919 VQAGNLYVNRgITGAIVRRQPFGGWKRSAIG 949
Cdd:cd07147 404 LEVGGVVIND-VPTFRVDHMPYGGVKDSGIG 433
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
543-949 |
6.73e-32 |
|
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: 130.54 E-value: 6.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 543 TNAEVDTLVTATAEA--AGVWqSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAesS 620
Cdd:cd07120 17 GVAEAEAAIAAARRAfdETDW-AHDPRLRARVLLELADAFEANAERLARLLALENGKILGEARFEISGAISELRYYA--G 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 621 LLLHDGGHMVGAR--------FIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDA-GI 691
Cdd:cd07120 94 LARTEAGRMIEPEpgsfslvlREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEIpSL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 692 PEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTAR-LFRSWKPDMHLLG-ETSGKNAIIVTPSADPDIAVRDAVYSA 769
Cdd:cd07120 174 PAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRaIMAAAAPTLKRLGlELGGKTPCIVFDDADLDAALPKLERAL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 770 FAHAGQKC-SASSLLVLVSSAgtsERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTT--LGSGEHWVLKP 846
Cdd:cd07120 254 TIFAGQFCmAGSRVLVQRSIA---DEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVEraIAAGAEVVLRG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 847 RYLGDGL-----WTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQA 921
Cdd:cd07120 331 GPVTEGLakgafLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRA 410
|
410 420
....*....|....*....|....*...
gi 2219515474 922 GNLYVNRgiTGAIVRRQPFGGWKRSAIG 949
Cdd:cd07120 411 GTVWIND--WNKLFAEAEEGGYRQSGLG 436
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
545-960 |
1.75e-31 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 130.03 E-value: 1.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 545 AEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESSLLLH 624
Cdd:PRK11241 48 DETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIY 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 625 DG---GHMVGARFI----PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVV 697
Cdd:PRK11241 128 GDtipGHQADKRLIvikqPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFN 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 698 LAPLEDGDVSRHLVTHKDVDRVVLTGSYDTAR-LFRSWKPDMHLLGETSGKNA-IIVTPSADPDIAVRDAVYSAFAHAGQ 775
Cdd:PRK11241 208 VVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRqLMEQCAKDIKKVSLELGGNApFIVFDDADLDKAVEGALASKFRNAGQ 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 776 KCSASSLLVLvsSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVvpdDEKAV------------RGLTTLGSGehwv 843
Cdd:PRK11241 288 TCVCANRLYV--QDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLI---DEKAVakveehiadaleKGARVVCGG---- 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 844 lKPRYLGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGN 923
Cdd:PRK11241 359 -KAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGI 437
|
410 420 430
....*....|....*....|....*....|....*...
gi 2219515474 924 LYVNRGITGAIVrrQPFGGWKRSAIGST-TKAGGPSYL 960
Cdd:PRK11241 438 VGINTGIISNEV--APFGGIKASGLGREgSKYGIEDYL 473
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
542-949 |
2.83e-31 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 129.85 E-value: 2.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 542 ATNAEVDTLVTATAEA-----AGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSD------------- 603
Cdd:PLN02467 42 ATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAwdmddvagcfeyy 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 604 PEVSEAIDfchHYAESSLLLHDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELV 683
Cdd:PLN02467 122 ADLAEALD---AKQKAPVSLPMETFKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 684 RAFHDAGIPED-LVVLAPLEDgDVSRHLVTHKDVDRVVLTGSYDTARLFRSW-----KPDMHLLGetsGKNAIIVTPSAD 757
Cdd:PLN02467 199 DICREVGLPPGvLNVVTGLGT-EAGAPLASHPGVDKIAFTGSTATGRKIMTAaaqmvKPVSLELG---GKSPIIVFDDVD 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 758 PDIAVRDAVYSAFAHAGQKCSASSLLVLvssagtSERIA----RQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAV--- 830
Cdd:PLN02467 275 LDKAVEWAMFGCFWTNGQICSATSRLLV------HERIAseflEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVlkf 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 831 ------RGLTTLGSGEhwvlKPRYLGDGLWT-PGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSG 903
Cdd:PLN02467 349 istaksEGATILCGGK----RPEHLKKGFFIePTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGA 424
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2219515474 904 IQTLDATELAIWLEGVQAGNLYVNrgITGAIVRRQPFGGWKRSAIG 949
Cdd:PLN02467 425 VISNDLERCERVSEAFQAGIVWIN--CSQPCFCQAPWGGIKRSGFG 468
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
525-949 |
4.82e-31 |
|
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: 128.38 E-value: 4.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 525 PDSTRGLAEVEAGAArlatnAEVDTLVTATAEA--AGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQS 602
Cdd:cd07142 26 PRNGEVIAHVAEGDA-----EDVDRAVKAARKAfdEGPWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 603 D-PEVSEAIDFCHHYAESSLLLH------DGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPA 675
Cdd:cd07142 101 RyAEVPLAARLFRYYAGWADKIHgmtlpaDGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 676 RRCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLF------RSWKPDMHLLGetsGKNA 749
Cdd:cd07142 181 PLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIImqlaakSNLKPVTLELG---GKSP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 750 IIVTPSADPDIAVRDAVYSAFAHAGQKCSASSLLVLvssagtSERIARQLVD-ATASLRVRL---PLSLDSQMGPVVvpD 825
Cdd:cd07142 258 FIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFV------HESIYDEFVEkAKARALKRVvgdPFRKGVEQGPQV--D 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 826 DEKAVRGLTTLGSGEHWVLKPRYLGDGLWT------PGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYG 899
Cdd:cd07142 330 KEQFEKILSYIEHGKEEGATLITGGDRIGSkgyyiqPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYG 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2219515474 900 LTSGIQTLDATELAIWLEGVQAGNLYVN--RGITGAIvrrqPFGGWKRSAIG 949
Cdd:cd07142 410 LAAGVFSKNIDTANTLSRALKAGTVWVNcyDVFDASI----PFGGYKMSGIG 457
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
533-949 |
5.77e-31 |
|
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: 128.33 E-value: 5.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 533 EVEAGAARLATNAEVDTLVtATAEAA--GVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDP-EVSEA 609
Cdd:cd07113 25 EQVIASVASATEADVDAAV-ASAWRAfvSAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHLSRAfEVGQS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 610 IDFCHHYA-----------ESSLLLhdgghMVGARFI------PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKP- 671
Cdd:cd07113 104 ANFLRYFAgwatkingetlAPSIPS-----MQGERYTaftrrePVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPs 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 672 --APPARRCAAELVRafhDAGIPeDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDmHLLG---ETSG 746
Cdd:cd07113 179 efTPLTLLRVAELAK---EAGIP-DGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAAS-DLTRvtlELGG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 747 KNAIIVTPSADPDIAVRDAVYSAFAHAGQKCSASSLLVLVSSagTSERIARQLVDATASLRVRLPLSLDSQMGPVV-VPD 825
Cdd:cd07113 254 KNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRS--KFDELVTKLKQALSSFQVGSPMDESVMFGPLAnQPH 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 826 DEKAVRGLTTLGSGEHWVLkprYLGDGLWTPGI----RAGVVPGSEFHLT--EYFAPVIGVMRVDTLQEAIEAVNAVDYG 899
Cdd:cd07113 332 FDKVCSYLDDARAEGDEIV---RGGEALAGEGYfvqpTLVLARSADSRLMreETFGPVVSFVPYEDEEELIQLINDTPFG 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2219515474 900 LTSGIQTLDATELAIWLEGVQAGNLYVN-RGITGAIVrrqPFGGWKRSAIG 949
Cdd:cd07113 409 LTASVWTNNLSKALRYIPRIEAGTVWVNmHTFLDPAV---PFGGMKQSGIG 456
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
542-952 |
1.55e-30 |
|
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: 127.07 E-value: 1.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 542 ATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARrAELIEVAgseagKTIDQSDP-------EVSEAIDFCH 614
Cdd:cd07559 35 STAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEEN-LELLAVA-----ETLDNGKPiretlaaDIPLAIDHFR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 615 HYA------ESSLLLHDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHD 688
Cdd:cd07559 109 YFAgviraqEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 689 AgIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDmHLLG---ETSGKNAIIVTPSA-DPDIAVRD 764
Cdd:cd07559 189 L-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE-NLIPvtlELGGKSPNIFFDDAmDADDDFDD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 765 AVYSAFA----HAGQKCSASS-LLVlvsSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAV--------- 830
Cdd:cd07559 267 KAEEGQLgfafNQGEVCTCPSrALV---QESIYDEFIERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKIlsyvdigke 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 831 RGLTTLGSGEHWVLkPRYLGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDAT 910
Cdd:cd07559 344 EGAEVLTGGERLTL-GGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDIN 422
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2219515474 911 ELAIWLEGVQAGNLYVNrgITGAIVRRQPFGGWKRSAIGSTT 952
Cdd:cd07559 423 RALRVARGIQTGRVWVN--CYHQYPAHAPFGGYKKSGIGRET 462
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
542-949 |
2.50e-30 |
|
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: 126.36 E-value: 2.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 542 ATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQS-DPEVSEAIDFCHHYAESS 620
Cdd:cd07111 56 AEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESrDCDIPLVARHFYHHAGWA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 621 LLLHDGGHMVGarfiPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDlVVLAP 700
Cdd:cd07111 136 QLLDTELAGWK----PVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPG-VLNIV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 701 LEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRS----WKPDMHLlgETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQK 776
Cdd:cd07111 211 TGNGSFGSALANHPGVDKVAFTGSTEVGRALRRatagTGKKLSL--ELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 777 CSASS-LLVLVSSAgtsERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLGSGEH---WVLKPRYLGDG 852
Cdd:cd07111 289 CCAGSrLLVQESVA---EELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGadvFQPGADLPSKG 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 853 LW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD---ATELAIwleGVQAGNLYVN- 927
Cdd:cd07111 366 PFyPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENlslALEVAL---SLKAGVVWINg 442
|
410 420
....*....|....*....|..
gi 2219515474 928 RGITGAIVrrqPFGGWKRSAIG 949
Cdd:cd07111 443 HNLFDAAA---GFGGYRESGFG 461
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
538-949 |
2.79e-30 |
|
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: 125.88 E-value: 2.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 538 AARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYA 617
Cdd:cd07151 25 EIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANIEWGAAMAITREAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 618 ESSLLLH--------DGGHMVGARfIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELV-RAFHD 688
Cdd:cd07151 105 TFPLRMEgrilpsdvPGKENRVYR-EPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGLLLaKIFEE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 689 AGIPEDL---VVLAPLEDGDvsrHLVTHKdVDRVV-LTGSYDTARLF-----RSWKpdmHLLGETSGKNAIIVTPSADPD 759
Cdd:cd07151 184 AGLPKGVlnvVVGAGSEIGD---AFVEHP-VPRLIsFTGSTPVGRHIgelagRHLK---KVALELGGNNPFVVLEDADID 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 760 IAVRDAVYSAFAHAGQKC-SASSLLVlvsSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDD--------EKAV 830
Cdd:cd07151 257 AAVNAAVFGKFLHQGQICmAINRIIV---HEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQvdglldkiEQAV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 831 R-GLTTLGSGEHwvlkprylGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD- 908
Cdd:cd07151 334 EeGATLLVGGEA--------EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDl 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2219515474 909 --ATELAiwlEGVQAGNLYVNRGITG--AIVrrqPFGGWKRSAIG 949
Cdd:cd07151 406 erGVQFA---RRIDAGMTHINDQPVNdePHV---PFGGEKNSGLG 444
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
539-950 |
6.76e-30 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 125.02 E-value: 6.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 539 ARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQS-DPEVSEAIDFCHHYA 617
Cdd:PRK13473 33 IAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLAlNDEIPAIVDVFRFFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 618 ESSLLLH-------DGGHMVGARFIPVDVtvVAS--PWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHD 688
Cdd:PRK13473 113 GAARCLEgkaageyLEGHTSMIRRDPVGV--VASiaPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAAD 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 689 AgIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLF-----RSWKpDMHLlgETSGKNAIIVTPSADPDIAVR 763
Cdd:PRK13473 191 I-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVlsaaaDSVK-RTHL--ELGGKAPVIVFDDADLDAVVE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 764 DAVYSAFAHAGQKCSASS-LLVlvsSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVV----------VPDDEKAVRG 832
Cdd:PRK13473 267 GIRTFGYYNAGQDCTAACrIYA---QRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLIsaahrdrvagFVERAKALGH 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 833 LTTLGSGEhwvlkpRYLGDG-LWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD--- 908
Cdd:PRK13473 344 IRVVTGGE------APDGKGyYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDvgr 417
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2219515474 909 ATELAIWLegvQAGNLYVNRGITgaIVRRQPFGGWKRSAIGS 950
Cdd:PRK13473 418 AHRVSARL---QYGCTWVNTHFM--LVSEMPHGGQKQSGYGK 454
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
531-949 |
1.16e-29 |
|
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: 124.38 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 531 LAEVEAGaarlaTNAEVDTLVTATAEA---AGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTI-DQSDPEV 606
Cdd:cd07141 35 ICEVQEG-----DKADVDKAVKAARAAfklGSPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFsKSYLVDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 607 SEAIDFCHHYAESSLLLH------DGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPA---PPARR 677
Cdd:cd07141 110 PGAIKVLRYYAGWADKIHgktipmDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAeqtPLTAL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 678 CAAELVRafhDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFR--SWKPDMHLLG-ETSGKNAIIVTP 754
Cdd:cd07141 190 YLASLIK---EAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQqaAGKSNLKRVTlELGGKSPNIVFA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 755 SADPDIAVRDAVYSAFAHAGQKCSASSlLVLVSSAGTSERIARqLVDATASLRVRLPLSLDSQMGPVVvpDDE--KAVRG 832
Cdd:cd07141 267 DADLDYAVEQAHEALFFNMGQCCCAGS-RTFVQESIYDEFVKR-SVERAKKRVVGNPFDPKTEQGPQI--DEEqfKKILE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 833 LTTLG---------SGEHWVLKPRYLgdglwTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSG 903
Cdd:cd07141 343 LIESGkkegaklecGGKRHGDKGYFI-----QPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAA 417
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2219515474 904 IQTLDATELAIWLEGVQAGNLYVNrgITGAIVRRQPFGGWKRSAIG 949
Cdd:cd07141 418 VFTKDIDKAITFSNALRAGTVWVN--CYNVVSPQAPFGGYKMSGNG 461
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
545-949 |
2.57e-29 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 123.65 E-value: 2.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 545 AEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESS---- 620
Cdd:PLN02278 62 AETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAkrvy 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 621 ---LLLHDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPA---PPARRCAAELVRafhDAGIPED 694
Cdd:PLN02278 142 gdiIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSeltPLTALAAAELAL---QAGIPPG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 695 LVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFrswkpdMHLLGETS-------GKNA-IIVTPSADPDIAVRDAV 766
Cdd:PLN02278 219 VLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKL------MAGAAATVkrvslelGGNApFIVFDDADLDVAVKGAL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 767 YSAFAHAGQKC-SASSLLVlvsSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVvpdDEKAVRGLTT-----LGSGE 840
Cdd:PLN02278 293 ASKFRNSGQTCvCANRILV---QEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLI---NEAAVQKVEShvqdaVSKGA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 841 HWVL--KPRYLGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEG 918
Cdd:PLN02278 367 KVLLggKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEA 446
|
410 420 430
....*....|....*....|....*....|.
gi 2219515474 919 VQAGNLYVNRGITGAIVrrQPFGGWKRSAIG 949
Cdd:PLN02278 447 LEYGIVGVNEGLISTEV--APFGGVKQSGLG 475
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
543-950 |
3.45e-29 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 123.33 E-value: 3.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 543 TNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESSL- 621
Cdd:PLN00412 51 TQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVr 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 622 LLHDGGHMVGARF-------------IPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHD 688
Cdd:PLN00412 131 ILGEGKFLVSDSFpgnernkycltskIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 689 AGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSyDTArLFRSWKPDM-HLLGETSGKNAIIVTPSADPDIAVRDAVY 767
Cdd:PLN00412 211 AGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTG-IAISKKAGMvPLQMELGGKDACIVLEDADLDLAAANIIK 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 768 SAFAHAGQKCSASSlLVLVssagtSERIARQLVDA----TASLRVRLPLSlDSQMGPVVVPDDEKAVRGLTT--LGSGEH 841
Cdd:PLN00412 289 GGFSYSGQRCTAVK-VVLV-----MESVADALVEKvnakVAKLTVGPPED-DCDITPVVSESSANFIEGLVMdaKEKGAT 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 842 WVLKPRYLGDGLWtPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQA 921
Cdd:PLN00412 362 FCQEWKREGNLIW-PLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMET 440
|
410 420 430
....*....|....*....|....*....|..
gi 2219515474 922 GNLYVNrgitGAIVR---RQPFGGWKRSAIGS 950
Cdd:PLN00412 441 GTVQIN----SAPARgpdHFPFQGLKDSGIGS 468
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
541-949 |
3.56e-29 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 122.66 E-value: 3.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 541 LATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAE-- 618
Cdd:PRK13968 25 WAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYAEhg 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 619 ------SSLLLHDGGHMVGARfiPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIP 692
Cdd:PRK13968 105 pamlkaEPTLVENQQAVIEYR--PLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKDAGIP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 693 EDLVVLAPLEDGDVSRhLVTHKDVDRVVLTGSYDT-----ARLFRSWKPDMHLLGetsGKNAIIVTPSADPDIAVRDAVY 767
Cdd:PRK13968 183 QGVYGWLNADNDGVSQ-MINDSRIAAVTVTGSVRAgaaigAQAGAALKKCVLELG---GSDPFIVLNDADLELAVKAAVA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 768 SAFAHAGQKCSASSLLVLvsSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPD--DEKAVRGLTTLGSGEHWVLK 845
Cdd:PRK13968 259 GRYQNTGQVCAAAKRFII--EEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDlrDELHHQVEATLAEGARLLLG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 846 PRYL-GDG-LWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGN 923
Cdd:PRK13968 337 GEKIaGAGnYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGG 416
|
410 420
....*....|....*....|....*.
gi 2219515474 924 LYVNrGITgAIVRRQPFGGWKRSAIG 949
Cdd:PRK13968 417 VFIN-GYC-ASDARVAFGGVKKSGFG 440
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
543-963 |
3.40e-27 |
|
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: 116.63 E-value: 3.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 543 TNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKT-IDQSDPEV---SEAIDFCHHYAE 618
Cdd:cd07098 16 TPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTmVDASLGEIlvtCEKIRWTLKHGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 619 SSL----------LLHDGGHMvgaRFIPVDVTVVASPWNFPLaiptggvaaalaagsAVILKPAPPAR--------RCA- 679
Cdd:cd07098 96 KALrpesrpggllMFYKRARV---EYEPLGVVGAIVSWNYPF---------------HNLLGPIIAALfagnaivvKVSe 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 680 ---------AELVR-AFHDAGIPEDLVVLAPLEdGDVSRHLVTHKDVDRVVLTGSYDTARLF-----RSWKPdmhLLGET 744
Cdd:cd07098 158 qvawssgffLSIIReCLAACGHDPDLVQLVTCL-PETAEALTSHPVIDHITFIGSPPVGKKVmaaaaESLTP---VVLEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 745 SGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCsASSLLVLVSSaGTSERIARQLVDATASLRVRLPLSLDSQMGPVVVP 824
Cdd:cd07098 234 GGKDPAIVLDDADLDQIASIIMRGTFQSSGQNC-IGIERVIVHE-KIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 825 DDEKAVRGL--------TTLGSGEHWVLKPRYLGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAV 896
Cdd:cd07098 312 ARFDRLEELvadavekgARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANST 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2219515474 897 DYGLTSGIQTLDATELAIWLEGVQAGNLYVNRGITGAIVRRQPFGGWKRSAIGsttKAGGPSYLLGL 963
Cdd:cd07098 392 EYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFG---RFAGEEGLRGL 455
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
564-949 |
2.50e-25 |
|
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: 110.97 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 564 LDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESslLLHDGGHMV-------GARFI- 635
Cdd:cd07148 41 LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVELAADE--LGQLGGREIpmgltpaSAGRIa 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 636 -----PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVVLAPLEDgDVSRHL 710
Cdd:cd07148 119 fttrePIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCEN-AVAEKL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 711 VTHKDVDRVVLTGSYDTARLFRS-WKPDMHLLGETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCsaSSLLVLVSSA 789
Cdd:cd07148 198 VTDPRVAFFSFIGSARVGWMLRSkLAPGTRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVC--VSVQRVFVPA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 790 GTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPD---------DEKAVRGLTTLGSGehwvlkpRYLGDGLWTPGIRA 860
Cdd:cd07148 276 EIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPRevdrveewvNEAVAAGARLLCGG-------KRLSDTTYAPTVLL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 861 GVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGI--QTLDATELAIwlEGVQAGNLYVNRGiTGAIVRRQ 938
Cdd:cd07148 349 DPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVftKDLDVALKAV--RRLDATAVMVNDH-TAFRVDWM 425
|
410
....*....|.
gi 2219515474 939 PFGGWKRSAIG 949
Cdd:cd07148 426 PFAGRRQSGYG 436
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
542-949 |
2.71e-25 |
|
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: 111.08 E-value: 2.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 542 ATNAEVDTLVTAtAEAA--GVW-QSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDP-EVSEAIDFCHHYA 617
Cdd:cd07143 41 ATEADVDIAVEV-AHAAfeTDWgLKVSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTFGTAKRvDVQASADTFRYYG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 618 ESSLLLH------DGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGI 691
Cdd:cd07143 120 GWADKIHgqvietDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGF 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 692 PEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDMHLLG---ETSGKNAIIVTPSADPDIAVRDAVYS 768
Cdd:cd07143 200 PPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSNLKKvtlELGGKSPNIVFDDADLESAVVWTAYG 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 769 AFAHAGQKCSASSlLVLVSSaGTSERIARQLVDATASLRVRLPLSLDSQMGPVVvpDDEKAVRGLTTLGSGehwvlkpRY 848
Cdd:cd07143 280 IFFNHGQVCCAGS-RIYVQE-GIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQV--SQIQYERIMSYIESG-------KA 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 849 LGDGLWTPGIRAG-------------VVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD---ATEL 912
Cdd:cd07143 349 EGATVETGGKRHGnegyfieptiftdVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNinnAIRV 428
|
410 420 430
....*....|....*....|....*....|....*..
gi 2219515474 913 AIWLEgvqAGNLYVNrgITGAIVRRQPFGGWKRSAIG 949
Cdd:cd07143 429 ANALK---AGTVWVN--CYNLLHHQVPFGGYKQSGIG 460
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
541-949 |
7.73e-25 |
|
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: 109.80 E-value: 7.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 541 LATNAEVDTLVTAtAEAA--GVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQ-SDPEVSEAIDFCHHYA 617
Cdd:cd07144 41 AAGEEDVDKAVKA-ARKAfeSWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYHSnALGDLDEIIAVIRYYA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 618 ESSLLLHdgghmvGARFI------------PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRA 685
Cdd:cd07144 120 GWADKIQ------GKTIPtspnklaytlhePYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 686 FHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFrswkpdMHLLG--------ETSGKNAIIVTPSAD 757
Cdd:cd07144 194 VKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLV------MKAAAqnlkavtlECGGKSPALVFEDAD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 758 PDIAVRDAVYSAFAHAGQKCSASSlLVLVssagtSERIARQLVD-----ATASLRVRLPLSLDSQMGPVVVPDDEKAVRG 832
Cdd:cd07144 268 LDQAVKWAAAGIMYNSGQNCTATS-RIYV-----QESIYDKFVEkfvehVKQNYKVGSPFDDDTVVGPQVSKTQYDRVLS 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 833 LTTLGS--GEHWVL----KPRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQ 905
Cdd:cd07144 342 YIEKGKkeGAKLVYggekAPEGLGKGYFiPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVF 421
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2219515474 906 TLDATELAIWLEGVQAGNLYVNRGITGAIvrRQPFGGWKRSAIG 949
Cdd:cd07144 422 TKDIRRAHRVARELEAGMVWINSSNDSDV--GVPFGGFKMSGIG 463
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
525-949 |
4.28e-24 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 107.67 E-value: 4.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 525 PDSTRGLAEVEAGaarlaTNAEVDTLVTATAEA--AGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQS 602
Cdd:PRK09847 42 PVTQAPLAKIARG-----KSVDIDRAVSAARGVfeRGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 603 -DPEVSEAIDFCHHYAESSLLLH------DGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPA 675
Cdd:PRK09847 117 lRDDIPGAARAIRWYAEAIDKVYgevattSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 676 RRCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDMHLLG---ETSGKNA-II 751
Cdd:PRK09847 197 PLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSNMKRvwlEAGGKSAnIV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 752 VTPSADPDIAVRDAVYSAFAHAGQKCSASSLLVLVSSAgTSERIARqLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVR 831
Cdd:PRK09847 277 FADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESI-ADEFLAL-LKQQAQNWQPGHPLDPATTMGTLIDCAHADSVH 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 832 GLTTLGSGEHWVL-------KPRYLGdglwtPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGI 904
Cdd:PRK09847 355 SFIREGESKGQLLldgrnagLAAAIG-----PTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAV 429
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2219515474 905 QTLDATELAIWLEGVQAGNLYVNRGITGAIVrrQPFGGWKRSAIG 949
Cdd:PRK09847 430 WTRDLSRAHRMSRRLKAGSVFVNNYNDGDMT--VPFGGYKQSGNG 472
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
542-949 |
8.99e-24 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 106.83 E-value: 8.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 542 ATNAEVDTLVTATAEA--AGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGK------TIDqsdpeVSEAIDFC 613
Cdd:PLN02766 55 GDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKlfalgkAVD-----IPAAAGLL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 614 HHYAESSLLLHDGGHMVGARFI------PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFH 687
Cdd:PLN02766 130 RYYAGAADKIHGETLKMSRQLQgytlkePIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAK 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 688 DAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLF-----RSWKPDMHLlgETSGKNAIIVTPSADPDIAV 762
Cdd:PLN02766 210 LAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKImqaaaTSNLKQVSL--ELGGKSPLLIFDDADVDMAV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 763 RDAVYSAFAHAGQKCSASSLlVLVSSaGTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLGSGEHW 842
Cdd:PLN02766 288 DLALLGIFYNKGEICVASSR-VYVQE-GIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGA 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 843 VL----KPryLGD-GLWT-PGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWL 916
Cdd:PLN02766 366 TLltggKP--CGDkGYYIePTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVS 443
|
410 420 430
....*....|....*....|....*....|...
gi 2219515474 917 EGVQAGNLYVNrgITGAIVRRQPFGGWKRSAIG 949
Cdd:PLN02766 444 RSIRAGTIWVN--CYFAFDPDCPFGGYKMSGFG 474
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
531-949 |
1.34e-23 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 106.12 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 531 LAEVEAgaarlATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQS---DPeVS 607
Cdd:PRK13252 35 LATVQA-----ATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQETsvvDI-VT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 608 EAiDFCHHYA------ESSLLLHDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAE 681
Cdd:PRK13252 109 GA-DVLEYYAglapalEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 682 LVRAFHDAGIPEDL--VVLApleDGDVSRHLVTHKDVDRVVLTGSYDTARLF-----RSWKpdmHLLGETSGKNAIIVTP 754
Cdd:PRK13252 188 LAEIYTEAGLPDGVfnVVQG---DGRVGAWLTEHPDIAKVSFTGGVPTGKKVmaaaaASLK---EVTMELGGKSPLIVFD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 755 SADPDIAVRDAVYSAFAHAGQKCSASSlLVLVSSAGTSERIARqLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLT 834
Cdd:PRK13252 262 DADLDRAADIAMLANFYSSGQVCTNGT-RVFVQKSIKAAFEAR-LLERVERIRIGDPMDPATNFGPLVSFAHRDKVLGYI 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 835 TLGSGEH-------WVLKPRYLGDGLWT-PGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQT 906
Cdd:PRK13252 340 EKGKAEGarllcggERLTEGGFANGAFVaPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFT 419
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2219515474 907 LDATELAIWLEGVQAGNLYVNR-GITGAivrRQPFGGWKRSAIG 949
Cdd:PRK13252 420 ADLSRAHRVIHQLEAGICWINTwGESPA---EMPVGGYKQSGIG 460
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
525-949 |
2.32e-21 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 99.50 E-value: 2.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 525 PDSTRGLAEVEAGAARlatnaEVDTLVTATAEA--AGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQS 602
Cdd:PLN02466 80 PRTGEVIAHVAEGDAE-----DVNRAVAAARKAfdEGPWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQS 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 603 -DPEVSEAIDFCHHYAESSLLLH------DGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPA 675
Cdd:PLN02466 155 aKAELPMFARLFRYYAGWADKIHgltvpaDGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQT 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 676 RRCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLF-----RS-WKPDMHLLGetsGKNA 749
Cdd:PLN02466 235 PLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVlelaaKSnLKPVTLELG---GKSP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 750 IIVTPSADPDIAVRDAVYSAFAHAGQKCSASSLLVLvssagtSERIARQLVD---ATASLR-VRLPLSLDSQMGPVVVPD 825
Cdd:PLN02466 312 FIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFV------HERVYDEFVEkakARALKRvVGDPFKKGVEQGPQIDSE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 826 D-EKAVR--------GLTTLGSGEHWVLKPRYLgdglwTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAV 896
Cdd:PLN02466 386 QfEKILRyiksgvesGATLECGGDRFGSKGYYI-----QPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNT 460
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2219515474 897 DYGLTSGIQTLDATELAIWLEGVQAGNLYVN--RGITGAIvrrqPFGGWKRSAIG 949
Cdd:PLN02466 461 RYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfDVFDAAI----PFGGYKMSGIG 511
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
541-927 |
3.48e-21 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 99.44 E-value: 3.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 541 LATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESS 620
Cdd:PLN02419 147 LTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMA 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 621 LL-----LHDGGHMVGARFI--PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPA---PPARRCAAELVRafhDAG 690
Cdd:PLN02419 227 TLqmgeyLPNVSNGVDTYSIrePLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSekdPGASVILAELAM---EAG 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 691 IPEDLVVLAPLEDgDVSRHLVTHKDVDRVVLTGSyDTARLF---RSWKPDMHLLGETSGKNAIIVTPSADPDIAVRDAVY 767
Cdd:PLN02419 304 LPDGVLNIVHGTN-DTVNAICDDEDIRAVSFVGS-NTAGMHiyaRAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLA 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 768 SAFAHAGQKCSASSLLVLVSSAGTSERiarQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLG--SGEHWVLK 845
Cdd:PLN02419 382 AGFGAAGQRCMALSTVVFVGDAKSWED---KLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGvdDGAKLLLD 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 846 ------PRYLGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGV 919
Cdd:PLN02419 459 grdivvPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDI 538
|
....*...
gi 2219515474 920 QAGNLYVN 927
Cdd:PLN02419 539 EAGQIGIN 546
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
573-949 |
4.44e-21 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 97.11 E-value: 4.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 573 LHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYA------ESSLLLHDGGH---MVGARfiPVDVTVVA 643
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAewarryEGEIIQSDRPGeniLLFKR--ALGVTTGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 644 SPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTG 723
Cdd:PRK10090 79 LPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 724 SYDT-ARLFRSWKPDMHLLG-ETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCSASSLlVLVSSaGTSERIARQLVD 801
Cdd:PRK10090 159 SVSAgEKIMAAAAKNITKVClELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAER-VYVQK-GIYDQFVNRLGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 802 ATASLRVRLPLS-LDSQMGPVVVPDD--------EKAV-RGLTTLGSGEhwvlkpRYLGDG-LWTPGIRAGVVPGSEFHL 870
Cdd:PRK10090 237 AMQAVQFGNPAErNDIAMGPLINAAAlerveqkvARAVeEGARVALGGK------AVEGKGyYYPPTLLLDVRQEMSIMH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 871 TEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGNLYVNRGITGAIvrrQPF-GGWKRSAIG 949
Cdd:PRK10090 311 EETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAM---QGFhAGWRKSGIG 387
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
541-949 |
1.13e-20 |
|
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: 96.80 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 541 LATNAEVDTLVTATAEA--AGVWQSLDPAERAAALHRVGDVLAARRAEL--IEVAGSEAGKTIdQSDPEVSEAIDFCHHY 616
Cdd:cd07140 39 LATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQEELatIESLDSGAVYTL-ALKTHVGMSIQTFRYF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 617 AESSLLLHD----------GGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAF 686
Cdd:cd07140 118 AGWCDKIQGktipinqarpNRNLTLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 687 HDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDMHLLG---ETSGKNAIIVTPSADPDIAVR 763
Cdd:cd07140 198 VKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAVSNLKKvslELGGKSPLIIFADCDMDKAVR 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 764 DAVYSAFAHAGQKCSASSLLVLVSSagTSERIARQLVDATASLRVRLPLSLDSQMGP--------VVVPDDEKAVRGLTT 835
Cdd:cd07140 278 MGMSSVFFNKGENCIAAGRLFVEES--IHDEFVRRVVEEVKKMKIGDPLDRSTDHGPqnhkahldKLVEYCERGVKEGAT 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 836 LGSGEHWVLKPRYlgdgLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDT--LQEAIEAVNAVDYGLTSGIQTLDATELA 913
Cdd:cd07140 356 LVYGGKQVDRPGF----FFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDgdVDGVLQRANDTEYGLASGVFTKDINKAL 431
|
410 420 430
....*....|....*....|....*....|....*.
gi 2219515474 914 IWLEGVQAGNLYVNRGITGAIVrrQPFGGWKRSAIG 949
Cdd:cd07140 432 YVSDKLEAGTVFVNTYNKTDVA--APFGGFKQSGFG 465
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
525-959 |
1.19e-19 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 94.13 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 525 PDSTRGLAEVEAGAARlatnaEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDP 604
Cdd:PLN02315 41 PANNQPIAEVVEASLE-----DYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 605 EVSEAIDFCHHYAESSLLLHDG-------GHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAP--PA 675
Cdd:PLN02315 116 EVQEIIDMCDFAVGLSRQLNGSiipserpNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPttPL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 676 RRCAAELVRA--FHDAGIPeDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDMH--LLGETSGKNAII 751
Cdd:PLN02315 196 ITIAMTKLVAevLEKNNLP-GAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFgkCLLELSGNNAII 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 752 VTPSADPDIAVRDAVYSAFAHAGQKCSASSLLVLVSSagTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAV- 830
Cdd:PLN02315 275 VMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHES--IYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFe 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 831 RGLTTLGS--GEHWVLKPRYLGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD 908
Cdd:PLN02315 353 KGIEIIKSqgGKILTGGSAIESEGNFVQPTIVEISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRN 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2219515474 909 ATELAIWL--EGVQAGNLYVNRGITGAIVrRQPFGGWKrsAIGSTTKAGGPSY 959
Cdd:PLN02315 433 PETIFKWIgpLGSDCGIVNVNIPTNGAEI-GGAFGGEK--ATGGGREAGSDSW 482
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
538-952 |
2.41e-18 |
|
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: 89.82 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 538 AARlATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARrAELIEVAGS-EAGKTI-DQSDPEVSEAIDFCHH 615
Cdd:cd07116 32 VPR-STAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEAN-LEMLAVAETwDNGKPVrETLAADIPLAIDHFRY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 616 YA------ESSLLLHDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDA 689
Cdd:cd07116 110 FAgciraqEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 690 gIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPD--MHLLGETSGKNAIIVTPS-ADPDIAVRDAV 766
Cdd:cd07116 190 -LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASEniIPVTLELGGKSPNIFFADvMDADDAFFDKA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 767 YSAFA----HAGQKCSASSLLVLVSSagTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDD-EKAVR--------GL 833
Cdd:cd07116 269 LEGFVmfalNQGEVCTCPSRALIQES--IYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQlEKILSyidigkeeGA 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 834 TTLGSGEHWVLkPRYLGDGLWTPGIRAGVVPGSEFHlTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELA 913
Cdd:cd07116 347 EVLTGGERNEL-GGLLGGGYYVPTTFKGGNKMRIFQ-EEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAY 424
|
410 420 430
....*....|....*....|....*....|....*....
gi 2219515474 914 IWLEGVQAGNLYVNrgITGAIVRRQPFGGWKRSAIGSTT 952
Cdd:cd07116 425 RMGRGIQAGRVWTN--CYHLYPAHAAFGGYKQSGIGREN 461
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
533-949 |
3.38e-18 |
|
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 275104 Cd Length: 480 Bit Score: 89.06 E-value: 3.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 533 EVEAGAARLATNAEVDTLVTATAEA--AGVWqSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTID-QSDPEVSEA 609
Cdd:TIGR04284 25 EEVLGVAADATAADMDAAIAAARRAfdETDW-SRDTALRVRCLRQLRDALRAHVEELRELTIAEVGAPRMlTAGAQLEGP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 610 ID---FCHHYAESSLLLHDGGHMV--------GARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRC 678
Cdd:TIGR04284 104 VDdlgFAADLAESYAWTTDLGVASpmgiptrrTLRREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWC 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 679 AAELVR-AFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTAR--LFRSWKPDMHLLGETSGKNAIIVTPS 755
Cdd:TIGR04284 184 AAVLGElIAEHTDFPPGVVNIVTSSDHRLGALLAKDPRVDMVSFTGSTATGRavMADAAATLKKVFLELGGKSAFIVLDD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 756 ADPDIAVRDAVYSAFAHAGQKCSASSLLVlVSSAGTSERIArQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTT 835
Cdd:TIGR04284 264 ADLAAACSMAAFTVCMHAGQGCAITTRLV-VPRARYDEAVA-AAAATMGSIKPGDPADPGTVCGPVISARQRDRVQSYLD 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 836 LGSGEHWVL-----KPRYLGDGLWT-PGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDA 909
Cdd:TIGR04284 342 LAVAEGGRFacgggRPADRDRGFFVePTVIAGLDNNARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVFGADP 421
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2219515474 910 TELAIWLEGVQAGNLYVNRGI-TGAIVrrqPFGGWKRSAIG 949
Cdd:TIGR04284 422 ERAAAVAARVRTGTVNVNGGVwYSADA---PFGGYKQSGIG 459
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
547-957 |
3.60e-17 |
|
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: 85.75 E-value: 3.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 547 VDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQsdpevseAIDFCHHYAE-------- 618
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMF-------AENICGDQVQlrarafvi 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 619 SSLLLHDG-------GHMVGARF--IPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDA 689
Cdd:cd07084 74 YSYRIPHEpgnhlgqGLKQQSHGyrWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 690 GI--PEDLVVLAplEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDMHLLGETSGKNAIIVTPSADP-DIAVRDAV 766
Cdd:cd07084 154 GLlpPEDVTLIN--GDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQARIYLELAGFNWKVLGPDAQAvDYVAWQCV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 767 YSAFAHAGQKCSASS-LLVLVSSAGtseriaRQLVDATASLRVRLPLSlDSQMGPVVVPDDEKAV--------RGLTTLG 837
Cdd:cd07084 232 QDMTACSGQKCTAQSmLFVPENWSK------TPLVEKLKALLARRKLE-DLLLGPVQTFTTLAMIahmenllgSVLLFSG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 838 SGEHWVLKPRYLGdglwtPGIRAGV-VPGSE------FHLTEYFAPV--IGVMRVDTLQEAIEAVNAVDYGLTSGIQT-- 906
Cdd:cd07084 305 KELKNHSIPSIYG-----ACVASALfVPIDEilktyeLVTEEIFGPFaiVVEYKKDQLALVLELLERMHGSLTAAIYSnd 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2219515474 907 ---LDATELAIWLEGVQagnLYVNRGITGAIVRRQPFGGWKRSAIGstTKAGGP 957
Cdd:cd07084 380 pifLQELIGNLWVAGRT---YAILRGRTGVAPNQNHGGGPAADPRG--AGIGGP 428
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
558-950 |
4.09e-11 |
|
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: 66.48 E-value: 4.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 558 AGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSD-----PEVSEAIDFCHHYAE--------SSLLlh 624
Cdd:cd07134 11 ALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDlteilPVLSEINHAIKHLKKwmkpkrvrTPLL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 625 dgghMVGA----RFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKP---APPARRCAAELVR-AFhdagiPEDLV 696
Cdd:cd07134 89 ----LFGTkskiRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPselTPHTSAVIAKIIReAF-----DEDEV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 697 vlAPLE-DGDVSRHLVThKDVDRVVLTGSYDTARLFrswkpdM-----HLLG---ETSGKNAIIVTPSADPDIAVRDAVY 767
Cdd:cd07134 160 --AVFEgDAEVAQALLE-LPFDHIFFTGSPAVGKIV------MaaaakHLASvtlELGGKSPTIVDETADLKKAAKKIAW 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 768 SAFAHAGQKCSA-----------SSLLVLVSSA-----GTSERIAR-----QLVDATASLRVRLPLsldsqmgpvvvpdD 826
Cdd:cd07134 231 GKFLNAGQTCIApdyvfvhesvkDAFVEHLKAEiekfyGKDAARKAspdlaRIVNDRHFDRLKGLL-------------D 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 827 EKAVRGLTTLGSGEHwVLKPRYLGdglwtPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQT 906
Cdd:cd07134 298 DAVAKGAKVEFGGQF-DAAQRYIA-----PTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFS 371
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2219515474 907 LDATELAIWLEGVQAGNLYVNRGITGAIVRRQPFGGWKRSAIGS 950
Cdd:cd07134 372 KDKANVNKVLARTSSGGVVVNDVVLHFLNPNLPFGGVNNSGIGS 415
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
633-950 |
1.27e-10 |
|
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: 64.93 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 633 RFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCA---AELVRAFHD--------AGIPEdlvvlapl 701
Cdd:cd07135 105 RKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAallAELVPKYLDpdafqvvqGGVPE-------- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 702 edgdVSRhLVTHKdVDRVVLTGSYDTARLFrSWKPDMHL------LGetsGKNAIIVTPSADPDIAVRDAVYSAFAHAGQ 775
Cdd:cd07135 177 ----TTA-LLEQK-FDKIFYTGSGRVGRII-AEAAAKHLtpvtleLG---GKSPVIVTKNADLELAAKRILWGKFGNAGQ 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 776 KC-SASSLLV-------LVSSAGT--SERIARQLVDATASLRV-------RLPLSLDSQMGPVVVPDDEKAvrglttlgs 838
Cdd:cd07135 247 ICvAPDYVLVdpsvydeFVEELKKvlDEFYPGGANASPDYTRIvnprhfnRLKSLLDTTKGKVVIGGEMDE--------- 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 839 gehwvlKPRYLgdglwTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEG 918
Cdd:cd07135 318 ------ATRFI-----PPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTR 386
|
330 340 350
....*....|....*....|....*....|..
gi 2219515474 919 VQAGNLYVNRGITGAIVRRQPFGGWKRSAIGS 950
Cdd:cd07135 387 TRSGGVVINDTLIHVGVDNAPFGGVGDSGYGA 418
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
636-950 |
1.79e-10 |
|
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: 64.47 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 636 PVDVTVVASPWNFP--LAIP----------TGgvaaalaagsavILKPAPPARRCAAELVRAFHDAgIPEDLVVLAPLeD 703
Cdd:cd07087 100 PLGVVLIIGPWNYPlqLALApligaiaagnTV------------VLKPSELAPATSALLAKLIPKY-FDPEAVAVVEG-G 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 704 GDVSRHLVTHKdVDRVVLTGSYDTARLFrswkpdM-----HL------LGetsGKNAIIVTPSADPDIAVRDAVYSAFAH 772
Cdd:cd07087 166 VEVATALLAEP-FDHIFFTGSPAVGKIV------MeaaakHLtpvtleLG---GKSPCIVDKDANLEVAARRIAWGKFLN 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 773 AGQKCSASS-LLVlvssagtSERIARQLVDAtaslrvrLPLSLDSQMG--PVVVPD-----DEKAVRGLTTLGSGEHWVL 844
Cdd:cd07087 236 AGQTCIAPDyVLV-------HESIKDELIEE-------LKKAIKEFYGedPKESPDygriiNERHFDRLASLLDDGKVVI 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 845 KPRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGN 923
Cdd:cd07087 302 GGQVDKEERYiAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGG 381
|
330 340
....*....|....*....|....*..
gi 2219515474 924 LYVNRGITGAIVRRQPFGGWKRSAIGS 950
Cdd:cd07087 382 VCVNDVLLHAAIPNLPFGGVGNSGMGA 408
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
562-913 |
6.43e-09 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 60.10 E-value: 6.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 562 QSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESSLLLHDGGHMVGA--------- 632
Cdd:PRK11903 58 RALTYAQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAKLGAALGDARLLRDGeavqlgkdp 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 633 ----RFIPVDVTVVA---SPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGI-PEDLVVLAPLEDG 704
Cdd:PRK11903 138 afqgQHVLVPTRGVAlfiNAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 705 DVSRHLvthKDVDRVVLTGSYDTARLFRSW----KPDMHLLGETSGKNAIIVTPSADP-----DIAVRDAVYSAFAHAGQ 775
Cdd:PRK11903 218 GLLDHL---QPFDVVSFTGSAETAAVLRSHpavvQRSVRVNVEADSLNSALLGPDAAPgseafDLFVKEVVREMTVKSGQ 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 776 KCSASSlLVLVSSAgTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVR-GLTTLGSGEHWVLKPRYLGDGLW 854
Cdd:PRK11903 295 KCTAIR-RIFVPEA-LYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRaGLAALRAQAEVLFDGGGFALVDA 372
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2219515474 855 TPGIRAGVVP----------GSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELA 913
Cdd:PRK11903 373 DPAVAACVGPtllgasdpdaATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLA 441
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
636-950 |
1.25e-08 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 58.89 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 636 PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAaELVRAFHDAGIPEDLVVLapLEDG-DVSRHLVTHK 714
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTS-KLMAKLLTKYLDPSYVRV--IEGGvEVTTELLKEP 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 715 dVDRVVLTGSYDTARLFRSWKPDmHLLG---ETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCSASSLLVLvssagt 791
Cdd:PTZ00381 186 -FDHIFFTGSPRVGKLVMQAAAE-NLTPctlELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLV------ 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 792 SERIARQLVDAtaslrvrLPLSLDSQMGP----------VVVPDDEKAVRGLTTLGSGEHWV-----LKPRYLgdglwTP 856
Cdd:PTZ00381 258 HRSIKDKFIEA-------LKEAIKEFFGEdpkksedysrIVNEFHTKRLAELIKDHGGKVVYggevdIENKYV-----AP 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 857 GIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGNLYVNRGITGAIVR 936
Cdd:PTZ00381 326 TIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNP 405
|
330
....*....|....
gi 2219515474 937 RQPFGGWKRSAIGS 950
Cdd:PTZ00381 406 NLPFGGVGNSGMGA 419
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
636-950 |
2.75e-08 |
|
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: 57.81 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 636 PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKP---APPARRCAAELVRAFHDAGipedlvVLAPLEDG-DVSRHLV 711
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPselAPATSALLAKLIPEYLDTK------AIKVIEGGvPETTALL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 712 THKdVDRVVLTGSYDTARLFRSwKPDMHLLG---ETSGKNAIIVTPSADPDIAVRDAVYSAF-AHAGQKCSASSLLVlvs 787
Cdd:cd07137 175 EQK-WDKIFFTGSPRVGRIIMA-AAAKHLTPvtlELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVL--- 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 788 sagTSERIARQLVDAtaslrvrLPLSLDSQMGPvvvpdDEKAVRGLTTLGSGEHWVLKPRYLGDglwtPGIRAGVVPG-- 865
Cdd:cd07137 250 ---VEESFAPTLIDA-------LKNTLEKFFGE-----NPKESKDLSRIVNSHHFQRLSRLLDD----PSVADKIVHGge 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 866 -------------------SEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGNLYV 926
Cdd:cd07137 311 rdeknlyieptilldppldSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTF 390
|
330 340
....*....|....*....|....
gi 2219515474 927 NRGITGAIVRRQPFGGWKRSAIGS 950
Cdd:cd07137 391 NDTVVQYAIDTLPFGGVGESGFGA 414
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
270-428 |
2.54e-07 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 54.71 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 270 QAYLPDslgAMQRLQEwASRRVAAGGSRIKVRVVKGANLSMEKVDAEIHGWELTTWPSKQATDTNYKRMLSWAMTPERTR 349
Cdd:PLN02681 274 QAYLKD---ARERLRL-DLERSEREGVPLGAKLVRGAYLSLERRLAASLGVPSPVHDTIQDTHACYNRCAEFLLEKASNG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 350 AIRLGVAGQNLFDIAFAYELRAARGVE---DGVEFEMLSGMATGLQEVVRRDTGHLLLYVPVvdpHEFDVAISYLVRRLE 426
Cdd:PLN02681 350 DGEVMLATHNVESGELAAAKMNELGLHkgdPRVQFAQLLGMSDNLSFGLGNAGFRVSKYLPY---GPVEEVIPYLLRRAE 426
|
..
gi 2219515474 427 EN 428
Cdd:PLN02681 427 EN 428
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
563-806 |
5.69e-07 |
|
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: 53.38 E-value: 5.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 563 SLDPAERAAALHRVGDVLAARRAELIEVAGSEAG-------------------KTIDQSDPEVSEAIDFCHHYAEssLLL 623
Cdd:cd07077 12 VNHDEQRDLIINAIANALYDTRQRLASEAVSERGayirslianwiammgcsesKLYKNIDTERGITASVGHIQDV--LLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 624 HDGGHMVgaRFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAvILKPAPPA---RRCAAELVRAFHDAGIPEDLVVLAP 700
Cdd:cd07077 90 DNGETYV--RAFPIGVTMHILPSTNPLSGITSALRGIATRNQC-IFRPHPSApftNRALALLFQAADAAHGPKILVLYVP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 701 LEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDMHLLGETSGKNAIIVTPSADPDIAVRDAVYSAFaHAGQKCSAS 780
Cdd:cd07077 167 HPSDELAEELLSHPKIDLIVATGGRDAVDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKF-FDQNACASE 245
|
250 260
....*....|....*....|....*...
gi 2219515474 781 SLLVLVSSAGTS--ERIARQLVDATASL 806
Cdd:cd07077 246 QNLYVVDDVLDPlyEEFKLKLVVEGLKV 273
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
668-913 |
1.48e-06 |
|
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: 52.27 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 668 ILKPAPPARRCAAELVRAFHDAGI-PEDLVVLAPLEDGDVSRHLvTHKDVdrVVLTGSYDTARLFRSwKPDMHLLG---- 742
Cdd:cd07128 176 IVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSVGDLLDHL-GEQDV--VAFTGSAATAAKLRA-HPNIVARSirfn 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 743 -ETSGKNAIIVTPSADP-----DIAVRDAVYSAFAHAGQKCSASSlLVLVsSAGTSERIARQLVDATASLRVRLPLSLDS 816
Cdd:cd07128 252 aEADSLNAAILGPDATPgtpefDLFVKEVAREMTVKAGQKCTAIR-RAFV-PEARVDAVIEALKARLAKVVVGDPRLEGV 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 817 QMGPVVVPDDEKAVR-GLTTLGSGEHWVLKPRYLGDGLWTPGIRAGVVP-----------GSEFHLTEYFAPVIGVMRVD 884
Cdd:cd07128 330 RMGPLVSREQREDVRaAVATLLAEAEVVFGGPDRFEVVGADAEKGAFFPptlllcddpdaATAVHDVEAFGPVATLMPYD 409
|
250 260
....*....|....*....|....*....
gi 2219515474 885 TLQEAIEAVNAVDYGLTSGIQTLDATELA 913
Cdd:cd07128 410 SLAEAIELAARGRGSLVASVVTNDPAFAR 438
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
547-596 |
3.49e-05 |
|
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: 47.92 E-value: 3.49e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2219515474 547 VDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAG 596
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETG 50
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
668-964 |
4.91e-05 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 47.10 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 668 ILKPAPPARRC---AAELVR-AFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSydtarlfrswkPDMHLLGE 743
Cdd:cd07122 127 IFSPHPRAKKCsieAAKIMReAAVAAGAPEGLIQWIEEPSIELTQELMKHPDVDLILATGG-----------PGMVKAAY 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 744 TSGKNAIIVTP---------SADPDIAVRDAVYS-AFAHaGQKCSASSLLVLVSSagtserIARQLVDATaslrvrlpls 813
Cdd:cd07122 196 SSGKPAIGVGPgnvpayideTADIKRAVKDIILSkTFDN-GTICASEQSVIVDDE------IYDEVRAEL---------- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 814 ldSQMGPVVVPDDEKAvrglttlgsgehwvlkprYLGDGLWTPG--------------I--RAGV-VP------------ 864
Cdd:cd07122 259 --KRRGAYFLNEEEKE------------------KLEKALFDDGgtlnpdivgksaqkIaeLAGIeVPedtkvlvaeetg 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 865 -GSEFHLT-EYFAPVIGVMRVDTLQEAIEAVNA-VDY---GLTSGIQTLD---ATELAIwleGVQAGNLYVNRGitgaiv 935
Cdd:cd07122 319 vGPEEPLSrEKLSPVLAFYRAEDFEEALEKARElLEYggaGHTAVIHSNDeevIEEFAL---RMPVSRILVNTP------ 389
|
330 340
....*....|....*....|....*....
gi 2219515474 936 rrQPFGGwkrsaIGSTTKAGGPSYLLGLG 964
Cdd:cd07122 390 --SSLGG-----IGDTYNGLAPSLTLGCG 411
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
624-803 |
9.31e-05 |
|
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: 46.33 E-value: 9.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 624 HDGGHMVGARFIPVDVTVVAsPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIP-EDLVVLAplE 702
Cdd:cd07126 131 HQGQQSSGYRWPYGPVAIIT-PFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPaTDVDLIH--S 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 703 DGDVSRHLVTHKDVDRVVLTGSYDTA-RLFRSWKPDMHLlgETSGKNAIIVTPS-ADPDIAVRDAVYSAFAHAGQKCSAS 780
Cdd:cd07126 208 DGPTMNKILLEANPRMTLFTGSSKVAeRLALELHGKVKL--EDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQ 285
|
170 180 190
....*....|....*....|....*....|.
gi 2219515474 781 SLLVLVSS---AGTSERIA-----RQLVDAT 803
Cdd:cd07126 286 SILFAHENwvqAGILDKLKalaeqRKLEDLT 316
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
636-950 |
1.99e-04 |
|
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: 45.29 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 636 PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCA---AELvrafhdagIPEDL------VVLAPLEDgdv 706
Cdd:cd07132 100 PLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAkllAEL--------IPKYLdkecypVVLGGVEE--- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 707 SRHLVTHKdVDRVVLTGSYDTARLFRSwKPDMHL------LGetsGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCSAS 780
Cdd:cd07132 169 TTELLKQR-FDYIFYTGSTSVGKIVMQ-AAAKHLtpvtleLG---GKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAP 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 781 SlLVLVssagtSERIARQLVDAtaslrvrLPLSLDSQMG--PVVVPD------DEKAVRGLTTLGSGE-----HWVLKPR 847
Cdd:cd07132 244 D-YVLC-----TPEVQEKFVEA-------LKKTLKEFYGedPKESPDygriinDRHFQRLKKLLSGGKvaiggQTDEKER 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 848 YLgdglwTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGNLYVN 927
Cdd:cd07132 311 YI-----APTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVN 385
|
330 340
....*....|....*....|...
gi 2219515474 928 RGITGAIVRRQPFGGWKRSAIGS 950
Cdd:cd07132 386 DTIMHYTLDSLPFGGVGNSGMGA 408
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
636-949 |
6.29e-04 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 43.95 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 636 PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAaelvrAFHDAGIPE--DLVVLAPLEDG-DVSRHLVT 712
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATS-----AFLAANIPKylDSKAVKVIEGGpAVGEQLLQ 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 713 HKdVDRVVLTGSYDTARLFRSwKPDMHLLG---ETSGKNAIIV---TPSADPDIAVRDAVYSAF-AHAGQKCSASSlLVL 785
Cdd:PLN02203 183 HK-WDKIFFTGSPRVGRIIMT-AAAKHLTPvalELGGKCPCIVdslSSSRDTKVAVNRIVGGKWgSCAGQACIAID-YVL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 786 VssagtSERIARQLVDAtaslrvrLPLSLDSQMGpvvvpDDEKAVRGLTTLGSGEHWVLKPRYLGDglwtPGIRAGVVPG 865
Cdd:PLN02203 260 V-----EERFAPILIEL-------LKSTIKKFFG-----ENPRESKSMARILNKKHFQRLSNLLKD----PRVAASIVHG 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 866 ---------------------SEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGNL 924
Cdd:PLN02203 319 gsidekklfieptillnppldSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSV 398
|
330 340
....*....|....*....|....*
gi 2219515474 925 YVNRGITGAIVRRQPFGGWKRSAIG 949
Cdd:PLN02203 399 TFNDAIIQYACDSLPFGGVGESGFG 423
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
671-900 |
9.29e-04 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 43.35 E-value: 9.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 671 PAPPARRCAAELVRAFHDA----GIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSydtarlfrswkPDMHLLGETSG 746
Cdd:PRK15398 164 PHPGAKKVSLRAIELLNEAivaaGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGG-----------PAVVKAAMKSG 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 747 KNAI---------IVTPSADPDIAVRDAVYSAFAHAGQKCSASSLLVLVSSAgtSERIARQLVDATAslrVRLPLSLDSQ 817
Cdd:PRK15398 233 KKAIgagagnppvVVDETADIEKAARDIVKGASFDNNLPCIAEKEVIVVDSV--ADELMRLMEKNGA---VLLTAEQAEK 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 818 MGPVVVPDDEKAVRGlttlgsgehWVLK-PRYLGD--GLWTP-GIRAGVVPGSEFH---LTEYFAPVIGVMRVDTLQEAI 890
Cdd:PRK15398 308 LQKVVLKNGGTVNKK---------WVGKdAAKILEaaGINVPkDTRLLIVETDANHpfvVTELMMPVLPVVRVKDVDEAI 378
|
250
....*....|
gi 2219515474 891 EAVNAVDYGL 900
Cdd:PRK15398 379 ALAVKLEHGN 388
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
668-906 |
6.94e-03 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 40.33 E-value: 6.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 668 ILKPAPPAR----RCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTAR-LFRSWKPdmhLLG 742
Cdd:cd07081 127 IFSPHPRAKkvtqRAATLLLQAAVAAGAPENLIGWIDNPSIELAQRLMKFPGIGLLLATGGPAVVKaAYSSGKP---AIG 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 743 ETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCSASSLLVLVSSagtserIARQLVDataslrvrlplSLDSQMGPVV 822
Cdd:cd07081 204 VGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVVDS------VYDEVMR-----------LFEGQGAYKL 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 823 VPDDEKAVRG--LTTLGSGEHWVLKPRY---LGDGLWTPG------IRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIE 891
Cdd:cd07081 267 TAEELQQVQPviLKNGDVNRDIVGQDAYkiaAAAGLKVPQetriliGEVTSLAEHEPFAHEKLSPVLAMYRAANFADADA 346
|
250
....*....|....*....
gi 2219515474 892 AVNAV----DYGLTSGIQT 906
Cdd:cd07081 347 KALALklegGCGHTSAMYS 365
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
567-950 |
9.94e-03 |
|
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: 39.78 E-value: 9.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 567 AERAAALHRVGDVLAARRAELIEvagseagkTIDQsdpevseaiDFCHHYAESSLLL--------------HDGGHM--- 629
Cdd:cd07133 20 EERRDRLDRLKALLLDNQDALAE--------AISA---------DFGHRSRHETLLAeilpsiagikharkHLKKWMkps 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 630 ---VGARFIPVDVTV---------VASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVV 697
Cdd:cd07133 83 rrhVGLLFLPAKAEVeyqplgvvgIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEVAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 698 LapLEDGDVSRHlVTHKDVDRVVLTGSYDTARLFrswkpdM-----HL------LGetsGKNAIIVTPSADPDIAVRDAV 766
Cdd:cd07133 163 V--TGGADVAAA-FSSLPFDHLLFTGSTAVGRHV------MraaaeNLtpvtleLG---GKSPAIIAPDADLAKAAERIA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 767 YSAFAHAGQKCSASSlLVLVsSAGTSERIARQLVDATASLRVRLPLSLDsqMGPVV----------VPDD--EKAVRGLT 834
Cdd:cd07133 231 FGKLLNAGQTCVAPD-YVLV-PEDKLEEFVAAAKAAVAKMYPTLADNPD--YTSIInerhyarlqgLLEDarAKGARVIE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 835 TLGSGEhwvlkpRYLGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAI 914
Cdd:cd07133 307 LNPAGE------DFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDR 380
|
410 420 430
....*....|....*....|....*....|....*.
gi 2219515474 915 WLEGVQAGNLYVNRGITGAIVRRQPFGGWKRSAIGS 950
Cdd:cd07133 381 VLRRTHSGGVTINDTLLHVAQDDLPFGGVGASGMGA 416
|
|
| |
