|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
1-862 |
0e+00 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 1711.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 1 MAVTNVAELNALVERVKKAQREYASFTQEQVDKIFRAAALAAADARIPLAKMAVAESGMGIVEDKVIKNHFASEYIYNAY 80
Cdd:PRK13805 6 MAVTNVAELDALVEKAKKAQEEFATFTQEQVDKIVRAAALAALDARIPLAKMAVEETGRGVVEDKVIKNHFASEYIYNSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 81 KDEKTCGVLSEDDTFGTITIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAAIAA 160
Cdd:PRK13805 86 KDEKTVGVIEEDDEFGIIEIAEPVGVIAGITPTTNPTSTAIFKALIALKTRNPIIFSFHPRAQKSSIAAAKIVLDAAVAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 161 GAPKDLIGWIDQPSVELSNALMHHPDINLILATGGPGMVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKTF 240
Cdd:PRK13805 166 GAPKDIIQWIEEPSVELTNALMNHPGIALILATGGPGMVKAAYSSGKPALGVGAGNVPAYIDKTADIKRAVNDILLSKTF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 241 DNGVICASEQSVVVVDSVYDAVRERFSSHGGYLLQGQELKAVQNIILK--NGALNAAIVGQPAYKIAELAGFTVPVSTKI 318
Cdd:PRK13805 246 DNGMICASEQAVIVDDEIYDEVKEEFASHGAYFLNKKELKKLEKFIFGkeNGALNADIVGQSAYKIAEMAGFKVPEDTKI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 319 LIGEVTDVDESEPFAHEKLSPTLAMYRAKNFEDAVDKAEKLVAMGGIGHTSCLYTdqdNQPERVAYFGQLMKTARILINT 398
Cdd:PRK13805 326 LIAEVKGVGESEPLSHEKLSPVLAMYKAKDFEDAVEKAEKLVEFGGLGHTAVIYT---NDDELIKEFGLRMKACRILVNT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 399 PASQGGIGDLYNfKLAPSLTLGCGSWGGNSISENVGPKHLINKKTVAKRAENMLWHKLPKSIYFRRGSLPIALDEVitDG 478
Cdd:PRK13805 403 PSSQGGIGDLYN-KLAPSLTLGCGSWGGNSVSENVGAKHLLNIKTVAKRRENMQWFKVPKKIYFERGSLPYLLDEL--DG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 479 HKRALIVTDRFLFNNGYADQITSVLKA--AGVETEVFFEVEADPTLTIVRKGAELANSFKPDVIIALGGGSPMDAAKIMW 556
Cdd:PRK13805 480 KKRAFIVTDRFMVELGYVDKVTDVLKKreNGVEYEVFSEVEPDPTLSTVRKGAELMRSFKPDTIIALGGGSPMDAAKIMW 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 557 VMYEHPETHFEELALRFMDIRKRIYKFPKMGVKAKMVAITTTSGTGSEVTPFAVVTDDATGQKYPLADYALTPDMAIVDA 636
Cdd:PRK13805 560 LFYEHPETDFEDLAQKFMDIRKRIYKFPKLGKKAKLVAIPTTSGTGSEVTPFAVITDDKTGVKYPLADYELTPDVAIVDP 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 637 NLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPASYHEGSKNPVARERVHSAATIAGIAFAN 716
Cdd:PRK13805 640 NLVMTMPKSLTADTGIDALTHALEAYVSVMASDYTDGLALQAIKLVFEYLPRSYKNGAKDPEAREKMHNASTIAGMAFAN 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 717 AFLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNANDNPtKQTAFSQYDRPQARRRYAEIADHLGLtaPGDRTAAKIE 796
Cdd:PRK13805 720 AFLGICHSMAHKLGAEFHIPHGRANAILLPHVIRYNATDPP-KQAAFPQYEYPRADERYAEIARHLGL--PGSTTEEKVE 796
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503995744 797 KLLGWLDEIKAELGIPKSIREAGVQEADFLAHVDKLSEDAFDDQCTGANPRYPLIAELKQILLDTF 862
Cdd:PRK13805 797 SLIKAIEELKAELGIPMSIKEAGVDEADFLAKLDELAELAFDDQCTGANPRYPLISELKEILLDAY 862
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
455-859 |
0e+00 |
|
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol dehydrogenase bifunctional two-domain protein (AAD); This alcohol dehydrogenase domain is located on the C-terminal of a bifunctional two-domain protein. The N-terminal of the protein contains an acetaldehyde-CoA dehydrogenase domain. This protein is involved in pyruvate metabolism whereby pyruvate is converted to acetyl-CoA and formate by pyruvate formate-lysase (PFL). Under anaerobic condition, acetyl-CoA is reduced to acetaldehyde and ethanol by this two-domain protein. Acetyl-CoA is first converted into an enzyme-bound thiohemiacetal by the N-terminal acetaldehyde dehydrogenase domain. The enzyme-bound thiohemiacetal is subsequently reduced by the C-terminal NAD+-dependent alcohol dehydrogenase domain. In E. coli, this protein is called AdhE and has been shown to have pyruvate formate-lyase (PFL) deactivase activity, which leads to the inactivation of PFL, a key enzyme in anaerobic metabolism. In Escherichia coli and Entamoeba histolytica, this enzyme forms homopolymeric peptides composed of more than 20 protomers associated in a helical rod-like structure.
Pssm-ID: 341457 [Multi-domain] Cd Length: 400 Bit Score: 731.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 455 KLPKSIYFRRGSLPIALDEviTDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANS 534
Cdd:cd08178 1 KVPPKIYFEPGCLPYLLLE--LPGVKRAFIVTDRVLYKLGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLEAMNA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 535 FKPDVIIALGGGSPMDAAKIMWVMYEHPETHFEELALRFMDIRKRIYKFPKMGVKAKMVAITTTSGTGSEVTPFAVVTDD 614
Cdd:cd08178 79 FKPDVIIALGGGSAMDAAKIMWLFYEHPETKFEDLAQRFMDIRKRVYKFPKLGKKAKLVAIPTTSGTGSEVTPFAVITDD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 615 ATGQKYPLADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPASYHEGs 694
Cdd:cd08178 159 KTGKKYPLADYALTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVSVMASDYTDGLALQAIKLIFEYLPRSYNNG- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 695 KNPVARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNANDNPTKQTAFSQYDRPQARRR 774
Cdd:cd08178 238 NDIEAREKMHNAATIAGMAFANAFLGICHSLAHKLGAAFHIPHGRANAILLPHVIRYNATDPPTKQAAFPQYKYYVAKER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 775 YAEIADHLGLTAPGDrtAAKIEKLLGWLDEIKAELGIPKSIREAGVQEADFLAHVDKLSEDAFDDQCTGANPRYPLIAEL 854
Cdd:cd08178 318 YAEIADLLGLGGKTP--EEKVESLIKAIEDLKKDLGIPTSIREAGIDEADFLAAVDKLAEDAFDDQCTGANPRYPLISEL 395
|
....*
gi 503995744 855 KQILL 859
Cdd:cd08178 396 KEILL 400
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
9-447 |
0e+00 |
|
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: 719.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 9 LNALVERVKKAQREYASFTQEQVDKIFRAAALAAADARIPLAKMAVAESGMGIVEDKVIKNHFASEYIYNAYKDEKTCGV 88
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIKNHFAAEYIYNVYKDEKTCGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 89 LSEDDTFGTITIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAAIAAGAPKDLIG 168
Cdd:cd07081 81 LTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 169 WIDQPSVELSNALMHHPDINLILATGGPGMVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKTFDNGVICAS 248
Cdd:cd07081 161 WIDNPSIELAQRLMKFPGIGLLLATGGPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 249 EQSVVVVDSVYDAVRERFSSHGGYLLQGQELKAVQNIILKNGALNAAIVGQPAYKIAELAGFTVPVSTKILIGEVTDVDE 328
Cdd:cd07081 241 EQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQQVQPVILKNGDVNRDIVGQDAYKIAAAAGLKVPQETRILIGEVTSLAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 329 SEPFAHEKLSPTLAMYRAKNFEDAVDKAEKLVAMGGIGHTSCLYTDQDNQPERVAYFGQLMKTARILINTPASQGGIGDL 408
Cdd:cd07081 321 HEPFAHEKLSPVLAMYRAANFADADAKALALKLEGGCGHTSAMYSDNIKAIENMNQFANAMKTSRFVKNGPCSQGGLGDL 400
|
410 420 430
....*....|....*....|....*....|....*....
gi 503995744 409 YNFKLAPSLTLGCGSWGGNSISENVGPKHLINKKTVAKR 447
Cdd:cd07081 401 YNFRGWPSMTLGCGTWGGNSVSENVGPKHLVNLKTVALR 439
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
9-447 |
0e+00 |
|
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: 718.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 9 LNALVERVKKAQREYASFTQEQVDKIFRAAALAAADARIPLAKMAVAESGMGIVEDKVIKNHFASEYIYNAYKDEKTCGV 88
Cdd:cd07122 1 VDELVERARKAQREFATFSQEQVDKIVEAVAWAAADAAEELAKMAVEETGMGVVEDKVIKNHFASEYVYNDIKDMKTVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 89 LSEDDTFGTITIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAAIAAGAPKDLIG 168
Cdd:cd07122 81 IEEDEEKGIVEIAEPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAAVAAGAPEGLIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 169 WIDQPSVELSNALMHHPDINLILATGGPGMVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKTFDNGVICAS 248
Cdd:cd07122 161 WIEEPSIELTQELMKHPDVDLILATGGPGMVKAAYSSGKPAIGVGPGNVPAYIDETADIKRAVKDIILSKTFDNGTICAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 249 EQSVVVVDSVYDAVRERFSSHGGYLLQGQELKAVQNIILK-NGALNAAIVGQPAYKIAELAGFTVPVSTKILIGEVTDVD 327
Cdd:cd07122 241 EQSVIVDDEIYDEVRAELKRRGAYFLNEEEKEKLEKALFDdGGTLNPDIVGKSAQKIAELAGIEVPEDTKVLVAEETGVG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 328 ESEPFAHEKLSPTLAMYRAKNFEDAVDKAEKLVAMGGIGHTSCLYTdqdNQPERVAYFGQLMKTARILINTPASQGGIGD 407
Cdd:cd07122 321 PEEPLSREKLSPVLAFYRAEDFEEALEKARELLEYGGAGHTAVIHS---NDEEVIEEFALRMPVSRILVNTPSSLGGIGD 397
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 503995744 408 LYNFkLAPSLTLGCGSWGGNSISENVGPKHLINKKTVAKR 447
Cdd:cd07122 398 TYNG-LAPSLTLGCGSWGGNSTSDNVGPKHLLNIKRVAYR 436
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
450-862 |
7.76e-163 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 480.00 E-value: 7.76e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 450 NMLWHKLPKSIYFRRGSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGA 529
Cdd:COG1454 1 MMFTFRLPTRIVFGAGALAELGEELKRLGAKRALIVTDPGLAKLGLLDRVLDALEAAGIEVVVFDDVEPNPTVETVEAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 530 ELANSFKPDVIIALGGGSPMDAAKIMWVMYEHPEThfeelalrFMDIrkrIYKFPKMGVKAKMVAITTTSGTGSEVTPFA 609
Cdd:COG1454 81 AAAREFGADVVIALGGGSAIDAAKAIALLATNPGD--------LEDY---LGIKKVPGPPLPLIAIPTTAGTGSEVTPFA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 610 VVTDDATGQKYPLADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPAS 689
Cdd:COG1454 150 VITDPETGVKKGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPLTDALALEAIRLIARNLPRA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 690 YHEGSkNPVARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNAndnptkqtafsqydrP 769
Cdd:COG1454 230 VADGD-DLEAREKMALASLLAGMAFANAGLGAVHALAHPLGGLFHVPHGLANAILLPHVLRFNA---------------P 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 770 QARRRYAEIADHLGLtAPGDRTAAKIEKLLGWLDEIKAELGIPKSIREAGVQEADFlahvDKLSEDAFDDQCTGANPRYP 849
Cdd:COG1454 294 AAPERYAEIARALGL-DVGLSDEEAAEALIEAIRELLRDLGIPTRLSELGVTEEDL----PELAELALADRCLANNPRPL 368
|
410
....*....|...
gi 503995744 850 LIAELKQILLDTF 862
Cdd:COG1454 369 TEEDIEAILRAAY 381
|
|
| EutH_ACDH |
TIGR02518 |
acetaldehyde dehydrogenase (acetylating); |
5-445 |
1.97e-162 |
|
acetaldehyde dehydrogenase (acetylating);
Pssm-ID: 131570 Cd Length: 488 Bit Score: 483.21 E-value: 1.97e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 5 NVAELNALVERVKKAQREYASFTQEQVDKIFRAAALAAADARIPLAKMAVAESGMGIVEDKVIKNHFASEYIYNAYKDEK 84
Cdd:TIGR02518 6 SIQQVRNLIRSAKVAQKKLANMTQEQIDKIVKAIVDAAYENAVKLAKMANEETGFGKWEDKVIKNVFAATIVYDSIKDMK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 85 TCGVLSEDDTFGTITIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAAIAAGAPK 164
Cdd:TIGR02518 86 TIGILSEDKEKKVIEIAVPVGVVAGLIPSTNPTSTAIYKTLISIKARNAIVFSPHPNAKKCIIETVKLMRKAAEEAGAPE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 165 DLIGWIDQPSVELSNALMHHPDINLILATGGPGMVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKTFDNGV 244
Cdd:TIGR02518 166 GAIGCITVPTIEGTNELMKNKDTSLILATGGEAMVKAAYSSGTPAIGVGPGNGPAYIERTANVKKAVRDIIDSKTFDNGT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 245 ICASEQSVVVVDSVYDAVRERFSSHGGYLLQGQELKAVQNIILK-NGALNAAIVGQPAYKIAELAGFTVPVSTKILIGEV 323
Cdd:TIGR02518 246 ICASEQSIIVEECNKDAVVEELKKQGGYFLTAEEAEKLGKFILRpNGTMNPQIVGKSPQVIANLAGLTVPEDAKVLIGEQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 324 TDVDESEPFAHEKLSPTLAMYRAKNFEDAVDKAEKLVAMGGIGHTSCLYTDQDnqpERVAYFGQLMKTARILINTPASQG 403
Cdd:TIGR02518 326 NGVGNKNPYSREKLTTILAFYTEENWHEACELSIELLQNEGAGHTLIIHSENK---DIVREFALKKPVSRMLVNTGGSLG 402
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 503995744 404 GIGDLYNfkLAPSLTLGCGSWGGNSISENVGPKHLINKKTVA 445
Cdd:TIGR02518 403 GIGATTN--LVPAFTLGCGAVGGSSTSDNITPENLINIRRVA 442
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
456-863 |
1.53e-157 |
|
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in bacteria; NADPH-dependent butanol dehydrogenase (BDH) is involved in the butanol and ethanol formation pathway of some bacteria. The fermentation process is characterized by an acid producing growth phase, followed by a solvent producing phase. The latter phase is associated with the induction of solventogenic enzymes such as butanol dehydrogenase. The activity of the enzyme requires NADPH as cofactor, as well as divalent ions zinc or iron. This family is a member of the iron-containing alcohol dehydrogenase superfamily. Protein structure has a dehydroquinate synthase-like fold.
Pssm-ID: 341458 [Multi-domain] Cd Length: 379 Bit Score: 466.28 E-value: 1.53e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 456 LPKSIYFRRGSLpialdEVITD-GHKRALIVTD-RFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELAN 533
Cdd:cd08179 4 VPRDIYFGEGAL-----EYLKTlKGKRAFIVTGgGSMKRNGFLDKVEDYLKEAGMEVKVFEGVEPDPSVETVEKGAEAMR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 534 SFKPDVIIALGGGSPMDAAKIMWVMYEHPETHFEELALRFmdirkriyKFPKMGVKAKMVAITTTSGTGSEVTPFAVVTD 613
Cdd:cd08179 79 EFEPDWIIAIGGGSVIDAAKAMWVFYEYPELTFEDALVPF--------PLPELRKKARFIAIPSTSGTGSEVTRASVITD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 614 DATGQKYPLADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPASYHEG 693
Cdd:cd08179 151 TEKGIKYPLASFEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLANDFTDALALGAILDIFENLPKSYNGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 694 sKNPVARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNANDnptkqtafsqydrPQARR 773
Cdd:cd08179 231 -KDLEAREKMHNASCLAGMAFSNSGLGIVHSMAHKGGAFFGIPHGLANAILLPYVIEFNSKD-------------PEARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 774 RYaeIADHLGLTApgdrtAAKIEKLLGWLDEIKAELGIPKSIREAGVQEADFLAHVDKLSEDAFDDQCTGANPRYPLIAE 853
Cdd:cd08179 297 RY--AALLIGLTD-----EELVEDLIEAIEELNKKLGIPLSFKEAGIDEDEFFAKLDEMAENAMNDACTGTNPRKPTVEE 369
|
410
....*....|
gi 503995744 854 LKQILLDTFY 863
Cdd:cd08179 370 MKELLKAAYY 379
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
14-446 |
4.06e-145 |
|
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: 435.11 E-value: 4.06e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 14 ERVKKAQREYASFTQEQVDKIFRAAALAAADARIPLAKMAVAESG-------------MGIVEDKVIKNHFASEYIYNAy 80
Cdd:cd07077 1 ESAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGayirslianwiamMGCSESKLYKNIDTERGITAS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 81 kDEKTCGVLSEDdTFGTITIAEPIGIICGIVPTTNPTStAIFKSLISLKTRNAIIFSPHPRAkDATNKAADIVLQAAIAA 160
Cdd:cd07077 80 -VGHIQDVLLPD-NGETYVRAFPIGVTMHILPSTNPLS-GITSALRGIATRNQCIFRPHPSA-PFTNRALALLFQAADAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 161 GAPKDLIGWIDQPSVELSNALMHHPDINLILATGGPGMVKAAYSS--GKPAIGVGAGNTPVVIDETADIKRAVASVLMSK 238
Cdd:cd07077 156 HGPKILVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAVKHspHIPVIGFGAGNSPVVVDETADEERASGSVHDSK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 239 TFDNgVICASEQSVVVVDSVYDAVRERFSSHGGYllqgqelkavqniilkngalnaaivgqpaykiaelAGFTVPVSTKI 318
Cdd:cd07077 236 FFDQ-NACASEQNLYVVDDVLDPLYEEFKLKLVV-----------------------------------EGLKVPQETKP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 319 LIGEVTdvDESEPFAHEKLSPTLAMYRAKNFEDAVDKAEKLVAMGGIGHTSCLYTDqdnQPERVAYFGQLMKTARILINT 398
Cdd:cd07077 280 LSKETT--PSFDDEALESMTPLECQFRVLDVISAVENAWMIIESGGGPHTRCVYTH---KINKVDDFVQYIDTASFYPNE 354
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 503995744 399 PASQGGiGDLYNFKLAPSLTLGCGSWGGnsisENVGPKHLINKKTVAK 446
Cdd:cd07077 355 SSKKGR-GAFAGKGVERIVTSGMNNIFG----AGVGHDALRPLKRLVR 397
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
457-854 |
2.59e-123 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 376.94 E-value: 2.59e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 457 PKSIYFRRGSLPiALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANSFK 536
Cdd:pfam00465 1 PTRIVFGAGALA-ELGEELKRLGARALIVTDPGSLKSGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALAREAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 537 PDVIIALGGGSPMDAAKIMWVMYEHPETHFEELalrfmdirkriYKFPKMGVKAKMVAITTTSGTGSEVTPFAVVTDDAT 616
Cdd:pfam00465 80 ADVIIAVGGGSVIDTAKAIALLLTNPGDVWDYL-----------GGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTET 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 617 GQKYPLADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPASYHEGSkN 696
Cdd:pfam00465 149 GEKLGIFSPKLLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDALALEAIRLIAENLPRAVADGE-D 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 697 PVARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNAndnptkqtafsqydrPQARRRYA 776
Cdd:pfam00465 228 LEARENMLLASTLAGLAFSNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNA---------------PAAPEKLA 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503995744 777 EIADHLGltapGDRTAAKIEKLLGWLDEIKAELGIPKSIREAGVQEADFlahvDKLSEDAFDDQCTGANPRYPLIAEL 854
Cdd:pfam00465 293 QLARALG----EDSDEEAAEEAIEALRELLRELGLPTTLSELGVTEEDL----DALAEAALRDRSLANNPRPLTAEDI 362
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
457-858 |
4.85e-123 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. They contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases, insect-type, or short-chain alcohol dehydrogenases, iron-containing alcohol dehydrogenases, among others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341481 [Multi-domain] Cd Length: 372 Bit Score: 376.79 E-value: 4.85e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 457 PKSIYFRRGSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANSFK 536
Cdd:cd08551 1 PTRIVFGAGALARLGEELKALGGKKVLLVTDPGLVKAGLLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELAREEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 537 PDVIIALGGGSPMDAAKIMWVMYEHPETHFEELALRfmdirkriyKFPKMGVKakMVAITTTSGTGSEVTPFAVVTDDAT 616
Cdd:cd08551 81 ADLVIAVGGGSVLDTAKAIAVLATNGGSIRDYEGIG---------KVPKPGLP--LIAIPTTAGTGSEVTPNAVITDPET 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 617 GQKYPLADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPASYHEGSkN 696
Cdd:cd08551 150 GRKMGIVSPYLLPDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANPISDALALEAIRLIGKNLRRAVADGS-D 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 697 PVARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNANDNPtkqtafsqydrpqarRRYA 776
Cdd:cd08551 229 LEAREAMLLASLLAGIAFGNAGLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPACP---------------EKYA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 777 EIADHLGLTAPGDRTAAKIEKLLGWLDEIKAELGIPKSIREAGVQEADFlahvDKLSEDAFDDQCTGAN-PRYPLIAELK 855
Cdd:cd08551 294 EIAEALGEDVEGLSDEEAAEAAVEAVRELLRDLGIPTSLSELGVTEEDI----PELAEDAMKSGRLLSNnPRPLTEEDIR 369
|
...
gi 503995744 856 QIL 858
Cdd:cd08551 370 EIY 372
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
453-858 |
1.45e-117 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341484 [Multi-domain] Cd Length: 375 Bit Score: 362.70 E-value: 1.45e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 453 WHKLPKSIYFRRGSLPiALDEVITdghKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELA 532
Cdd:cd14862 2 WYFSSPKIVFGEDALS-HLEQLSG---KRALIVTDKVLVKLGLLKKVLKRLLQAGFEVEVFDEVEPEPPLETVLKGAEAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 533 NSFKPDVIIALGGGSPMDAAKIMWVMYEHPETHFEEL-ALRFMDIRKriykfpkmgvKAKMVAITTTSGTGSEVTPFAVV 611
Cdd:cd14862 78 REFEPDLIIALGGGSVMDAAKAAWVLYERPDLDPEDIsPLDLLGLRK----------KAKLIAIPTTSGTGSEATWAIVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 612 TDDATGQKYPLADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPASYh 691
Cdd:cd14862 148 TDTEEPRKIAVANPELVPDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLSTWSNDFSDALALKAIELIFKYLPRAY- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 692 EGSKNPVARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNANDnptkqtafsqydrpqA 771
Cdd:cd14862 227 KDGDDLEAREKMHNAATIAGLAFGNSQAGLAHALGHSLGAVFHVPHGIAVGLFLPYVIEFYAKV---------------T 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 772 RRRYAEIAdHLGLTAPGDRTAAKieKLLGWLDEIKAELGIPKSIREAGVQEADFLAHVDKLSEDAFDDQCTGANPRYPLI 851
Cdd:cd14862 292 DERYDLLK-LLGIEARDEEEALK--KLVEAIRELYKEVGQPLSIKDLGISEEEFEEKLDELVEYAMEDSCTITSPRPPSE 368
|
....*..
gi 503995744 852 AELKQIL 858
Cdd:cd14862 369 EDLKKLF 375
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
457-857 |
2.89e-115 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341473 [Multi-domain] Cd Length: 378 Bit Score: 356.84 E-value: 2.89e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 457 PKSIYFRRGSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANSFK 536
Cdd:cd08194 1 PRTIIIGGGALEELGEEAASLGGKRALIVTDKVMVKLGLVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVEEGLALYKEGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 537 PDVIIALGGGSPMDAAKIMWVMYEHPEthfeelalrfmDIRKriYKFPKMGVKAK--MVAITTTSGTGSEVTPFAVVTDD 614
Cdd:cd08194 81 CDFIVALGGGSPIDTAKAIAVLATNGG-----------PIRD--YMGPRKVDKPGlpLIAIPTTAGTGSEVTRFTVITDT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 615 ATGQKYPLADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPASYHEGs 694
Cdd:cd08194 148 ETDVKMLLKGPALLPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQPLTDTLALSAIKLIGRNLRRAYADG- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 695 KNPVARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNANDNPTkqtafsqydrpqarrR 774
Cdd:cd08194 227 DDLEAREAMMLAALEAGIAFSNSSVALVHGMSRPIGALFHVPHGLSNAMLLPAVTEFSLPGAPE---------------R 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 775 YAEIADHLGLTAPGDRTAAKIEKLLGWLDEIKAELGIPkSIREAGVQEADFLAHVDKLSEDAFDDQCTGANPRYPLIAEL 854
Cdd:cd08194 292 YAEIARAMGIATEGDSDEEAAEKLVEALERLCADLEIP-TLREYGIDEEEFEAALDKMAEDALASGSPANNPRVPTKEEI 370
|
...
gi 503995744 855 KQI 857
Cdd:cd08194 371 IEL 373
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
455-859 |
4.74e-115 |
|
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol in glycerol metabolism; 1,3-propanediol dehydrogenase (PPD) plays a role in glycerol metabolism of some bacteria in anaerobic conditions. In this degradation pathway, glycerol is converted in a two-step process to 1,3-propanediol (1,3-PD) which is then excreted into the extracellular medium. The first reaction involves the transformation of glycerol into 3-hydroxypropionaldehyde (3-HPA) by a coenzyme B-12-dependent dehydratase. The second reaction involves the dismutation of the 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol by the NADH-linked 1,3-propanediol dehydrogenase (PPD). The enzyme requires iron ion for its function. Because many genes in this pathway are present in the propanediol utilization (pdu) operon, they are also named pdu genes. PPD is a member of the iron-containing alcohol dehydrogenase superfamily. The PPD structure has a dehydroquinate synthase-like fold.
Pssm-ID: 341459 [Multi-domain] Cd Length: 333 Bit Score: 354.49 E-value: 4.74e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 455 KLPKSIYFRRGSLPiALDEVitdGHKRALIVTDRFLFNNGYADQITSVLKAAgVETEVFFEVEADPTLTIVRKGAELANS 534
Cdd:cd08180 2 SLKTKIYSGEDSLE-RLKEL---KGKRVFIVTDPFMVKSGMVDKVTDELDKS-NEVEIFSDVVPDPSIEVVAKGLAKILE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 535 FKPDVIIALGGGSPMDAAKimwvmyehpethfeelALRFMdirkrIYKFPKMGVKAKMVAITTTSGTGSEVTPFAVVTDD 614
Cdd:cd08180 77 FKPDTIIALGGGSAIDAAK----------------AIIYF-----ALKQKGNIKKPLFIAIPTTSGTGSEVTSFAVITDP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 615 ATGQKYPLADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPASYHEGS 694
Cdd:cd08180 136 EKGIKYPLVDDSMLPDIAILDPELVKSVPPKVTADTGMDVLTHALEAYVSTNANDFTDALAEKAIKLVFENLPRAYRDGD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 695 kNPVARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYnandnptkqtafsqydrpqarrr 774
Cdd:cd08180 216 -DLEAREKMHNASCMAGIAFNNAGLGINHSLAHALGGRFHIPHGRANAILLPYVIEF----------------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 775 yaeiadhlgltapgdrtaakiekLLGWLDEIKAELGIPKSIREAGVQEADFLAHVDKLSEDAFDDQCTGANPRYPLIAEL 854
Cdd:cd08180 272 -----------------------LIAAIRRLNKKLGIPSTLKELGIDEEEFEKAIDEMAEAALADRCTATNPRKPTAEDL 328
|
....*
gi 503995744 855 KQILL 859
Cdd:cd08180 329 IELLR 333
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
456-858 |
7.39e-108 |
|
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria; Lactadehyde:propanediol oxidoreductase (LPO) is a member of the group III iron-activated dehydrogenases which catalyze the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria. L-fucose and L-rhamnose are used by Escherichia coli through an inducible pathway mediated by the fucose regulon comprising four linked operons fucO, fucA, fucPIK, and fucR. The fucA-encoded aldolase catalyzes the formation of dihydroxyacetone phosphate and L-lactaldehyde. Under anaerobic conditions, with NADH as a cofactor, lactaldehyde is converted by a fucO-encoded lactadehyde:propanediol oxidoreductase (LPO) to L-1,2-propanediol, which is excreted as a fermentation product. In mutant strains, E. coli adapted to grow on L-1,2-propanediol, FucO catalyzes the oxidation of the polyol to L-lactaldehyde. FucO is induced regardless of the respiratory conditions of the culture, remains fully active in the absence of oxygen. In the presence of oxygen, this enzyme becomes oxidatively inactivated by a metal-catalyzed oxidation mechanism. FucO is an iron-dependent metalloenzyme that is inactivated by other metals, such as zinc, copper, or cadmium. This enzyme can also reduce glycol aldehyde with similar efficiency. Beside L-1,2-propanediol, the enzyme is also able to oxidize methanol as an alternative substrate.
Pssm-ID: 341455 [Multi-domain] Cd Length: 378 Bit Score: 337.21 E-value: 7.39e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 456 LPKSIYFRRGSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANSF 535
Cdd:cd08176 5 LNPTSYFGWGAIEEIGEEAKKRGFKKALIVTDKGLVKFGIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGVAAYKES 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 536 KPDVIIALGGGSPMDAAKIMWVMYEHPethfeelalrFMDIRKRIYKFPKMGVKAKMVAITTTSGTGSEVTPFAVVTDDA 615
Cdd:cd08176 85 GADGIIAVGGGSSIDTAKAIGIIVANP----------GADVRSLEGVAPTKNPAVPIIAVPTTAGTGSEVTINYVITDTE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 616 TGQKYPLADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPASYHEGsK 695
Cdd:cd08176 155 KKRKFVCVDPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYITKGAWELSDMLALKAIELIAKNLRKAVANP-N 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 696 NPVARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNANDNPTKqtafsqydrpqarrrY 775
Cdd:cd08176 234 NVEARENMALAQYIAGMAFSNVGLGIVHSMAHPLSAFYDTPHGVANAILLPYVMEFNAPATGEK---------------Y 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 776 AEIADHLG--LTAPGDRTAAK-----IEKLLgwldeikAELGIPKSIREAGVQEADflahVDKLSEDAFDDQCTGANPRY 848
Cdd:cd08176 299 RDIARAMGvdTTGMSDEEAAEaavdaVKKLS-------KDVGIPQKLSELGVKEED----IEALAEDALNDVCTPGNPRE 367
|
410
....*....|
gi 503995744 849 PLIAELKQIL 858
Cdd:cd08176 368 ATKEDIIALY 377
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
456-857 |
6.55e-105 |
|
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) dehydrogenase, a key enzyme in the microbial production of 1,3-PD that has been previously characterized as the product of dhaT gene in Klebsiella pneumoniae. 1,3-PD dehydrogenase is a member of the family III metal-dependent polyol dehydrogenases, which are shown to require a divalent metal ion for catalysis. However, some members of this family showed a dependence on Fe(2+) or Zn(2+) for activity.
Pssm-ID: 341467 [Multi-domain] Cd Length: 377 Bit Score: 329.48 E-value: 6.55e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 456 LPKSIYFRRGSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANSF 535
Cdd:cd08188 5 IPPVNLFGPGCLKEIGDELKKLGGKKALIVTDKGLVKLGLVKKVTDVLEEAGIEYVIFDGVQPNPTVTNVNEGLELFKEN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 536 KPDVIIALGGGSPMDAAKIMWVmyehpethfeeLALRFMDIRKR--IYKFPKMGVKakMVAITTTSGTGSEVTPFAVVTD 613
Cdd:cd08188 85 GCDFIISVGGGSAHDCAKAIGI-----------LATNGGEIEDYegVDKSKKPGLP--LIAINTTAGTASEVTRFAVITD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 614 DATGQKYPLADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPASYHEG 693
Cdd:cd08188 152 EERHVKMVIVDWNVTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVSTGATPLTDALALEAIRLIAENLPKAVANG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 694 sKNPVARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNandnptkqtafsqydRPQARR 773
Cdd:cd08188 232 -KDLEARENMAYAQFLAGMAFNNAGLGYVHAMAHQLGGFYNLPHGVCNAILLPHVMEFN---------------LPACPE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 774 RYAEIADHLGLTAPGDRTAAKIEKLLGWLDEIKAELGIPKSIREAGVQEADFlahvDKLSEDAFDDQCTGANPRYPLIAE 853
Cdd:cd08188 296 RFADIARALGENTEGLSDEEAAEAAIEAIRKLSRRVGIPSGLKELGVKEEDF----PLLAENALKDACGPTNPRQATKED 371
|
....
gi 503995744 854 LKQI 857
Cdd:cd08188 372 VIAI 375
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
465-849 |
1.12e-97 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.
Pssm-ID: 341468 [Multi-domain] Cd Length: 378 Bit Score: 310.55 E-value: 1.12e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 465 GSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANSFKPDVIIALG 544
Cdd:cd08189 13 GSLLQLPEALKKLGIKRVLIVTDKGLVKLGLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALYKENGCDAIIAIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 545 GGSPMDAAKIMWVMYEHPETHFEELAlRFMDIRKRIYKFpkmgvkakmVAITTTSGTGSEVTPFAVVTDDATGQKYPLAD 624
Cdd:cd08189 93 GGSVIDCAKVIAARAANPKKSVRKLK-GLLKVRKKLPPL---------IAVPTTAGTGSEATIAAVITDPETHEKYAIND 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 625 YALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPASYHEGSkNPVARERVH 704
Cdd:cd08189 163 PKLIPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETDEYALEAVKLIFENLPKAYEDGS-DLEARENML 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 705 SAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNandnptkqtafsqydRPQARRRYAEIADHLGL 784
Cdd:cd08189 242 LASYYAGLAFTRAYVGYVHAIAHQLGGLYGVPHGLANAVVLPHVLEFY---------------GPAAEKRLAELADAAGL 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503995744 785 TAPGDRTAAKIEKLLGWLDEIKAELGIPKSIreAGVQEADFlahvDKLSEDAFDDqctgANPRYP 849
Cdd:cd08189 307 GDSGESDSEKAEAFIAAIRELNRRMGIPTTL--EELKEEDI----PEIAKRALKE----ANPLYP 361
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
478-862 |
2.59e-95 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341485 [Multi-domain] Cd Length: 380 Bit Score: 304.46 E-value: 2.59e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 478 GHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANSFKPDVIIALGGGSPMDAAKIMWV 557
Cdd:cd14863 26 GCKKVLLVTDKGLKKAGIVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEIAREEGADGVIGIGGGSVLDTAKAIAV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 558 MYEHPEThfeelALRFMDIRKRIYKFPKmgvkaKMVAITTTSGTGSEVTPFAVVTDDATGQKYPLADYALTPDMAIVDAN 637
Cdd:cd14863 106 LLTNPGP-----IIDYALAGPPVPKPGI-----PLIAIPTTAGTGSEVTPIAVITDEENGVKKSLLGPFLVPDLAILDPE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 638 LVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPASYHEGsKNPVARERVHSAATIAGIAFANA 717
Cdd:cd14863 176 LTVGLPPSLTAATGMDALSHAIEAYTSKLANPMTDALALQAIRLIVKNLPRAVKDG-DNLEARENMLLASNLAGIAFNNA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 718 FLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNANDNPTKqtafsqydrpqarrrYAEIADHLGLTAPGDRTAAKIEK 797
Cdd:cd14863 255 GTHIGHAIAHALGALYHIPHGLACALALPVVLEFNAEAYPEK---------------VKKIAKALGVSFPGESDEELGEA 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503995744 798 LLGWLDEIKAELGIPKSIREAGVQEADFlahvDKLSEDAFDDQCTGANPRYPLIAELKQILLDTF 862
Cdd:cd14863 320 VADAIREFMKELGIPSLFEDYGIDKEDL----DKIAEAVLKDPFAMFNPRPITEEEVAEILEAIY 380
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
457-862 |
4.15e-90 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341487 [Multi-domain] Cd Length: 383 Bit Score: 290.60 E-value: 4.15e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 457 PKSIYFRRGSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANSFK 536
Cdd:cd14865 6 PTKIVSGAGALENLPAELARLGARRPLIVTDKGLAAAGLLKKVEDALGDAIEIVGVFDDVPPDSSVAVVNEAAARAREAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 537 PDVIIALGGGSPMDAAKIMWVMYEHPETHFEELALRFMDIRKRIykfPkmgvkakMVAITTTSGTGSEVTPFAVVTDDAT 616
Cdd:cd14865 86 ADGIIAVGGGSVIDTAKGVNILLSEGGDDLDDYGGANRLTRPLK---P-------LIAIPTTAGTGSEVTLVAVIKDEEK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 617 GQKYPLADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPASYHEGsKN 696
Cdd:cd14865 156 KVKLLFVSPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDALALQAIRLISENLPKAVKNG-KD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 697 PVARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNAndnptkqtafsqydrPQARRRYA 776
Cdd:cd14865 235 LEARLALAIAATMAGIAFSNSMVGLVHAIAHAVGAVAGVPHGLANSILLPHVMRYNL---------------DAAAERYA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 777 EIADHL--GLTAPGDRTAAKIEKLLGWLDEIKAELGIPKSIREAGVQEADFLAhvdkLSEDAFDDQCTGANPRYPLIAEL 854
Cdd:cd14865 300 ELALALayGVTPAGRRAEEAIEAAIDLVRRLHELCGLPTRLRDVGVPEEQLEA----IAELALNDGAILFNPREVDPEDI 375
|
....*...
gi 503995744 855 KQILLDTF 862
Cdd:cd14865 376 LAILEAAY 383
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
456-858 |
1.15e-89 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase-like (ADH) proteins. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase fold and is a member of the iron-containing alcohol dehydrogenase-like family. They are distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341464 [Multi-domain] Cd Length: 379 Bit Score: 289.40 E-value: 1.15e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 456 LPKSIYFRRGSLPiALDEVITDGHKRALIVTDR-FLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANS 534
Cdd:cd08185 3 QPTRILFGAGKLN-ELGEEALRPGKKALIVTGKgSSKKTGLLDRVKKLLEKAGVEVVVFDKVEPNPLTTTVMEGAALAKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 535 FKPDVIIALGGGSPMDAAKIMWVMYEHPETHFEelalrfmdirkriYKFPKMGVKAK------MVAITTTSGTGSEVTPF 608
Cdd:cd08185 82 EGCDFVIGLGGGSSMDAAKAIAFMATNPGDIWD-------------YIFGGTGKGPPpekalpIIAIPTTAGTGSEVDPW 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 609 AVVTDDATGQKYPLADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPA 688
Cdd:cd08185 149 AVITNPETKEKKGIGHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISKNANPFSDMLALEAIRLVAKYLPR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 689 SYHEGSkNPVARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQF-HIPHGLANALLISNVIRYNANDNPTKqtafsqyd 767
Cdd:cd08185 229 AVKDGS-DLEAREKMAWASTLAGIVIANSGTTLPHGLEHPLSGYHpNIPHGAGLAALYPAYFEFTIEKAPEK-------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 768 rpqarrrYAEIADhlgLTAPGDRTAAKIEKLLGWLDEIKAELGIPKSIREAGVQEADFlahvDKLSEDAFD--DQCTGAN 845
Cdd:cd08185 300 -------FAFVAR---AEASGLSDAKAAEDFIEALRKLLKDIGLDDLLSDLGVTEEDI----PWLAENAMEtmGGLFANN 365
|
410
....*....|...
gi 503995744 846 PRYPLIAELKQIL 858
Cdd:cd08185 366 PVELTEEDIVEIY 378
|
|
| lactal_redase |
TIGR02638 |
lactaldehyde reductase; This clade of genes encoding iron-containing alcohol dehydrogenase ... |
456-854 |
1.49e-87 |
|
lactaldehyde reductase; This clade of genes encoding iron-containing alcohol dehydrogenase (pfam00465) proteins is generally found in apparent operons for the catabolism of rhamnose or fucose. Catabolism of both of these monosaccharides results in lactaldehyde which is reduced by this enzyme to 1,2 propanediol. This protein is alternatively known by the name 1,2 propanediol oxidoreductase. This enzyme is active under anaerobic conditions in E. coli while being inactivated by reactive oxygen species under aerobic conditions. Under aerobic conditions the lactaldehyde product of rhamnose and fucose catabolism is believed to be oxidized to lactate by a separate enzyme, lactaldehyde dehydrogenase. [Energy metabolism, Sugars]
Pssm-ID: 131686 [Multi-domain] Cd Length: 379 Bit Score: 283.94 E-value: 1.49e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 456 LPKSIYFRRGSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANSF 535
Cdd:TIGR02638 6 LNETSYFGAGAIEDIVDEVKRRGFKKALVVTDKDLIKFGVADKVTDLLDEAGIAYELFDEVKPNPTITVVKAGVAAFKAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 536 KPDVIIALGGGSPMDAAKIMWVMYEHPEthfeelalrFMDIR--KRIYKFPKMGVKakMVAITTTSGTGSEVTPFAVVTD 613
Cdd:TIGR02638 86 GADYLIAIGGGSPIDTAKAIGIISNNPE---------FADVRslEGVAPTKKPGVP--IIAIPTTAGTAAEVTINYVITD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 614 DATGQKYPLADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPASYhEG 693
Cdd:TIGR02638 155 EENKRKFVCVDPHDIPDVAVIDAEMMYSMPKSLTAATGMDALTHAIEGYITKGAWELTDMLHLKAIEIIARWLRSAV-EG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 694 SKNPVARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNAndnptkqtafsqydrPQARR 773
Cdd:TIGR02638 234 GKDLEAREQMALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEFNA---------------EFTGE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 774 RYAEIADHLGLTAPGDRTAAKIEKLLGWLDEIKAELGIPKSIREAGVQEADflahVDKLSEDAFDDQCTGANPRYPLIAE 853
Cdd:TIGR02638 299 KYREIAKAMGVKTEGMSDEEARDAAVEAVKTLSKRVGIPEGLSELGVKEED----IPALAEAALADVCTGGNPRETTVEE 374
|
.
gi 503995744 854 L 854
Cdd:TIGR02638 375 I 375
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
460-862 |
1.81e-87 |
|
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to iron-containing alcohol dehydrogenase (Fe-ADH), most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341483 [Multi-domain] Cd Length: 374 Bit Score: 283.25 E-value: 1.81e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 460 IYFRRGS---LPIALDEvitDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANSFK 536
Cdd:cd14861 6 IRFGAGAiaeLPEELKA---LGIRRPLLVTDPGLAALGIVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAYREGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 537 PDVIIALGGGSPMDAAKIMWVMYEHPE--THFEELALRFMDIRKRIykfpkmgvkAKMVAITTTSGTGSEVTPFAVVTDD 614
Cdd:cd14861 83 CDGIIALGGGSAIDAAKAIALMATHPGplWDYEDGEGGPAAITPAV---------PPLIAIPTTAGTGSEVGRAAVITDD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 615 ATGQKYPLADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPASYHEGS 694
Cdd:cd14861 154 DTGRKKIIFSPKLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGFHPMADGIALEGLRLISEWLPRAVADGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 695 kNPVARERVHSAATIAGIAFANAfLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNandnptkqtafsqydRPQARRR 774
Cdd:cd14861 234 -DLEARGEMMMAALMGAVAFQKG-LGAVHALAHALGALYGLHHGLLNAILLPYVLRFN---------------RPAVEDK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 775 YAEIADHLGLTAPGDrtaakiEKLLGWLDEIKAELGIPKSIREAGVQEadflAHVDKLSEDAFDDQCTGANPRYPLIAEL 854
Cdd:cd14861 297 LARLARALGLGLGGF------DDFIAWVEDLNERLGLPATLSELGVTE----DDLDELAELALADPCHATNPRPVTAEDY 366
|
....*...
gi 503995744 855 KQILLDTF 862
Cdd:cd14861 367 RALLREAL 374
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
460-857 |
1.17e-85 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341489 [Multi-domain] Cd Length: 374 Bit Score: 278.66 E-value: 1.17e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 460 IYFRRGSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANSFKPDV 539
Cdd:cd17814 7 FIFGVGARKLAGRYAKNLGARKVLVVTDPGVIKAGWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAELYREEGCDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 540 IIALGGGSPMDAAKIMWVMYEHPethfeelalrfMDIRKR--IYKFPKMGVKakMVAITTTSGTGSEVTPFAVVTDDATG 617
Cdd:cd17814 87 IVAVGGGSPIDCAKGIGIVVSNG-----------GHILDYegVDKVRRPLPP--LICIPTTAGSSADVSQFAIITDTERR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 618 QKYPLADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPASYHEgSKNP 697
Cdd:cd17814 154 VKMAIISKTLVPDVSLIDPETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDLHALEAIRLISENLPKAVAD-PDDL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 698 VARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNAndnptkqtafsqydrPQARRRYAE 777
Cdd:cd17814 233 EAREKMMLASLQAGLAFSNASLGAVHAMAHSLGGLLDLPHGECNALLLPHVIRFNF---------------PAAPERYRK 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 778 IADHLGLTAPGDRTAAKIEKLLGWLDEIKAELGIPKSIREAGVQEADflahVDKLSEDAFDDQCTGANPRYPLIAELKQI 857
Cdd:cd17814 298 IAEAMGLDVDGLDDEEVAERLIEAIRDLREDLGIPETLSELGVDEED----IPELAKRAMKDPCLVTNPRRPTREDIEEI 373
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
455-858 |
2.24e-83 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341475 [Multi-domain] Cd Length: 367 Bit Score: 272.15 E-value: 2.24e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 455 KLPKSIYFRRGSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKaaGVETEVFFEVEADPTLTIVRKGAELANS 534
Cdd:cd08196 4 YQPVKIIFGEGILKELPDIIKELGGKRGLLVTDPSFIKSGLAKRIVESLK--GRIVAVFSDVEPNPTVENVDKCARLARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 535 FKPDVIIALGGGSPMDAAKIMWVMYEHPEThfeelalrFMDIRKRIYKFPKMGVKakMVAITTTSGTGSEVTPFAVVTDD 614
Cdd:cd08196 82 NGADFVIAIGGGSVLDTAKAAACLAKTDGS--------IEDYLEGKKKIPKKGLP--LIAIPTTAGTGSEVTPVAVLTDK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 615 ATGQKYPLADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPASYHEGS 694
Cdd:cd08196 152 EKGKKAPLVSPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSINHQPISDALALEAAKLVLENLEKAYNNPN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 695 kNPVARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNANDNPTKQTAFSQYdrpqarrr 774
Cdd:cd08196 232 -DKEAREKMALASLLAGLAFSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNAEALPGRLDELAKQ-------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 775 yaeiadhLGLTAPGDrTAAKIEKLlgwldeiKAELGIPKSIREAGVQEADflahVDKLSEDAFDDQCTGANPRYPLIAEL 854
Cdd:cd08196 303 -------LGFKDAEE-LADKIEEL-------KKRIGLRTRLSELGITEED----LEEIVEESFHPNRANNNPVEVTKEDL 363
|
....
gi 503995744 855 KQIL 858
Cdd:cd08196 364 EKLL 367
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
457-836 |
6.18e-83 |
|
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor; 5-hydroxyvalerate dehydrogenase (HVD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the cyclopentanol metabolism biochemical pathway. It catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor. This cyclopentanol (cpn) degradation pathway is present in some bacteria which can use cyclopentanol as sole carbon source. In Comamonas sp. strain NCIMB 9872, this enzyme is encoded by the CpnD gene.
Pssm-ID: 341472 [Multi-domain] Cd Length: 379 Bit Score: 271.31 E-value: 6.18e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 457 PKSIYFRRGSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANSFK 536
Cdd:cd08193 4 VPRIICGAGAAARLGELLRELGARRVLLVTDPGLVKAGLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQAREAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 537 PDVIIALGGGSPMDAAKIMWVMYEHPEThfeeLAlrfmdirkRIYkfpkmGV-KAK-----MVAITTTSGTGSEVTPFAV 610
Cdd:cd08193 84 ADGVIGFGGGSSMDVAKLVALLAGSDQP----LD--------DIY-----GVgKATgprlpLILVPTTAGTGSEVTPISI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 611 VTDDATgQKYPLADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVS-VLASEFSDGQALQALKLLKENLPAS 689
Cdd:cd08193 147 VTTGET-EKKGVVSPQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSrHKKNPISDALAREALRLLGANLRRA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 690 YHEGSkNPVARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNAndnptkqtafsqydrP 769
Cdd:cd08193 226 VEDGS-DLEAREAMLLGSMLAGQAFANAPVAAVHALAYPLGGHFHVPHGLSNALVLPHVLRFNL---------------P 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503995744 770 QARRRYAEIADHLGLTAPGDRTAAKIEKLLGWLDEIKAELGIPKSIREAGVQEADflahVDKLSEDA 836
Cdd:cd08193 290 AAEALYAELARALLPGLAFGSDAAAAEAFIDALEELVEASGLPTRLRDVGVTEED----LPMLAEDA 352
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
7-406 |
8.79e-82 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 270.26 E-value: 8.79e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 7 AELNALVERVKKAQREYASFTQEQVDKIFRAAALAAADARIPLAKMAVAESGMGIVEDKVIKNHFASEyiynaykdeKTC 86
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGMGRVEDKIAKNHLAAE---------KTP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 87 G-------VLSEDDTFgTITIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAAIA 159
Cdd:cd07121 75 GtedltttAWSGDNGL-TLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 160 AGAPKDLIGWIDQPSVELSNALMHHPDINLILATGGPGMVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKT 239
Cdd:cd07121 154 AGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVKAALSSGKKAIGAGAGNPPVVVDETADIEKAARDIVQGAS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 240 FDNGVICASEQSVVVVDSVYDAVRERFSSHGGYLLQGQELKAVQNIILKNG---ALNAAIVGQPAYKIAELAGFTVPVST 316
Cdd:cd07121 234 FDNNLPCIAEKEVIAVDSVADYLIAAMQRNGAYVLNDEQAEQLLEVVLLTNkgaTPNKKWVGKDASKILKAAGIEVPADI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 317 KILIGEvtdVDESEPFA-HEKLSPTLAMYRAKNFEDAVDKAekLVAMGGIGHTSCLYTdqdNQPERVAYFGQLMKTARIL 395
Cdd:cd07121 314 RLIIVE---TDKDHPFVvEEQMMPILPVVRVKNFDEAIELA--VELEHGNRHTAIIHS---KNVENLTKMARAMQTTIFV 385
|
410
....*....|.
gi 503995744 396 INTPaSQGGIG 406
Cdd:cd07121 386 KNGP-SYAGLG 395
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
457-858 |
3.68e-81 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341462 [Multi-domain] Cd Length: 377 Bit Score: 266.68 E-value: 3.68e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 457 PKSIYFRRGSLPIALDEVITDGhKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFfEVEADPTLTIVRKGAELANSFK 536
Cdd:cd08183 1 PPRIVFGRGSLQELGELAAELG-KRALLVTGRSSLRSGRLARLLEALEAAGIEVALF-SVSGEPTVETVDAAVALAREAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 537 PDVIIALGGGSPMDAAKIMWVMYEHPEThfeelALRFMDIrkrIYKFPKMGVK-AKMVAITTTSGTGSEVTPFAVVTDDA 615
Cdd:cd08183 79 CDVVIAIGGGSVIDAAKAIAALLTNEGS-----VLDYLEV---VGKGRPLTEPpLPFIAIPTTAGTGSEVTKNAVLSSPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 616 TGQKYPLADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPASYHEGSk 695
Cdd:cd08183 151 HGVKVSLRSPSMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTDALAREGLRLAARSLRRAYEDGE- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 696 NPVARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNAndnptkQTAFSQYDRPQARRRY 775
Cdd:cd08183 230 DLEAREDMALASLLGGLALANAGLGAVHGLAGPLGGMFGAPHGAICAALLPPVLEANL------RALREREPDSPALARY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 776 AEIADHLGLTApgdrtAAKIEKLLGWLDEIKAELGIPkSIREAGVQEADFlahvDKLSEDAFDDQCTGANPRYPLIAELK 855
Cdd:cd08183 304 RELAGILTGDP-----DAAAEDGVEWLEELCEELGIP-RLSEYGLTEEDF----PEIVEKARGSSSMKGNPIELSDEELL 373
|
...
gi 503995744 856 QIL 858
Cdd:cd08183 374 EIL 376
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
7-406 |
5.29e-80 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 266.38 E-value: 5.29e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 7 AELNALVERVKKAQREYASFTQEQVDKIFRAAALAAADARIPLAKMAVAESGMGIVEDKVIKNHFASEyiynaykdeKTC 86
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGMGRVEDKIAKNVAAAE---------KTP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 87 GV-------LSEDDTFGTITIAePIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAAIA 159
Cdd:PRK15398 107 GVedltteaLTGDNGLTLIEYA-PFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELLNEAIVA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 160 AGAPKDLIGWIDQPSVELSNALMHHPDINLILATGGPGMVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKT 239
Cdd:PRK15398 186 AGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPAVVKAAMKSGKKAIGAGAGNPPVVVDETADIEKAARDIVKGAS 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 240 FDNGVICASEQSVVVVDSVYDAVRERFSSHGGYLLQGQELKAVQNIILKNG-ALNAAIVGQPAYKIAELAGFTVPVSTKI 318
Cdd:PRK15398 266 FDNNLPCIAEKEVIVVDSVADELMRLMEKNGAVLLTAEQAEKLQKVVLKNGgTVNKKWVGKDAAKILEAAGINVPKDTRL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 319 LIGEvtdVDESEPFA-HEKLSPTLAMYRAKNFEDAVDKAekLVAMGGIGHTSCLYTdqdNQPERVAYFGQLMKTARILIN 397
Cdd:PRK15398 346 LIVE---TDANHPFVvTELMMPVLPVVRVKDVDEAIALA--VKLEHGNRHTAIMHS---RNVDNLNKMARAIQTSIFVKN 417
|
....*....
gi 503995744 398 TPaSQGGIG 406
Cdd:PRK15398 418 GP-SYAGLG 425
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
461-857 |
4.91e-79 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 261.08 E-value: 4.91e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 461 YFRRGSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANSFKPDVI 540
Cdd:PRK10624 12 YFGRGAIGALTDEVKRRGFKKALIVTDKTLVKCGVVAKVTDVLDAAGLAYEIYDGVKPNPTIEVVKEGVEVFKASGADYL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 541 IALGGGSPMDAAKIMWVMYEHPEthfeelalrFMDIRKRiykfpkMGV---KAKMV---AITTTSGTGSEVTPFAVVTDD 614
Cdd:PRK10624 92 IAIGGGSPQDTCKAIGIISNNPE---------FADVRSL------EGVaptKKPSVpiiAIPTTAGTAAEVTINYVITDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 615 ATGQKYPLADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPASYHEgs 694
Cdd:PRK10624 157 EKRRKFVCVDPHDIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYITRGAWALTDMLHLKAIEIIAGALRGAVAG-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 695 kNPVARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNAndnptkqtafsqydrPQARRR 774
Cdd:PRK10624 235 -DKEAGEGMALGQYIAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEYNA---------------DFTGEK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 775 YAEIADHLG-----LTAPGDRTAA--KIEKLlgwldeiKAELGIPKSIREAGVQEADflahVDKLSEDAFDDQCTGANPR 847
Cdd:PRK10624 299 YRDIARAMGvkvegMSLEEARNAAveAVKAL-------NRDVGIPPHLRDVGVKEED----IPALAQAAFDDVCTGGNPR 367
|
410
....*....|
gi 503995744 848 YPLIAELKQI 857
Cdd:PRK10624 368 EATLEDIVEL 377
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
456-858 |
3.75e-75 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.
Pssm-ID: 341470 [Multi-domain] Cd Length: 392 Bit Score: 250.99 E-value: 3.75e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 456 LPKSIYFRRGSLPiALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANSF 535
Cdd:cd08191 3 SPSRLLFGPGARR-ALGRVAARLGSRVLIVTDPRLASTPLVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAARAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 536 KPDVIIALGGGSPMDAAKIMWVMYEH---PETHFEELALRfmdirkriykfpkmGVKAKMVAITTTSGTGSEVTPFAVVT 612
Cdd:cd08191 82 DPDVVIGLGGGSNMDLAKVVALLLAHggdPRDYYGEDRVP--------------GPVLPLIAVPTTAGTGSEVTPVAVLT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 613 DDATGQKYPLADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEF---------------SDGQALQ 677
Cdd:cd08191 148 DPARGMKVGVSSPYLRPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYTARDFPPFprldpdpvyvgknplTDLLALE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 678 ALKLLKENLPASYHEGSKNPvARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNandnp 757
Cdd:cd08191 228 AIRLIGRHLPRAVRDGDDLE-ARSGMALAALLAGLAFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLPYVMRFN----- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 758 tkqtafsqydRPQARRRYAEIADHLGLTaPGDRTAAKIEKLLGWLDEIKAELGIPKSIREAGVQEADFlahvDKLSEDAF 837
Cdd:cd08191 302 ----------RPARAAELAEIARALGVT-TAGTSEEAADRAIERVEELLARIGIPTTLADLGVTEADL----PGLAEKAL 366
|
410 420
....*....|....*....|..
gi 503995744 838 DDQ-CTGANPRYPLIAELKQIL 858
Cdd:cd08191 367 SVTrLIANNPRPPTEEDLLRIL 388
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
460-858 |
1.54e-72 |
|
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP); Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP) with either NADH or NADPH as a cofactor, although NADH is the preferred cofactor. PnAA is a biosynthetic intermediate for several phosphonates such as the antibiotic fosfomycin, phosphinothricin tripeptide (PTT), and 2-aminoethylphosphonate (AEP). This enzyme is named PhpC in PTT biosynthesis pathway in Streptomyces hygroscopicus and S. viridochromogenes.
Pssm-ID: 341461 [Multi-domain] Cd Length: 370 Bit Score: 243.29 E-value: 1.54e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 460 IYFRRGSLPiALDEVITD-GHKRALIVTDRFLFNNGYADQITSVLkAAGVETEVFFEVEADPTLTIVRKGAELANSFKPD 538
Cdd:cd08182 4 IIFGPGALA-ELKDLLGGlGARRVLLVTGPSAVRESGAADILDAL-GGRIPVVVFSDFSPNPDLEDLERGIELFRESGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 539 VIIALGGGSPMDAAKIMWVMYEHPETHFEELalrfmdiRKRIYKFPKMGVKakMVAITTTSGTGSEVTPFAVVTDDATGQ 618
Cdd:cd08182 82 VIIAVGGGSVIDTAKAIAALLGSPGENLLLL-------RTGEKAPEENALP--LIAIPTTAGTGSEVTPFATIWDEAEGK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 619 KYPLADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPAsYHEGSKNPV 698
Cdd:cd08182 153 KYSLAHPSLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYALRAIRLILENLPL-LLENLPNLE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 699 ARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNAndnptkqtafSQYDRPQARRRYAEI 778
Cdd:cd08182 232 AREAMAEASLLAGLAISITKTTAAHAISYPLTSRYGVPHGHACALTLPAVLRYNA----------GADDECDDDPRGREI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 779 ADHLGltapgdrtAAKIEKLLGWLDEIKAELGIPKSIREAGVQEADflahVDKLSEDAFDDQCTGANPRYPLIAELKQIL 858
Cdd:cd08182 302 LLALG--------ASDPAEAAERLRALLESLGLPTRLSEYGVTAED----LEALAASVNTPERLKNNPVRLSEEDLLRLL 369
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
459-860 |
8.67e-67 |
|
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This family contains hydroxyacid-oxoacid transhydrogenase (HOT), also known as D-2-hydroxyglutarate transhydrogenase. It catalyzes the conversion of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA), coupled to the stoichiometric conversion of alpha-ketoglutarate to D-2-hydroxyglutarate in gamma-Hydroxybutyrate catabolism. Unlike many other alcohols, which are oxidized by NAD-linked dehydrogenases, gamma-hydroxybutyrate is metabolized to succinate semialdehyde by hydroxyacid-oxoacid transhydrogenase which does not require free NAD or NADP; instead, it uses alpha-ketoglutarate as an acceptor, converting it to d-2-hydroxyglutarate. Alpha-ketoglutarate serves as an intermediate acceptor to regenerate NAD(P) required for the oxidation of GHB. HOT also catalyzes the reversible oxidation of a hydroxyacid obligatorily coupled to the reduction of an oxoacid, and requires no cofactor. In mammals, the HOT enzyme is located in mitochondria, and is expressed with an N-terminal mitochondrial targeting sequence. HOT enzyme is member of the metal-containing alcohol dehydrogenase family. It typically contains an iron although other metal ions may be used.
Pssm-ID: 341469 [Multi-domain] Cd Length: 412 Bit Score: 228.97 E-value: 8.67e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 459 SIYFRRGslpiALDEVITD----GHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANS 534
Cdd:cd08190 3 NIRFGPG----ATRELGMDlkrlGAKKVLVVTDPGLAKLGLVERVLESLEKAGIEVVVYDGVRVEPTDESFEEAIEFAKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 535 FKPDVIIALGGGSPMDAAKIMWVMYEHPEthfeelalRFMDirkriYKFPKMGVKAK-------MVAITTTSGTGSEVTP 607
Cdd:cd08190 79 GDFDAFVAVGGGSVIDTAKAANLYATHPG--------DFLD-----YVNAPIGKGKPvpgplkpLIAIPTTAGTGSETTG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 608 FAVVTDDATGQKYPLADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVL------------------ASE 669
Cdd:cd08190 146 VAIFDLEELKVKTGISSRYLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTARPynarprpanpderpayqgSNP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 670 FSDGQALQALKLLKENLPASYHEGSkNPVARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQ-------------FHIP 736
Cdd:cd08190 226 ISDVWAEKAIELIGKYLRRAVNDGD-DLEARSNMLLASTLAGIGFGNAGVHLPHAMAYPIAGLvkdyrppgypvdhPHVP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 737 HGLANALLISNVIRYNANDNPtkqtafsqydrpqarRRYAEIADHLGLTAPGDRTAAKIEKLLGWLDEIKAELGIPKSIR 816
Cdd:cd08190 305 HGLSVALTAPAVFRFTAPACP---------------ERHLEAAELLGADTSGASDRDAGEVLADALIKLMRDIGIPNGLS 369
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 503995744 817 EAGVQEADflahVDKLSEDAFDDQ-CTGANPRYPLIAELKQILLD 860
Cdd:cd08190 370 ALGYSEDD----IPALVEGTLPQQrLLKLNPRPVTEEDLEEIFED 410
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
455-759 |
1.27e-62 |
|
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1,3-propanediol dehydrogenase (PPD) which is a member of the iron-containing alcohol dehydrogenase superfamily, and exhibits a dehydroquinate synthase-like fold. Protein sequence similarity search and other biochemical evidences suggest that they are close to the iron-containing 1,3-propanediol dehydrogenase (EC 1.1.1.202). 1,3-propanediol dehydrogenase catalyzes the oxidation of propane-1,3-diol to 3-hydroxypropanal with the simultaneous reduction of NADP+ to NADPH. The protein structure of Thermotoga maritima TM0920 gene contains one NADP+ and one iron ion.
Pssm-ID: 341460 [Multi-domain] Cd Length: 358 Bit Score: 215.53 E-value: 1.27e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 455 KLPKSIYFRRGSLPIALDEVITDGhKRALIVTDRF-LFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELAN 533
Cdd:cd08181 2 YMPTKVYFGKNCVEKHADELAALG-KKALIVTGKHsAKKNGSLDDVTEALEENGIEYFIFDEVEENPSIETVEKGAELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 534 SFKPDVIIALGGGSPMDAAKIMWVMYEHPEtHFEELalrfmdirkriYKFPKMGVKAKMVAITTTSGTGSEVTPFAVVTD 613
Cdd:cd08181 81 KEGADFVIGIGGGSPLDAAKAIALLAANKD-GDEDL-----------FQNGKYNPPLPIVAIPTTAGTGSEVTPYSILTD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 614 DATGQKYPLADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPAsYHEG 693
Cdd:cd08181 149 HEKGTKKSFGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSVKATPLSDALALEALRLIGECLPN-LLGD 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503995744 694 SKNPVARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNANDNPTK 759
Cdd:cd08181 228 ELDEEDREKLMYASTLAGMVIAQTGTTLPHGLGYPLTYFKGIPHGRANGILLPAYLKLCEKQEPEK 293
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
465-846 |
1.30e-61 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 213.66 E-value: 1.30e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 465 GSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANSFKPDVIIALG 544
Cdd:PRK09860 17 DSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKENNCDSVISLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 545 GGSPMDAAKIMWVmyehpethfeeLALRFMDIRKriYKFPKMGVKAK--MVAITTTSGTGSEVTPFAVVTDDATGQKYPL 622
Cdd:PRK09860 97 GGSPHDCAKGIAL-----------VAANGGDIRD--YEGVDRSAKPQlpMIAINTTAGTASEMTRFCIITDEARHIKMAI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 623 ADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPASYHEGSkNPVARER 702
Cdd:PRK09860 164 VDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGS-NAKAREA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 703 VHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNANdnptkqtafsqydrpQARRRYAEIADHL 782
Cdd:PRK09860 243 MAYAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSK---------------VAAARLRDCAAAM 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503995744 783 GLTAPGDRTAAKIEKLLGWLDEIKAELGIPKSIREAGVQEADFlahvDKLSEDAFDDQCTGANP 846
Cdd:PRK09860 308 GVNVTGKNDAEGAEACINAIRELAKKVDIPAGLRDLNVKEEDF----AVLATNALKDACGFTNP 367
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
465-858 |
1.72e-57 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 202.57 E-value: 1.72e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 465 GSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANSFKPDVIIALG 544
Cdd:PRK15454 35 GAVSSCGQQAQTRGLKHLFVMADSFLHQAGMTAGLTRSLAVKGIAMTLWPCPVGEPCITDVCAAVAQLRESGCDGVIAFG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 545 GGSPMDAAKIMWVMYEHPETHFEELALRfMDIRKRIykfpkmgvkaKMVAITTTSGTGSEVTPFAVVTDDATGQKYPLAD 624
Cdd:PRK15454 115 GGSVLDAAKAVALLVTNPDSTLAEMSET-SVLQPRL----------PLIAIPTTAGTGSETTNVTVIIDAVSGRKQVLAH 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 625 YALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPASYHEGsKNPVARERVH 704
Cdd:PRK15454 184 ASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGAIAMIGKSLPKAVGYG-HDLAARESML 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 705 SAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNandnptkqtafsqydRPQARRRYAEIADHLGL 784
Cdd:PRK15454 263 LASCMAGMAFSSAGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEFN---------------RMVCRERFSQIGRALRT 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503995744 785 TAPGDRTAakieklLGWLDEIKAELGIPKSIREAGVQEadflAHVDKLSEDAFDDQCTGANPRyplIAELKQIL 858
Cdd:PRK15454 328 KKSDDRDA------INAVSELIAEVGIGKRLGDVGATS----AHYGAWAQAALEDICLRSNPR---TASLEQIV 388
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
14-446 |
1.51e-56 |
|
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: 198.99 E-value: 1.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 14 ERVKKAQREYASFTQEQVDKIFRAAALAAADARIPLAKMAVAESG--MGIVEDKVIKNHFASEYIYNAYKDEKTCGVLSE 91
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGkpIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 92 DDTFGTITIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVlqaaIAAGAPKDLIGWID 171
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELL----QEAGLPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 172 QPSVELSNALMHHPDINLILATGGPGMVKAAY----SSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKTFDNGVICA 247
Cdd:cd06534 157 GGGDEVGAALLSHPRVDKISFTGSTAVGKAIMkaaaENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 248 seqsvvvvdsvydavrerfsshggyllqgqelkAVQNIILKNGALNAAivgqpaykIAELAGFtvpvstkiligeVTDVD 327
Cdd:cd06534 237 ---------------------------------AASRLLVHESIYDEF--------VEKLVTV------------LVDVD 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 328 ESEPFAHEKLS-PTLAMYRAKNFEDAVDKAEklvaMGGIGHTSCLYTdqdNQPERVAYFGQLMKTARILINTPASQGGig 406
Cdd:cd06534 264 PDMPIAQEEIFgPVLPVIRFKDEEEAIALAN----DTEYGLTAGVFT---RDLNRALRVAERLRAGTVYINDSSIGVG-- 334
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 503995744 407 dlynfklaPSLTLG--CGSWGGNSiSENVGPKHLINKKTVAK 446
Cdd:cd06534 335 --------PEAPFGgvKNSGIGRE-GGPYGLEEYTRTKTVVI 367
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
457-858 |
1.57e-49 |
|
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic microbes; Maleylacetate reductase (MAR) plays an important role in the degradation of aromatic compounds in aerobic microbes. In fungi and yeasts, the enzyme is involved in the catabolism of compounds such as phenol, tyrosine, benzoate, 4-hydroxybenzoate and resorcinol. In bacteria, the enzyme contributes to the degradation of resorcinol, 2,4-dihydroxybenzoate ([beta]-resorcylate) and 2,6-dihydroxybenzoate ([gamma]-resorcylate) via hydroxyquinol and maleylacetate. Maleylacetate reductase (MAR) catalyzes NADH- or NADPH-dependent reduction, at the carbon-carbon double bond, of maleylacetate or 2-chloromaleylacetate to 3-oxoadipate. In the case of 2-chloromaleylacetate, MAR initially catalyzes the NAD(P)H-dependent dechlorination to maleylacetate, which is then reduced to 3-oxoadipate. This enzyme is a homodimer. It is inhibited by thiol-blocking reagents such as p-chloromercuribenzoate and Hg++, indicating that the cysteine residue is probably necessary for the catalytic activity of maleylacetate reductase.
Pssm-ID: 341471 [Multi-domain] Cd Length: 380 Bit Score: 179.75 E-value: 1.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 457 PKSIYFRRGSLPIALDEVITDGHKRALIVTDRFL-FNNGYADQITSVLKAAGVETevFFEVEADPTLTIVRKGAELANSF 535
Cdd:cd08192 1 LERVSYGPGAVEALLHELATLGASRVFIVTSKSLaTKTDVIKRLEEALGDRHVGV--FSGVRQHTPREDVLEAARAVREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 536 KPDVIIALGGGSPMDAAKIMWVMYEHPETHFEELALRFMDIRKRIYkfpKMGVKAKMVAITTT-SgtGSEVTPFAVVTDD 614
Cdd:cd08192 79 GADLLVSLGGGSPIDAAKAVALALAEDVTDVDQLDALEDGKRIDPN---VTGPTLPHIAIPTTlS--GAEFTAGAGATDD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 615 ATGQKYPLADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPAsYHEGS 694
Cdd:cd08192 154 DTGHKQGFAHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETLCSPQATPFVDALALKALRLLFEGLPR-SKADP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 695 KNPVARERVHSAATIAGIAFANAF-LGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNANDNPTKqtafsqydrpQARR 773
Cdd:cd08192 233 EDLEARLKCQLAAWLSLFGLGSGVpMGASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAPVNAER----------QRLI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 774 RYAEIADHLGLTAPGDRTAAKIEKLLgwldeikAELGIPKSIREAGVQEADFlahvDKLSEDAFDDQCTGANPRYPL-IA 852
Cdd:cd08192 303 ARALGLVTGGLGREAADAADAIDALI-------RELGLPRTLRDVGVGRDQL----EKIAENALTDVWCRTNPRPITdKD 371
|
....*.
gi 503995744 853 ELKQIL 858
Cdd:cd08192 372 DVLEIL 377
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
457-860 |
9.20e-47 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341488 [Multi-domain] Cd Length: 384 Bit Score: 172.03 E-value: 9.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 457 PKSIYFRRGS---LPIALDEVitdGHKRALIVTDRFLfnNGYADQITSVLKAAGVE-TEVFFEVEADPTLTIVRKGAELA 532
Cdd:cd14866 5 PLRLFSGRGAlarLGRELDRL---GARRALVVCGSSV--GANPDLMDPVRAALGDRlAGVFDGVRPHSPLETVEAAAEAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 533 NSFKPDVIIALGGGSPMDAAKIMWVMYEHPEThFEELALRFMDirKRIYKFPK-MGVKAKMVAITTTSGTGSEVTPFAVv 611
Cdd:cd14866 80 READADAVVAVGGGSAIVTARAASILLAEDRD-VRELCTRRAE--DGLMVSPRlDAPKLPIFVVPTTPTTADVKAGSAV- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 612 TDDATGQKYPLADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPASyh 691
Cdd:cd14866 156 TDPPAGQRLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHADPLADATLMHALRLLADGLPRL-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 692 EGSKNPVARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNAndnptkqtafsqydrPQA 771
Cdd:cd14866 234 ADDDDPAARADLVLAAVLAGYGTDHTGGGVIHALGHAIGARYGVQNGVVHAILLPHVLRFNA---------------PAT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 772 RRRYAEIADHLGLTAPGDRTAAkiEKLLGWLDEIKAELGIPKSIREAGVQEADFlahvDKLSEDAFDDQCTGANPRYPLI 851
Cdd:cd14866 299 DGRLDRLAEALGVADAGDEASA--AAVVDAVEALLDALGVPTRLRDLGVSREDL----PAIAEAAMDDWFMDNNPRPVPT 372
|
410
....*....|
gi 503995744 852 A-ELKQILLD 860
Cdd:cd14866 373 AeELEALLEA 382
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
459-751 |
1.08e-43 |
|
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol dehydrogenase (ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. The ADH of hyperthermophilic archaeon Thermococcus hydrothermalis oxidizes a series of primary aliphatic and aromatic alcohols, preferentially from C2 to C8, but is also active towards methanol and glycerol, and is stereospecific for monoterpenes. It has been suggested that the type III ADHs in microorganisms are involved in acetaldehyde detoxication rather than in alcohol turnover.
Pssm-ID: 341465 [Multi-domain] Cd Length: 380 Bit Score: 162.82 E-value: 1.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 459 SIYFRRGSLPiALDEVITD-GHKRALIVTDRFLFN-NGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANSFK 536
Cdd:cd08186 3 TLYFGVGAIA-KIKDILKDlGIDKVIIVTGRSSYKkSGAWDDVEKALEENGIEYVVYDKVTPNPTVDQADEAAKLARDFG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 537 PDVIIALGGGSPMDAAKIMWVMYEHPETHFEELalrfmdirkriYKFPKMGVKAK-MVAITTTSGTGSEVTPFAVVTDDA 615
Cdd:cd08186 82 ADAVIAIGGGSPIDTAKSVAVLLAYGGKTARDL-----------YGFRFAPERALpLVAINLTHGTGSEVDRFAVATIPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 616 TGQKYPLADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPASYHEgSK 695
Cdd:cd08186 151 KGYKPGIAYDCIYPLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAIRLIAEYLPRALAN-PK 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 503995744 696 NPVARERVHSAATIAGIAFANAFLGVCHSMAHKL-GSQFHIPHGLANALLISNVIRY 751
Cdd:cd08186 230 DLEARYWLLYASMIAGIAIDNGLLHLTHALEHPLsGLKPELPHGLGLALLGPAVVKY 286
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
455-862 |
1.15e-41 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341486 [Multi-domain] Cd Length: 376 Bit Score: 157.08 E-value: 1.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 455 KLPKSIYFRRGSLPIALDEVITDGhKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANS 534
Cdd:cd14864 2 KIPPNIVFGADSLERIGEEVKEYG-SRFLLITDPVLKESGLADKIVSSLEKAGISVIVFDEIPASATSDTIDEAAELARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 535 FKPDVIIALGGGSPMDAAKIMWVMYEhpETHFeelALRFMDIRKriykfpkmgVKAK---MVAITTTSGTGSEVTPFAVV 611
Cdd:cd14864 81 AGADGIIAVGGGKVLDTAKAVAILAN--NDGG---AYDFLEGAK---------PKKKplpLIAVPTTPRSGFEFSDRFPV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 612 TDDATGQKYPLADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPaSYH 691
Cdd:cd14864 147 VDSRSREVKLLKAQPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNFFSDALALKAIELVSENLD-GAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 692 EGSKNPVARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNAndnptkqtafsqydrPQA 771
Cdd:cd14864 226 ADPKNTPAEELLAQAGCLAGLAASSSSPGLATALALAVNSRYKVSKSLVASILLPHVIEYAA---------------TSA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 772 RRRYAEIADHLGLTAPGDRTAAKIEKLLGWLDEIKAELGIPKSIREAGVQeadflAHVDKLSEDAFDDQCTGANPRYPLI 851
Cdd:cd14864 291 PDKYAKIARALGEDVEGASPEEAAIAAVEGVRRLIAQLNLPTRLKDLDLA-----SSLEQLAAIAEDAPKLNGLPRSMSS 365
|
410
....*....|.
gi 503995744 852 AELKQILLDTF 862
Cdd:cd14864 366 DDIFDILKAAF 376
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
480-824 |
2.55e-36 |
|
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes the reduction of succinic simialdehyde to 4-hydroxybutyrate in the succinic degradation pathway; 4-hydroxybutyrate dehydrogenase (4HBD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the succinate metabolism biochemical pathway. It catalyzes the reduction of succinic simialdehide to 4-hydroxybutyrate in the succinate degradation pathway This succinate degradation pathway is present in some bacteria which can use succinate as sole carbon source.
Pssm-ID: 341482 Cd Length: 371 Bit Score: 141.20 E-value: 2.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 480 KRALIVTDRFLFNNGYADQitsVLKAAGVETEVFFEVEadPTLTIVRKGAELANSFKPDVIIALGGGSPMDAAKIMWVMY 559
Cdd:cd14860 27 KDDLVLTNEYIYEPYFEPL---NLDCAVIFQEKYGTGE--PSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAKLLALKG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 560 EHPethFEELALRFMDIRKriykfpkmgvKAKMVAITTTSGTGSEVTPFAVVTDDATGQKYPLADYALTPDMAIVDANLV 639
Cdd:cd14860 102 ISP---VLDLFDGKIPLIK----------EKELIIVPTTCGTGSEVTNISIVELTSLGTKKGLAVDELYADKAVLIPELL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 640 MEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLP--ASYHEGSKNPVARERVhSAATIAGIAFANA 717
Cdd:cd14860 169 KGLPYKVFATSSIDALIHAIESYLSPKATPYTEMFSYKAIEMILEGYQeiAEKGEEARFPLLGDFL-IASNYAGIAFGNA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 718 FLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNANDNPT----KQTAFsqydrpqarrryaeIADHLGLTApgDRTAA 793
Cdd:cd14860 248 GCAAVHALSYPLGGKYHVPHGEANYAVFTGVLKNYQEKNPDgeikKLNEF--------------LAKILGCDE--EDVYD 311
|
330 340 350
....*....|....*....|....*....|..
gi 503995744 794 KIEKLLGWLdeikaelgIP-KSIREAGVQEAD 824
Cdd:cd14860 312 ELEELLNKI--------LPkKPLHEYGMKEEE 335
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
457-847 |
5.46e-30 |
|
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic microbes; Maleylacetate reductase (MAR) plays an important role in the degradation of aromatic compounds in aerobic microbes. In fungi and yeasts, the enzyme is involved in the catabolism of compounds such as phenol, tyrosine, benzoate, 4-hydroxybenzoate and resorcinol. In bacteria, the enzyme contributes to the degradation of resorcinol, 2,4-dihydroxybenzoate ([beta]-resorcylate) and 2,6-dihydroxybenzoate ([gamma]-resorcylate) via hydroxyquinol and maleylacetate. Maleylacetate reductase catalyzes NADH- or NADPH-dependent reduction, at the carbon-carbon double bond, of maleylacetate or 2-chloromaleylacetate to 3-oxoadipate. In the case of 2-chloromaleylacetate, MAR initially catalyzes the NAD(P)H-dependent dechlorination to maleylacetate, which is then reduced to 3-oxoadipate. This enzyme is a homodimer and is inhibited by thiol-blocking reagents such as p-chloromercuribenzoate and Hg++, indicating that the cysteine residue is probably necessary for the catalytic activity of maleylacetate reductase.
Pssm-ID: 341456 [Multi-domain] Cd Length: 337 Bit Score: 121.84 E-value: 5.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 457 PKSIYFRRGSLPIALDEVITDGHKRALIVTDRFlfNNGYADQITSVLKAAGVEteVFFEVEADPTLTIVRKGAELANSFK 536
Cdd:cd08177 1 PQRVVFGAGTLAELAEELERLGARRALVLSTPR--QRALAERVAALLGDRVAG--VFDGAVMHVPVEVAERALAAAREAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 537 PDVIIALGGGSPMDAAKImwvmyehpethfeeLALRfmdirkriykfpkmgVKAKMVAITTTSgTGSEVTPFAVVTDDat 616
Cdd:cd08177 77 ADGLVAIGGGSAIGLAKA--------------IALR---------------TGLPIVAVPTTY-AGSEMTPIWGETED-- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 617 GQKYPLADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLPASYHEGSkN 696
Cdd:cd08177 125 GVKTTGRDPRVLPRTVIYDPDLTLGLPAALSVASGLNALAHAVEALYAPDANPITSLLAEEGIRALARALPRLVADPS-D 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 697 PVARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNAndnptkqtafsqydrPQARRRYA 776
Cdd:cd08177 204 LEARSDALYGAWLAGVVLGSVGMGLHHKLCHVLGGTFDLPHAETHAVVLPHVLAYNA---------------PAAPDAMA 268
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503995744 777 EIADHLGLTAPGDRtaakiekllgwLDEIKAELGIPKSIREAGVQEADflahVDKLSEDAFDDQctGANPR 847
Cdd:cd08177 269 RLARALGGGDAAGG-----------LYDLARRLGAPTSLRDLGMPEDD----IDRAADLALANP--YPNPR 322
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
457-766 |
3.58e-26 |
|
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); This superfamily consists of two subgroups: the dehydroquinate synthase (DHQS)-like, and a large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. Dehydroquinate synthase-like group includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. The alcohol dehydrogenases (ADHs) in this superfamily contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases; insect-type, or short-chain alcohol dehydrogenases; iron-containing alcohol dehydrogenases, and others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341447 [Multi-domain] Cd Length: 271 Bit Score: 108.99 E-value: 3.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 457 PKSIYFRRGSLPiALDEVITDGHKRALIVTDRFLfNNGYADQITSVLKAaGVETEVFFEVEADPTLTIVRKGAELANSFK 536
Cdd:cd07766 1 PTRIVFGEGAIA-KLGEIKRRGFDRALVVSDEGV-VKGVGEKVADSLKK-GLAVAIFDFVGENPTFEEVKNAVERARAAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 537 PDVIIALGGGSPMDAAKIMWVMyehpethfeelalrfmdirkriykfpkMGVKAKMVAITTTSGTGSEVTPFAVVTDDAT 616
Cdd:cd07766 78 ADAVIAVGGGSTLDTAKAVAAL---------------------------LNRGIPFIIVPTTASTDSEVSPKSVITDKGG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 617 GQKYplADYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEayvsvlasefsdgqalqalkllkenlpasyhegskn 696
Cdd:cd07766 131 KNKQ--VGPHYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVE------------------------------------ 172
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503995744 697 pvaRERVHSAATIAGIAFANA-FLGVCHSMAHKLGSQFHIPHGLANALLISNVIRYNANDNPTKQTAFSQY 766
Cdd:cd07766 173 ---LEKVVEAATLAGMGLFESpGLGLAHAIGHALTAFEGIPHGEAVAVGLPYVLKVANDMNPEPEAAIEAV 240
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
462-741 |
2.13e-24 |
|
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N biosynthesis; This family contains iron-containing alcohol dehydrogenase-like proteins, many of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the iron-containing alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron or zinc ions. This family also includes Shewanella oneidensis KdnB which is required for biosynthesis of 8-Amino-3,8-dideoxy-D-manno-octulosonic acid (Kdo8N), a unique amino sugar that has thus far only been observed on the lipopolysaccharides of marine bacteria belonging to the genus Shewanella, and thought to be important for the integrity of the bacterial cell outer membrane. KdnB requires NAD(P) and zinc ion for activity.
Pssm-ID: 341463 [Multi-domain] Cd Length: 348 Bit Score: 105.43 E-value: 2.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 462 FRRGS---LPIALDEVITDGHKRALIVTDRFLFNNGYADQitsvLKAAGVETEVFFEVEADPTLTIV---RKGAELANSF 535
Cdd:cd08184 6 FGRGSfdqLGELLAERRKSNNDYVVFFIDDVFKGKPLLDR----LPLQNGDLLIFVDTTDEPKTDQIdalRAQIRAENDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 536 KPDVIIALGGGSPMDAAKIMWVMYEHPE--THFEELALrfmdIRKR-IYKfpkmgvkakmVAITTTSGTGSEVTPFAVVT 612
Cdd:cd08184 82 LPAAVVGIGGGSTMDIAKAVSNMLTNPGsaADYQGWDL----VKNPgIYK----------IGVPTLSGTGAEASRTAVLT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 613 DdaTGQKYPL-ADYALtPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDGQALQALKLLKENLpasYH 691
Cdd:cd08184 148 G--PEKKLGInSDYTV-FDQVILDPELIATVPRDQYFYTGMDCYIHCVESLNGTYRNAFGDAYAEKALELCRDVF---LS 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 503995744 692 EGSKNPVARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLAN 741
Cdd:cd08184 222 DDMMSPENREKLMVASYLGGSSIANSQVGVCHALSYGLSVVLGTHHGVAN 271
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
10-404 |
2.87e-15 |
|
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: 79.17 E-value: 2.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 10 NALVERVKKAQREYASFTQEQVDKIFRAAALAAADARIPLAKMAVAESGMGIVE-----DKVIKN-HFASEYIYNAYKDE 83
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEalgevARAADTfRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 84 KtcgvLSEDDTFGTITIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAaiaaGAP 163
Cdd:cd07078 81 I----PSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEA----GLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 164 KDLIGWIDQPSVELSNALMHHPDINLILATGGPG----MVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKT 239
Cdd:cd07078 153 PGVLNVVTGDGDEVGAALASHPRVDKISFTGSTAvgkaIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 240 FDNGVICASEQSVVVVDSVYDAVRERFsshggyllqgqeLKAVQNIILKNGALNA----AIVGQPAYK-------IAELA 308
Cdd:cd07078 233 GNAGQVCTAASRLLVHESIYDEFVERL------------VERVKALKVGNPLDPDtdmgPLISAAQLDrvlayieDAKAE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 309 GFTVPVSTKILIGE---------VTDVDESEPFAHEKL-SPTLAMYRAKNFEDAVDKAEKLVAmggiGHTSCLYTdqdNQ 378
Cdd:cd07078 301 GAKLLCGGKRLEGGkgyfvpptvLTDVDPDMPIAQEEIfGPVLPVIPFKDEEEAIELANDTEY----GLAAGVFT---RD 373
|
410 420
....*....|....*....|....*.
gi 503995744 379 PERVAYFGQLMKTARILINTPASQGG 404
Cdd:cd07078 374 LERALRVAERLEAGTVWINDYSVGAE 399
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
5-399 |
9.34e-13 |
|
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: 71.41 E-value: 9.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 5 NVAELNALVERVKKAQREYASFTQEQVDKIFRAAALAAADARIPLAKMAVAESGMGIVE-----DKVIknHFASEYIYNA 79
Cdd:pfam00171 27 TAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEargevDRAI--DVLRYYAGLA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 80 YKDEKTcgVLSEDDTFGTITIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRakdaTNKAADIVLQAAIA 159
Cdd:pfam00171 105 RRLDGE--TLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSEL----TPLTALLLAELFEE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 160 AGAPKDLIGWIDQPSVELSNALMHHPDINLILATGGPG----MVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVL 235
Cdd:pfam00171 179 AGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAvgrhIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 236 MSKTFDNGVICASEQSVVVVDSVYDAVRERFsshggyllqgqeLKAVQNIILKNGALNAAIVG----QPAYK-------- 303
Cdd:pfam00171 259 FGAFGNAGQVCTATSRLLVHESIYDEFVEKL------------VEAAKKLKVGDPLDPDTDMGplisKAQLErvlkyved 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 304 -IAELAgftvpvstKILIGE--------------VTDVDESEPFAHEKL-SPTLAMYRAKNFEDAVDKAEKLVAmggiGH 367
Cdd:pfam00171 327 aKEEGA--------KLLTGGeagldngyfveptvLANVTPDMRIAQEEIfGPVLSVIRFKDEEEAIEIANDTEY----GL 394
|
410 420 430
....*....|....*....|....*....|..
gi 503995744 368 TSCLYTdqdNQPERVAYFGQLMKTARILINTP 399
Cdd:pfam00171 395 AAGVFT---SDLERALRVARRLEAGMVWINDY 423
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
6-246 |
9.79e-13 |
|
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: 71.53 E-value: 9.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 6 VAELNALVERVKKAQREYASFTQEQVDKIFRAAALAAADARIPLAKMAVAESGMgIVEDKVIKNHFASEYI-Y---NAYK 81
Cdd:cd07088 34 AEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGK-TLSLARVEVEFTADYIdYmaeWARR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 82 DEKTcgVLSEDDTFGTITIA-EPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHprakDATNKAADIVLQAAIAA 160
Cdd:cd07088 113 IEGE--IIPSDRPNENIFIFkVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPS----EETPLNALEFAELVDEA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 161 GAPKDLIGWIDQPSVELSNALMHHPDINLILATGGPG-----MVKAAYSSGKPAIGVGaGNTPVVIDETADIKRAVASVL 235
Cdd:cd07088 187 GLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEagqkiMEAAAENITKVSLELG-GKAPAIVMKDADLDLAVKAIV 265
|
250
....*....|.
gi 503995744 236 MSKTFDNGVIC 246
Cdd:cd07088 266 DSRIINCGQVC 276
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
493-834 |
2.05e-12 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 69.82 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 493 NGYADQITSVLKaaGVETEVFFEVEADPTLTIVRKGAELANSFKPDVIIALGGGSPMDAAKIMWVMYEHPETH--FEELA 570
Cdd:PRK15138 44 TGVLDQVLDALK--GMDVLEFGGIEPNPTYETLMKAVKLVREEKITFLLAVGGGSVLDGTKFIAAAANYPENIdpWHILE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 571 LRFMDIRKRIykfpkmgvkaKMVAITTTSGTGSEVTPFAVVTDDATGQKYPLADYALTPDMAIVDANLVMEMPKSLCAFG 650
Cdd:PRK15138 122 TGGKEIKSAI----------PMGSVLTLPATGSESNAGAVISRKTTGDKQAFHSPHVQPVFAVLDPVYTYTLPPRQVANG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 651 GLDAVTHALEAYVSV-----LASEFSDGQALQAL----KLLKEnlPASYHegsknpvARERVHSAATIAGIAFANAflGV 721
Cdd:PRK15138 192 VVDAFVHTVEQYVTYpvdakIQDRFAEGILLTLIeegpKALKE--PENYD-------VRANVMWAATQALNGLIGA--GV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 722 CHSMA-HKLGSQFHIPHGLANALLISNVIrynandnptkqTAFSQYDRPQARRRYAEIADHL-GLTAPGD--RTAAKIEK 797
Cdd:PRK15138 261 PQDWAtHMLGHELTAMHGLDHAQTLAIVL-----------PALWNEKRDTKRAKLLQYAERVwNITEGSDdeRIDAAIAA 329
|
330 340 350
....*....|....*....|....*....|....*..
gi 503995744 798 LLGWLDeikaELGIPKSIREAGVQEADFLAHVDKLSE 834
Cdd:PRK15138 330 TRNFFE----QMGVPTRLSDYGLDGSSIPALLKKLEE 362
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
49-232 |
8.58e-12 |
|
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: 68.15 E-value: 8.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 49 LAKMAVAESGMGIVEDKVIKNHFASEYIYNAYKDEKTCG-VLSEDDTFG-----TITIAEPIGIICGIVPTTNPTSTAIF 122
Cdd:cd07146 60 FARLITLESGLCLKDTRYEVGRAADVLRFAAAEALRDDGeSFSCDLTANgkarkIFTLREPLGVVLAITPFNHPLNQVAH 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 123 KSLISLKTRNAIIFSPHPRAKDATNKAADIVLQaaiaAGAPKDLIGWIDQPSVELSNALMHHPDINLILATGGPGMVK-- 200
Cdd:cd07146 140 KIAPAIAANNRIVLKPSEKTPLSAIYLADLLYE----AGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKai 215
|
170 180 190
....*....|....*....|....*....|..
gi 503995744 201 AAYSSGKPAIGVGAGNTPVVIDETADIKRAVA 232
Cdd:cd07146 216 AATAGYKRQLLELGGNDPLIVMDDADLERAAT 247
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
98-248 |
3.86e-11 |
|
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: 66.22 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 98 ITIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAAIAAGAPKDLIGWidqpSVEL 177
Cdd:cd07145 118 FTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAGLPPGVINVVTGY----GSEV 193
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503995744 178 SNALMHHPDINLILATG----GPGMVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKtFDN-GVICAS 248
Cdd:cd07145 194 GDEIVTNPKVNMISFTGstavGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGR-FENaGQVCNA 268
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
7-250 |
4.90e-11 |
|
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: 65.92 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 7 AELNALVERVKKAQREYASFTQEQVDKIFRAAALAAADARIPLAKMAVAESGMGIVEDKV--------IKNhfASEYIYN 78
Cdd:cd07094 21 ADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVevdraidtLRL--AAEEAER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 79 AYKDEKTCGVLSEDDTFGTITIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQaai 158
Cdd:cd07094 99 IRGEEIPLDATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILVE--- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 159 aAGAPKDLIGWIDQPSVELSNALMHHPDINLILATGGPGM---VKAAYSSGKPAIGVGaGNTPVVIDETADIKRAVASVL 235
Cdd:cd07094 176 -AGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVgeaLRANAGGKRIALELG-GNAPVIVDRDADLDAAIEALA 253
|
250
....*....|....*
gi 503995744 236 MSKTFDNGVICASEQ 250
Cdd:cd07094 254 KGGFYHAGQVCISVQ 268
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
453-738 |
5.96e-11 |
|
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and conversion]; Glycerol dehydrogenase or related enzyme, iron-containing ADH family is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440140 [Multi-domain] Cd Length: 355 Bit Score: 65.19 E-value: 5.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 453 WHKLPKSIYFRRGSLPiALDEVITDGHKRALIVTDRFLFNNgYADQITSVLKAAGVETEvFFEVEADPTLTIVRKGAELA 532
Cdd:COG0371 2 VIILPRRYVQGEGALD-ELGEYLADLGKRALIITGPTALKA-AGDRLEESLEDAGIEVE-VEVFGGECSEEEIERLAEEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 533 NSFKPDVIIALGGGSPMDAAKimwvmyehpethfeelALRFMdirkriykfpkmgVKAKMVAITTTSGTGSEVTPFAVVT 612
Cdd:COG0371 79 KEQGADVIIGVGGGKALDTAK----------------AVAYR-------------LGLPVVSVPTIASTDAPASPLSVIY 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 613 DDATGQKYPLAdYALTPDMAIVDANLVMEMPKSLCAFGGLDAVTHALEAYVSVLASEFSDG---------QALQALKLLK 683
Cdd:COG0371 130 TEDGAFDGYSF-LAKNPDLVLVDTDIIAKAPVRLLAAGIGDALAKWYEARDWSLAHRDLAGeyyteaavaLARLCAETLL 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503995744 684 ENLPASYHEGSKNPV--ARERVHSAATI-AGIAFANAF----LGVCHSMAH---KLGSQFHIPHG 738
Cdd:COG0371 209 EYGEAAIKAVEAGVVtpALERVVEANLLlSGLAMGIGSsrpgSGAAHAIHNgltALPETHHALHG 273
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
102-246 |
2.17e-10 |
|
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: 63.86 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 102 EPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVlqaaIAAGAPKDLIGWIdQPSVELSNAL 181
Cdd:cd07090 115 EPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEIL----TEAGLPDGVFNVV-QGGGETGQLL 189
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503995744 182 MHHPDINLILATG----GPGMVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKTFDNGVIC 246
Cdd:cd07090 190 CEHPDVAKVSFTGsvptGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVC 258
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
99-250 |
4.17e-09 |
|
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: 59.92 E-value: 4.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 99 TIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAaiaaGAPKDLIGWIDQPSVELS 178
Cdd:cd07149 119 TIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEA----GLPKGALNVVTGSGETVG 194
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503995744 179 NALMHHPDINLILATGGPGMVKA-AYSSG--KPAIGVGaGNTPVVIDETADIKRAVASVLMSKTFDNGVICASEQ 250
Cdd:cd07149 195 DALVTDPRVRMISFTGSPAVGEAiARKAGlkKVTLELG-SNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQ 268
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
97-356 |
3.58e-08 |
|
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: 57.06 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 97 TITIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRakdaTNKAADIVLQAAIAAGAPKDLIGWIDQPSVE 176
Cdd:COG1012 135 AYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQ----TPLSALLLAELLEEAGLPAGVLNVVTGDGSE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 177 LSNALMHHPDINLILATGGPG----MVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKTFDNGVICAS---- 248
Cdd:COG1012 211 VGAALVAHPDVDKISFTGSTAvgrrIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAasrl 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 249 -------EQsvvvvdsvydaVRERFsshggyllqgqeLKAVQNIILKNGALNAAIVG----QPAY-KIAEL------AGF 310
Cdd:COG1012 291 lvhesiyDE-----------FVERL------------VAAAKALKVGDPLDPGTDMGplisEAQLeRVLAYiedavaEGA 347
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503995744 311 TVPVSTKILIGE---------VTDVDES------EPFAheklsPTLAMYRAKNFEDAVDKA 356
Cdd:COG1012 348 ELLTGGRRPDGEggyfveptvLADVTPDmriareEIFG-----PVLSVIPFDDEEEAIALA 403
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
128-239 |
8.48e-08 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 55.46 E-value: 8.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 128 LKTRNAIIFsphpRA-KDA--TNKA-ADIVLQAAIAAGAPKDLIGWIDQPSVELSNALMHHPD-INLILATGGPGMVKAA 202
Cdd:PRK00197 138 LKSGNAVIL----RGgSEAihSNRAlVAVIQEALEEAGLPADAVQLVETTDRAAVGELLKLDGyVDVIIPRGGAGLIRRV 213
|
90 100 110
....*....|....*....|....*....|....*...
gi 503995744 203 YSSGK-PAIGVGAGNTPVVIDETADIKRAVASVLMSKT 239
Cdd:PRK00197 214 VENATvPVIEHGDGICHIYVDESADLDKALKIVLNAKT 251
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
99-237 |
1.05e-07 |
|
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: 55.43 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 99 TIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPhprAKDaTNKAADIVLQAAIAAGAPKDLIGWIDQPSVELS 178
Cdd:cd07131 131 TRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKP---AED-TPACALKLVELFAEAGLPPGVVNVVHGRGEEVG 206
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503995744 179 NALMHHPDINLILATG----GPGMVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMS 237
Cdd:cd07131 207 EALVEHPDVDVVSFTGstevGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWS 269
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
98-237 |
1.20e-07 |
|
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: 55.26 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 98 ITIAEPIGIiCGIVPTTN-PTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAAIAAGAPKDLIGWIdQPSVE 176
Cdd:cd07086 128 MEQWNPLGV-VGVITAFNfPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPGVVNLV-TGGGD 205
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503995744 177 LSNALMHHPDINLILATGGPGM-----VKAAYSSGKPAIGVGaGNTPVVIDETADIKRAVASVLMS 237
Cdd:cd07086 206 GGELLVHDPRVPLVSFTGSTEVgrrvgETVARRFGRVLLELG-GNNAIIVMDDADLDLAVRAVLFA 270
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
2-356 |
1.96e-07 |
|
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: 54.64 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 2 AVTNVAELNALVERVKKAQREYASFTQEQVDKIFRAAALAAADARIPLAKMAVAESGmGIVEDKVIKNHFASEYIYNA-- 79
Cdd:cd07150 16 AVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGG-STYGKAWFETTFTPELLRAAag 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 80 ----YKDEktcgVLSEDDTfGTI--TIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIV 153
Cdd:cd07150 95 ecrrVRGE----TLPSDSP-GTVsmSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 154 LQAaiaaGAPKDLIGWIDQPSVELSNALMHHPDINLILATG----GPGM-VKAAYSSGKPAIGVGaGNTPVVIDETADIK 228
Cdd:cd07150 170 EEA----GLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGstavGREIaEKAGRHLKKITLELG-GKNPLIVLADADLD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 229 RAVASVLMSKTFDNGVICASEQSVVVVDSVYDAVRERFSSHGGYLLQGQELKAvQNII--LKNGALNAAIVGQPAYKIAE 306
Cdd:cd07150 245 YAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDP-DTVIgpLISPRQVERIKRQVEDAVAK 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503995744 307 LAgftvpvstKILIGE-----------VTDVDES-EPFAHEKLSPTLAMYRAKNFEDAVDKA 356
Cdd:cd07150 324 GA--------KLLTGGkydgnfyqptvLTDVTPDmRIFREETFGPVTSVIPAKDAEEALELA 377
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
88-268 |
3.62e-07 |
|
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: 53.60 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 88 VLSEDDTFGTITIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAAIAAGAPKDLI 167
Cdd:cd07115 102 VIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAGFPAGVLNVVT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 168 GwidqPSVELSNALMHHPDINLILATGGPG-----MVKAAYSSGKPAIGVGaGNTPVVIDETADIKRAVASVLMSKTFDN 242
Cdd:cd07115 182 G----FGEVAGAALVEHPDVDKITFTGSTAvgrkiMQGAAGNLKRVSLELG-GKSANIVFADADLDAAVRAAATGIFYNQ 256
|
170 180
....*....|....*....|....*.
gi 503995744 243 GVICASEQSVVVVDSVYDAVRERFSS 268
Cdd:cd07115 257 GQMCTAGSRLLVHESIYDEFLERFTS 282
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
103-246 |
7.10e-07 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 52.43 E-value: 7.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 103 PIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPhprAKDATNKA---ADIVLQAaiaaGAPKDLIGWIDQPSVELSN 179
Cdd:PRK10090 71 ALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKP---SEFTPNNAiafAKIVDEI----GLPKGVFNLVLGRGETVGQ 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503995744 180 ALMHHPDINLILATGGPG-----MVKAAYSSGKPAIGVGaGNTPVVIDETADIKRAVASVLMSKTFDNGVIC 246
Cdd:PRK10090 144 ELAGNPKVAMVSMTGSVSagekiMAAAAKNITKVCLELG-GKAPAIVMDDADLDLAVKAIVDSRVINSGQVC 214
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
2-247 |
1.36e-06 |
|
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: 51.76 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 2 AVTNVAELNALVERVKKAQREYASFTQEQVDKIFRAAALAAADARIPLAKMAVAESG------MGIVEDKV-IKNHFASe 74
Cdd:cd07106 14 PVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGkplaeaQFEVGGAVaWLRYTAS- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 75 yiyNAYKDEktcgVLSEDDTFGTITIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIvL 154
Cdd:cd07106 93 ---LDLPDE----VIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGEL-A 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 155 QAAIAAGAPKDLIGwidqpSVELSNALMHHPDINLILATG----GPGMVKAAYSSGKPA---IGvgaGNTPVVIDETADI 227
Cdd:cd07106 165 QEVLPPGVLNVVSG-----GDELGPALTSHPDIRKISFTGstatGKKVMASAAKTLKRVtleLG---GNDAAIVLPDVDI 236
|
250 260
....*....|....*....|
gi 503995744 228 KRAVASVLMSKTFDNGVICA 247
Cdd:cd07106 237 DAVAPKLFWGAFINSGQVCA 256
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
480-654 |
1.70e-06 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site. Some subfamilies have yet to be characterized.
Pssm-ID: 341480 [Multi-domain] Cd Length: 347 Bit Score: 51.00 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 480 KRALIVTDrflfNNGYA---DQITSVLKAAGVETEVFFeVEADPTLTIVRKGAELANSFKPDVIIALGGGSPMDAAKImw 556
Cdd:cd08550 23 KKALIIGG----KTALEavgEKLEKSLEEAGIDYEVEV-FGGECTEENIERLAEKAKEEGADVIIGIGGGKVLDTAKA-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 557 vmyehpethfeeLALRfmdirkriykfpkMGVkaKMVAITTTSGTGSEVTPFAVVTDDAtGQKYPLADYALTPDMAIVDA 636
Cdd:cd08550 96 ------------VADR-------------LGL--PVVTVPTIAATCAAWSALSVLYDEE-GEFLGYSLLKRSPDLVLVDT 147
|
170
....*....|....*...
gi 503995744 637 NLVMEMPKSLCAFGGLDA 654
Cdd:cd08550 148 DIIAAAPVRYLAAGIGDT 165
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
456-555 |
2.22e-06 |
|
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme; Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH, EC 1.1.1.261) plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. It catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme. The activity is zinc-dependent. One characteristic feature of archaea is that their cellular membrane has an ether linkage between the glycerol backbone and the hydrocarbon residues. The polar lipids of the members of Archaea consist of di- and tetra-ethers of glycerol with isoprenoid alcohols bound at the sn-2 and sn-3 positions of the glycerol moiety. The archaeal polar lipids have the enantiomeric configuration of a glycerophosphate backbone [sn-glycerol-1-phosphate (G-1-P)] that is the mirror image structure of the bacterial or eukaryal counterpart [sn-glycerol- 3-phosphate (G-3-P)]. The absolute stereochemistry of the glycerol moiety in all archaeal polar lipids is opposite to that of glycerol ester lipids in bacteria and eukarya.
Pssm-ID: 341452 Cd Length: 343 Bit Score: 50.63 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 456 LPKSIYFRRGSLPIaLDEVITDGH--KRALIVTDRFLFNNgYADQITSVLKAAGVETEV--FFEVEADPTLTIVRKgaeL 531
Cdd:cd08173 1 LPRNVVVGHGAINK-IGEVLKKLLlgKRALIITGPNTYKI-AGKRVEDLLESSGVEVVIvdIATIEEAAEVEKVKK---L 75
|
90 100
....*....|....*....|....
gi 503995744 532 ANSFKPDVIIALGGGSPMDAAKIM 555
Cdd:cd08173 76 IKESKADFIIGVGGGKVIDVAKYA 99
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
480-553 |
2.44e-06 |
|
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in glycerol dissmilation; Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341449 [Multi-domain] Cd Length: 351 Bit Score: 50.49 E-value: 2.44e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503995744 480 KRALIVTDRFLFNNgYADQITSVLKAAGVE-TEVFFEVEADPTlTIVRKgAELANSFKPDVIIALGGGSPMDAAK 553
Cdd:cd08170 23 KKALVIADPFVLDL-VGERLEESLEKAGLEvVFEVFGGECSRE-EIERL-AAIARANGADVVIGIGGGKTIDTAK 94
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
99-246 |
4.91e-06 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 50.26 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 99 TIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVlqaaIAAGAPKDLIGWIdQPSVELS 178
Cdd:PRK13252 138 TRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIY----TEAGLPDGVFNVV-QGDGRVG 212
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503995744 179 NALMHHPDINLILATGGPGMVK----AAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKTFDNGVIC 246
Cdd:PRK13252 213 AWLTEHPDIAKVSFTGGVPTGKkvmaAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVC 284
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
99-248 |
1.13e-05 |
|
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: 48.98 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 99 TIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAAIAAGAPKDLIGwidqpSVELS 178
Cdd:cd07113 138 TRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNG-----KGAVG 212
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503995744 179 NALMHHPDINLILATG----GPGMVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKTFDNGVICAS 248
Cdd:cd07113 213 AQLISHPDVAKVSFTGsvatGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAA 286
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
106-250 |
1.42e-05 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 48.63 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 106 IICGIVPTTNpTSTAIFKSLIslkTRNAIIFSPHPRAkdatnkaadiVLQAAI----------AAGAPKDLIGWI-DQPS 174
Cdd:cd07127 200 IGCSTFPTWN-GYPGLFASLA---TGNPVIVKPHPAA----------ILPLAItvqvarevlaEAGFDPNLVTLAaDTPE 265
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503995744 175 VELSNALMHHPDINLILATGGP--GMVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKTFDNGVICASEQ 250
Cdd:cd07127 266 EPIAQTLATRPEVRIIDFTGSNafGDWLEANARQAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQ 343
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
92-240 |
1.66e-05 |
|
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: 48.51 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 92 DDTFgTITIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIvLQAAIAAGAPKDLIGWID 171
Cdd:cd07108 107 PDVL-TYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEI-LAQVLPAGVLNVITGYGE 184
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503995744 172 qpsvELSNALMHHPDINLILATGGPGMVKAAY-SSGKPAIGVG---AGNTPVVIDETADIKRAVASVLMSKTF 240
Cdd:cd07108 185 ----ECGAALVDHPDVDKVTFTGSTEVGKIIYrAAADRLIPVSlelGGKSPMIVFPDADLDDAVDGAIAGMRF 253
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
132-364 |
2.17e-05 |
|
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: 48.04 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 132 NAIIFSPHPRakdaTNKAADIVLQAAIAAGAPKDLIGWIdQPSVELSNALMHHPDINLILATGGP--GMVKAAYSSGKP- 208
Cdd:cd07095 126 NTVVFKPSEL----TPAVAELMVELWEEAGLPPGVLNLV-QGGRETGEALAAHEGIDGLLFTGSAatGLLLHRQFAGRPg 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 209 ---AIGVGaGNTPVVIDETADIKRAVASVLMSktfdngvicaseqsvvvvdsvydavrerfsshgGYLLQGQELKAVQNI 285
Cdd:cd07095 201 kilALEMG-GNNPLVVWDVADIDAAAYLIVQS---------------------------------AFLTAGQRCTCARRL 246
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503995744 286 ILKNGALNAAIVGQpaykIAELAGftvpvstKILIGevtDVDESEPFahekLSPTLAMYRAknfEDAVDKAEKLVAMGG 364
Cdd:cd07095 247 IVPDGAVGDAFLER----LVEAAK-------RLRIG---APDAEPPF----MGPLIIAAAA---ARYLLAQQDLLALGG 304
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
71-248 |
2.74e-05 |
|
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: 47.49 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 71 FASEYIYNAYKDEKTCG-VLSEDDTFGTITIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPhpraKDATNKA 149
Cdd:cd07142 108 AARLFRYYAGWADKIHGmTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKP----AEQTPLS 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 150 ADIVLQAAIAAGAPKDLIGWIDQPSVELSNALMHHPDINLILATGGPG-----MVKAAYSSGKPAIGVGAGNTPVVIDET 224
Cdd:cd07142 184 ALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEvgkiiMQLAAKSNLKPVTLELGGKSPFIVCED 263
|
170 180
....*....|....*....|....
gi 503995744 225 ADIKRAVASVLMSKTFDNGVICAS 248
Cdd:cd07142 264 ADVDKAVELAHFALFFNQGQCCCA 287
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
99-246 |
3.44e-05 |
|
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: 47.24 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 99 TIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVlqaaIAAGAPKDLIGWIDQPSVELS 178
Cdd:cd07097 131 TTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEIL----EEAGLPAGVFNLVMGSGSEVG 206
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503995744 179 NALMHHPDINLILATGGPGMVKAAYSSgkpAIGVGA-------GNTPVVIDETADIKRAVASVLMSKTFDNGVIC 246
Cdd:cd07097 207 QALVEHPDVDAVSFTGSTAVGRRIAAA---AAARGArvqlemgGKNPLVVLDDADLDLAVECAVQGAFFSTGQRC 278
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
99-246 |
3.58e-05 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 47.51 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 99 TIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPhpraKDATNKAADIVLQAAIAAGAPKDLIGWIDQPSVELS 178
Cdd:PLN02766 154 TLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKP----AEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAG 229
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503995744 179 NALMHHPDINLILATGGPG-----MVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKTFDNGVIC 246
Cdd:PLN02766 230 AAIASHMDVDKVSFTGSTEvgrkiMQAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEIC 302
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
102-237 |
4.32e-05 |
|
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: 47.22 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 102 EPIGIICGIVPTTNPTstAIFKSLIS--LKTRNAIIFSPhprAKDATNKAADIVlQAAIAAGAPKDLIGWIDQPSVELSN 179
Cdd:cd07124 165 RPLGVGAVISPWNFPL--AILAGMTTaaLVTGNTVVLKP---AEDTPVIAAKLV-EILEEAGLPPGVVNFLPGPGEEVGD 238
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503995744 180 ALMHHPDINLILATG---------------GPGMVKAayssgKPAIGVGAGNTPVVIDETADIKRAVASVLMS 237
Cdd:cd07124 239 YLVEHPDVRFIAFTGsrevglriyeraakvQPGQKWL-----KRVIAEMGGKNAIIVDEDADLDEAAEGIVRS 306
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
49-248 |
4.68e-05 |
|
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: 47.06 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 49 LAKMAVAESGMGIVEDKVIKNHFASEYI-YNA---YKDEKTCGVLSEDdtFGTITIAEPIGIICGIVPTTNPTSTAIFKS 124
Cdd:cd07117 80 LAMVETLDNGKPIRETRAVDIPLAADHFrYFAgviRAEEGSANMIDED--TLSIVLREPIGVVGQIIPWNFPFLMAAWKL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 125 LISLKTRNAIIFSPhprakDATNKAADIVLQAAIAAGAPKDLIGWIDQPSVELSNALMHHPDINLILATG----GPGMVK 200
Cdd:cd07117 158 APALAAGNTVVIKP-----SSTTSLSLLELAKIIQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGstevGRDVAI 232
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503995744 201 AAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKTFDNGVICAS 248
Cdd:cd07117 233 AAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCA 280
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
102-248 |
6.19e-05 |
|
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: 46.55 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 102 EPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVlQAAIAAGAPKDLIGwiDQPSVelSNAL 181
Cdd:cd07092 117 EPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELA-AEVLPPGVVNVVCG--GGASA--GDAL 191
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503995744 182 MHHPDINLILATG----GPGMVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKTFDNGVICAS 248
Cdd:cd07092 192 VAHPRVRMVSLTGsvrtGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTA 262
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
91-269 |
6.93e-05 |
|
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: 46.19 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 91 EDDTFGTITIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAAIAAGAPKDLIGWI 170
Cdd:cd07110 108 PSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 171 DqpsvELSNALMHHPDINLILATG----GPGMVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKTFDNGVIC 246
Cdd:cd07110 188 D----EAGAPLAAHPGIDKISFTGstatGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQIC 263
|
170 180
....*....|....*....|...
gi 503995744 247 ASEQSVVVVDSVYDAVRERFSSH 269
Cdd:cd07110 264 SATSRLLVHESIADAFLERLATA 286
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
102-246 |
1.23e-04 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 45.66 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 102 EPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIvlqaAIAAGAPKDLIGWIDQPSVELSNAL 181
Cdd:PRK09847 156 EPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGL----AKEAGLPDGVLNVVTGFGHEAGQAL 231
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503995744 182 MHHPDINLILATG----GPGMVKAAYSSGKPAIGVGAG--NTPVVIDETADIKRAVASVLMSKTFDNGVIC 246
Cdd:PRK09847 232 SRHNDIDAIAFTGstrtGKQLLKDAGDSNMKRVWLEAGgkSANIVFADCPDLQQAASATAAGIFYNQGQVC 302
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
7-356 |
1.53e-04 |
|
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: 45.38 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 7 AELNALVERVKKAQREYASFTQEQVDKIFRAAALAAADARIPLAKMAVAESG----MGIVE--DKVIKnhfASEYIYNA- 79
Cdd:cd07101 18 ADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGkarrHAFEEvlDVAIV---ARYYARRAe 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 80 --YKDEKTCG---VLSEddtfgTITIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPhpraKDATNKAADIVL 154
Cdd:cd07101 95 rlLKPRRRRGaipVLTR-----TTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKP----DSQTALTALWAV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 155 QAAIAAGAPKDLIGWIDQPSVELSNALMHHPDinLILATGGP--GMVKAAySSGKPAIGVGA---GNTPVVIDETADIKR 229
Cdd:cd07101 166 ELLIEAGLPRDLWQVVTGPGSEVGGAIVDNAD--YVMFTGSTatGRVVAE-RAGRRLIGCSLelgGKNPMIVLEDADLDK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 230 AVASVLMSkTFDN-GVICASEQSVVVVDSVYDAVRERFSSHG---------------GYLLQGQELKAVQniilkngaln 293
Cdd:cd07101 243 AAAGAVRA-CFSNaGQLCVSIERIYVHESVYDEFVRRFVARTralrlgaaldygpdmGSLISQAQLDRVT---------- 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503995744 294 aAIVGQPAYKIAE-LAG----------FTVPVstkILigevTDVDES-EPFAHEKLSPTLAMYRAKNFEDAVDKA 356
Cdd:cd07101 312 -AHVDDAVAKGATvLAGgrarpdlgpyFYEPT---VL----TGVTEDmELFAEETFGPVVSIYRVADDDEAIELA 378
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
7-248 |
1.54e-04 |
|
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: 45.31 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 7 AELNALVERVKKAQREYASFTQEQVDKIFRAAALAAADARIPLAKMAVAESGMGIVEDKVIKNHFA--SEYIYNAYKDEK 84
Cdd:cd07102 18 EAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLerARYMISIAEEAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 85 TCGVLSEDDTFGTITIAEPIGIICGIVPTTNPTSTAIfKSLI-SLKTRNAIIFSPHPRakdaTNKAADIVLQAAIAAGAP 163
Cdd:cd07102 98 ADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAV-NAVIpALLAGNAVILKHSPQ----TPLCGERFAAAFAEAGLP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 164 KDLIGWIdQPSVELSNALMHHPDINLILATGG-PGMVKAAYSSGKPAIGVG---AGNTPVVIDETADIKRAVASVLMSKT 239
Cdd:cd07102 173 EGVFQVL-HLSHETSAALIADPRIDHVSFTGSvAGGRAIQRAAAGRFIKVGlelGGKDPAYVRPDADLDAAAESLVDGAF 251
|
....*....
gi 503995744 240 FDNGVICAS 248
Cdd:cd07102 252 FNSGQSCCS 260
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
478-646 |
2.08e-04 |
|
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like proteins have not been characterized. The protein sequences have high similarity with that of glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion.
Pssm-ID: 341453 [Multi-domain] Cd Length: 332 Bit Score: 44.43 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 478 GHKRALIVTDRFLfNNGYADQITSVLKAAGVETEVffEVEADPTLTIVRKgaELANSFKPDVIIALGGGSPMDAAKIMwv 557
Cdd:cd08174 24 GFGKVAIVTGEGI-DELLGEDILESLEEAGEIVTV--EENTDNSAEELAE--KAFSLPKVDAIVGIGGGKVLDVAKYA-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 558 myehpethfeelALRfmdirkriykfpkmgVKAKMVAI-TTTS--GTGSevtPFAVVTDDATGQKYPladyALTPDMAIV 634
Cdd:cd08174 97 ------------AFL---------------SKLPFISVpTSLSndGIAS---PVAVLKVDGKRKSLG----AKMPYGVIV 142
|
170
....*....|..
gi 503995744 635 DANLVMEMPKSL 646
Cdd:cd08174 143 DLDVIKSAPRRL 154
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
77-246 |
2.71e-04 |
|
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: 44.44 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 77 YNAYKDEKTCGVLSEDDTFGTITIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQa 156
Cdd:cd07143 118 YGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPE- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 157 aiaAGAPKDLIGWIDQPSVELSNALMHHPDINLILATGGPG-----MVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAV 231
Cdd:cd07143 197 ---AGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLvgrkvMEAAAKSNLKKVTLELGGKSPNIVFDDADLESAV 273
|
170
....*....|....*
gi 503995744 232 ASVLMSKTFDNGVIC 246
Cdd:cd07143 274 VWTAYGIFFNHGQVC 288
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
480-555 |
4.54e-04 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 43.65 E-value: 4.54e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503995744 480 KRALIVTDRFLFNNgYADQITSVLKAAGVE-TEVFFEVEAdpTLTIVRKGAELANSFKPDVIIALGGGSPMDAAKIM 555
Cdd:PRK09423 30 KRALVIADEFVLGI-VGDRVEASLKEAGLTvVFEVFNGEC--SDNEIDRLVAIAEENGCDVVIGIGGGKTLDTAKAV 103
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
99-246 |
4.87e-04 |
|
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: 43.76 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 99 TIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPhprAKDATNKAADIVlQAAIAAGAPKDLIGWIDQPSVELS 178
Cdd:cd07109 113 TVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKP---AEDAPLTALRLA-ELAEEAGLPAGALNVVTGLGAEAG 188
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503995744 179 NALMHHPDINLILATGGPGMVKA-AYSSGKPAIGVG---AGNTPVVIDETADIKRAVASVLMSKTFDNGVIC 246
Cdd:cd07109 189 AALVAHPGVDHISFTGSVETGIAvMRAAAENVVPVTlelGGKSPQIVFADADLEAALPVVVNAIIQNAGQTC 260
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
90-231 |
7.99e-04 |
|
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: 42.94 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 90 SEDDTFGTITIA--EPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPhprakdATNKAADIV--LQAAIAAGAPKD 165
Cdd:cd07082 126 WFPGTKGKIAQVrrEPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKP------ATQGVLLGIplAEAFHDAGFPKG 199
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503995744 166 LIGWIDQPSVELSNALMHHPDINLILATGGPG----MVKAAysSGKPAI-GVGAGNtPVVIDETADIKRAV 231
Cdd:cd07082 200 VVNVVTGRGREIGDPLVTHGRIDVISFTGSTEvgnrLKKQH--PMKRLVlELGGKD-PAIVLPDADLELAA 267
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
97-246 |
8.49e-04 |
|
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: 42.68 E-value: 8.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 97 TITIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQaaiaAGAPKDLIGWIDQPSVE 176
Cdd:cd07119 128 SRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEE----AGLPAGVVNLVTGSGAT 203
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503995744 177 LSNALMHHPDINLILATGGPG-----MVKAAYSSGKPAIGVGAGNTPVVIDEtADIKRAVASVLMSKTFDNGVIC 246
Cdd:cd07119 204 VGAELAESPDVDLVSFTGGTAtgrsiMRAAAGNVKKVALELGGKNPNIVFAD-ADFETAVDQALNGVFFNAGQVC 277
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
102-235 |
9.46e-04 |
|
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: 42.54 E-value: 9.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 102 EPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAAIAAGAPKDLIGWidqpSVELSNAL 181
Cdd:cd07114 118 EPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGF----GPETGEAL 193
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 503995744 182 MHHPDINLILATGGP----GMVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVL 235
Cdd:cd07114 194 VEHPLVAKIAFTGGTetgrHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVV 251
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
100-246 |
1.03e-03 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 42.71 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 100 IAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAAiaagaPKDLIGWIdQPSVELSN 179
Cdd:PTZ00381 106 IPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYL-----DPSYVRVI-EGGVEVTT 179
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503995744 180 ALMHHPdINLILATGGP--GMV--KAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKTFDNGVIC 246
Cdd:PTZ00381 180 ELLKEP-FDHIFFTGSPrvGKLvmQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTC 249
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
92-248 |
1.20e-03 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 42.41 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 92 DDTFGTITIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAAIAAGAPKDLIGWID 171
Cdd:PLN02467 140 METFKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGT 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 172 QPSVELSNalmhHPDINLILATG----GPGMVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKTFDNGVICA 247
Cdd:PLN02467 220 EAGAPLAS----HPGVDKIAFTGstatGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICS 295
|
.
gi 503995744 248 S 248
Cdd:PLN02467 296 A 296
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
102-248 |
1.30e-03 |
|
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: 42.29 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 102 EPIGIICGIVPTTNPTSTAIfKSLI-SLKTRNAIIFSPhprAKDATNKAADIVLQAAIAAGAPKDLIGWIDQPSVELSNA 180
Cdd:cd07151 129 EPLGVVGVISPWNFPLHLSM-RSVApALALGNAVVLKP---ASDTPITGGLLLAKIFEEAGLPKGVLNVVVGAGSEIGDA 204
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503995744 181 LMHHPDINLILATGGP--GMVKAAYSSG---KPAIGVGaGNTPVVIDETADIKRAVASVLMSKTFDNGVICAS 248
Cdd:cd07151 205 FVEHPVPRLISFTGSTpvGRHIGELAGRhlkKVALELG-GNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMA 276
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
103-250 |
2.26e-03 |
|
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: 41.45 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 103 PIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAAIAAGAPKDLIgwidQPSVELSNALM 182
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLLPPEDVTLI----NGDGKTMQALL 175
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503995744 183 HHPDINLILATGGPGMVKAAYSSGKPA--IGVGAGNTPVVIDETADIKRAVA-SVLMSKTFDNGVICASEQ 250
Cdd:cd07084 176 LHPNPKMVLFTGSSRVAEKLALDAKQAriYLELAGFNWKVLGPDAQAVDYVAwQCVQDMTACSGQKCTAQS 246
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
90-246 |
2.54e-03 |
|
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: 41.43 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 90 SEDDTFGTITiAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAAIAAGAPKDLIGW 169
Cdd:cd07112 112 TGPDALALIT-REPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGF 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 170 idqpSVELSNALMHHPDINLILATGGPG-----MVKAAYSSGKPAIGVGAGNTP-VVIDETADIKRAVASVLMSKTFDNG 243
Cdd:cd07112 191 ----GHTAGEALGLHMDVDALAFTGSTEvgrrfLEYSGQSNLKRVWLECGGKSPnIVFADAPDLDAAAEAAAAGIFWNQG 266
|
...
gi 503995744 244 VIC 246
Cdd:cd07112 267 EVC 269
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
103-235 |
2.99e-03 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 41.28 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 103 PIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPhpRAKDATnkAADIVLQAAIAAGAPKDLIGWIDQPSVELSNALM 182
Cdd:PLN00412 158 PLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKP--PTQGAV--AALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLT 233
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 503995744 183 HHPDINLILATGGPGMVKAAYSSGKPAIGVGAGNTPV-VIDETADIKRAVASVL 235
Cdd:PLN00412 234 MHPGVNCISFTGGDTGIAISKKAGMVPLQMELGGKDAcIVLEDADLDLAAANII 287
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
453-554 |
3.66e-03 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 40.65 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 453 WHKLPKSIYFRRGSLPiALDEVITDGH--KRALIVTDRfLFNNGYADQITSVLKAAGvETEVFFEVEAdpTLTIVRKGAE 530
Cdd:PRK00843 7 WIQLPRDVVVGHGVLD-DIGDVCSDLKltGRALIVTGP-TTKKIAGDRVEENLEDAG-DVEVVIVDEA--TMEEVEKVEE 81
|
90 100
....*....|....*....|....
gi 503995744 531 LANSFKPDVIIALGGGSPMDAAKI 554
Cdd:PRK00843 82 KAKDVNAGFLIGVGGGKVIDVAKL 105
|
|
| EEVS |
cd08199 |
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ... |
470-552 |
4.57e-03 |
|
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the cyclization of sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone in the biosynthesis of C(7)N-aminocyclitol-containing products. The cyclization product, 2-epi-5-epi-valiolone ((2S,3S,4S,5R)-5-(hydroxymethyl)cyclohexanon-2,3,4,5-tetrol), is a precursor of the valienamine moiety. The valienamine unit is responsible for their biological activities as various glycosidic hydrolases inhibitors. Two important microbial secondary metabolites, validamycin and acarbose, are used in agricultural and biomedical applications. Validamycin A is an antifungal antibiotic which has a strong trehalase inhibitory activity and has been used to control sheath blight disease in rice caused by Rhizoctonia solani. Acarbose is an alpha-glucosidase inhibitor used for the treatment of type II insulin-independent diabetes. Salbostatin produced by Streptomyces albus also belongs to this family. It exhibits strong trehalase inhibitory activity.
Pssm-ID: 341478 Cd Length: 349 Bit Score: 40.20 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 470 ALDEVITDGHKRALIVTDRFLFNNgYADQITSVLKAAGVETEVF-FEV-EADPTLTIVRKGAELANSFKPD---VIIALG 544
Cdd:cd08199 17 TLADAYGRPGRRRLVVVDENVDRL-YGARIRAYFAAHGIEATILvLPGgEANKTMETVLRIVDALDDFGLDrrePVIAIG 95
|
....*...
gi 503995744 545 GGSPMDAA 552
Cdd:cd08199 96 GGVLLDVV 103
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
99-248 |
5.19e-03 |
|
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: 40.47 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 99 TIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPhprakdATNKAADIVLQAAIA--AGAPKDLIGWIDQPSVE 176
Cdd:cd07144 140 TLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKP------AENTPLSLLYFANLVkeAGFPPGVVNIIPGYGAV 213
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503995744 177 LSNALMHHPDINLILATG----GPGMVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKTFDNGVICAS 248
Cdd:cd07144 214 AGSALAEHPDVDKIAFTGstatGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTA 289
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
154-246 |
5.77e-03 |
|
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: 40.29 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 154 LQAAIAAG----------AP------KDLIGWIDQPS--------VELSNALMHHPdINLILATGGPG-----MVKAA-- 202
Cdd:cd07134 121 LVSAIAAGntailkpselTPhtsaviAKIIREAFDEDevavfegdAEVAQALLELP-FDHIFFTGSPAvgkivMAAAAkh 199
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 503995744 203 YSSGKPAIGvgaGNTPVVIDETADIKRAVASVLMSKTFDNGVIC 246
Cdd:cd07134 200 LASVTLELG---GKSPTIVDETADLKKAAKKIAWGKFLNAGQTC 240
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
102-383 |
6.93e-03 |
|
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: 39.98 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 102 EPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAAIAAGAPKDLIG-WIDQPsvELSNA 180
Cdd:cd07098 119 EPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIRECLAACGHDPDLVQlVTCLP--ETAEA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 181 LMHHPDINLILATGGPG---MV-KAAYSSGKPAIGVGAGNTPVVIDETADIKrAVASVLMSKTFDN-GVICASEqsvvvv 255
Cdd:cd07098 197 LTSHPVIDHITFIGSPPvgkKVmAAAAESLTPVVLELGGKDPAIVLDDADLD-QIASIIMRGTFQSsGQNCIGI------ 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995744 256 dsvydavrERFSSHGGylLQGQELKAVQNII--LKNGA-------LNAAIVGQPAYKIAELAGFTVPVSTKILIGE---- 322
Cdd:cd07098 270 --------ERVIVHEK--IYDKLLEILTDRVqaLRQGPpldgdvdVGAMISPARFDRLEELVADAVEKGARLLAGGkryp 339
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503995744 323 --------------VTDVDESEPFAHEKL-SPTLAMYRAKNFEDAVDKAEKlvAMGGIGhtSCLYTDQDNQPERVA 383
Cdd:cd07098 340 hpeypqghyfpptlLVDVTPDMKIAQEEVfGPVMVVMKASDDEEAVEIANS--TEYGLG--ASVFGKDIKRARRIA 411
|
|
| |
