|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
1-860 |
0e+00 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 1723.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 1 MPVTNMAELDAMVARVKAAQQEFATFSQEQVDKIFRAASLAANNARIPLAQQAVAESGMGIVEDKVIKNHFASEFIYNKY 80
Cdd:PRK13805 6 MAVTNVAELDALVEKAKKAQEEFATFTQEQVDKIVRAAALAALDARIPLAKMAVEETGRGVVEDKVIKNHFASEYIYNSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 81 KDEKTCGILEENEEFGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVLDAAVAA 160
Cdd:PRK13805 86 KDEKTVGVIEEDDEFGIIEIAEPVGVIAGITPTTNPTSTAIFKALIALKTRNPIIFSFHPRAQKSSIAAAKIVLDAAVAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 161 GAPKNIIGWIDQPSVELSNALMKHNDINLILATGGPGMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTF 240
Cdd:PRK13805 166 GAPKDIIQWIEEPSVELTNALMNHPGIALILATGGPGMVKAAYSSGKPALGVGAGNVPAYIDKTADIKRAVNDILLSKTF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 241 DNGVVCASEQAVIVMDEVYDEVKARFASHNGYVLSKAEADKVRKILL--INGNLNADIVGQPATKIAEMAGITVPADTKI 318
Cdd:PRK13805 246 DNGMICASEQAVIVDDEIYDEVKEEFASHGAYFLNKKELKKLEKFIFgkENGALNADIVGQSAYKIAEMAGFKVPEDTKI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 319 LIGEGDEVKYEDEFAHEKLSPTLGMFRASSFENAVEQACTMVDIGGIGHTSGLYTNqdvNKDRIKYFGDKMKTARILVNI 398
Cdd:PRK13805 326 LIAEVKGVGESEPLSHEKLSPVLAMYKAKDFEDAVEKAEKLVEFGGLGHTAVIYTN---DDELIKEFGLRMKACRILVNT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 399 PTTHGGIGDLYNfNVAPSLTLGCGSWGGNSISENVGPKHLINKKTVAKRAENMLWHKLPKSIYFRRGSLPIALSDLEGKK 478
Cdd:PRK13805 403 PSSQGGIGDLYN-KLAPSLTLGCGSWGGNSVSENVGAKHLLNIKTVAKRRENMQWFKVPKKIYFERGSLPYLLDELDGKK 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 479 RAFLVTDRFLFNNGYADDVVKLLKA--QGIEVQTFFDVEADPTLSIVEKGAEAMKSFQPDVIIALGGGSPMDAAKIMWVM 556
Cdd:PRK13805 482 RAFIVTDRFMVELGYVDKVTDVLKKreNGVEYEVFSEVEPDPTLSTVRKGAELMRSFKPDTIIALGGGSPMDAAKIMWLF 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 557 YEHPETHFEELAMRFMDIRKRIYKFPKMGKKAELVCITTTSGTGSEVTPFAVVTDDKTGAKYPLADYELTPHMAIVDANL 636
Cdd:PRK13805 562 YEHPETDFEDLAQKFMDIRKRIYKFPKLGKKAKLVAIPTTSGTGSEVTPFAVITDDKTGVKYPLADYELTPDVAIVDPNL 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 637 VMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPSSYANGANDPIAREKVHNAATIAGIAFANAF 716
Cdd:PRK13805 642 VMTMPKSLTADTGIDALTHALEAYVSVMASDYTDGLALQAIKLVFEYLPRSYKNGAKDPEAREKMHNASTIAGMAFANAF 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 717 LGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNANDNPtKQTAFSQYASPQARRRYAEVADHLSLsqAGDRTAQKIERL 796
Cdd:PRK13805 722 LGICHSMAHKLGAEFHIPHGRANAILLPHVIRYNATDPP-KQAAFPQYEYPRADERYAEIARHLGL--PGSTTEEKVESL 798
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46912724 797 LTWLEELKIALDIPLSIQAAGIPEADFLAKLDQLSIEAFDDQCTGANPRYPLISELKEVLTSAY 860
Cdd:PRK13805 799 IKAIEELKAELGIPMSIKEAGVDEADFLAKLDELAELAFDDQCTGANPRYPLISELKEILLDAY 862
|
|
| 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: 743.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 9 LDAMVARVKAAQQEFATFSQEQVDKIFRAASLAANNARIPLAQQAVAESGMGIVEDKVIKNHFASEFIYNKYKDEKTCGI 88
Cdd:cd07122 1 VDELVERARKAQREFATFSQEQVDKIVEAVAWAAADAAEELAKMAVEETGMGVVEDKVIKNHFASEYVYNDIKDMKTVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 89 LEENEEFGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVLDAAVAAGAPKNIIG 168
Cdd:cd07122 81 IEEDEEKGIVEIAEPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAAVAAGAPEGLIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 169 WIDQPSVELSNALMKHNDINLILATGGPGMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCAS 248
Cdd:cd07122 161 WIEEPSIELTQELMKHPDVDLILATGGPGMVKAAYSSGKPAIGVGPGNVPAYIDETADIKRAVKDIILSKTFDNGTICAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 249 EQAVIVMDEVYDEVKARFASHNGYVLSKAEADKVRKILLI-NGNLNADIVGQPATKIAEMAGITVPADTKILIGEGDEVK 327
Cdd:cd07122 241 EQSVIVDDEIYDEVRAELKRRGAYFLNEEEKEKLEKALFDdGGTLNPDIVGKSAQKIAELAGIEVPEDTKVLVAEETGVG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 328 YEDEFAHEKLSPTLGMFRASSFENAVEQACTMVDIGGIGHTSGLYTNqdvNKDRIKYFGDKMKTARILVNIPTTHGGIGD 407
Cdd:cd07122 321 PEEPLSREKLSPVLAFYRAEDFEEALEKARELLEYGGAGHTAVIHSN---DEEVIEEFALRMPVSRILVNTPSSLGGIGD 397
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 46912724 408 LYNFnVAPSLTLGCGSWGGNSISENVGPKHLINKKTVAKR 447
Cdd:cd07122 398 TYNG-LAPSLTLGCGSWGGNSTSDNVGPKHLLNIKRVAYR 436
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
455-856 |
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: 710.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 455 KLPKSIYFRRGSLPIALSDLEGKKRAFLVTDRFLFNNGYADDVVKLLKAQGIEVQTFFDVEADPTLSIVEKGAEAMKSFQ 534
Cdd:cd08178 1 KVPPKIYFEPGCLPYLLLELPGVKRAFIVTDRVLYKLGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLEAMNAFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 535 PDVIIALGGGSPMDAAKIMWVMYEHPETHFEELAMRFMDIRKRIYKFPKMGKKAELVCITTTSGTGSEVTPFAVVTDDKT 614
Cdd:cd08178 81 PDVIIALGGGSAMDAAKIMWLFYEHPETKFEDLAQRFMDIRKRVYKFPKLGKKAKLVAIPTTSGTGSEVTPFAVITDDKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 615 GAKYPLADYELTPHMAIVDANLVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPSSYANGaND 694
Cdd:cd08178 161 GKKYPLADYALTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVSVMASDYTDGLALQAIKLIFEYLPRSYNNG-ND 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 695 PIAREKVHNAATIAGIAFANAFLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNANDNPTKQTAFSQYASPQARRRYA 774
Cdd:cd08178 240 IEAREKMHNAATIAGMAFANAFLGICHSLAHKLGAAFHIPHGRANAILLPHVIRYNATDPPTKQAAFPQYKYYVAKERYA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 775 EVADHLSLsqAGDRTAQKIERLLTWLEELKIALDIPLSIQAAGIPEADFLAKLDQLSIEAFDDQCTGANPRYPLISELKE 854
Cdd:cd08178 320 EIADLLGL--GGKTPEEKVESLIKAIEDLKKDLGIPTSIREAGIDEADFLAAVDKLAEDAFDDQCTGANPRYPLISELKE 397
|
..
gi 46912724 855 VL 856
Cdd:cd08178 398 IL 399
|
|
| 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: 669.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 9 LDAMVARVKAAQQEFATFSQEQVDKIFRAASLAANNARIPLAQQAVAESGMGIVEDKVIKNHFASEFIYNKYKDEKTCGI 88
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIKNHFAAEYIYNVYKDEKTCGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 89 LEENEEFGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVLDAAVAAGAPKNIIG 168
Cdd:cd07081 81 LTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 169 WIDQPSVELSNALMKHNDINLILATGGPGMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCAS 248
Cdd:cd07081 161 WIDNPSIELAQRLMKFPGIGLLLATGGPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 249 EQAVIVMDEVYDEVKARFASHNGYVLSKAEADKVRKILLINGNLNADIVGQPATKIAEMAGITVPADTKILIGEGDEVKY 328
Cdd:cd07081 241 EQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQQVQPVILKNGDVNRDIVGQDAYKIAAAAGLKVPQETRILIGEVTSLAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 329 EDEFAHEKLSPTLGMFRASSFENAVEQACTMVDIGGIGHTSGLYTNQDVNKDRIKYFGDKMKTARILVNIPTTHGGIGDL 408
Cdd:cd07081 321 HEPFAHEKLSPVLAMYRAANFADADAKALALKLEGGCGHTSAMYSDNIKAIENMNQFANAMKTSRFVKNGPCSQGGLGDL 400
|
410 420 430
....*....|....*....|....*....|....*....
gi 46912724 409 YNFNVAPSLTLGCGSWGGNSISENVGPKHLINKKTVAKR 447
Cdd:cd07081 401 YNFRGWPSMTLGCGTWGGNSVSENVGPKHLVNLKTVALR 439
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
456-861 |
1.83e-163 |
|
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: 481.69 E-value: 1.83e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 456 LPKSIYFRRGSLPiALSDLEGKkRAFLVTD-RFLFNNGYADDVVKLLKAQGIEVQTFFDVEADPTLSIVEKGAEAMKSFQ 534
Cdd:cd08179 4 VPRDIYFGEGALE-YLKTLKGK-RAFIVTGgGSMKRNGFLDKVEDYLKEAGMEVKVFEGVEPDPSVETVEKGAEAMREFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 535 PDVIIALGGGSPMDAAKIMWVMYEHPETHFEELAMRFmdirkriyKFPKMGKKAELVCITTTSGTGSEVTPFAVVTDDKT 614
Cdd:cd08179 82 PDWIIAIGGGSVIDAAKAMWVFYEYPELTFEDALVPF--------PLPELRKKARFIAIPSTSGTGSEVTRASVITDTEK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 615 GAKYPLADYELTPHMAIVDANLVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPSSYANGaND 694
Cdd:cd08179 154 GIKYPLASFEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLANDFTDALALGAILDIFENLPKSYNGG-KD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 695 PIAREKVHNAATIAGIAFANAFLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNANDnptkqtafsqyasPQARRRYA 774
Cdd:cd08179 233 LEAREKMHNASCLAGMAFSNSGLGIVHSMAHKGGAFFGIPHGLANAILLPYVIEFNSKD-------------PEARARYA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 775 EVADHLSlsqagdrTAQKIERLLTWLEELKIALDIPLSIQAAGIPEADFLAKLDQLSIEAFDDQCTGANPRYPLISELKE 854
Cdd:cd08179 300 ALLIGLT-------DEELVEDLIEAIEELNKKLGIPLSFKEAGIDEDEFFAKLDEMAENAMNDACTGTNPRKPTVEEMKE 372
|
....*..
gi 46912724 855 VLTSAYY 861
Cdd:cd08179 373 LLKAAYY 379
|
|
| EutH_ACDH |
TIGR02518 |
acetaldehyde dehydrogenase (acetylating); |
17-445 |
3.77e-163 |
|
acetaldehyde dehydrogenase (acetylating);
Pssm-ID: 131570 Cd Length: 488 Bit Score: 485.14 E-value: 3.77e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 17 KAAQQEFATFSQEQVDKIFRAASLAANNARIPLAQQAVAESGMGIVEDKVIKNHFASEFIYNKYKDEKTCGILEENEEFG 96
Cdd:TIGR02518 18 KVAQKKLANMTQEQIDKIVKAIVDAAYENAVKLAKMANEETGFGKWEDKVIKNVFAATIVYDSIKDMKTIGILSEDKEKK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 97 TMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVLDAAVAAGAPKNIIGWIDQPSVE 176
Cdd:TIGR02518 98 VIEIAVPVGVVAGLIPSTNPTSTAIYKTLISIKARNAIVFSPHPNAKKCIIETVKLMRKAAEEAGAPEGAIGCITVPTIE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 177 LSNALMKHNDINLILATGGPGMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIVMD 256
Cdd:TIGR02518 178 GTNELMKNKDTSLILATGGEAMVKAAYSSGTPAIGVGPGNGPAYIERTANVKKAVRDIIDSKTFDNGTICASEQSIIVEE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 257 EVYDEVKARFASHNGYVLSKAEADKVRKILL-INGNLNADIVGQPATKIAEMAGITVPADTKILIGEGDEVKYEDEFAHE 335
Cdd:TIGR02518 258 CNKDAVVEELKKQGGYFLTAEEAEKLGKFILrPNGTMNPQIVGKSPQVIANLAGLTVPEDAKVLIGEQNGVGNKNPYSRE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 336 KLSPTLGMFRASSFENAVEQACTMVDIGGIGHTSGLYTNqdvNKDRIKYFGDKMKTARILVNIPTTHGGIGdlYNFNVAP 415
Cdd:TIGR02518 338 KLTTILAFYTEENWHEACELSIELLQNEGAGHTLIIHSE---NKDIVREFALKKPVSRMLVNTGGSLGGIG--ATTNLVP 412
|
410 420 430
....*....|....*....|....*....|
gi 46912724 416 SLTLGCGSWGGNSISENVGPKHLINKKTVA 445
Cdd:TIGR02518 413 AFTLGCGAVGGSSTSDNITPENLINIRRVA 442
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
450-860 |
5.54e-159 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 470.37 E-value: 5.54e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 450 NMLWHKLPKSIYFRRGS---LPIALSDLeGKKRAFLVTDRFLFNNGYADDVVKLLKAQGIEVQTFFDVEADPTLSIVEKG 526
Cdd:COG1454 1 MMFTFRLPTRIVFGAGAlaeLGEELKRL-GAKRALIVTDPGLAKLGLLDRVLDALEAAGIEVVVFDDVEPNPTVETVEAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 527 AEAMKSFQPDVIIALGGGSPMDAAKIMWVMYEHPEThfeelamrFMDIrkrIYKFPKMGKKAELVCITTTSGTGSEVTPF 606
Cdd:COG1454 80 AAAAREFGADVVIALGGGSAIDAAKAIALLATNPGD--------LEDY---LGIKKVPGPPLPLIAIPTTAGTGSEVTPF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 607 AVVTDDKTGAKYPLADYELTPHMAIVDANLVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPS 686
Cdd:COG1454 149 AVITDPETGVKKGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPLTDALALEAIRLIARNLPR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 687 SYANGaNDPIAREKVHNAATIAGIAFANAFLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNAndnptkqtafsqyas 766
Cdd:COG1454 229 AVADG-DDLEAREKMALASLLAGMAFANAGLGAVHALAHPLGGLFHVPHGLANAILLPHVLRFNA--------------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 767 PQARRRYAEVADHLSLSqAGDRTAQKIERLLTWLEELKIALDIPLSIQAAGIPEADflakLDQLSIEAFDDQCTGANPRY 846
Cdd:COG1454 293 PAAPERYAEIARALGLD-VGLSDEEAAEALIEAIRELLRDLGIPTRLSELGVTEED----LPELAELALADRCLANNPRP 367
|
410
....*....|....
gi 46912724 847 PLISELKEVLTSAY 860
Cdd:COG1454 368 LTEEDIEAILRAAY 381
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
14-446 |
3.90e-123 |
|
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: 378.49 E-value: 3.90e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 14 ARVKAAQQEFATFSQEQVDKIFRAASLAANNARIPLAQQAVAESG-------------MGIVEDKVIKNHFASEFIYNKy 80
Cdd:cd07077 1 ESAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGayirslianwiamMGCSESKLYKNIDTERGITAS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 81 kDEKTCGILEEnEEFGTMTIAEPVGIICGIVPTTNPTStAIFKSLISLKTRNAIIFSPHPRAKnSTNAAAKLVLDAAVAA 160
Cdd:cd07077 80 -VGHIQDVLLP-DNGETYVRAFPIGVTMHILPSTNPLS-GITSALRGIATRNQCIFRPHPSAP-FTNRALALLFQAADAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 161 GAPKNIIGWIDQPSVELSNALMKHNDINLILATGGPGMVKAAYSS--GKPAIGVGAGNVPVVIDETADIKRAVASVLMSK 238
Cdd:cd07077 156 HGPKILVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAVKHspHIPVIGFGAGNSPVVVDETADEERASGSVHDSK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 239 TFDNgVVCASEQAVIVMDEVYDEVKARFASHNGYvlskaeadkvrkillingnlnadivgqpatkiaemAGITVPADTKI 318
Cdd:cd07077 236 FFDQ-NACASEQNLYVVDDVLDPLYEEFKLKLVV-----------------------------------EGLKVPQETKP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 319 LIGEgdEVKYEDEFAHEKLSPTLGMFRASSFENAVEQACTMVDIGGIGHTSGLYTNQDvnkDRIKYFGDKMKTARILVNI 398
Cdd:cd07077 280 LSKE--TTPSFDDEALESMTPLECQFRVLDVISAVENAWMIIESGGGPHTRCVYTHKI---NKVDDFVQYIDTASFYPNE 354
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 46912724 399 PTTHGGiGDLYNFNVAPSLTLGCGSWGGnsisENVGPKHLINKKTVAK 446
Cdd:cd07077 355 SSKKGR-GAFAGKGVERIVTSGMNNIFG----AGVGHDALRPLKRLVR 397
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
457-852 |
3.76e-121 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 371.55 E-value: 3.76e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 457 PKSIYFRRGSLPIALSDLEG-KKRAFLVTDRFLFNNGYADDVVKLLKAQGIEVQTFFDVEADPTLSIVEKGAEAMKSFQP 535
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRlGARALIVTDPGSLKSGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALAREAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 536 DVIIALGGGSPMDAAKIMWVMYEHPETHFEELamrfmdirkriYKFPKMGKKAELVCITTTSGTGSEVTPFAVVTDDKTG 615
Cdd:pfam00465 81 DVIIAVGGGSVIDTAKAIALLLTNPGDVWDYL-----------GGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 616 AKYPLADYELTPHMAIVDANLVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPSSYANGaNDP 695
Cdd:pfam00465 150 EKLGIFSPKLLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDALALEAIRLIAENLPRAVADG-EDL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 696 IAREKVHNAATIAGIAFANAFLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNAndnptkqtafsqyasPQARRRYAE 775
Cdd:pfam00465 229 EARENMLLASTLAGLAFSNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNA---------------PAAPEKLAQ 293
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46912724 776 VADHLSlsqaGDRTAQKIERLLTWLEELKIALDIPLSIQAAGIPEADflakLDQLSIEAFDDQCTGANPRYPLISEL 852
Cdd:pfam00465 294 LARALG----EDSDEEAAEEAIEALRELLRELGLPTTLSELGVTEED----LDALAEAALRDRSLANNPRPLTAEDI 362
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
453-856 |
1.60e-119 |
|
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: 368.09 E-value: 1.60e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 453 WHKLPKSIYFRRGSLPiALSDLEGKkRAFLVTDRFLFNNGYADDVVKLLKAQGIEVQTFFDVEADPTLSIVEKGAEAMKS 532
Cdd:cd14862 2 WYFSSPKIVFGEDALS-HLEQLSGK-RALIVTDKVLVKLGLLKKVLKRLLQAGFEVEVFDEVEPEPPLETVLKGAEAMRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 533 FQPDVIIALGGGSPMDAAKIMWVMYEHPETHFEELAmrfmdirkriyKFPKMG--KKAELVCITTTSGTGSEVTPFAVVT 610
Cdd:cd14862 80 FEPDLIIALGGGSVMDAAKAAWVLYERPDLDPEDIS-----------PLDLLGlrKKAKLIAIPTTSGTGSEATWAIVLT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 611 DDKTGAKYPLADYELTPHMAIVDANLVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPSSYAN 690
Cdd:cd14862 149 DTEEPRKIAVANPELVPDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLSTWSNDFSDALALKAIELIFKYLPRAYKD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 691 GaNDPIAREKVHNAATIAGIAFANAFLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNANDnptkqtafsqyaspqAR 770
Cdd:cd14862 229 G-DDLEAREKMHNAATIAGLAFGNSQAGLAHALGHSLGAVFHVPHGIAVGLFLPYVIEFYAKV---------------TD 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 771 RRYAEVADHLSLSQAGDRTAQKierLLTWLEELKIALDIPLSIQAAGIPEADFLAKLDQLSIEAFDDQCTGANPRYPLIS 850
Cdd:cd14862 293 ERYDLLKLLGIEARDEEEALKK---LVEAIRELYKEVGQPLSIKDLGISEEEFEEKLDELVEYAMEDSCTITSPRPPSEE 369
|
....*.
gi 46912724 851 ELKEVL 856
Cdd:cd14862 370 DLKKLF 375
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
455-856 |
5.05e-116 |
|
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: 357.19 E-value: 5.05e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 455 KLPKSIYFRRGSLPiALSDLEGKkRAFLVTDRFLFNNGYADDVVKLLKaQGIEVQTFFDVEADPTLSIVEKGAEAMKSFQ 534
Cdd:cd08180 2 SLKTKIYSGEDSLE-RLKELKGK-RVFIVTDPFMVKSGMVDKVTDELD-KSNEVEIFSDVVPDPSIEVVAKGLAKILEFK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 535 PDVIIALGGGSPMDAAKimwvmyehpethfeelAMRFMdirkrIYKFPKMGKKAELVCITTTSGTGSEVTPFAVVTDDKT 614
Cdd:cd08180 79 PDTIIALGGGSAIDAAK----------------AIIYF-----ALKQKGNIKKPLFIAIPTTSGTGSEVTSFAVITDPEK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 615 GAKYPLADYELTPHMAIVDANLVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPSSYANGaND 694
Cdd:cd08180 138 GIKYPLVDDSMLPDIAILDPELVKSVPPKVTADTGMDVLTHALEAYVSTNANDFTDALAEKAIKLVFENLPRAYRDG-DD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 695 PIAREKVHNAATIAGIAFANAFLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYnandnptkqtafsqyaspqarrrya 774
Cdd:cd08180 217 LEAREKMHNASCMAGIAFNNAGLGINHSLAHALGGRFHIPHGRANAILLPYVIEF------------------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 775 evadhlslsqagdrtaqkierLLTWLEELKIALDIPLSIQAAGIPEADFLAKLDQLSIEAFDDQCTGANPRYPLISELKE 854
Cdd:cd08180 272 ---------------------LIAAIRRLNKKLGIPSTLKELGIDEEEFEKAIDEMAEAALADRCTATNPRKPTAEDLIE 330
|
..
gi 46912724 855 VL 856
Cdd:cd08180 331 LL 332
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
457-848 |
8.19e-115 |
|
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: 355.60 E-value: 8.19e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 457 PKSIYFRRGSLPiALSDL---EGKKRAFLVTDRFLFNNGYADDVVKLLKAQGIEVQTFFDVEADPTLSIVEKGAEAMKSF 533
Cdd:cd08551 1 PTRIVFGAGALA-RLGEElkaLGGKKVLLVTDPGLVKAGLLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELAREE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 534 QPDVIIALGGGSPMDAAKIMWVMYEHPETHFEELAMRfmdirkriyKFPKmgKKAELVCITTTSGTGSEVTPFAVVTDDK 613
Cdd:cd08551 80 GADLVIAVGGGSVLDTAKAIAVLATNGGSIRDYEGIG---------KVPK--PGLPLIAIPTTAGTGSEVTPNAVITDPE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 614 TGAKYPLADYELTPHMAIVDANLVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPSSYANGaN 693
Cdd:cd08551 149 TGRKMGIVSPYLLPDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANPISDALALEAIRLIGKNLRRAVADG-S 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 694 DPIAREKVHNAATIAGIAFANAFLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNANDNPtkqtafsqyaspqarRRY 773
Cdd:cd08551 228 DLEAREAMLLASLLAGIAFGNAGLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPACP---------------EKY 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46912724 774 AEVADHLSLSQAGDRTAQKIERLLTWLEELKIALDIPLSIQAAGIPEADFlaklDQLSIEAFDDQCTGANPRYPL 848
Cdd:cd08551 293 AEIAEALGEDVEGLSDEEAAEAAVEAVRELLRDLGIPTSLSELGVTEEDI----PELAEDAMKSGRLLSNNPRPL 363
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
457-860 |
7.50e-103 |
|
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: 324.48 E-value: 7.50e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 457 PKSIYFRRGS---LPIALSDLEGKkRAFLVTDRFLFNNGYADDVVKLLKAQGIEVQTFFDVEADPTLSIVEKGAEAMKSF 533
Cdd:cd08194 1 PRTIIIGGGAleeLGEEAASLGGK-RALIVTDKVMVKLGLVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVEEGLALYKEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 534 QPDVIIALGGGSPMDAAKIMWVMYEHPEthfeelamrfmDIRKriYKFPKMGKKA--ELVCITTTSGTGSEVTPFAVVTD 611
Cdd:cd08194 80 GCDFIVALGGGSPIDTAKAIAVLATNGG-----------PIRD--YMGPRKVDKPglPLIAIPTTAGTGSEVTRFTVITD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 612 DKTGAKYPLADYELTPHMAIVDANLVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPSSYANG 691
Cdd:cd08194 147 TETDVKMLLKGPALLPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQPLTDTLALSAIKLIGRNLRRAYADG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 692 ANDPiAREKVHNAATIAGIAFANAFLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNANDNPTkqtafsqyaspqarr 771
Cdd:cd08194 227 DDLE-AREAMMLAALEAGIAFSNSSVALVHGMSRPIGALFHVPHGLSNAMLLPAVTEFSLPGAPE--------------- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 772 RYAEVADHLSLSQAGDRTAQKIERLLTWLEELKIALDIPlSIQAAGIPEADFLAKLDQLSIEAFDDQCTGANPRYPLISE 851
Cdd:cd08194 291 RYAEIARAMGIATEGDSDEEAAEKLVEALERLCADLEIP-TLREYGIDEEEFEAALDKMAEDALASGSPANNPRVPTKEE 369
|
....*....
gi 46912724 852 LKEVLTSAY 860
Cdd:cd08194 370 IIELYREAW 378
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
456-856 |
4.66e-101 |
|
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: 319.88 E-value: 4.66e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 456 LPKSIYFRRGSLPIALSDL--EGKKRAFLVTDRFLFNNGYADDVVKLLKAQGIEVQTFFDVEADPTLSIVEKGAEAMKSF 533
Cdd:cd08176 5 LNPTSYFGWGAIEEIGEEAkkRGFKKALIVTDKGLVKFGIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGVAAYKES 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 534 QPDVIIALGGGSPMDAAKIMWVMYEHPethfeelamrFMDIRKRIYKFPKMGKKAELVCITTTSGTGSEVTPFAVVTDDK 613
Cdd:cd08176 85 GADGIIAVGGGSSIDTAKAIGIIVANP----------GADVRSLEGVAPTKNPAVPIIAVPTTAGTGSEVTINYVITDTE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 614 TGAKYPLADYELTPHMAIVDANLVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPSSYANGAN 693
Cdd:cd08176 155 KKRKFVCVDPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYITKGAWELSDMLALKAIELIAKNLRKAVANPNN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 694 dPIAREKVHNAATIAGIAFANAFLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNANDNPTKqtafsqyaspqarrrY 773
Cdd:cd08176 235 -VEARENMALAQYIAGMAFSNVGLGIVHSMAHPLSAFYDTPHGVANAILLPYVMEFNAPATGEK---------------Y 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 774 AEVADHLSLSQAGDRTAQKIERLLTWLEELKIALDIPLSIQAAGIPEADflakLDQLSIEAFDDQCTGANPRYPLISELK 853
Cdd:cd08176 299 RDIARAMGVDTTGMSDEEAAEAAVDAVKKLSKDVGIPQKLSELGVKEED----IEALAEDALNDVCTPGNPREATKEDII 374
|
...
gi 46912724 854 EVL 856
Cdd:cd08176 375 ALY 377
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
476-860 |
9.77e-93 |
|
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: 297.91 E-value: 9.77e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 476 GKKRAFLVTDRFLFNNGYADDVVKLLKAQGIEVQTFFDVEADPTLSIVEKGAEAMKSFQPDVIIALGGGSPMDAAKIMWV 555
Cdd:cd14863 26 GCKKVLLVTDKGLKKAGIVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEIAREEGADGVIGIGGGSVLDTAKAIAV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 556 MYEHPEThfeelAMRFMDIRKRIYKFPKmgkkaELVCITTTSGTGSEVTPFAVVTDDKTGAKYPLADYELTPHMAIVDAN 635
Cdd:cd14863 106 LLTNPGP-----IIDYALAGPPVPKPGI-----PLIAIPTTAGTGSEVTPIAVITDEENGVKKSLLGPFLVPDLAILDPE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 636 LVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPSSYANGANDPiAREKVHNAATIAGIAFANA 715
Cdd:cd14863 176 LTVGLPPSLTAATGMDALSHAIEAYTSKLANPMTDALALQAIRLIVKNLPRAVKDGDNLE-ARENMLLASNLAGIAFNNA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 716 FLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNANDNPTKqtafsqyaspqarrrYAEVADHLSLSQAGDRTAQKIER 795
Cdd:cd14863 255 GTHIGHAIAHALGALYHIPHGLACALALPVVLEFNAEAYPEK---------------VKKIAKALGVSFPGESDEELGEA 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46912724 796 LLTWLEELKIALDIPLSIQAAGIPEADFLAKLDqlsiEAFDDQCTGANPRYPLISELKEVLTSAY 860
Cdd:cd14863 320 VADAIREFMKELGIPSLFEDYGIDKEDLDKIAE----AVLKDPFAMFNPRPITEEEVAEILEAIY 380
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
456-855 |
2.03e-91 |
|
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: 294.04 E-value: 2.03e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 456 LPKSIYFRRGSLPIALSDLE--GKKRAFLVTDRFLFNNGYADDVVKLLKAQGIEVQTFFDVEADPTLSIVEKGAEAMKSF 533
Cdd:cd08188 5 IPPVNLFGPGCLKEIGDELKklGGKKALIVTDKGLVKLGLVKKVTDVLEEAGIEYVIFDGVQPNPTVTNVNEGLELFKEN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 534 QPDVIIALGGGSPMDAAKIMWVMYEHPEthfeelamrfmDIRKR--IYKFPKMGkkAELVCITTTSGTGSEVTPFAVVTD 611
Cdd:cd08188 85 GCDFIISVGGGSAHDCAKAIGILATNGG-----------EIEDYegVDKSKKPG--LPLIAINTTAGTASEVTRFAVITD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 612 DKTGAKYPLADYELTPHMAIVDANLVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPSSYANG 691
Cdd:cd08188 152 EERHVKMVIVDWNVTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVSTGATPLTDALALEAIRLIAENLPKAVANG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 692 aNDPIAREKVHNAATIAGIAFANAFLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNAndnptkqtafsqyasPQARR 771
Cdd:cd08188 232 -KDLEARENMAYAQFLAGMAFNNAGLGYVHAMAHQLGGFYNLPHGVCNAILLPHVMEFNL---------------PACPE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 772 RYAEVADHLSLSQAGDRTAQKIERLLTWLEELKIALDIPLSIQAAGIPEADFlaklDQLSIEAFDDQCTGANPRYPLISE 851
Cdd:cd08188 296 RFADIARALGENTEGLSDEEAAEAAIEAIRKLSRRVGIPSGLKELGVKEEDF----PLLAENALKDACGPTNPRQATKED 371
|
....
gi 46912724 852 LKEV 855
Cdd:cd08188 372 VIAI 375
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
465-860 |
3.16e-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: 291.37 E-value: 3.16e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 465 GSLPIALSDLeGKKRAFLVTDRFLFNNGYADDVVKLLKAQGIEVQTFFDVEADPTLSIVEKGAEAMKSFQPDVIIALGGG 544
Cdd:cd14865 17 ENLPAELARL-GARRPLIVTDKGLAAAGLLKKVEDALGDAIEIVGVFDDVPPDSSVAVVNEAAARAREAGADGIIAVGGG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 545 SPMDAAKIMWVMYEHPETHFEELAMRFMDIRKRIykfPkmgkkaeLVCITTTSGTGSEVTPFAVVTDDKTGAKYPLADYE 624
Cdd:cd14865 96 SVIDTAKGVNILLSEGGDDLDDYGGANRLTRPLK---P-------LIAIPTTAGTGSEVTLVAVIKDEEKKVKLLFVSPF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 625 LTPHMAIVDANLVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPSSYANGAnDPIAREKVHNA 704
Cdd:cd14865 166 LLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDALALQAIRLISENLPKAVKNGK-DLEARLALAIA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 705 ATIAGIAFANAFLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNandnptkqtafsqyaSPQARRRYAEVADHLSLSQ 784
Cdd:cd14865 245 ATMAGIAFSNSMVGLVHAIAHAVGAVAGVPHGLANSILLPHVMRYN---------------LDAAAERYAELALALAYGV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 785 --AGDRTAQKIERLLTWLEELKIALDIPLSIQAAGIPEADF--LAKLdqlsieAFDDQCTGANPRYPLISELKEVLTSAY 860
Cdd:cd14865 310 tpAGRRAEEAIEAAIDLVRRLHELCGLPTRLRDVGVPEEQLeaIAEL------ALNDGAILFNPREVDPEDILAILEAAY 383
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
466-847 |
1.96e-89 |
|
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: 288.98 E-value: 1.96e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 466 SLPIALSDLeGKKRAFLVTDRFLFNNGYADDVVKLLKAQGIEVQTFFDVEADPTLSIVEKGAEAMKSFQPDVIIALGGGS 545
Cdd:cd08189 17 QLPEALKKL-GIKRVLIVTDKGLVKLGLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALYKENGCDAIIAIGGGS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 546 PMDAAKIMWVMYEHPETHFEELAmRFMDIRKRIykfpkmgkkAELVCITTTSGTGSEVTPFAVVTDDKTGAKYPLADYEL 625
Cdd:cd08189 96 VIDCAKVIAARAANPKKSVRKLK-GLLKVRKKL---------PPLIAVPTTAGTGSEATIAAVITDPETHEKYAINDPKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 626 TPHMAIVDANLVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPSSYANGANDpIAREKVHNAA 705
Cdd:cd08189 166 IPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETDEYALEAVKLIFENLPKAYEDGSDL-EARENMLLAS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 706 TIAGIAFANAFLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNAndnptkqtafsqyasPQARRRYAEVADHLSLSQA 785
Cdd:cd08189 245 YYAGLAFTRAYVGYVHAIAHQLGGLYGVPHGLANAVVLPHVLEFYG---------------PAAEKRLAELADAAGLGDS 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46912724 786 GDRTAQKIERLLTWLEELKIALDIPLSIqaAGIPEADFlaklDQLSIEAFDDqctgANPRYP 847
Cdd:cd08189 310 GESDSEKAEAFIAAIRELNRRMGIPTTL--EELKEEDI----PEIAKRALKE----ANPLYP 361
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
7-406 |
2.07e-89 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 291.81 E-value: 2.07e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 7 AELDAMVARVKAAQQEFATFSQEQVDKIFRAA-SLAANNARiPLAQQAVAESGMGIVEDKVIKNHFASEfiynkykdeKT 85
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIrEALLPHAE-ELAELAVEETGMGRVEDKIAKNVAAAE---------KT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 86 CGIleenEEFGT--------MTIAE--PVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVLD 155
Cdd:PRK15398 106 PGV----EDLTTealtgdngLTLIEyaPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELLNE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 156 AAVAAGAPKNIIGWIDQPSVELSNALMKHNDINLILATGGPGMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVL 235
Cdd:PRK15398 182 AIVAAGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPAVVKAAMKSGKKAIGAGAGNPPVVVDETADIEKAARDIV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 236 MSKTFDNGVVCASEQAVIVMDEVYDEVKARFASHNGYVLSKAEADKVRKILLINGN-LNADIVGQPATKIAEMAGITVPA 314
Cdd:PRK15398 262 KGASFDNNLPCIAEKEVIVVDSVADELMRLMEKNGAVLLTAEQAEKLQKVVLKNGGtVNKKWVGKDAAKILEAAGINVPK 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 315 DTKILIGEGDEvkyEDEFA-HEKLSPTLGMFRASSFENAVEQAcTMVDiGGIGHTSGLYTNqdvNKDRIKYFGDKMKTAR 393
Cdd:PRK15398 342 DTRLLIVETDA---NHPFVvTELMMPVLPVVRVKDVDEAIALA-VKLE-HGNRHTAIMHSR---NVDNLNKMARAIQTSI 413
|
410
....*....|...
gi 46912724 394 ILVNIPtTHGGIG 406
Cdd:PRK15398 414 FVKNGP-SYAGLG 425
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
7-407 |
3.08e-88 |
|
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: 287.60 E-value: 3.08e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 7 AELDAMVARVKAAQQEFATFSQEQVDKI---FRAASLaaNNARiPLAQQAVAESGMGIVEDKVIKNHFASEfiynkykde 83
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIieaIREALL--SNAE-ELAEMAVEETGMGRVEDKIAKNHLAAE--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 84 KTCGI--LEENEEFGT--MTIAE--PVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVLDAA 157
Cdd:cd07121 72 KTPGTedLTTTAWSGDngLTLVEyaPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 158 VAAGAPKNIIGWIDQPSVELSNALMKHNDINLILATGGPGMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMS 237
Cdd:cd07121 152 AEAGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVKAALSSGKKAIGAGAGNPPVVVDETADIEKAARDIVQG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 238 KTFDNGVVCASEQAVIVMDEVYDEVKARFASHNGYVLSKAEADKVRKILLINGN---LNADIVGQPATKIAEMAGITVPA 314
Cdd:cd07121 232 ASFDNNLPCIAEKEVIAVDSVADYLIAAMQRNGAYVLNDEQAEQLLEVVLLTNKgatPNKKWVGKDASKILKAAGIEVPA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 315 DTKILIGEGDEvkyEDEFA-HEKLSPTLGMFRASSFENAVEQActmVDI-GGIGHTSGLYTNqdvNKDRIKYFGDKMKTA 392
Cdd:cd07121 312 DIRLIIVETDK---DHPFVvEEQMMPILPVVRVKNFDEAIELA---VELeHGNRHTAIIHSK---NVENLTKMARAMQTT 382
|
410
....*....|....*.
gi 46912724 393 RILVNIPTTHG-GIGD 407
Cdd:cd07121 383 IFVKNGPSYAGlGVGG 398
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
456-823 |
7.90e-86 |
|
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: 279.38 E-value: 7.90e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 456 LPKSIYFRRGSL-PIALSDLEGKKRAFLVTDR-FLFNNGYADDVVKLLKAQGIEVQTFFDVEADPTLSIVEKGAEAMKSF 533
Cdd:cd08185 3 QPTRILFGAGKLnELGEEALRPGKKALIVTGKgSSKKTGLLDRVKKLLEKAGVEVVVFDKVEPNPLTTTVMEGAALAKEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 534 QPDVIIALGGGSPMDAAKIMWVMYEHPETHFEelamrfmdirkriYKFPKMGKKAE------LVCITTTSGTGSEVTPFA 607
Cdd:cd08185 83 GCDFVIGLGGGSSMDAAKAIAFMATNPGDIWD-------------YIFGGTGKGPPpekalpIIAIPTTAGTGSEVDPWA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 608 VVTDDKTGAKYPLADYELTPHMAIVDANLVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPSS 687
Cdd:cd08185 150 VITNPETKEKKGIGHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISKNANPFSDMLALEAIRLVAKYLPRA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 688 YANGANDPiAREKVHNAATIAGIAFANAFLGVCHSMAHKVGAEF-HVPHGLANALLISNTIRYNANDNPTKqtafsqyas 766
Cdd:cd08185 230 VKDGSDLE-AREKMAWASTLAGIVIANSGTTLPHGLEHPLSGYHpNIPHGAGLAALYPAYFEFTIEKAPEK--------- 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 46912724 767 pqarrrYAEVAdhlSLSQAGDRTAQKIERLLTWLEELKIALDIPLSIQAAGIPEADF 823
Cdd:cd08185 300 ------FAFVA---RAEASGLSDAKAAEDFIEALRKLLKDIGLDDLLSDLGVTEEDI 347
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
460-859 |
4.48e-84 |
|
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: 274.39 E-value: 4.48e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 460 IYFRRGS---LPIALSDLeGKKRAFLVTDRFLFNNGYADDVVKLLKAQGIEVQTFFDVEADPTLSIVEKGAEAMKSFQPD 536
Cdd:cd14861 6 IRFGAGAiaeLPEELKAL-GIRRPLLVTDPGLAALGIVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAYREGGCD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 537 VIIALGGGSPMDAAKIMWVMYEHPE--THFEELAMRFMDIRKRIykfpkmgkkAELVCITTTSGTGSEVTPFAVVTDDKT 614
Cdd:cd14861 85 GIIALGGGSAIDAAKAIALMATHPGplWDYEDGEGGPAAITPAV---------PPLIAIPTTAGTGSEVGRAAVITDDDT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 615 GAKYPLADYELTPHMAIVDANLVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPSSYANGAND 694
Cdd:cd14861 156 GRKKIIFSPKLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGFHPMADGIALEGLRLISEWLPRAVADGSDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 695 pIAREKVHNAATIAGIAFANAfLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNAndnptkqtafsqyasPQARRRYA 774
Cdd:cd14861 236 -EARGEMMMAALMGAVAFQKG-LGAVHALAHALGALYGLHHGLLNAILLPYVLRFNR---------------PAVEDKLA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 775 EVADHLSLSQAGDrtaqkiERLLTWLEELKIALDIPLSIQAAGIPEADflakLDQLSIEAFDDQCTGANPRYPLISELKE 854
Cdd:cd14861 299 RLARALGLGLGGF------DDFIAWVEDLNERLGLPATLSELGVTEDD----LDELAELALADPCHATNPRPVTAEDYRA 368
|
....*
gi 46912724 855 VLTSA 859
Cdd:cd14861 369 LLREA 373
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
455-856 |
2.92e-80 |
|
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: 264.06 E-value: 2.92e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 455 KLPKSIYFRRGSLPIaLSDL---EGKKRAFLVTDRFLFNNGYADDVVKLLKAQGIEVqtFFDVEADPTLSIVEKGAEAMK 531
Cdd:cd08196 4 YQPVKIIFGEGILKE-LPDIikeLGGKRGLLVTDPSFIKSGLAKRIVESLKGRIVAV--FSDVEPNPTVENVDKCARLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 532 SFQPDVIIALGGGSPMDAAKIMWVMYEHPEthfeelamrfmDIRKRIYKFPKMGKKA-ELVCITTTSGTGSEVTPFAVVT 610
Cdd:cd08196 81 ENGADFVIAIGGGSVLDTAKAAACLAKTDG-----------SIEDYLEGKKKIPKKGlPLIAIPTTAGTGSEVTPVAVLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 611 DDKTGAKYPLADYELTPHMAIVDANLVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPSSYAN 690
Cdd:cd08196 150 DKEKGKKAPLVSPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSINHQPISDALALEAAKLVLENLEKAYNN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 691 GaNDPIAREKVHNAATIAGIAFANAFLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNANDNPTKQTAFSqyaspqar 770
Cdd:cd08196 230 P-NDKEAREKMALASLLAGLAFSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNAEALPGRLDELA-------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 771 rRYAEVADHLSLSQAgdrtaqkierlltwLEELKIALDIPLSIQAAGIPEADflakLDQLSIEAFDDQCTGANPRYPLIS 850
Cdd:cd08196 301 -KQLGFKDAEELADK--------------IEELKKRIGLRTRLSELGITEED----LEEIVEESFHPNRANNNPVEVTKE 361
|
....*.
gi 46912724 851 ELKEVL 856
Cdd:cd08196 362 DLEKLL 367
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
476-855 |
2.28e-78 |
|
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: 259.40 E-value: 2.28e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 476 GKKRAFLVTDRFLFNNGYADDVVKLLKAQGIEVQTFFDVEADPTLSIVEKGAEAMKSFQPDVIIALGGGSPMDAAKIMWV 555
Cdd:cd17814 25 GARKVLVVTDPGVIKAGWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAELYREEGCDGIVAVGGGSPIDCAKGIGI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 556 MYEHPethfeelamrfMDIRKR--IYKFPKMGkkAELVCITTTSGTGSEVTPFAVVTDDKTGAKYPLADYELTPHMAIVD 633
Cdd:cd17814 105 VVSNG-----------GHILDYegVDKVRRPL--PPLICIPTTAGSSADVSQFAIITDTERRVKMAIISKTLVPDVSLID 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 634 ANLVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPSSYANgANDPIAREKVHNAATIAGIAFA 713
Cdd:cd17814 172 PETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDLHALEAIRLISENLPKAVAD-PDDLEAREKMMLASLQAGLAFS 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 714 NAFLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNAndnptkqtafsqyasPQARRRYAEVADHLSLSQAGDRTAQKI 793
Cdd:cd17814 251 NASLGAVHAMAHSLGGLLDLPHGECNALLLPHVIRFNF---------------PAAPERYRKIAEAMGLDVDGLDDEEVA 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46912724 794 ERLLTWLEELKIALDIPLSIQAAGIPEADflakLDQLSIEAFDDQCTGANPRYPLISELKEV 855
Cdd:cd17814 316 ERLIEAIRDLREDLGIPETLSELGVDEED----IPELAKRAMKDPCLVTNPRRPTREDIEEI 373
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
457-829 |
6.82e-78 |
|
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: 258.21 E-value: 6.82e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 457 PKSIYFRRGS---LPIALSDLeGKKRAFLVTDRFLFNNGYADDVVKLLKAQGIEVQTFFDVEADPTLSIVEKGAEAMKSF 533
Cdd:cd08193 4 VPRIICGAGAaarLGELLREL-GARRVLLVTDPGLVKAGLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQAREA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 534 QPDVIIALGGGSPMDAAKIMWVmyehpethfeeLAMRFMDIRkRIYKFPKM-GKKAELVCITTTSGTGSEVTPFAVVTDD 612
Cdd:cd08193 83 GADGVIGFGGGSSMDVAKLVAL-----------LAGSDQPLD-DIYGVGKAtGPRLPLILVPTTAGTGSEVTPISIVTTG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 613 kTGAKYPLADYELTPHMAIVDANLVMNMPRSLTAFGGYDAVTHALEAYVS-VLANEYSDGQALQALKMLKEYLPSSYANG 691
Cdd:cd08193 151 -ETEKKGVVSPQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSrHKKNPISDALAREALRLLGANLRRAVEDG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 692 aNDPIAREKVHNAATIAGIAFANAFLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNAndnptkqtafsqyasPQARR 771
Cdd:cd08193 230 -SDLEAREAMLLGSMLAGQAFANAPVAAVHALAYPLGGHFHVPHGLSNALVLPHVLRFNL---------------PAAEA 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 46912724 772 RYAEVADHLSLSQAGDRTAQKIERLLTWLEELKIALDIPLSIQAAGIPEADfLAKLDQ 829
Cdd:cd08193 294 LYAELARALLPGLAFGSDAAAAEAFIDALEELVEASGLPTRLRDVGVTEED-LPMLAE 350
|
|
| lactal_redase |
TIGR02638 |
lactaldehyde reductase; This clade of genes encoding iron-containing alcohol dehydrogenase ... |
456-855 |
4.20e-76 |
|
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: 253.51 E-value: 4.20e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 456 LPKSIYFRRGSLPIALSDLE--GKKRAFLVTDRFLFNNGYADDVVKLLKAQGIEVQTFFDVEADPTLSIVEKGAEAMKSF 533
Cdd:TIGR02638 6 LNETSYFGAGAIEDIVDEVKrrGFKKALVVTDKDLIKFGVADKVTDLLDEAGIAYELFDEVKPNPTITVVKAGVAAFKAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 534 QPDVIIALGGGSPMDAAKIMWVMYEHPEthfeelamrFMDIRKRIYKFPKMGKKAELVCITTTSGTGSEVTPFAVVTDDK 613
Cdd:TIGR02638 86 GADYLIAIGGGSPIDTAKAIGIISNNPE---------FADVRSLEGVAPTKKPGVPIIAIPTTAGTAAEVTINYVITDEE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 614 TGAKYPLADYELTPHMAIVDANLVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPSSYANGaN 693
Cdd:TIGR02638 157 NKRKFVCVDPHDIPDVAVIDAEMMYSMPKSLTAATGMDALTHAIEGYITKGAWELTDMLHLKAIEIIARWLRSAVEGG-K 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 694 DPIAREKVHNAATIAGIAFANAFLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNAndnptkqtafsqyasPQARRRY 773
Cdd:TIGR02638 236 DLEAREQMALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEFNA---------------EFTGEKY 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 774 AEVADHLSLSQAGDRTAQKIERLLTWLEELKIALDIPLSIQAAGIPEADflakLDQLSIEAFDDQCTGANPRYPLISELK 853
Cdd:TIGR02638 301 REIAKAMGVKTEGMSDEEARDAAVEAVKTLSKRVGIPEGLSELGVKEED----IPALAEAALADVCTGGNPRETTVEEIE 376
|
..
gi 46912724 854 EV 855
Cdd:TIGR02638 377 EL 378
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
457-857 |
8.36e-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 domains. Proteins of this family have not been characterized.
Pssm-ID: 341462 [Multi-domain] Cd Length: 377 Bit Score: 249.73 E-value: 8.36e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 457 PKSIYFRRGS---LPIALSDLEgkKRAFLVTDRFLFNNGYADDVVKLLKAQGIEVqTFFDVEADPTLSIVEKGAEAMKSF 533
Cdd:cd08183 1 PPRIVFGRGSlqeLGELAAELG--KRALLVTGRSSLRSGRLARLLEALEAAGIEV-ALFSVSGEPTVETVDAAVALAREA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 534 QPDVIIALGGGSPMDAAKIMWVMYEHPEThfeelAMRFMDIRKRiyKFPKMGKKAELVCITTTSGTGSEVTPFAVVTDDK 613
Cdd:cd08183 78 GCDVVIAIGGGSVIDAAKAIAALLTNEGS-----VLDYLEVVGK--GRPLTEPPLPFIAIPTTAGTGSEVTKNAVLSSPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 614 TGAKYPLADYELTPHMAIVDANLVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPSSYANGaN 693
Cdd:cd08183 151 HGVKVSLRSPSMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTDALAREGLRLAARSLRRAYEDG-E 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 694 DPIAREKVHNAATIAGIAFANAFLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNAndnptkQTAFSQYASPQARRRY 773
Cdd:cd08183 230 DLEAREDMALASLLGGLALANAGLGAVHGLAGPLGGMFGAPHGAICAALLPPVLEANL------RALREREPDSPALARY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 774 AEVADHLslsqAGDRTAQkIERLLTWLEELKIALDIPlSIQAAGIPEADFlaklDQLSIEAFDDQCTGANPRYPLISELK 853
Cdd:cd08183 304 RELAGIL----TGDPDAA-AEDGVEWLEELCEELGIP-RLSEYGLTEEDF----PEIVEKARGSSSMKGNPIELSDEELL 373
|
....
gi 46912724 854 EVLT 857
Cdd:cd08183 374 EILE 377
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
456-860 |
1.68e-71 |
|
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: 241.36 E-value: 1.68e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 456 LPKSIYFRRGS---LPIALSDLegKKRAFLVTDRFLFNNGYADDVVKLLKAQGIEVQTFFDVEADPTLSIVEKGAEAMKS 532
Cdd:cd08191 3 SPSRLLFGPGArraLGRVAARL--GSRVLIVTDPRLASTPLVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 533 FQPDVIIALGGGSPMDAAKIMWVMYEH---PETHFEElamrfmdirkriYKFPkmGKKAELVCITTTSGTGSEVTPFAVV 609
Cdd:cd08191 81 FDPDVVIGLGGGSNMDLAKVVALLLAHggdPRDYYGE------------DRVP--GPVLPLIAVPTTAGTGSEVTPVAVL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 610 TDDKTGAKYPLADYELTPHMAIVDANLVMNMPRSLTAFGGYDAVTHALEAY---------------VSVLANEYSDGQAL 674
Cdd:cd08191 147 TDPARGMKVGVSSPYLRPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYtardfppfprldpdpVYVGKNPLTDLLAL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 675 QALKMLKEYLPSSYANGANDPiAREKVHNAATIAGIAFANAFLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNAndn 754
Cdd:cd08191 227 EAIRLIGRHLPRAVRDGDDLE-ARSGMALAALLAGLAFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLPYVMRFNR--- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 755 ptkqtafsqyasPQARRRYAEVADHLSLsQAGDRTAQKIERLLTWLEELKIALDIPLSIQAAGIPEADflakLDQLSIEA 834
Cdd:cd08191 303 ------------PARAAELAEIARALGV-TTAGTSEEAADRAIERVEELLARIGIPTTLADLGVTEAD----LPGLAEKA 365
|
410 420
....*....|....*....|....*..
gi 46912724 835 FDDQ-CTGANPRYPLISELKEVLTSAY 860
Cdd:cd08191 366 LSVTrLIANNPRPPTEEDLLRILRAAF 392
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
476-860 |
1.19e-70 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 238.74 E-value: 1.19e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 476 GKKRAFLVTDRFLFNNGYADDVVKLLKAQGIEVQTFFDVEADPTLSIVEKGAEAMKSFQPDVIIALGGGSPMDAAKIMWV 555
Cdd:PRK10624 29 GFKKALIVTDKTLVKCGVVAKVTDVLDAAGLAYEIYDGVKPNPTIEVVKEGVEVFKASGADYLIAIGGGSPQDTCKAIGI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 556 MYEHPEthfeelamrFMDIRKRIYKFPKMGKKAELVCITTTSGTGSEVTPFAVVTDDKTGAKYPLADYELTPHMAIVDAN 635
Cdd:PRK10624 109 ISNNPE---------FADVRSLEGVAPTKKPSVPIIAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIPQVAFVDAD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 636 LVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPSSYangANDPIAREKVHNAATIAGIAFANA 715
Cdd:PRK10624 180 MMDSMPPGLKAATGVDALTHAIEGYITRGAWALTDMLHLKAIEIIAGALRGAV---AGDKEAGEGMALGQYIAGMGFSNV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 716 FLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNAndnptkqtafsqyasPQARRRYAEVA-------DHLSLSQAGDR 788
Cdd:PRK10624 257 GLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEYNA---------------DFTGEKYRDIAramgvkvEGMSLEEARNA 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46912724 789 TAQKIERlltwleeLKIALDIPLSIQAAGIPEADflakLDQLSIEAFDDQCTGANPRYPLISELKEVLTSAY 860
Cdd:PRK10624 322 AVEAVKA-------LNRDVGIPPHLRDVGVKEED----IPALAQAAFDDVCTGGNPREATLEDIVELYKKAW 382
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
460-825 |
1.19e-70 |
|
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: 238.28 E-value: 1.19e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 460 IYFRRGSLPiALSDL---EGKKRAFLVTDRFLFNNGYADDVVKLLkAQGIEVQTFFDVEADPTLSIVEKGAEAMKSFQPD 536
Cdd:cd08182 4 IIFGPGALA-ELKDLlggLGARRVLLVTGPSAVRESGAADILDAL-GGRIPVVVFSDFSPNPDLEDLERGIELFRESGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 537 VIIALGGGSPMDAAKIMWVMYEHPETHFEELAmrfmDIRKRIYKfpkmgKKAELVCITTTSGTGSEVTPFAVVTDDKTGA 616
Cdd:cd08182 82 VIIAVGGGSVIDTAKAIAALLGSPGENLLLLR----TGEKAPEE-----NALPLIAIPTTAGTGSEVTPFATIWDEAEGK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 617 KYPLADYELTPHMAIVDANLVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPsSYANGANDPI 696
Cdd:cd08182 153 KYSLAHPSLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYALRAIRLILENLP-LLLENLPNLE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 697 AREKVHNAATIAGIAFANAFLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNAndnptkqtafSQYASPQARRRYAEV 776
Cdd:cd08182 232 AREAMAEASLLAGLAISITKTTAAHAISYPLTSRYGVPHGHACALTLPAVLRYNA----------GADDECDDDPRGREI 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 46912724 777 ADHLSLSQAGDrTAQKIERLLTwleelkiALDIPLSIQAAGIPEADFLA 825
Cdd:cd08182 302 LLALGASDPAE-AAERLRALLE-------SLGLPTRLSEYGVTAEDLEA 342
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
459-860 |
1.36e-68 |
|
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: 233.98 E-value: 1.36e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 459 SIYFRRGSLPIALSDLE--GKKRAFLVTDRFLFNNGYADDVVKLLKAQGIEVQTFFDVEADPTLSIVEKGAEAMKSFQPD 536
Cdd:cd08190 3 NIRFGPGATRELGMDLKrlGAKKVLVVTDPGLAKLGLVERVLESLEKAGIEVVVYDGVRVEPTDESFEEAIEFAKEGDFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 537 VIIALGGGSPMDAAKIMWVMYEHPETHFEelamrfmDIRKRIYK-FPKMGKKAELVCITTTSGTGSEVTPFAVVTDDKTG 615
Cdd:cd08190 83 AFVAVGGGSVIDTAKAANLYATHPGDFLD-------YVNAPIGKgKPVPGPLKPLIAIPTTAGTGSETTGVAIFDLEELK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 616 AKYPLADYELTPHMAIVDANLVMNMPRSLTAFGGYDAVTHALEAYVSVL------------------ANEYSDGQALQAL 677
Cdd:cd08190 156 VKTGISSRYLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTARPynarprpanpderpayqgSNPISDVWAEKAI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 678 KMLKEYLPSSYANGANDPiAREKVHNAATIAGIAFANAFLGVCHSMAHKVGA-------------EFHVPHGLANALLIS 744
Cdd:cd08190 236 ELIGKYLRRAVNDGDDLE-ARSNMLLASTLAGIGFGNAGVHLPHAMAYPIAGlvkdyrppgypvdHPHVPHGLSVALTAP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 745 NTIRYNANDNPtkqtafsqyaspqarRRYAEVADHLSLSQAGDRTAQKIERLLTWLEELKIALDIPLSIQAAGIPEADfl 824
Cdd:cd08190 315 AVFRFTAPACP---------------ERHLEAAELLGADTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSEDD-- 377
|
410 420 430
....*....|....*....|....*....|....*..
gi 46912724 825 akLDQLSIEAFDDQ-CTGANPRYPLISELKEVLTSAY 860
Cdd:cd08190 378 --IPALVEGTLPQQrLLKLNPRPVTEEDLEEIFEDAL 412
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
455-757 |
5.13e-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: 213.99 E-value: 5.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 455 KLPKSIYFRRGSLpIALSDL---EGKKrAFLVTDRF-LFNNGYADDVVKLLKAQGIEVQTFFDVEADPTLSIVEKGAEAM 530
Cdd:cd08181 2 YMPTKVYFGKNCV-EKHADElaaLGKK-ALIVTGKHsAKKNGSLDDVTEALEENGIEYFIFDEVEENPSIETVEKGAELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 531 KSFQPDVIIALGGGSPMDAAKIMWVMYEHPEtHFEELamrfmdirkriYKFPKMGKKAELVCITTTSGTGSEVTPFAVVT 610
Cdd:cd08181 80 RKEGADFVIGIGGGSPLDAAKAIALLAANKD-GDEDL-----------FQNGKYNPPLPIVAIPTTAGTGSEVTPYSILT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 611 DDKTGAKYPLADYELTPHMAIVDANLVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPsSYAN 690
Cdd:cd08181 148 DHEKGTKKSFGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSVKATPLSDALALEALRLIGECLP-NLLG 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46912724 691 GANDPIAREKVHNAATIAGIAFANAFLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNANDNPTK 757
Cdd:cd08181 227 DELDEEDREKLMYASTLAGMVIAQTGTTLPHGLGYPLTYFKGIPHGRANGILLPAYLKLCEKQEPEK 293
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
476-844 |
6.70e-56 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 197.87 E-value: 6.70e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 476 GKKRAFLVTDRFLFNNGYADDVVKLLKAQGIEVQTFFDVEADPTLSIVEKGAEAMKSFQPDVIIALGGGSPMDAAKIMWV 555
Cdd:PRK09860 30 GFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKENNCDSVISLGGGSPHDCAKGIAL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 556 myehpethfeeLAMRFMDIRKriYKFPKMGKKAEL--VCITTTSGTGSEVTPFAVVTDDKTGAKYPLADYELTPHMAIVD 633
Cdd:PRK09860 110 -----------VAANGGDIRD--YEGVDRSAKPQLpmIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTPLLSVND 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 634 ANLVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPSSYANGANdPIAREKVHNAATIAGIAFA 713
Cdd:PRK09860 177 SSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSN-AKAREAMAYAQFLAGMAFN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 714 NAFLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNandnptkqtafSQYASPQARrryaEVADHLSLSQAGDRTAQKI 793
Cdd:PRK09860 256 NASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFN-----------SKVAAARLR----DCAAAMGVNVTGKNDAEGA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 46912724 794 ERLLTWLEELKIALDIPLSIQAAGIPEADFlaklDQLSIEAFDDQCTGANP 844
Cdd:PRK09860 321 EACINAIRELAKKVDIPAGLRDLNVKEEDF----AVLATNALKDACGFTNP 367
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
14-446 |
9.09e-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: 197.07 E-value: 9.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 14 ARVKAAQQEFATFSQEQVDKIFRAASLAANNARIPLAQQAVAESG--MGIVEDKVIKNHFASEFIYNKYKDEKTCGILEE 91
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGkpIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 92 NEEFGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVldaaVAAGAPKNIIGWID 171
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELL----QEAGLPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 172 QPSVELSNALMKHNDINLILATGGPGMVKAAY----SSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCA 247
Cdd:cd06534 157 GGGDEVGAALLSHPRVDKISFTGSTAVGKAIMkaaaENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 248 SEQAVIVMDEVYDEVKARFashngyvlskaeadkvrKILLINgnlnadivgqpatkiaemagitVPADTKIligegdevk 327
Cdd:cd06534 237 AASRLLVHESIYDEFVEKL-----------------VTVLVD----------------------VDPDMPI--------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 328 yedefAHEKLS-PTLGMFRASSFENAVEqactMVDIGGIGHTSGLYTNqdvNKDRIKYFGDKMKTARILVNIPTTHGGig 406
Cdd:cd06534 269 -----AQEEIFgPVLPVIRFKDEEEAIA----LANDTEYGLTAGVFTR---DLNRALRVAERLRAGTVYINDSSIGVG-- 334
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 46912724 407 dlynfnVAPSLTLGCGSWGGNSiSENVGPKHLINKKTVAK 446
Cdd:cd06534 335 ------PEAPFGGVKNSGIGRE-GGPYGLEEYTRTKTVVI 367
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
476-859 |
8.16e-52 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 186.77 E-value: 8.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 476 GKKRAFLVTDRFLFNNGYADDVVKLLKAQGIEVQTFFDVEADPTLSIVEKGAEAMKSFQPDVIIALGGGSPMDAAKIMWV 555
Cdd:PRK15454 48 GLKHLFVMADSFLHQAGMTAGLTRSLAVKGIAMTLWPCPVGEPCITDVCAAVAQLRESGCDGVIAFGGGSVLDAAKAVAL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 556 MYEHPETHFEELAMRfMDIRKRIykfpkmgkkaELVCITTTSGTGSEVTPFAVVTDDKTGAKYPLADYELTPHMAIVDAN 635
Cdd:PRK15454 128 LVTNPDSTLAEMSET-SVLQPRL----------PLIAIPTTAGTGSETTNVTVIIDAVSGRKQVLAHASLMPDVAILDAA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 636 LVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPSSYANGaNDPIAREKVHNAATIAGIAFANA 715
Cdd:PRK15454 197 LTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGAIAMIGKSLPKAVGYG-HDLAARESMLLASCMAGMAFSSA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 716 FLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNandnptkqtafsqyaSPQARRRYAEVADHLSLSQAGDRTAqkier 795
Cdd:PRK15454 276 GLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEFN---------------RMVCRERFSQIGRALRTKKSDDRDA----- 335
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46912724 796 lLTWLEELKIALDIPLSIQAAGIPEADFLAkldqLSIEAFDDQCTGANPRYPLISELKEVLTSA 859
Cdd:PRK15454 336 -INAVSELIAEVGIGKRLGDVGATSAHYGA----WAQAALEDICLRSNPRTASLEQIVGLYAAA 394
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
457-859 |
2.46e-45 |
|
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: 167.81 E-value: 2.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 457 PKSIYFRRGSLPIALSDLE--GKKRAFLVTDRFLFNNgyADDVVKLLKAQGIE-VQTFFDVEADPTLSIVEKGAEAMKSF 533
Cdd:cd08192 1 LERVSYGPGAVEALLHELAtlGASRVFIVTSKSLATK--TDVIKRLEEALGDRhVGVFSGVRQHTPREDVLEAARAVREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 534 QPDVIIALGGGSPMDAAKIMWVMYEHPETHFEELAMRFMDIRKRIYkfpKMGKKAELVCITTT-SgtGSEVTPFAVVTDD 612
Cdd:cd08192 79 GADLLVSLGGGSPIDAAKAVALALAEDVTDVDQLDALEDGKRIDPN---VTGPTLPHIAIPTTlS--GAEFTAGAGATDD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 613 KTGAKYPLADYELTPHMAIVDANLVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPsSYANGA 692
Cdd:cd08192 154 DTGHKQGFAHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETLCSPQATPFVDALALKALRLLFEGLP-RSKADP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 693 NDPIAREKVHNAATIAGIAFANAF-LGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNANDNPTKqtafsqyaspQARR 771
Cdd:cd08192 233 EDLEARLKCQLAAWLSLFGLGSGVpMGASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAPVNAER----------QRLI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 772 RYAEVADHLSLSQAGDRTAQKIERLLTwleelkiALDIPLSIQAAGIPEADFlaklDQLSIEAFDDQCTGANPRyPLIS- 850
Cdd:cd08192 303 ARALGLVTGGLGREAADAADAIDALIR-------ELGLPRTLRDVGVGRDQL----EKIAENALTDVWCRTNPR-PITDk 370
|
410
....*....|
gi 46912724 851 -ELKEVLTSA 859
Cdd:cd08192 371 dDVLEILESA 380
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
471-749 |
3.95e-42 |
|
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: 158.58 E-value: 3.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 471 LSDLeGKKRAFLVTDRFLFN-NGYADDVVKLLKAQGIEVQTFFDVEADPTLSIVEKGAEAMKSFQPDVIIALGGGSPMDA 549
Cdd:cd08186 18 LKDL-GIDKVIIVTGRSSYKkSGAWDDVEKALEENGIEYVVYDKVTPNPTVDQADEAAKLARDFGADAVIAIGGGSPIDT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 550 AKIMWVMYEHPETHFEELamrfmdirkriYKFPKMGKKA-ELVCITTTSGTGSEVTPFAVVTDDKTGAKYPLADYELTPH 628
Cdd:cd08186 97 AKSVAVLLAYGGKTARDL-----------YGFRFAPERAlPLVAINLTHGTGSEVDRFAVATIPEKGYKPGIAYDCIYPL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 629 MAIVDANLVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPSSYANgANDPIAREKVHNAATIA 708
Cdd:cd08186 166 YAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAIRLIAEYLPRALAN-PKDLEARYWLLYASMIA 244
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 46912724 709 GIAFANAFLGVCHSMAHKV-GAEFHVPHGLANALLISNTIRY 749
Cdd:cd08186 245 GIAIDNGLLHLTHALEHPLsGLKPELPHGLGLALLGPAVVKY 286
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
457-859 |
3.13e-40 |
|
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: 153.16 E-value: 3.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 457 PKSIYFRRGS---LPIALSDLeGKKRAFLVTDRFLfnnGYADDVVKLLKAqGIE---VQTFFDVEADPTLSIVEKGAEAM 530
Cdd:cd14866 5 PLRLFSGRGAlarLGRELDRL-GARRALVVCGSSV---GANPDLMDPVRA-ALGdrlAGVFDGVRPHSPLETVEAAAEAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 531 KSFQPDVIIALGGGSPMDAAKIMWVMYEHPEThFEELAMRFMDirKRIYKFPKMGK-KAELVCITTTSGTGSEVTPFAVv 609
Cdd:cd14866 80 READADAVVAVGGGSAIVTARAASILLAEDRD-VRELCTRRAE--DGLMVSPRLDApKLPIFVVPTTPTTADVKAGSAV- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 610 TDDKTGAKYPLADYELTPHMAIVDANLVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPSsyA 689
Cdd:cd14866 156 TDPPAGQRLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHADPLADATLMHALRLLADGLPR--L 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 690 NGANDPIAREKVHNAATIAGIAFANAFLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNAndnptkqtafsqyasPQA 769
Cdd:cd14866 234 ADDDDPAARADLVLAAVLAGYGTDHTGGGVIHALGHAIGARYGVQNGVVHAILLPHVLRFNA---------------PAT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 770 RRRYAEVADHLSLsqAGDRTAQKIERLLTWLEELKIALDIPLSIQAAGIPEADFlaklDQLSIEAFDDQCTGANPR-YPL 848
Cdd:cd14866 299 DGRLDRLAEALGV--ADAGDEASAAAVVDAVEALLDALGVPTRLRDLGVSREDL----PAIAEAAMDDWFMDNNPRpVPT 372
|
410
....*....|.
gi 46912724 849 ISELKEVLTSA 859
Cdd:cd14866 373 AEELEALLEAA 383
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
455-826 |
1.39e-36 |
|
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: 142.05 E-value: 1.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 455 KLPKSIYFRRGSL---PIALSDLegKKRAFLVTDRFLFNNGYADDVVKLLKAQGIEVQTFFDVEADPTLSIVEKGAEAMK 531
Cdd:cd14864 2 KIPPNIVFGADSLeriGEEVKEY--GSRFLLITDPVLKESGLADKIVSSLEKAGISVIVFDEIPASATSDTIDEAAELAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 532 SFQPDVIIALGGGSPMDAAKIMWVMYEHPethfeelamrfMDIRKRIYKFPKMGKKAELVCITTTSGTGSEVTPFAVVTD 611
Cdd:cd14864 80 KAGADGIIAVGGGKVLDTAKAVAILANND-----------GGAYDFLEGAKPKKKPLPLIAVPTTPRSGFEFSDRFPVVD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 612 DKTGAKYPLADYELTPHMAIVDANLVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPSSYANG 691
Cdd:cd14864 149 SRSREVKLLKAQPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNFFSDALALKAIELVSENLDGALADP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 692 ANDPiAREKVHNAATIAGIAFANAFLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNANDNPTKqtafsqYASPqARR 771
Cdd:cd14864 229 KNTP-AEELLAQAGCLAGLAASSSSPGLATALALAVNSRYKVSKSLVASILLPHVIEYAATSAPDK------YAKI-ARA 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46912724 772 RYAEVADhLSLSQAGDRTAQKIERLL------TWLEELKIALDIP-LSIQAAGIPEADFLAK 826
Cdd:cd14864 301 LGEDVEG-ASPEEAAIAAVEGVRRLIaqlnlpTRLKDLDLASSLEqLAAIAEDAPKLNGLPR 361
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
478-756 |
5.26e-34 |
|
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: 134.65 E-value: 5.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 478 KRAFLVTDRFLFNngyaddvvKLLKAQGIEVQTFFD---VEADPTLSIVEKGAEAMKSFQPDVIIALGGGSPMDAAKIMW 554
Cdd:cd14860 27 KDDLVLTNEYIYE--------PYFEPLNLDCAVIFQekyGTGEPSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAKLLA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 555 VMYEHPethFEELAMRFMDIRKriykfpkmgkKAELVCITTTSGTGSEVTPFAVVTDDKTGAKYPLADYELTPHMAIVDA 634
Cdd:cd14860 99 LKGISP---VLDLFDGKIPLIK----------EKELIIVPTTCGTGSEVTNISIVELTSLGTKKGLAVDELYADKAVLIP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 635 NLVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEylpsSYANGA-NDPIAREKVHN----AATIAG 709
Cdd:cd14860 166 ELLKGLPYKVFATSSIDALIHAIESYLSPKATPYTEMFSYKAIEMILE----GYQEIAeKGEEARFPLLGdfliASNYAG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 46912724 710 IAFANAFLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNANDNPT 756
Cdd:cd14860 242 IAFGNAGCAAVHALSYPLGGKYHVPHGEANYAVFTGVLKNYQEKNPD 288
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
457-860 |
2.40e-25 |
|
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: 108.36 E-value: 2.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 457 PKSIYFRRGSLPIALSDLE--GKKRAFLVTDRFlfNNGYADDVVKLLKAQGIEVqtFFDVEADPTLSIVEKGAEAMKSFQ 534
Cdd:cd08177 1 PQRVVFGAGTLAELAEELErlGARRALVLSTPR--QRALAERVAALLGDRVAGV--FDGAVMHVPVEVAERALAAAREAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 535 PDVIIALGGGSPMDAAKImwvmyehpethfeeLAMRfmdirkriYKFPkmgkkaeLVCITTTSgTGSEVTPFAVVTDDkt 614
Cdd:cd08177 77 ADGLVAIGGGSAIGLAKA--------------IALR--------TGLP-------IVAVPTTY-AGSEMTPIWGETED-- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 615 GAKYPLADYELTPHMAIVDANLVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPSSYANGAnD 694
Cdd:cd08177 125 GVKTTGRDPRVLPRTVIYDPDLTLGLPAALSVASGLNALAHAVEALYAPDANPITSLLAEEGIRALARALPRLVADPS-D 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 695 PIAREKVHNAATIAGIAFANAFLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNANdnptkqtafsqyASPQARRRya 774
Cdd:cd08177 204 LEARSDALYGAWLAGVVLGSVGMGLHHKLCHVLGGTFDLPHAETHAVVLPHVLAYNAP------------AAPDAMAR-- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 775 eVADHLSLSQAGDRtaqkierlltwLEELKIALDIPLSIQAAGIPEADfLAKLDQLSIEAfddqcTGANPRyPLISE-LK 853
Cdd:cd08177 270 -LARALGGGDAAGG-----------LYDLARRLGAPTSLRDLGMPEDD-IDRAADLALAN-----PYPNPR-PVERDaLR 330
|
....*..
gi 46912724 854 EVLTSAY 860
Cdd:cd08177 331 ALLERAW 337
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
457-764 |
2.10e-24 |
|
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: 103.98 E-value: 2.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 457 PKSIYFRRGSLP-IALSDLEGKKRAFLVTDRFLfNNGYADDVVKLLKAqGIEVQTFFDVEADPTLSIVEKGAEAMKSFQP 535
Cdd:cd07766 1 PTRIVFGEGAIAkLGEIKRRGFDRALVVSDEGV-VKGVGEKVADSLKK-GLAVAIFDFVGENPTFEEVKNAVERARAAEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 536 DVIIALGGGSPMDAAKIMWVMyehpethfeelamrfmdirkriykfpkMGKKAELVCITTTSGTGSEVTPFAVVTDDKTG 615
Cdd:cd07766 79 DAVIAVGGGSTLDTAKAVAAL---------------------------LNRGIPFIIVPTTASTDSEVSPKSVITDKGGK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 616 AKYplADYELTPHMAIVDANLVMNMPRSLTAFGGYDAVTHALEayvsvlaneysdgqalqalkmlkeylpssyangandp 695
Cdd:cd07766 132 NKQ--VGPHYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVE------------------------------------- 172
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 696 iaREKVHNAATIAGIAFANA-FLGVCHSMAHKVGAEFHVPHGLANALLISNTIRYNANDNPTKQTAFSQY 764
Cdd:cd07766 173 --LEKVVEAATLAGMGLFESpGLGLAHAIGHALTAFEGIPHGEAVAVGLPYVLKVANDMNPEPEAAIEAV 240
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
462-739 |
1.92e-23 |
|
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: 102.73 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 462 FRRGSLPIALSDLEGKKRA-----FLVTDRFLFNNGYADDvvklLKAQGIEVQTFFDVEADPTLSIVEKGAEAMKSFQ-- 534
Cdd:cd08184 6 FGRGSFDQLGELLAERRKSnndyvVFFIDDVFKGKPLLDR----LPLQNGDLLIFVDTTDEPKTDQIDALRAQIRAENdk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 535 -PDVIIALGGGSPMDAAKIMWVMYEHPE--THFE--ELAMRfmdirKRIYKfpkmgkkaelVCITTTSGTGSEVTPFAVV 609
Cdd:cd08184 82 lPAAVVGIGGGSTMDIAKAVSNMLTNPGsaADYQgwDLVKN-----PGIYK----------IGVPTLSGTGAEASRTAVL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 610 TDD--KTGAKyplADYELTPHmAIVDANLVMNMPRSLTAFGGYDAVTHALEAYVSVLANEYSDGQALQALKMLKEYLPSS 687
Cdd:cd08184 147 TGPekKLGIN---SDYTVFDQ-VILDPELIATVPRDQYFYTGMDCYIHCVESLNGTYRNAFGDAYAEKALELCRDVFLSD 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 46912724 688 YANGANDpiaREKVHNAATIAGIAFANAFLGVCHSMAHKVGAEFHVPHGLAN 739
Cdd:cd08184 223 DMMSPEN---REKLMVASYLGGSSIANSQVGVCHALSYGLSVVLGTHHGVAN 271
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
7-407 |
1.00e-21 |
|
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: 99.53 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 7 AELDAMVARVKAAQQEFATFSQEQVDKI-FRAASLAANNARiPLAQQAVAESGMGIVE-----DKVIKN-HFASEFIyNK 79
Cdd:pfam00171 29 EDVDAAIAAARAAFPAWRKTPAAERAAIlRKAADLLEERKD-ELAELETLENGKPLAEargevDRAIDVlRYYAGLA-RR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 80 YKDEktcgILEENEEFGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVLDAava 159
Cdd:pfam00171 107 LDGE----TLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEA--- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 160 aGAPKNIIGWIDQPSVELSNALMKHNDINLILATGGPG----MVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVL 235
Cdd:pfam00171 180 -GLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAvgrhIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 236 MSKTFDNGVVCASEQAVIVMDEVYDEVKARFA---------------SHNGYVLSKAEADKVRKILlingnlnadivgqp 300
Cdd:pfam00171 259 FGAFGNAGQVCTATSRLLVHESIYDEFVEKLVeaakklkvgdpldpdTDMGPLISKAQLERVLKYV-------------- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 301 atKIAEMAGITVPADTKILIGEG--------DEVKYEDEFAHEKL-SPTLGMFRASSFENAVEQA--CTMvdiggiGHTS 369
Cdd:pfam00171 325 --EDAKEEGAKLLTGGEAGLDNGyfveptvlANVTPDMRIAQEEIfGPVLSVIRFKDEEEAIEIAndTEY------GLAA 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 46912724 370 GLYTNqdvNKDRIKYFGDKMKTARILVNIPTT-------HGGIGD 407
Cdd:pfam00171 397 GVFTS---DLERALRVARRLEAGMVWINDYTTgdadglpFGGFKQ 438
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
10-404 |
1.13e-20 |
|
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: 95.74 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 10 DAMVARVKAAQQEFATFSQEQVDKIFRAAS--LAANNARIplAQQAVAESGMGIVE-----DKVIKN-HFASEFIYNKYK 81
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLAdlLEERREEL--AALETLETGKPIEEalgevARAADTfRYYAGLARRLHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 82 DEktcgILEENEEFGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVLDAavaaG 161
Cdd:cd07078 79 EV----IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEA----G 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 162 APKNIIGWIDQPSVELSNALMKHNDINLILATGGPG----MVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMS 237
Cdd:cd07078 151 LPPGVLNVVTGDGDEVGAALASHPRVDKISFTGSTAvgkaIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 238 KTFDNGVVCASEQAVIVMDEVYDEVKARFASH-------NGY--------VLSKAEADKVRKilLINgnlnadivgqpat 302
Cdd:cd07078 231 AFGNAGQVCTAASRLLVHESIYDEFVERLVERvkalkvgNPLdpdtdmgpLISAAQLDRVLA--YIE------------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 303 kIAEMAGITVPADTKILIGEG---------DEVKYEDEFAHEKL-SPTLGMFRASSFENAVEQACTMVDiggiGHTSGLY 372
Cdd:cd07078 296 -DAKAEGAKLLCGGKRLEGGKgyfvpptvlTDVDPDMPIAQEEIfGPVLPVIPFKDEEEAIELANDTEY----GLAAGVF 370
|
410 420 430
....*....|....*....|....*....|..
gi 46912724 373 TNqdvNKDRIKYFGDKMKTARILVNIPTTHGG 404
Cdd:cd07078 371 TR---DLERALRVAERLEAGTVWINDYSVGAE 399
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
7-407 |
1.11e-18 |
|
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: 90.19 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 7 AELDAMVARVKAAQQEFATFS-QEQVDKIFRAASL-AANNARipLAQQAVAESGMGIVE-----DKVIKN--HFASEfiY 77
Cdd:COG1012 43 EDVDAAVAAARAAFPAWAATPpAERAAILLRAADLlEERREE--LAALLTLETGKPLAEargevDRAADFlrYYAGE--A 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 78 NKYKDEKTCGILEENEefgTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVLDAa 157
Cdd:COG1012 119 RRLYGETIPSDAPGTR---AYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEA- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 158 vaaGAPK---NII-GwidqPSVELSNALMKHNDINLILATGGPG----MVKAAYSSGKPAIGVGAGNVPVVIDETADIKR 229
Cdd:COG1012 195 ---GLPAgvlNVVtG----DGSEVGAALVAHPDVDKISFTGSTAvgrrIAAAAAENLKRVTLELGGKNPAIVLDDADLDA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 230 AVASVLMSKTFDNGVVCASEQAVIVMDEVYDEVKARFASH-------NGY--------VLSKAEADKVRKILlingnlna 294
Cdd:COG1012 268 AVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAakalkvgDPLdpgtdmgpLISEAQLERVLAYI-------- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 295 divgqpatKIAEMAGITVPADTKILIGEG---------DEVKYEDEFAHEKL-SPTLGMFRASSFENAVEQActmvdIGG 364
Cdd:COG1012 340 --------EDAVAEGAELLTGGRRPDGEGgyfveptvlADVTPDMRIAREEIfGPVLSVIPFDDEEEAIALA-----NDT 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 46912724 365 I-GHTSGLYTNqdvNKDRIKYFGDKMKTARILVNIPTT-------HGGIGD 407
Cdd:COG1012 407 EyGLAASVFTR---DLARARRVARRLEAGMVWINDGTTgavpqapFGGVKQ 454
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
1-397 |
5.76e-18 |
|
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: 87.87 E-value: 5.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 1 MPVTNMAELDAMVARVKAAQQEFATFSQEQVDKIFRAASLAANNARIPLAQQAVAESGMGIVE-----DKVIKN-HFASE 74
Cdd:cd07094 15 VPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDarvevDRAIDTlRLAAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 75 FIYNKYKDEKTCGILEENEEFGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVL 154
Cdd:cd07094 95 EAERIRGEEIPLDATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 155 DaavaAGAPKNIIGWIDQPSVELSNALMKHNDINLILATGGPGM---VKAAYSSGKPAIGVGaGNVPVVIDETADIKRAV 231
Cdd:cd07094 175 E----AGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVgeaLRANAGGKRIALELG-GNAPVIVDRDADLDAAI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 232 ASVLMSKTFDNGVVCASEQAVIVMDEVYDEVKARFASHN---------------GYVLSKAEADKVRKIL---------L 287
Cdd:cd07094 250 EALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVkklkvgdpldedtdvGPLISEEAAERVERWVeeaveagarL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 288 INGNLNADIVGQPAtkIAEmagiTVPADTKILigegdevkyedefAHEKLSPTLGMFRASSFENAVEQACTMvdigGIGH 367
Cdd:cd07094 330 LCGGERDGALFKPT--VLE----DVPRDTKLS-------------TEETFGPVVPIIRYDDFEEAIRIANST----DYGL 386
|
410 420 430
....*....|....*....|....*....|
gi 46912724 368 TSGLYTNqDVNKdrIKYFGDKMKTARILVN 397
Cdd:cd07094 387 QAGIFTR-DLNV--AFKAAEKLEVGGVMVN 413
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
16-401 |
1.29e-16 |
|
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: 83.55 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 16 VKAAQQEFATFSQ----EQVDKIFRAASLAANNARiPLAQQAVAESGMGIVEDKVIKN-------HFASEF--IYNKY-- 80
Cdd:cd07145 27 IEVAEKAKDVMSNlpayKRYKILMKVAELIERRKE-ELAKLLTIEVGKPIKQSRVEVErtirlfkLAAEEAkvLRGETip 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 81 KDEktcgiLEENEEFGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVLDAavaa 160
Cdd:cd07145 106 VDA-----YEYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEA---- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 161 GAPKNIIGWIDQPSVELSNALMKHNDINLILATG----GPGMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLM 236
Cdd:cd07145 177 GLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGstavGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 237 SKtFDN-GVVCASEQAVIVMDEVYDEVKARFashngyvlskaeADKVRKI-----LLINGNLNADIVGQPATKIAEMAGI 310
Cdd:cd07145 257 GR-FENaGQVCNAVKRILVEEEVYDKFLKLL------------VEKVKKLkvgdpLDESTDLGPLISPEAVERMENLVND 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 311 TVPADTKILI-GEGDEVKY------------EDEFAHEKLSPTLGMFRASSFENAVEQActmvDIGGIGHTSGLYTNqDV 377
Cdd:cd07145 324 AVEKGGKILYgGKRDEGSFfpptvlendtpdMIVMKEEVFGPVLPIAKVKDDEEAVEIA----NSTEYGLQASVFTN-DI 398
|
410 420
....*....|....*....|....
gi 46912724 378 NkdRIKYFGDKMKTARILVNIPTT 401
Cdd:cd07145 399 N--RALKVARELEAGGVVINDSTR 420
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
1-384 |
2.25e-16 |
|
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: 82.70 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 1 MPVTNMAELDAMVARVKAAQQEFATFSQEQVDKIFRAASLAANNARIPLAQQAVAESGMgIVEDKVIKNHFASEFI-Y-- 77
Cdd:cd07088 29 VPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGK-TLSLARVEVEFTADYIdYma 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 78 -NKYKDEKTcgILE-ENEEFGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVld 155
Cdd:cd07088 108 eWARRIEGE--IIPsDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELV-- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 156 aaVAAGAPKNIIGWIDQPSVELSNALMKHNDINLILATGGPG-----MVKAAYSSGKPAIGVGaGNVPVVIDETADIKRA 230
Cdd:cd07088 184 --DEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEagqkiMEAAAENITKVSLELG-GKAPAIVMKDADLDLA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 231 VASVLMSKTFDNGVVCASEQAVIVMDEVYDEVKARFashngyvlskaeADKVRKILLinGNLNAD------IVGQPA-TK 303
Cdd:cd07088 261 VKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKL------------VEKMKAVKV--GDPFDAatdmgpLVNEAAlDK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 304 IAEMAGITVPADTKILIG----EGDE-----------VKYEDEFAHEKL-SPTLGMFRASSFENAVEQA--CTMvdiggi 365
Cdd:cd07088 327 VEEMVERAVEAGATLLTGgkrpEGEKgyfyeptvltnVRQDMEIVQEEIfGPVLPVVKFSSLDEAIELAndSEY------ 400
|
410 420
....*....|....*....|....
gi 46912724 366 GHTSGLYTnQDVNK-----DRIKY 384
Cdd:cd07088 401 GLTSYIYT-ENLNTamratNELEF 423
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
98-267 |
1.69e-15 |
|
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: 79.95 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 98 MTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVLDAavaaGAPKNIIGWIDQPSVEL 177
Cdd:cd07149 118 FTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEA----GLPKGALNVVTGSGETV 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 178 SNALMKHNDINLILATGGPGMVKA-AYSSG--KPAIGVGaGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIV 254
Cdd:cd07149 194 GDALVTDPRVRMISFTGSPAVGEAiARKAGlkKVTLELG-SNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFV 272
|
170
....*....|...
gi 46912724 255 MDEVYDEVKARFA 267
Cdd:cd07149 273 HEDIYDEFLERFV 285
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
98-400 |
7.29e-15 |
|
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: 78.16 E-value: 7.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 98 MTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVLDAavaaGAPKNIIGWIDQPSVEL 177
Cdd:cd07131 130 MTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEA----GLPPGVVNVVHGRGEEV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 178 SNALMKHNDINLILATG----GPGMVKAAYSSGKP-AIGVGAGNvPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAV 252
Cdd:cd07131 206 GEALVEHPDVDVVSFTGstevGERIGETCARPNKRvALEMGGKN-PIIVMDDADLDLALEGALWSAFGTTGQRCTATSRL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 253 IVMDEVYDEVKARFashngyvlskaeADKVRKILLINGNLNADIVGqPA------------TKIAEMAGITVPADTKILI 320
Cdd:cd07131 285 IVHESVYDEFLKRF------------VERAKRLRVGDGLDEETDMG-PLineaqlekvlnyNEIGKEEGATLLLGGERLT 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 321 GEGDE------------VKYEDEFAHEKL-SPTLGMFRASSFENAVEqactMVDIGGIGHTSGLYTnQDVNKdrIKYFGD 387
Cdd:cd07131 352 GGGYEkgyfveptvftdVTPDMRIAQEEIfGPVVALIEVSSLEEAIE----IANDTEYGLSSAIYT-EDVNK--AFRARR 424
|
330
....*....|...
gi 46912724 388 KMKTARILVNIPT 400
Cdd:cd07131 425 DLEAGITYVNAPT 437
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
99-269 |
6.68e-14 |
|
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: 75.09 E-value: 6.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 99 TIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRaknsTNAAAKLVLDAAVAAGAPKNIIGWIDQPSVELS 178
Cdd:cd07146 116 TLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEK----TPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIG 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 179 NALMKHNDINLILATGGPGMVK--AAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIVMD 256
Cdd:cd07146 192 DELITHPDVDLVTFTGGVAVGKaiAATAGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHE 271
|
170
....*....|...
gi 46912724 257 EVYDEVKARFASH 269
Cdd:cd07146 272 SVADEFVDLLVEK 284
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
103-378 |
4.66e-13 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 72.08 E-value: 4.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 103 PVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVLDAavaaGAPKNIIGWIDQPSVELSNALM 182
Cdd:PRK10090 71 ALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEI----GLPKGVFNLVLGRGETVGQELA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 183 KHNDINLILATGGPG-----MVKAAYSSGKPAIGVGaGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIVMDE 257
Cdd:PRK10090 147 GNPKVAMVSMTGSVSagekiMAAAAKNITKVCLELG-GKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 258 VYDEVKARFASHNGYVLS--KAEADKVRKILLIngnlNADIVGQPATKI--AEMAGITVPADTKILIGEG--------DE 325
Cdd:PRK10090 226 IYDQFVNRLGEAMQAVQFgnPAERNDIAMGPLI----NAAALERVEQKVarAVEEGARVALGGKAVEGKGyyypptllLD 301
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 46912724 326 VKYEDEFAHEK-LSPTLGMFRASSFENAVEqactMVDIGGIGHTSGLYTnQDVN 378
Cdd:PRK10090 302 VRQEMSIMHEEtFGPVLPVVAFDTLEEAIA----MANDSDYGLTSSIYT-QNLN 350
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
10-407 |
1.77e-12 |
|
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: 70.44 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 10 DAMVArVKAAQQEFATFSQ---EQVDKIFRAASlAANNARIP-LAQQAVAESGmGIVEDKVIKNHFASEFIYN------K 79
Cdd:cd07150 22 DAERA-IAAAYDAFPAWAAttpSERERILLKAA-EIMERRADdLIDLLIDEGG-STYGKAWFETTFTPELLRAaagecrR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 80 YKDEKtcgILEENEEFGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVldaaVA 159
Cdd:cd07150 99 VRGET---LPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIM----EE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 160 AGAPKNIIGWIDQPSVELSNALMKHNDINLILATG----GPGM-VKAAYSSGKPAIGVGaGNVPVVIDETADIKRAVASV 234
Cdd:cd07150 172 AGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGstavGREIaEKAGRHLKKITLELG-GKNPLIVLADADLDYAVRAA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 235 LMSKTFDNGVVCASEQAVIVMDEVYDEVKARFAshngyvlSKAEADKVrkillinGN-LNADIVGQPATKIAEMAGI--- 310
Cdd:cd07150 251 AFGAFMHQGQICMSASRIIVEEPVYDEFVKKFV-------ARASKLKV-------GDpRDPDTVIGPLISPRQVERIkrq 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 311 ---TVPADTKILIGEGDEVKY----------EDE--FAHEKLSPTLGMFRASSFENAVEQActmvDIGGIGHTSGLYTNq 375
Cdd:cd07150 317 vedAVAKGAKLLTGGKYDGNFyqptvltdvtPDMriFREETFGPVTSVIPAKDAEEALELA----NDTEYGLSAAILTN- 391
|
410 420 430
....*....|....*....|....*....|....*....
gi 46912724 376 dvNKDRIKYFGDKMKTARILVNIPTTH-------GGIGD 407
Cdd:cd07150 392 --DLQRAFKLAERLESGMVHINDPTILdeahvpfGGVKA 428
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
95-268 |
9.39e-12 |
|
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: 68.23 E-value: 9.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 95 FGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVLDAAVAAGAPKNIIGwidqPS 174
Cdd:cd07115 109 FLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAGFPAGVLNVVTG----FG 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 175 VELSNALMKHNDINLILATGGPG-----MVKAAYSSGKPAIGVGaGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASE 249
Cdd:cd07115 185 EVAGAALVEHPDVDKITFTGSTAvgrkiMQGAAGNLKRVSLELG-GKSANIVFADADLDAAVRAAATGIFYNQGQMCTAG 263
|
170
....*....|....*....
gi 46912724 250 QAVIVMDEVYDEVKARFAS 268
Cdd:cd07115 264 SRLLVHESIYDEFLERFTS 282
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
102-333 |
2.00e-11 |
|
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: 67.33 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 102 EPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPraknSTNAAAKLVLDAAVAAGAPK---NIIgwidQPSVELS 178
Cdd:cd07090 115 EPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSP----FTPLTALLLAEILTEAGLPDgvfNVV----QGGGETG 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 179 NALMKHNDINLILATG----GPGMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIV 254
Cdd:cd07090 187 QLLCEHPDVAKVSFTGsvptGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFV 266
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46912724 255 MDEVYDEVKARfashngyVLSKAEADKVRKILLINGNLNADIVGQPATKIAEMAGITVPADTKILIGeGDEVKYEDEFA 333
Cdd:cd07090 267 QRSIKDEFTER-------LVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQEGAKVLCG-GERVVPEDGLE 337
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
453-736 |
2.75e-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: 65.96 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 453 WHKLPKSIYFRRG---SLPIALSDLegKKRAFLVTDRFLFNNgYADDVVKLLKAQGIEVQTFFdVEADPTLSIVEKGAEA 529
Cdd:COG0371 2 VIILPRRYVQGEGaldELGEYLADL--GKRALIITGPTALKA-AGDRLEESLEDAGIEVEVEV-FGGECSEEEIERLAEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 530 MKSFQPDVIIALGGGSPMDAAKImwvmyehpethfeeLAMRfmdirkriykfpkmgKKAELVCITTTSGTGSEVTPFAVV 609
Cdd:COG0371 78 AKEQGADVIIGVGGGKALDTAKA--------------VAYR---------------LGLPVVSVPTIASTDAPASPLSVI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 610 -TDDKTGAKY-PLADyelTPHMAIVDANLVMNMPRSLTAFGGYDAVTHALEAYVSVLANE------YSD---GQALQALK 678
Cdd:COG0371 129 yTEDGAFDGYsFLAK---NPDLVLVDTDIIAKAPVRLLAAGIGDALAKWYEARDWSLAHRdlageyYTEaavALARLCAE 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46912724 679 MLKEYLPSSY-ANGANDPI-AREKVHNAATI-AGIAFANAF----LGVCHSMAH---KVGAEFHVPHG 736
Cdd:COG0371 206 TLLEYGEAAIkAVEAGVVTpALERVVEANLLlSGLAMGIGSsrpgSGAAHAIHNgltALPETHHALHG 273
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
98-402 |
3.17e-11 |
|
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: 66.50 E-value: 3.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 98 MTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNStnaAAKLVlDAAVAAGAPKNIIGWIDQPSVEL 177
Cdd:cd07097 130 ETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPAS---AWALV-EILEEAGLPAGVFNLVMGSGSEV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 178 SNALMKHNDINLILATGGPGMVKAAYSSgkpAIGVGA-------GNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQ 250
Cdd:cd07097 206 GQALVEHPDVDAVSFTGSTAVGRRIAAA---AAARGArvqlemgGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASS 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 251 AVIVMDEVYDEVKARfashngyVLSKAEADKVrkillinGN-LNADIVGQPATKIAEMAG------ITVPADTKILIGeG 323
Cdd:cd07097 283 RLIVTEGIHDRFVEA-------LVERTKALKV-------GDaLDEGVDIGPVVSERQLEKdlryieIARSEGAKLVYG-G 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 324 DEVKYEDE--------FA----------HEKLSPTLGMFRASSFENAVEqactMVDIGGIGHTSGLYTNqdvNKDRIKYF 385
Cdd:cd07097 348 ERLKRPDEgyylapalFAgvtndmriarEEIFGPVAAVIRVRDYDEALA----IANDTEFGLSAGIVTT---SLKHATHF 420
|
330
....*....|....*..
gi 46912724 386 GDKMKTARILVNIPTTH 402
Cdd:cd07097 421 KRRVEAGVVMVNLPTAG 437
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
491-765 |
9.50e-11 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 64.82 E-value: 9.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 491 NGYADDVVKLLKaqGIEVQTFFDVEADPTLSIVEKGAEAMKSFQPDVIIALGGGSPMDAAKIMWVMYEHPETH--FEELA 568
Cdd:PRK15138 44 TGVLDQVLDALK--GMDVLEFGGIEPNPTYETLMKAVKLVREEKITFLLAVGGGSVLDGTKFIAAAANYPENIdpWHILE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 569 MRFMDIRKRIykfpKMGkkaelvCITTTSGTGSEVTPFAVVTDDKTGAKYPLADYELTPHMAIVDANLVMNMPRSLTAFG 648
Cdd:PRK15138 122 TGGKEIKSAI----PMG------SVLTLPATGSESNAGAVISRKTTGDKQAFHSPHVQPVFAVLDPVYTYTLPPRQVANG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 649 GYDAVTHALEAYVSVLAN-----EYSDGQALQAL----KMLKEylPSSYANGANdpiarekVHNAATIAGIAFANAflGV 719
Cdd:PRK15138 192 VVDAFVHTVEQYVTYPVDakiqdRFAEGILLTLIeegpKALKE--PENYDVRAN-------VMWAATQALNGLIGA--GV 260
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 46912724 720 CHSMA-HKVGAEFHVPHGL--ANALLISNTIRYNANDNpTKQTAFSQYA 765
Cdd:PRK15138 261 PQDWAtHMLGHELTAMHGLdhAQTLAIVLPALWNEKRD-TKRAKLLQYA 308
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
77-266 |
8.22e-10 |
|
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: 62.16 E-value: 8.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 77 YNKYKDEKTCGILEENEEFGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVLDa 156
Cdd:cd07143 118 YGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPE- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 157 avaAGAPKNIIGWIDQPSVELSNALMKHNDINLILATGGPG-----MVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAV 231
Cdd:cd07143 197 ---AGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLvgrkvMEAAAKSNLKKVTLELGGKSPNIVFDDADLESAV 273
|
170 180 190
....*....|....*....|....*....|....*
gi 46912724 232 ASVLMSKTFDNGVVCASEQAVIVMDEVYDEVKARF 266
Cdd:cd07143 274 VWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRF 308
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
10-296 |
9.25e-10 |
|
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: 61.94 E-value: 9.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 10 DAMVArVKAAQQEF------ATFSQEQVDKIFRAASLAANNARiPLAQQAVAESGMGIVEDKVIKNHFASEF-IYNKYKD 82
Cdd:cd07119 36 DAKRA-IAAARRAFdsgewpHLPAQERAALLFRIADKIREDAE-ELARLETLNTGKTLRESEIDIDDVANCFrYYAGLAT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 83 EKTCGILEENEEFGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVLDaavaAGA 162
Cdd:cd07119 114 KETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEE----AGL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 163 PKNIIGWIDQPSVELSNALMKHNDINLILATGGPG-----MVKAAYSSGKPAIGVGAGNVPVVIDEtADIKRAVASVLMS 237
Cdd:cd07119 190 PAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTAtgrsiMRAAAGNVKKVALELGGKNPNIVFAD-ADFETAVDQALNG 268
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 46912724 238 KTFDNGVVCASEQAVIVMDEVYDEVKARFashngyvlskaeADKVRKILLINGnLNADI 296
Cdd:cd07119 269 VFFNAGQVCSAGSRLLVEESIHDKFVAAL------------AERAKKIKLGNG-LDADT 314
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
23-270 |
1.62e-09 |
|
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: 61.36 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 23 FATFSQEQVDKIfraASLAANNARIPLAQQAVAESGMgivedkviknhFASEFIYNKYKDEKTCGI-LEENEEFGTMTIA 101
Cdd:cd07142 74 FADLLEKHADEL---AALETWDNGKPYEQARYAEVPL-----------AARLFRYYAGWADKIHGMtLPADGPHHVYTLH 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 102 EPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVLDAavaaGAPKNIIGWIDQPSVELSNAL 181
Cdd:cd07142 140 EPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEA----GLPDGVLNIVTGFGPTAGAAI 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 182 MKHNDINLILATGGPG-----MVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIVMD 256
Cdd:cd07142 216 ASHMDVDKVAFTGSTEvgkiiMQLAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHE 295
|
250
....*....|....*...
gi 46912724 257 EVYDEV----KARFASHN 270
Cdd:cd07142 296 SIYDEFvekaKARALKRV 313
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
128-239 |
6.48e-09 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 58.93 E-value: 6.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 128 LKTRNAIIFsphpR----AKNSTNAAAKLVLDAAVAAGAPKNIIGWIDQPSVELSNALMKHND-INLILATGGPGMVKAA 202
Cdd:PRK00197 138 LKSGNAVIL----RggseAIHSNRALVAVIQEALEEAGLPADAVQLVETTDRAAVGELLKLDGyVDVIIPRGGAGLIRRV 213
|
90 100 110
....*....|....*....|....*....|....*...
gi 46912724 203 YSSGK-PAIGVGAGNVPVVIDETADIKRAVASVLMSKT 239
Cdd:PRK00197 214 VENATvPVIEHGDGICHIYVDESADLDKALKIVLNAKT 251
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
90-401 |
7.26e-09 |
|
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: 59.16 E-value: 7.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 90 EENEEFgtmtiAEPVGIICGIVPTTNPTstAIFKSLIS--LKTRNAIIFSPhprAKNSTNAAAKLVlDAAVAAGAPKNII 167
Cdd:cd07124 158 EDNRYV-----YRPLGVGAVISPWNFPL--AILAGMTTaaLVTGNTVVLKP---AEDTPVIAAKLV-EILEEAGLPPGVV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 168 GWIDQPSVELSNALMKHNDINLILATG---------------GPGMVKAayssgKPAIGVGAGNVPVVIDETADIKRAVA 232
Cdd:cd07124 227 NFLPGPGEEVGDYLVEHPDVRFIAFTGsrevglriyeraakvQPGQKWL-----KRVIAEMGGKNAIIVDEDADLDEAAE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 233 SVLMSKTFDNGVVCASEQAVIVMDEVYDEVKARfashngyVLSKAEADKVRkilliNGNLNADIVG----QPA-TKIAEM 307
Cdd:cd07124 302 GIVRSAFGFQGQKCSACSRVIVHESVYDEFLER-------LVERTKALKVG-----DPEDPEVYMGpvidKGArDRIRRY 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 308 AGITVPADTKILIGEGDE---------------VKYEDEFAHEKL-SPTLGMFRASSFENAVEQActmVDiGGIGHTSGL 371
Cdd:cd07124 370 IEIGKSEGRLLLGGEVLElaaegyfvqptifadVPPDHRLAQEEIfGPVLAVIKAKDFDEALEIA---ND-TEYGLTGGV 445
|
330 340 350
....*....|....*....|....*....|
gi 46912724 372 YTNqdvNKDRIKYFGDKMKTARILVNIPTT 401
Cdd:cd07124 446 FSR---SPEHLERARREFEVGNLYANRKIT 472
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
98-269 |
7.58e-09 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 59.14 E-value: 7.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 98 MTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLvldaAVAAGAPKNIIGWIDQPSVEL 177
Cdd:PRK09847 152 MIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGL----AKEAGLPDGVLNVVTGFGHEA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 178 SNALMKHNDINLILATG----GPGMVKAAYSSGKPAIGVGAG--NVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQA 251
Cdd:PRK09847 228 GQALSRHNDIDAIAFTGstrtGKQLLKDAGDSNMKRVWLEAGgkSANIVFADCPDLQQAASATAAGIFYNQGQVCIAGTR 307
|
170
....*....|....*...
gi 46912724 252 VIVMDEVYDEVKARFASH 269
Cdd:PRK09847 308 LLLEESIADEFLALLKQQ 325
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
20-356 |
9.41e-09 |
|
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: 58.85 E-value: 9.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 20 QQEFATF---SQEQVDKIFRAASLAANN--ARIPLAQQAVAESGMGIVEDK--VIKNHFASE----FIYNKYKDEKTCGI 88
Cdd:cd07151 20 GETLAEIpaaSKEDVDEAYRAAAAAQKEwaATLPQERAEILEKAAQILEERrdEIVEWLIREsgstRIKANIEWGAAMAI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 89 LEENEEF-GTMT---------------IAEPVGIICGIVPTTNPTSTAIfKSLI-SLKTRNAIIFSPhprAKNSTNAAAK 151
Cdd:cd07151 100 TREAATFpLRMEgrilpsdvpgkenrvYREPLGVVGVISPWNFPLHLSM-RSVApALALGNAVVLKP---ASDTPITGGL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 152 LVLDAAVAAGAPKNIIGWIDQPSVELSNALMKHNDINLILATGGP--GMVKAAYSSG---KPAIGVGaGNVPVVIDETAD 226
Cdd:cd07151 176 LLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTpvGRHIGELAGRhlkKVALELG-GNNPFVVLEDAD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 227 IKRAVASVLMSKTFDNGVVCASEQAVIVMDEVYDEVKARFASHngyVLSKAEADKVRKILLINGNLNADIVGQPATKI-- 304
Cdd:cd07151 255 IDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVER---VKALPYGDPSDPDTVVGPLINESQVDGLLDKIeq 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46912724 305 AEMAGITVPADTKIligEGD--------EVKYEDEFAHEKL-SPTLGMFRASSFENAVEQA 356
Cdd:cd07151 332 AVEEGATLLVGGEA---EGNvleptvlsDVTNDMEIAREEIfGPVAPIIKADDEEEALELA 389
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
91-286 |
1.12e-08 |
|
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: 58.52 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 91 ENEEFGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVLDAAVAAGAPKNIIGWI 170
Cdd:cd07110 108 PSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 171 DqpsvELSNALMKHNDINLILATG----GPGMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVC 246
Cdd:cd07110 188 D----EAGAPLAAHPGIDKISFTGstatGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQIC 263
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 46912724 247 ASEQAVIVMDEVYDEVKARFASHN---------------GYVLSKAEADKVRKIL 286
Cdd:cd07110 264 SATSRLLVHESIADAFLERLATAAeairvgdpleegvrlGPLVSQAQYEKVLSFI 318
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
8-267 |
1.15e-08 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 58.31 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 8 ELDAMVARVKAAQQEFATFSQEQVDKIFRAAS--LAANNARIplAQQAVAESGmGIVedkvIKNHFASEFIYNKYKDEKT 85
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAeiLEERRDEI--ADWLIRESG-STR----PKAAFEVGAAIAILREAAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 86 CGILEENEEF-----GTMTIA--EPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRaknsTNAAAKLVLdAAV 158
Cdd:cd07104 74 LPRRPEGEILpsdvpGKESMVrrVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSR----TPVTGGLLI-AEI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 159 --AAGAPKNIIGWIDQPSVELSNALMKHNDINLILATGGPGM-----VKAAYSSGKPAIGVGaGNVPVVIDETADIKRAV 231
Cdd:cd07104 149 feEAGLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVgrhigELAGRHLKKVALELG-GNNPLIVLDDADLDLAV 227
|
250 260 270
....*....|....*....|....*....|....*.
gi 46912724 232 ASVLMSKTFDNGVVCASEQAVIVMDEVYDEVKARFA 267
Cdd:cd07104 228 SAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLV 263
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
2-269 |
1.23e-08 |
|
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: 58.31 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 2 PVTNMAELDAMVARVKAAQQEFATFSQEQVDKIFR--AASLAANN---ARI-------PLAQqAVAESGMGIvedKVIKn 69
Cdd:cd07106 14 PVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLaiADAIEANAeelARLltleqgkPLAE-AQFEVGGAV---AWLR- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 70 HFASefiyNKYKDEktcgILEENEEFGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPrakNSTNAA 149
Cdd:cd07106 89 YTAS----LDLPDE----VIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSP---FTPLCT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 150 AKLV--LDAAVAAGAPKNIIGwidqpSVELSNALMKHNDINLILATG----GPGMVKAAYSSGKPA---IGvgaGNVPVV 220
Cdd:cd07106 158 LKLGelAQEVLPPGVLNVVSG-----GDELGPALTSHPDIRKISFTGstatGKKVMASAAKTLKRVtleLG---GNDAAI 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 46912724 221 IDETADIKRAVASVLMSKTFDNGVVCASEQAVIVMDEVYDEVKARFASH 269
Cdd:cd07106 230 VLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVAL 278
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
16-341 |
1.83e-08 |
|
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: 57.85 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 16 VKAAQQEFATFSQ----EQVDKIFRAASLAANNARIpLAQQAVAESGMGIVEDKVIKNHFASE-FIYNK---YKDEKTCG 87
Cdd:cd07117 44 VKAAQEAFKTWRKttvaERANILNKIADIIDENKEL-LAMVETLDNGKPIRETRAVDIPLAADhFRYFAgviRAEEGSAN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 88 ILeeNEEFGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPhprakNSTNAAAKLVLDAAVAAGAPKNII 167
Cdd:cd07117 123 MI--DEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKP-----SSTTSLSLLELAKIIQDVLPKGVV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 168 GWIDQPSVELSNALMKHNDINLILATG----GPGMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNG 243
Cdd:cd07117 196 NIVTGKGSKSGEYLLNHPGLDKLAFTGstevGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 244 VVCASEQAVIVMDEVYDEVKARFAshngyvlSKAEADKVRKILLINGNLNADIVGQPATKIAEMAGITVPADTKILIGeG 323
Cdd:cd07117 276 QVCCAGSRIFVQEGIYDEFVAKLK-------EKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTG-G 347
|
330
....*....|....*...
gi 46912724 324 DEVKYEDEFAHEKLSPTL 341
Cdd:cd07117 348 HRLTENGLDKGFFIEPTL 365
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
88-356 |
2.62e-08 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 57.52 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 88 ILEENEEFGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLvldaAVAAGAPKNII 167
Cdd:PLN02766 143 TLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHL----AKLAGVPDGVI 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 168 GWIDQPSVELSNALMKHNDINLILATGGPG-----MVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDN 242
Cdd:PLN02766 219 NVVTGFGPTAGAAIASHMDVDKVSFTGSTEvgrkiMQAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNK 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 243 GVVCASEQAVIVMDEVYDEVKARFA---------------SHNGYVLSKAEADKVRKILLINGNLNADIV--GQPATKIA 305
Cdd:PLN02766 299 GEICVASSRVYVQEGIYDEFVKKLVekakdwvvgdpfdprARQGPQVDKQQFEKILSYIEHGKREGATLLtgGKPCGDKG 378
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 46912724 306 EMAGITVPADTKiligeGDEVKYEDEFahekLSPTLGMFRASSFENAVEQA 356
Cdd:PLN02766 379 YYIEPTIFTDVT-----EDMKIAQDEI----FGPVMSLMKFKTVEEAIKKA 420
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
132-407 |
3.44e-08 |
|
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: 56.90 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 132 NAIIFSPHPRaknsTNAAAKLVLDAAVAAGAPKNIIGWIdQPSVELSNALMKHNDINLILATGGP--GMVKAAYSSGKP- 208
Cdd:cd07095 126 NTVVFKPSEL----TPAVAELMVELWEEAGLPPGVLNLV-QGGRETGEALAAHEGIDGLLFTGSAatGLLLHRQFAGRPg 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 209 ---AIGVGaGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIVMD-EVYDEVKARF-ASHNGYVLSKAEADKVR 283
Cdd:cd07095 201 kilALEMG-GNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIVPDgAVGDAFLERLvEAAKRLRIGAPDAEPPF 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 284 KILLINGNLNADIVGQPATKIAE-----MAGITVPADTKIL----IGEGDEVKYEDEfahEKLSPTLGMFRASSFENAVE 354
Cdd:cd07095 280 MGPLIIAAAAARYLLAQQDLLALggeplLAMERLVAGTAFLspgiIDVTDAADVPDE---EIFGPLLQVYRYDDFDEAIA 356
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 355 QActmvDIGGIGHTSGLYTNqdvNKDRIKYFGDKMKTARILVNIPTT-------HGGIGD 407
Cdd:cd07095 357 LA----NATRFGLSAGLLSD---DEALFERFLARIRAGIVNWNRPTTgasstapFGGVGL 409
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
102-268 |
4.13e-08 |
|
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: 56.57 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 102 EPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTnaaakLVLDAAVAAGAPKNIIGWIDQPSVELSNAL 181
Cdd:cd07092 117 EPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTT-----LLLAELAAEVLPPGVVNVVCGGGASAGDAL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 182 MKHNDINLILATG----GPGMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIVMDE 257
Cdd:cd07092 192 VAHPRVRMVSLTGsvrtGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHES 271
|
170
....*....|.
gi 46912724 258 VYDEVKARFAS 268
Cdd:cd07092 272 VYDEFVAALVE 282
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
93-267 |
4.84e-08 |
|
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: 56.68 E-value: 4.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 93 EEFGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVLDAAVAAGAPKNIIGwidq 172
Cdd:cd07113 132 ERYTAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNG---- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 173 pSVELSNALMKHNDINLILATG----GPGMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCAS 248
Cdd:cd07113 208 -KGAVGAQLISHPDVAKVSFTGsvatGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAA 286
|
170
....*....|....*....
gi 46912724 249 EQAVIVMDEVYDEVKARFA 267
Cdd:cd07113 287 PERFYVHRSKFDELVTKLK 305
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
98-267 |
6.21e-08 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 56.24 E-value: 6.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 98 MTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLvldaAVAAGAPKNIIGWIDQPSVEL 177
Cdd:PLN02278 155 LVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAEL----ALQAGIPPGVLNVVMGDAPEI 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 178 SNALMKHNDINLILATGGPG-----MVKAAYSSGKPAIGVGaGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAV 252
Cdd:PLN02278 231 GDALLASPKVRKITFTGSTAvgkklMAGAAATVKRVSLELG-GNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRI 309
|
170
....*....|....*
gi 46912724 253 IVMDEVYDEVKARFA 267
Cdd:PLN02278 310 LVQEGIYDKFAEAFS 324
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
102-269 |
8.03e-08 |
|
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: 55.66 E-value: 8.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 102 EPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPhprAKNSTNAAAKLvLDAAVAAGAPKNIIGWIDQPSVELSNAL 181
Cdd:cd07082 140 EPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKP---ATQGVLLGIPL-AEAFHDAGFPKGVVNVVTGRGREIGDPL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 182 MKHNDINLILATGGPG----MVKAAysSGKPAI-GVGAGNVPVVIDEtADIKRAVASVLMSKTFDNGVVCASEQAVIVMD 256
Cdd:cd07082 216 VTHGRIDVISFTGSTEvgnrLKKQH--PMKRLVlELGGKDPAIVLPD-ADLELAAKEIVKGALSYSGQRCTAIKRVLVHE 292
|
170
....*....|...
gi 46912724 257 EVYDEVKARFASH 269
Cdd:cd07082 293 SVADELVELLKEE 305
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
102-265 |
1.61e-07 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 54.71 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 102 EPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPraknSTNAAAKLVLDAAVAAGAPKNIIGWIDQPSvELSNAL 181
Cdd:cd07111 146 KPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAE----YTPLTALLFAEICAEAGLPPGVLNIVTGNG-SFGSAL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 182 MKHNDINLILATGGPGMVKA-----AYSSGKPAIGVGaGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIVMD 256
Cdd:cd07111 221 ANHPGVDKVAFTGSTEVGRAlrratAGTGKKLSLELG-GKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQE 299
|
....*....
gi 46912724 257 EVYDEVKAR 265
Cdd:cd07111 300 SVAEELIRK 308
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
478-551 |
1.97e-07 |
|
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: 53.95 E-value: 1.97e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46912724 478 KRAFLVTDRFLFNNgYADDVVKLLKAQGIEVQT-FFDVEAdpTLSIVEKGAEAMKSFQPDVIIALGGGSPMDAAK 551
Cdd:cd08170 23 KKALVIADPFVLDL-VGERLEESLEKAGLEVVFeVFGGEC--SREEIERLAAIARANGADVVIGIGGGKTIDTAK 94
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
2-268 |
7.22e-07 |
|
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: 52.75 E-value: 7.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 2 PVTNMAELDAMVARVKAAQQEFA-TFSQEQVDKIFRAASLAANNARiPLAQQAVAESGMGI-----VEDKVIKNHF---- 71
Cdd:cd07108 14 PRSRAADVDRAVAAAKAAFPEWAaTPARERGKLLARIADALEARSE-ELARLLALETGNALrtqarPEAAVLADLFryfg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 72 --ASEFiynkyKDEktcgILEENEEFGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFsphpraKNSTNAA 149
Cdd:cd07108 93 glAGEL-----KGE----TLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVL------KAAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 150 AKLVLDAAVAAGA-PKNIIGWIDQPSVELSNALMKHNDINLILATGGPGMVKAAY-SSGKPAIGVG---AGNVPVVIDET 224
Cdd:cd07108 158 LAVLLLAEILAQVlPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYrAAADRLIPVSlelGGKSPMIVFPD 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 46912724 225 ADIKRAVASVLMSKTFD-NGVVCASEQAVIVMDEVYDEVKARFAS 268
Cdd:cd07108 238 ADLDDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVA 282
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
456-553 |
8.30e-07 |
|
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: 52.17 E-value: 8.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 456 LPKSIYFRRGSL---PIALSDLEGKKRAFLVTDRFLFNNgYADDVVKLLKAQGIEVQT--FFDVEadpTLSIVEKGAEAM 530
Cdd:cd08173 1 LPRNVVVGHGAInkiGEVLKKLLLGKRALIITGPNTYKI-AGKRVEDLLESSGVEVVIvdIATIE---EAAEVEKVKKLI 76
|
90 100
....*....|....*....|...
gi 46912724 531 KSFQPDVIIALGGGSPMDAAKIM 553
Cdd:cd08173 77 KESKADFIIGVGGGKVIDVAKYA 99
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
2-274 |
9.21e-07 |
|
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: 52.25 E-value: 9.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 2 PVTNMAELDAMVARVKAAQQEFATFS-QEQVDKIFRA-ASLAANNARI----------PLAQQAVAESGMgivEDKVikN 69
Cdd:cd07102 13 PLASLEAVRAALERARAAQKGWRAVPlEERKAIVTRAvELLAANTDEIaeeltwqmgrPIAQAGGEIRGM---LERA--R 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 70 HFASefIYNKYKDEKtcgILEENEEFGTMTIAEPVGIICGIVPTTNPTSTAIfKSLI-SLKTRNAIIFSPHPRaknsTNA 148
Cdd:cd07102 88 YMIS--IAEEALADI---RVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAV-NAVIpALLAGNAVILKHSPQ----TPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 149 AAKLVLDAAVAAGAPKNIIGWIdQPSVELSNALMKHNDINLILATGG-PGMVKAAYSSGKPAIGVG---AGNVPVVIDET 224
Cdd:cd07102 158 CGERFAAAFAEAGLPEGVFQVL-HLSHETSAALIADPRIDHVSFTGSvAGGRAIQRAAAGRFIKVGlelGGKDPAYVRPD 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 46912724 225 ADIKRAVASVLMSKTFDNGVVCASEQAVIVMDEVYDEVKARFASH-NGYVL 274
Cdd:cd07102 237 ADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVvKGYKL 287
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
92-266 |
1.20e-06 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 52.21 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 92 NEEFGTMTIAEPVGIiCG-IVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVLDAavaaGAPKNIIGWI 170
Cdd:cd07091 130 DGNFLAYTRREPIGV-CGqIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEA----GFPPGVVNIV 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 171 DQPSVELSNALMKHNDINLI-----LATGGPGMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVV 245
Cdd:cd07091 205 PGFGPTAGAAISSHMDVDKIaftgsTAVGRTIMEAAAKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQC 284
|
170 180
....*....|....*....|.
gi 46912724 246 CASEQAVIVMDEVYDEVKARF 266
Cdd:cd07091 285 CCAGSRIFVQESIYDEFVEKF 305
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
103-269 |
1.29e-06 |
|
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: 51.93 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 103 PVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPhpraKNSTNAAAKLVLDAAVAAGAPKNIIGWIDQPSVELSNALM 182
Cdd:cd07101 118 PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKP----DSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIV 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 183 KHNDinLILATGGP--GMVKAAySSGKPAIGVGA---GNVPVVIDETADIKRAVASVLMSkTFDN-GVVCASEQAVIVMD 256
Cdd:cd07101 194 DNAD--YVMFTGSTatGRVVAE-RAGRRLIGCSLelgGKNPMIVLEDADLDKAAAGAVRA-CFSNaGQLCVSIERIYVHE 269
|
170
....*....|...
gi 46912724 257 EVYDEVKARFASH 269
Cdd:cd07101 270 SVYDEFVRRFVAR 282
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
97-267 |
1.54e-06 |
|
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: 51.78 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 97 TMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVLdaavAAGAPKNIIGWIDQPSVE 176
Cdd:cd07114 113 NFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAE----EAGFPPGVVNVVTGFGPE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 177 LSNALMKHNDINLILATGGP----GMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMsktfdnGVVCASEQA- 251
Cdd:cd07114 189 TGEALVEHPLVAKIAFTGGTetgrHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVA------GIFAAAGQTc 262
|
170 180
....*....|....*....|.
gi 46912724 252 -----VIVMDEVYDEVKARFA 267
Cdd:cd07114 263 vagsrLLVQRSIYDEFVERLV 283
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
98-289 |
2.51e-06 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 51.04 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 98 MTIAEPVGIICGIVPTTNPtstaifkslISLKTR---------NAIIFSPHPRAKNSTNAAAKLVLDAavaaGAPKNIIG 168
Cdd:cd07105 93 MVVKEPVGVVLGIAPWNAP---------VILGTRaiayplaagNTVVLKASELSPRTHWLIGRVFHEA----GLPKGVLN 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 169 WI-----DQPSVelSNALMKHNDINLILATG----GPGMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKT 239
Cdd:cd07105 160 VVthspeDAPEV--VEALIAHPAVRKVNFTGstrvGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAF 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 46912724 240 FDNGVVCASEQAVIVMDEVYDEVKARFAShngyVLSKAEADKVRKILLIN 289
Cdd:cd07105 238 LNSGQICMSTERIIVHESIADEFVEKLKA----AAEKLFAGPVVLGSLVS 283
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
102-356 |
2.59e-06 |
|
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: 51.06 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 102 EPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPhprAKNSTNAAAKLVlDAAVAAGAPKNIIGWIDQPSVELSNAL 181
Cdd:cd07112 123 EPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP---AEQSPLTALRLA-ELALEAGLPAGVLNVVPGFGHTAGEAL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 182 MKHNDINLILATGGPG-----MVKAAYSSGKP-AIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIVM 255
Cdd:cd07112 199 GLHMDVDALAFTGSTEvgrrfLEYSGQSNLKRvWLECGGKSPNIVFADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVH 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 256 DEVYDEVKARF---------------ASHNGYVLSKAEADKVRKILLINGNLNADIVgqpatkiaeMAGITVPADTKILI 320
Cdd:cd07112 279 ESIKDEFLEKVvaaarewkpgdpldpATRMGALVSEAHFDKVLGYIESGKAEGARLV---------AGGKRVLTETGGFF 349
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 46912724 321 GEG---DEVKYEDEFAHEKL-SPTLGMFRASSFENAVEQA 356
Cdd:cd07112 350 VEPtvfDGVTPDMRIAREEIfGPVLSVITFDSEEEAVALA 389
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
102-397 |
3.21e-06 |
|
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: 50.76 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 102 EPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVLDAAVAAGAPKN----IIGWIDQpsvel 177
Cdd:cd07098 119 EPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIRECLAACGHDPDlvqlVTCLPET----- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 178 SNALMKHNDINLILATGGPG---MV-KAAYSSGKPAIGVGAGNVPVVIDETADIKrAVASVLMSKTFDN-GVVCASEQAV 252
Cdd:cd07098 194 AEALTSHPVIDHITFIGSPPvgkKVmAAAAESLTPVVLELGGKDPAIVLDDADLD-QIASIIMRGTFQSsGQNCIGIERV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 253 IVMDEVYDEVKARFAshngyvlSKAEADKVRKILLINGNLNADIVGQPATKIAEMAGITVPADTKILIGeGD-------- 324
Cdd:cd07098 273 IVHEKIYDKLLEILT-------DRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAG-GKryphpeyp 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 325 -----------EVKYEDEFAHEKL-SPTLGMFRASSFENAVEQActmvDIGGIGHTSGLYTNqdvNKDRIKYFGDKMKTA 392
Cdd:cd07098 345 qghyfpptllvDVTPDMKIAQEEVfGPVMVVMKASDDEEAVEIA----NSTEYGLGASVFGK---DIKRARRIASQLETG 417
|
....*
gi 46912724 393 RILVN 397
Cdd:cd07098 418 MVAIN 422
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
100-263 |
4.52e-06 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 50.41 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 100 IAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVLDAAvaagaPKNIIGWIdQPSVELSN 179
Cdd:PTZ00381 106 IPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYL-----DPSYVRVI-EGGVEVTT 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 180 ALMKHNdINLILATGGP--GMV--KAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIV- 254
Cdd:PTZ00381 180 ELLKEP-FDHIFFTGSPrvGKLvmQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVh 258
|
170
....*....|..
gi 46912724 255 ---MDEVYDEVK 263
Cdd:PTZ00381 259 rsiKDKFIEALK 270
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
3-267 |
5.31e-06 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 49.98 E-value: 5.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 3 VTNMAELDAMVARVKAAQQEFATFSQEQVDKIFRAASLAANNARIPLAQQAVAESGmGIVEdkviKNHFASEFIYNKYKD 82
Cdd:cd07152 9 VADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESG-SIRP----KAGFEVGAAIGELHE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 83 EKTCGILEENEEF----GTMTIAE--PVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVLDA 156
Cdd:cd07152 84 AAGLPTQPQGEILpsapGRLSLARrvPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIARLFEE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 157 AvaaGAPKNII----GwidqpSVELSNALMKHNDINLILATGGPGM-----VKAAYSSGKPAIGVGAGNVPVVIDEtADI 227
Cdd:cd07152 164 A---GLPAGVLhvlpG-----GADAGEALVEDPNVAMISFTGSTAVgrkvgEAAGRHLKKVSLELGGKNALIVLDD-ADL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 46912724 228 KRAVASVLMSKTFDNGVVCASEQAVIVMDEVYDEVKARFA 267
Cdd:cd07152 235 DLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLA 274
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
8-267 |
7.05e-06 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 49.75 E-value: 7.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 8 ELDAMVARVKAAQQEFA-TFSQEQVDKIFRAASLAANNARiPLAQQAVAESGMGiVEDKVIKNHFASEFIynKYKDEKTC 86
Cdd:PLN00412 54 EVNKAMESAKAAQKAWAkTPLWKRAELLHKAAAILKEHKA-PIAECLVKEIAKP-AKDAVTEVVRSGDLI--SYTAEEGV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 87 GILEE-----NEEF-GT------MTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKnstnAAAKLVL 154
Cdd:PLN00412 130 RILGEgkflvSDSFpGNernkycLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGA----VAALHMV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 155 DAAVAAGAPKNIIGWIDQPSVELSNALMKHNDINLILATGG-PGMvkaayssgkpAIGVGAGNVPV----------VIDE 223
Cdd:PLN00412 206 HCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGdTGI----------AISKKAGMVPLqmelggkdacIVLE 275
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 46912724 224 TADIKRAVASVLMSKTFDNGVVCASEQAVIVMDEVYDE----VKARFA 267
Cdd:PLN00412 276 DADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADAlvekVNAKVA 323
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
99-267 |
7.37e-06 |
|
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: 49.54 E-value: 7.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 99 TIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPhprAKNSTNAAAKLVlDAAVAAGAPKNIIGWIDQPSVELS 178
Cdd:cd07109 113 TVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKP---AEDAPLTALRLA-ELAEEAGLPAGALNVVTGLGAEAG 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 179 NALMKHNDINLILATGGPGMVKA-AYSSGKPAIGVG---AGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIV 254
Cdd:cd07109 189 AALVAHPGVDHISFTGSVETGIAvMRAAAENVVPVTlelGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLV 268
|
170
....*....|...
gi 46912724 255 MDEVYDEVKARFA 267
Cdd:cd07109 269 HRSIYDEVLERLV 281
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
3-269 |
1.12e-05 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 48.97 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 3 VTNMAELDAMVArVKAAQQEFATFSQ----EQVDKIFRAASLAANN----ARI-------PLAQqAVAESGMGI------ 61
Cdd:cd07103 13 VPDAGAADADAA-IDAAAAAFKTWRKttarERAAILRRWADLIRERaedlARLltleqgkPLAE-ARGEVDYAAsflewf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 62 ------VEDKVIKNHFASEFIynkykdektcgileeneefgtMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAII 135
Cdd:cd07103 91 aeearrIYGRTIPSPAPGKRI---------------------LVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 136 FSPHPRAKNSTNAAAKLVLDAavaaGAPKNIIGWIDQPSVELSNALMKHNDINLILATG----GPGMVKAAYSSGKPAI- 210
Cdd:cd07103 150 LKPAEETPLSALALAELAEEA----GLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGstavGKLLMAQAADTVKRVSl 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46912724 211 --GvgaGNVPVVIDETADIKRAVASVLMSKtFDN-GVVCASEQAVIVMDEVYDEVKARFASH 269
Cdd:cd07103 226 elG---GNAPFIVFDDADLDKAVDGAIASK-FRNaGQTCVCANRIYVHESIYDEFVEKLVER 283
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
102-268 |
1.28e-05 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 48.73 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 102 EPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPraknSTNAAAKLVLDAAVAAGAPK---NIIgwidqPS-VEL 177
Cdd:cd07139 136 EPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSP----ETPLDAYLLAEAAEEAGLPPgvvNVV-----PAdREV 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 178 SNALMKHNDINLILATGGpgmvKAAyssGKpAIGVGAGN--VPV----------VIDETADIKRAVASVLMSKTFDNGVV 245
Cdd:cd07139 207 GEYLVRHPGVDKVSFTGS----TAA---GR-RIAAVCGErlARVtlelggksaaIVLDDADLDAAVPGLVPASLMNNGQV 278
|
170 180
....*....|....*....|...
gi 46912724 246 CASEQAVIVMDEVYDEVKARFAS 268
Cdd:cd07139 279 CVALTRILVPRSRYDEVVEALAA 301
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
2-261 |
1.29e-05 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 48.76 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 2 PVTNMAELDAMVARVKAAQQEFATFS-QEQVDKIFRAAS-LAANNARIplAQQAVAESGMGIvEDKVIKNHFASEFIYnk 79
Cdd:cd07099 13 PVTDPAEVAAAVARARAAQRAWAALGvEGRAQRLLRWKRaLADHADEL--AELLHAETGKPR-ADAGLEVLLALEAID-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 80 YKDEKTCGILEENEEFGTMTIA--------EPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRaknsTNAAAK 151
Cdd:cd07099 88 WAARNAPRVLAPRKVPTGLLMPnkkatveyRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEV----TPLVGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 152 LVLDAAVAAGAPKNIIGWIdQPSVELSNALMKHNdINLILATGGPG-----MVKAAySSGKPAIGVGAGNVPVVIDETAD 226
Cdd:cd07099 164 LLAEAWAAAGPPQGVLQVV-TGDGATGAALIDAG-VDKVAFTGSVAtgrkvMAAAA-ERLIPVVLELGGKDPMIVLADAD 240
|
250 260 270
....*....|....*....|....*....|....*
gi 46912724 227 IKRAVASVLMSKTFDNGVVCASEQAVIVMDEVYDE 261
Cdd:cd07099 241 LERAAAAAVWGAMVNAGQTCISVERVYVHESVYDE 275
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
103-429 |
1.39e-05 |
|
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: 48.39 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 103 PVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVLDAAVaagAPKNIIGWIdQPSVELSNALM 182
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGL---LPPEDVTLI-NGDGKTMQALL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 183 KHNDINLILATGGPGMVKAAYSSGKPA-IGVGAGNV-PVVIDETADIKRAVA-SVLMSKTFDNGVVCASEQAVIVMDE-- 257
Cdd:cd07084 176 LHPNPKMVLFTGSSRVAEKLALDAKQArIYLELAGFnWKVLGPDAQAVDYVAwQCVQDMTACSGQKCTAQSMLFVPENws 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 258 ---VYDEVKARFA--SHNGYVLSKAEADKVRKILLINGNLNADIVG-----QPATKIAEMAGITVPADTKILIGEGDevK 327
Cdd:cd07084 256 ktpLVEKLKALLArrKLEDLLLGPVQTFTTLAMIAHMENLLGSVLLfsgkeLKNHSIPSIYGACVASALFVPIDEIL--K 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 328 YEDEFAHEKLSPTlgmfrASSFENAVEQACTMVDIGGIGH---TSGLYTNQDVNKDRIkyFGDKMKTARILVNIPTTHGG 404
Cdd:cd07084 334 TYELVTEEIFGPF-----AIVVEYKKDQLALVLELLERMHgslTAAIYSNDPIFLQEL--IGNLWVAGRTYAILRGRTGV 406
|
330 340
....*....|....*....|....*.
gi 46912724 405 -IGDLYNFNVAPSlTLGCGSWGGNSI 429
Cdd:cd07084 407 aPNQNHGGGPAAD-PRGAGIGGPEAI 431
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
94-267 |
1.71e-05 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 48.11 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 94 EFGTMtIAEPVGIICGIVPTTNPTSTAIfKSLI-SLKTRNAIIFSPHPRAKnSTNAAAKLVLDAAvaAGAPKNIIGWIDQ 172
Cdd:cd07120 109 SFSLV-LREPMGVAGIIVPWNSPVVLLV-RSLApALAAGCTVVVKPAGQTA-QINAAIIRILAEI--PSLPAGVVNLFTE 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 173 PSVELSNALMKHNDINLI-----LATGGPGMVKAAYSSGKPAIGVGaGNVPVVIDETADIKRAVASVLMSKTFDNGVVCA 247
Cdd:cd07120 184 SGSEGAAHLVASPDVDVIsftgsTATGRAIMAAAAPTLKRLGLELG-GKTPCIVFDDADLDAALPKLERALTIFAGQFCM 262
|
170 180
....*....|....*....|
gi 46912724 248 SEQAVIVMDEVYDEVKARFA 267
Cdd:cd07120 263 AGSRVLVQRSIADEVRDRLA 282
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
453-552 |
2.20e-05 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 47.58 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 453 WHKLPKSIYFRRG---SLPIALSDLEGKKRAFLVTDRfLFNNGYADDVVKLLKAQGiEVQTFFDVEAdpTLSIVEKGAEA 529
Cdd:PRK00843 7 WIQLPRDVVVGHGvldDIGDVCSDLKLTGRALIVTGP-TTKKIAGDRVEENLEDAG-DVEVVIVDEA--TMEEVEKVEEK 82
|
90 100
....*....|....*....|...
gi 46912724 530 MKSFQPDVIIALGGGSPMDAAKI 552
Cdd:PRK00843 83 AKDVNAGFLIGVGGGKVIDVAKL 105
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
106-373 |
5.95e-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: 46.70 E-value: 5.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 106 IICGIVPTTNpTSTAIFKSLIslkTRNAIIFSPHPRAKNSTNAAAKLVLDAAVAAGAPKNIIGWI-DQPSVELSNALMKH 184
Cdd:cd07127 200 IGCSTFPTWN-GYPGLFASLA---TGNPVIVKPHPAAILPLAITVQVAREVLAEAGFDPNLVTLAaDTPEEPIAQTLATR 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 185 NDINLILATGGP--GMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIV-------M 255
Cdd:cd07127 276 PEVRIIDFTGSNafGDWLEANARQAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVprdgiqtD 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 256 DEV--YDEVKARFAShngyVLSKAEADKVRKILLInGNLNADIVGQPATKIAEMAGITVPAD-------------TKILI 320
Cdd:cd07127 356 DGRksFDEVAADLAA----AIDGLLADPARAAALL-GAIQSPDTLARIAEARQLGEVLLASEavahpefpdarvrTPLLL 430
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 46912724 321 GEGDEvkYEDEFAHEKLSPTLGMFRASSFENAVEQACTMVDIGGiGHTSGLYT 373
Cdd:cd07127 431 KLDAS--DEAAYAEERFGPIAFVVATDSTDHSIELARESVREHG-AMTVGVYS 480
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
102-267 |
8.96e-05 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 46.08 E-value: 8.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 102 EPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLvldaAVAAGAPKNIIGWIDQPSVELSNAL 181
Cdd:cd07089 122 EPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEI----IAETDLPAGVVNVVTGSDNAVGEAL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 182 MKHNDINLILATGGPG-----MVKAAYSSGKPAIGVGAGNVPVVIDEtADIKRAVASVLMSKTFDNGVVCASEQAVIVMD 256
Cdd:cd07089 198 TTDPRVDMVSFTGSTAvgrriMAQAAATLKRVLLELGGKSANIVLDD-ADLAAAAPAAVGVCMHNAGQGCALTTRLLVPR 276
|
170
....*....|.
gi 46912724 257 EVYDEVKARFA 267
Cdd:cd07089 277 SRYDEVVEALA 287
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
99-265 |
9.48e-05 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 46.03 E-value: 9.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 99 TIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPhprAKNSTNAAAKLVlDAAVAAGAPK---NIIgwidQPSV 175
Cdd:PRK13252 138 TRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKP---SEVTPLTALKLA-EIYTEAGLPDgvfNVV----QGDG 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 176 ELSNALMKHNDINLILATGGPGMVK----AAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQA 251
Cdd:PRK13252 210 RVGAWLTEHPDIAKVSFTGGVPTGKkvmaAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTR 289
|
170
....*....|....
gi 46912724 252 VIVMDEVYDEVKAR 265
Cdd:PRK13252 290 VFVQKSIKAAFEAR 303
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
180-267 |
1.19e-04 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 45.63 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 180 ALMKHNDINLILATGGPG-----MVKAAYSSGKPAIGVGaGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIV 254
Cdd:cd07093 190 ALVAHPDVDLISFTGETAtgrtiMRAAAPNLKPVSLELG-GKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILV 268
|
90
....*....|...
gi 46912724 255 MDEVYDEVKARFA 267
Cdd:cd07093 269 QRSIYDEFLERFV 281
|
|
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
460-550 |
1.27e-04 |
|
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440106 Cd Length: 355 Bit Score: 45.08 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 460 IYFRRG---SLPIALSDLEGKKRAFLVTDRFLFNnGYADDVVKLLKAQGIEVQTFF--DVEADPTLSIVEKGAEAMKSFQ 534
Cdd:COG0337 15 IRIGRGlldELGELLAELLKGRRVLVVTDENVAP-LYGERLRAALEAAGFEVHLLVlpDGEASKTLETLERILDALLEAG 93
|
90
....*....|....*....
gi 46912724 535 ---PDVIIALGGGSPMDAA 550
Cdd:COG0337 94 ldrDDLVVALGGGVVGDLA 112
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
90-356 |
1.44e-04 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 45.31 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 90 EENEEFgtmtiAEPVGIICGIVPTTNPTstAIF--KSLISLKTRNAIIFSPhprAKNSTNAAAKLVlDAAVAAGAPKNII 167
Cdd:PRK03137 163 EHNRYF-----YIPLGVGVVISPWNFPF--AIMagMTLAAIVAGNTVLLKP---ASDTPVIAAKFV-EVLEEAGLPAGVV 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 168 GWIDQPSVELSNALMKHNDINLILATGG---------------PGMVKAayssgKPAIGVGAGNVPVVIDETADIKRAVA 232
Cdd:PRK03137 232 NFVPGSGSEVGDYLVDHPKTRFITFTGSrevglriyeraakvqPGQIWL-----KRVIAEMGGKDAIVVDEDADLDLAAE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 233 SVLMSKTFDNGVVCASEQAVIVMDEVYDEVKARF-----------ASHNGY---VLSKAEADKVRKIL--------LING 290
Cdd:PRK03137 307 SIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVveltkeltvgnPEDNAYmgpVINQASFDKIMSYIeigkeegrLVLG 386
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 291 NLNADIVG---QPatkiaemagiTVPADtkiligegdeVKYEDEFAHEKL-SPTLGMFRASSFENAVEQA 356
Cdd:PRK03137 387 GEGDDSKGyfiQP----------TIFAD----------VDPKARIMQEEIfGPVVAFIKAKDFDHALEIA 436
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
98-267 |
1.45e-04 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 45.44 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 98 MTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVLDAavaagAPKNIIGWIDQPSVEL 177
Cdd:cd07107 111 YTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREV-----LPPGVFNILPGDGATA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 178 SNALMKHNDINLILATG----GPGMVKAAYSSGKP-AIGVGAGNvPVVIDETADIKRAVASVLMSKTFD-NGVVCASEQA 251
Cdd:cd07107 186 GAALVRHPDVKRIALIGsvptGRAIMRAAAEGIKHvTLELGGKN-ALIVFPDADPEAAADAAVAGMNFTwCGQSCGSTSR 264
|
170
....*....|....*.
gi 46912724 252 VIVMDEVYDEVKARFA 267
Cdd:cd07107 265 LFVHESIYDEVLARVV 280
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
103-269 |
2.79e-04 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 44.54 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 103 PVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRaknsTNAAAKLVLDAAVAAGAPKNIIGWIDQPSvELSNALM 182
Cdd:cd07147 123 PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASR----TPLSALILGEVLAETGLPKGAFSVLPCSR-DDADLLV 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 183 KHNDINLILATGGPG---MVKAAYSSGKPAIGVGaGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIVMDEVY 259
Cdd:cd07147 198 TDERIKLLSFTGSPAvgwDLKARAGKKKVVLELG-GNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVY 276
|
170
....*....|
gi 46912724 260 DEVKARFASH 269
Cdd:cd07147 277 DEFKSRLVAR 286
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
459-544 |
3.20e-04 |
|
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis; 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, which involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds, is found in bacteria, microbial eukaryotes, and plants, but not in mammals. Therefore, enzymes of this pathway are attractive targets for the development of non-toxic antimicrobial compounds, herbicides and anti-parasitic agents. The activity of DHQS requires nicotinamide adenine dinucleotide (NAD) as cofactor. A single active site in DHQS catalyzes five sequential reactions involving alcohol oxidation, phosphate elimination, carbonyl reduction, ring opening, and intramolecular aldol condensation. The binding of substrates and ligands induces domain conformational changes. In some fungi and protozoa, this domain is fused with the other four domains in shikimate pathway and forms a penta-domain AROM protein, which catalyzes steps 2-6 in the shikimate pathway.
Pssm-ID: 341474 Cd Length: 343 Bit Score: 43.97 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 459 SIYFRRGSLP--IALSDLEGKKRAFLVTDRFLFNNgYADDVVKLLKAQGIEVQTFF--DVEADPTLSIVEKGAEAMKSFQ 534
Cdd:cd08195 3 PILIGSGLLDklGELLELKKGSKVVIVTDENVAKL-YGELLLKSLEAAGFKVEVIVipAGEKSKSLETVERIYDFLLEAG 81
|
90
....*....|...
gi 46912724 535 PD---VIIALGGG 544
Cdd:cd08195 82 LDrdsLLIALGGG 94
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
478-551 |
5.41e-04 |
|
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: 43.29 E-value: 5.41e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46912724 478 KRAFLVTDrflfNNGYA---DDVVKLLKAQGIEVQTFFdVEADPTLSIVEKGAEAMKSFQPDVIIALGGGSPMDAAK 551
Cdd:cd08550 23 KKALIIGG----KTALEavgEKLEKSLEEAGIDYEVEV-FGGECTEENIERLAEKAKEEGADVIIGIGGGKVLDTAK 94
|
|
| EEVS |
cd08199 |
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ... |
470-550 |
1.30e-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: 42.13 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 470 ALSDLEGK--KRAFLVTDRFLFNNgYADDVVKLLKAQGIEVQTF-FDV-EADPTLSIVEKGAEAMKSFQPD---VIIALG 542
Cdd:cd08199 17 TLADAYGRpgRRRLVVVDENVDRL-YGARIRAYFAAHGIEATILvLPGgEANKTMETVLRIVDALDDFGLDrrePVIAIG 95
|
....*...
gi 46912724 543 GGSPMDAA 550
Cdd:cd08199 96 GGVLLDVV 103
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
215-269 |
1.79e-03 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 41.68 E-value: 1.79e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 46912724 215 GNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIVMDEVYDEVKARFASH 269
Cdd:cd07100 207 GSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEA 261
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
132-269 |
2.26e-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: 41.44 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 132 NAIIFSPHPRAKNSTNAAAKLVLDA------AVAAGApkniigwidqpsVELSNALMK----HndinlILATGGPG---- 197
Cdd:cd07134 129 NTAILKPSELTPHTSAVIAKIIREAfdedevAVFEGD------------AEVAQALLElpfdH-----IFFTGSPAvgki 191
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46912724 198 -MVKAA--YSSGKPAIGvgaGNVPVVIDETADIKRAVASVLMSKTFDNGVVCaseqavIVMDEVY--DEVKARFASH 269
Cdd:cd07134 192 vMAAAAkhLASVTLELG---GKSPTIVDETADLKKAAKKIAWGKFLNAGQTC------IAPDYVFvhESVKDAFVEH 259
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
218-269 |
3.35e-03 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 40.93 E-value: 3.35e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 46912724 218 PVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIV----MDEVYDEVKARFASH 269
Cdd:cd07133 213 PAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVpedkLEEFVAAAKAAVAKM 268
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
478-553 |
4.30e-03 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 40.57 E-value: 4.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46912724 478 KRAFLVTDRFLFNNgYADDVVKLLKAQGIEVqTF--FDVEAdpTLSIVEKGAEAMKSFQPDVIIALGGGSPMDAAKIM 553
Cdd:PRK09423 30 KRALVIADEFVLGI-VGDRVEASLKEAGLTV-VFevFNGEC--SDNEIDRLVAIAEENGCDVVIGIGGGKTLDTAKAV 103
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
98-406 |
5.72e-03 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 40.20 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 98 MTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKNSTNAAAKLVLDAAVAAGAPKNIIGWIdQPSVEL 177
Cdd:PLN02315 149 MEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTSF-CGGAEI 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 178 SNALMKHNDINLILATGGPG---MVKAAYSS--GKPAIGVGAGNVPVVIDEtADIKRAVASVLMSKTFDNGVVCASEQAV 252
Cdd:PLN02315 228 GEAIAKDTRIPLVSFTGSSKvglMVQQTVNArfGKCLLELSGNNAIIVMDD-ADIQLAVRSVLFAAVGTAGQRCTTCRRL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 253 IVMDEVYDEVKARFASHNGYVlskAEADKVRKILLInGNLNAdivgqPATKIAEMAGITVPADT--KILIG------EGD 324
Cdd:PLN02315 307 LLHESIYDDVLEQLLTVYKQV---KIGDPLEKGTLL-GPLHT-----PESKKNFEKGIEIIKSQggKILTGgsaiesEGN 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46912724 325 -------EVKYEDEFAHEKL-SPTLGMFRASSFENAVEQACTMVDiggiGHTSGLYTNqdvNKDRI-KYFGDKMKTARIL 395
Cdd:PLN02315 378 fvqptivEISPDADVVKEELfGPVLYVMKFKTLEEAIEINNSVPQ----GLSSSIFTR---NPETIfKWIGPLGSDCGIV 450
|
330
....*....|..
gi 46912724 396 -VNIPTTHGGIG 406
Cdd:PLN02315 451 nVNIPTNGAEIG 462
|
|
| |
