|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
1-864 |
0e+00 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 1669.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 1 MVVKEKVVNEMQEvkemIDTLVNNGRKALQALESFTQEQIDNIVHEMALAGVDQHMPLAKLAVEETGRGVYEDKCIKNIF 80
Cdd:PRK13805 1 MTKEEMAVTNVAE----LDALVEKAKKAQEEFATFTQEQVDKIVRAAALAALDARIPLAKMAVEETGRGVVEDKVIKNHF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 81 ATEYIWHSIKKDKTVGIIHEDPHEEIIEIAEPVGVVAGVTPVTNPTSTTMFKALIAIKTRNPIIFAFHPSAQKCSIAAAK 160
Cdd:PRK13805 77 ASEYIYNSYKDEKTVGVIEEDDEFGIIEIAEPVGVIAGITPTTNPTSTAIFKALIALKTRNPIIFSFHPRAQKSSIAAAK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 161 TVYDAAVKAGAPKHCIQWIEKPSVEATKQLMNHEGVALVLATGGAGMVKSAYSTGKPALGVGPGNVPCYIEKSAHVKRAV 240
Cdd:PRK13805 157 IVLDAAVAAGAPKDIIQWIEEPSVELTNALMNHPGIALILATGGPGMVKAAYSSGKPALGVGAGNVPAYIDKTADIKRAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 241 NDLILSKTFDNGMICASEQAIIVDKEIYDDVKTEMIANNCYFVTEEERRQLEKLVINENTCAVNSDIVGKSAQYIAELVG 320
Cdd:PRK13805 237 NDILLSKTFDNGMICASEQAVIVDDEIYDEVKEEFASHGAYFLNKKELKKLEKFIFGKENGALNADIVGQSAYKIAEMAG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 321 ITVPENTKMLVAEIQGIGAAYPLSREKLSPVLACVKANSLEEGFAYCEEMLNLGGLGHSAVIHSVNKAVQKQFGLRMKAC 400
Cdd:PRK13805 317 FKVPEDTKILIAEVKGVGESEPLSHEKLSPVLAMYKAKDFEDAVEKAEKLVEFGGLGHTAVIYTNDDELIKEFGLRMKAC 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 401 RLIVNAPSSQGGIGDIYNGFIPSLTLGCGSYGKNSVSQNVTATHLLNIKRLANRKKNMQWFKLPPKIYFEKHATAYLAN- 479
Cdd:PRK13805 397 RILVNTPSSQGGIGDLYNKLAPSLTLGCGSWGGNSVSENVGAKHLLNIKTVAKRRENMQWFKVPKKIYFERGSLPYLLDe 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 480 MPNISRAFIVTDPGMVEHGYVDTVTHYLRKHANDVKVEVFFEVEPDPSDETVFKGAEMMRSFQPDVIIALGGGSAMDAAK 559
Cdd:PRK13805 477 LDGKKRAFIVTDRFMVELGYVDKVTDVLKKRENGVEYEVFSEVEPDPTLSTVRKGAELMRSFKPDTIIALGGGSPMDAAK 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 560 GMWLFYEYPETTFYGIKQKFLDIRKRTCKYPELGSKAQFVAIPTTSGTGSEVTPFAVITDKKNNIKYPLADYELTPDVAI 639
Cdd:PRK13805 557 IMWLFYEHPETDFEDLAQKFMDIRKRIYKFPKLGKKAKLVAIPTTSGTGSEVTPFAVITDDKTGVKYPLADYELTPDVAI 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 640 VDPQFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLVFKYLPRAFKDG-NDEEAREKMHNASAIAGMA 718
Cdd:PRK13805 637 VDPNLVMTMPKSLTADTGIDALTHALEAYVSVMASDYTDGLALQAIKLVFEYLPRSYKNGaKDPEAREKMHNASTIAGMA 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 719 FANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVVRYNAIKPRKHALFPKYEHFVADERYAHIARMLGLPASSAAEGVE 798
Cdd:PRK13805 717 FANAFLGICHSMAHKLGAEFHIPHGRANAILLPHVIRYNATDPPKQAAFPQYEYPRADERYAEIARHLGLPGSTTEEKVE 796
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872568246 799 SLVQAIIELGKSLNINMSIAGQGVDKDQFEEVVGLLAERAFEDQCTTANPKLPLISELKEIYMKAY 864
Cdd:PRK13805 797 SLIKAIEELKAELGIPMSIKEAGVDEADFLAKLDELAELAFDDQCTGANPRYPLISELKEILLDAY 862
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
18-454 |
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: 745.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 18 IDTLVNNGRKALQALESFTQEQIDNIVHEMALAGVDQHMPLAKLAVEETGRGVYEDKCIKNIFATEYIWHSIKKDKTVGI 97
Cdd:cd07122 1 VDELVERARKAQREFATFSQEQVDKIVEAVAWAAADAAEELAKMAVEETGMGVVEDKVIKNHFASEYVYNDIKDMKTVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 98 IHEDPHEEIIEIAEPVGVVAGVTPVTNPTSTTMFKALIAIKTRNPIIFAFHPSAQKCSIAAAKTVYDAAVKAGAPKHCIQ 177
Cdd:cd07122 81 IEEDEEKGIVEIAEPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAAVAAGAPEGLIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 178 WIEKPSVEATKQLMNHEGVALVLATGGAGMVKSAYSTGKPALGVGPGNVPCYIEKSAHVKRAVNDLILSKTFDNGMICAS 257
Cdd:cd07122 161 WIEEPSIELTQELMKHPDVDLILATGGPGMVKAAYSSGKPAIGVGPGNVPAYIDETADIKRAVKDIILSKTFDNGTICAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 258 EQAIIVDKEIYDDVKTEMIANNCYFVTEEERRQLEKLVINENTcAVNSDIVGKSAQYIAELVGITVPENTKMLVAEIQGI 337
Cdd:cd07122 241 EQSVIVDDEIYDEVRAELKRRGAYFLNEEEKEKLEKALFDDGG-TLNPDIVGKSAQKIAELAGIEVPEDTKVLVAEETGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 338 GAAYPLSREKLSPVLACVKANSLEEGFAYCEEMLNLGGLGHSAVIHSVNKAVQKQFGLRMKACRLIVNAPSSQGGIGDIY 417
Cdd:cd07122 320 GPEEPLSREKLSPVLAFYRAEDFEEALEKARELLEYGGAGHTAVIHSNDEEVIEEFALRMPVSRILVNTPSSLGGIGDTY 399
|
410 420 430
....*....|....*....|....*....|....*..
gi 872568246 418 NGFIPSLTLGCGSYGKNSVSQNVTATHLLNIKRLANR 454
Cdd:cd07122 400 NGLAPSLTLGCGSWGGNSTSDNVGPKHLLNIKRVAYR 436
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
462-860 |
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: 724.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 462 KLPPKIYFEKHATAYLAN-MPNISRAFIVTDPGMVEHGYVDTVTHYLRKHanDVKVEVFFEVEPDPSDETVFKGAEMMRS 540
Cdd:cd08178 1 KVPPKIYFEPGCLPYLLLeLPGVKRAFIVTDRVLYKLGYVDKVLDVLEAR--GVETEVFSDVEPDPTLSTVRKGLEAMNA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 541 FQPDVIIALGGGSAMDAAKGMWLFYEYPETTFYGIKQKFLDIRKRTCKYPELGSKAQFVAIPTTSGTGSEVTPFAVITDK 620
Cdd:cd08178 79 FKPDVIIALGGGSAMDAAKIMWLFYEHPETKFEDLAQRFMDIRKRVYKFPKLGKKAKLVAIPTTSGTGSEVTPFAVITDD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 621 KNNIKYPLADYELTPDVAIVDPQFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLVFKYLPRAFKDGN 700
Cdd:cd08178 159 KTGKKYPLADYALTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVSVMASDYTDGLALQAIKLIFEYLPRSYNNGN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 701 DEEAREKMHNASAIAGMAFANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVVRYNAIK-PRKHALFPKYEHFVADERY 779
Cdd:cd08178 239 DIEAREKMHNAATIAGMAFANAFLGICHSLAHKLGAAFHIPHGRANAILLPHVIRYNATDpPTKQAAFPQYKYYVAKERY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 780 AHIARMLGLPASSAAEGVESLVQAIIELGKSLNINMSIAGQGVDKDQFEEVVGLLAERAFEDQCTTANPKLPLISELKEI 859
Cdd:cd08178 319 AEIADLLGLGGKTPEEKVESLIKAIEDLKKDLGIPTSIREAGIDEADFLAAVDKLAEDAFDDQCTGANPRYPLISELKEI 398
|
.
gi 872568246 860 Y 860
Cdd:cd08178 399 L 399
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
457-864 |
0e+00 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 541.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 457 NMQWFKLPPKIYFEKHATAYLANM---PNISRAFIVTDPGMVEHGYVDTVTHYLRKHanDVKVEVFFEVEPDPSDETVFK 533
Cdd:COG1454 1 MMFTFRLPTRIVFGAGALAELGEElkrLGAKRALIVTDPGLAKLGLLDRVLDALEAA--GIEVVVFDDVEPNPTVETVEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 534 GAEMMRSFQPDVIIALGGGSAMDAAKGMWLFYEYPETTfygikQKFLDIRKRTckypelGSKAQFVAIPTTSGTGSEVTP 613
Cdd:COG1454 79 GAAAAREFGADVVIALGGGSAIDAAKAIALLATNPGDL-----EDYLGIKKVP------GPPLPLIAIPTTAGTGSEVTP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 614 FAVITDKKNNIKYPLADYELTPDVAIVDPQFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLVFKYLP 693
Cdd:COG1454 148 FAVITDPETGVKKGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPLTDALALEAIRLIARNLP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 694 RAFKDGNDEEAREKMHNASAIAGMAFANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVVRYNAIkprkhalfpkyehf 773
Cdd:COG1454 228 RAVADGDDLEAREKMALASLLAGMAFANAGLGAVHALAHPLGGLFHVPHGLANAILLPHVLRFNAP-------------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 774 VADERYAHIARMLGLP-ASSAAEGVESLVQAIIELGKSLNINMSIAGQGVDKDQFEEvvglLAERAFEDQCTTANPKLPL 852
Cdd:COG1454 294 AAPERYAEIARALGLDvGLSDEEAAEALIEAIRELLRDLGIPTRLSELGVTEEDLPE----LAELALADRCLANNPRPLT 369
|
410
....*....|..
gi 872568246 853 ISELKEIYMKAY 864
Cdd:COG1454 370 EEDIEAILRAAY 381
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
460-864 |
2.69e-179 |
|
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: 521.37 E-value: 2.69e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 460 WFKLPPKIYFEKHATAYLANMPNiSRAFIVTDPG-MVEHGYVDTVTHYLRKhaNDVKVEVFFEVEPDPSDETVFKGAEMM 538
Cdd:cd08179 1 RFFVPRDIYFGEGALEYLKTLKG-KRAFIVTGGGsMKRNGFLDKVEDYLKE--AGMEVKVFEGVEPDPSVETVEKGAEAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 539 RSFQPDVIIALGGGSAMDAAKGMWLFYEYPETTFygikqkfLDIrKRTCKYPELGSKAQFVAIPTTSGTGSEVTPFAVIT 618
Cdd:cd08179 78 REFEPDWIIAIGGGSVIDAAKAMWVFYEYPELTF-------EDA-LVPFPLPELRKKARFIAIPSTSGTGSEVTRASVIT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 619 DKKNNIKYPLADYELTPDVAIVDPQFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLVFKYLPRAFKD 698
Cdd:cd08179 150 DTEKGIKYPLASFEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLANDFTDALALGAILDIFENLPKSYNG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 699 GNDEEAREKMHNASAIAGMAFANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVVRYNAIKPRKhalfpkyehfvadeR 778
Cdd:cd08179 230 GKDLEAREKMHNASCLAGMAFSNSGLGIVHSMAHKGGAFFGIPHGLANAILLPYVIEFNSKDPEA--------------R 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 779 YAHIARMLGLpasSAAEGVESLVQAIIELGKSLNINMSIAGQGVDKDQFEEVVGLLAERAFEDQCTTANPKLPLISELKE 858
Cdd:cd08179 296 ARYAALLIGL---TDEELVEDLIEAIEELNKKLGIPLSFKEAGIDEDEFFAKLDEMAENAMNDACTGTNPRKPTVEEMKE 372
|
....*.
gi 872568246 859 IYMKAY 864
Cdd:cd08179 373 LLKAAY 378
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
461-860 |
1.25e-163 |
|
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: 479.30 E-value: 1.25e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 461 FKLPPKIYFEKHATAYLANMPNiSRAFIVTDPGMVEHGYVDTVTHYLRKHAndvKVEVFFEVEPDPSDETVFKGAEMMRS 540
Cdd:cd08180 1 FSLKTKIYSGEDSLERLKELKG-KRVFIVTDPFMVKSGMVDKVTDELDKSN---EVEIFSDVVPDPSIEVVAKGLAKILE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 541 FQPDVIIALGGGSAMDAAKGMWLFYEypettfygikqkfldirkrtcKYPELGSKAQFVAIPTTSGTGSEVTPFAVITDK 620
Cdd:cd08180 77 FKPDTIIALGGGSAIDAAKAIIYFAL---------------------KQKGNIKKPLFIAIPTTSGTGSEVTSFAVITDP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 621 KNNIKYPLADYELTPDVAIVDPQFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLVFKYLPRAFKDGN 700
Cdd:cd08180 136 EKGIKYPLVDDSMLPDIAILDPELVKSVPPKVTADTGMDVLTHALEAYVSTNANDFTDALAEKAIKLVFENLPRAYRDGD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 701 DEEAREKMHNASAIAGMAFANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVVRYnaikprkhalfpkyehfvaderya 780
Cdd:cd08180 216 DLEAREKMHNASCMAGIAFNNAGLGINHSLAHALGGRFHIPHGRANAILLPYVIEF------------------------ 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 781 hiarmlglpassaaegvesLVQAIIELGKSLNINMSIAGQGVDKDQFEEVVGLLAERAFEDQCTTANPKLPLISELKEIY 860
Cdd:cd08180 272 -------------------LIAAIRRLNKKLGIPSTLKELGIDEEEFEKAIDEMAEAALADRCTATNPRKPTAEDLIELL 332
|
|
| EutH_ACDH |
TIGR02518 |
acetaldehyde dehydrogenase (acetylating); |
11-452 |
1.48e-161 |
|
acetaldehyde dehydrogenase (acetylating);
Pssm-ID: 131570 Cd Length: 488 Bit Score: 480.13 E-value: 1.48e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 11 MQEVKEMIDTlvnnGRKALQALESFTQEQIDNIVHEMALAGVDQHMPLAKLAVEETGRGVYEDKCIKNIFATEYIWHSIK 90
Cdd:TIGR02518 7 IQQVRNLIRS----AKVAQKKLANMTQEQIDKIVKAIVDAAYENAVKLAKMANEETGFGKWEDKVIKNVFAATIVYDSIK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 91 KDKTVGIIHEDPHEEIIEIAEPVGVVAGVTPVTNPTSTTMFKALIAIKTRNPIIFAFHPSAQKCSIAAAKTVYDAAVKAG 170
Cdd:TIGR02518 83 DMKTIGILSEDKEKKVIEIAVPVGVVAGLIPSTNPTSTAIYKTLISIKARNAIVFSPHPNAKKCIIETVKLMRKAAEEAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 171 APKHCIQWIEKPSVEATKQLMNHEGVALVLATGGAGMVKSAYSTGKPALGVGPGNVPCYIEKSAHVKRAVNDLILSKTFD 250
Cdd:TIGR02518 163 APEGAIGCITVPTIEGTNELMKNKDTSLILATGGEAMVKAAYSSGTPAIGVGPGNGPAYIERTANVKKAVRDIIDSKTFD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 251 NGMICASEQAIIVDKEIYDDVKTEMIANNCYFVTEEERRQLEKLVINENTcAVNSDIVGKSAQYIAELVGITVPENTKML 330
Cdd:TIGR02518 243 NGTICASEQSIIVEECNKDAVVEELKKQGGYFLTAEEAEKLGKFILRPNG-TMNPQIVGKSPQVIANLAGLTVPEDAKVL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 331 VAEIQGIGAAYPLSREKLSPVLACVKANSLEEGFAYCEEMLNLGGLGHSAVIHSVNKAVQKQFGLRMKACRLIVNAPSSQ 410
Cdd:TIGR02518 322 IGEQNGVGNKNPYSREKLTTILAFYTEENWHEACELSIELLQNEGAGHTLIIHSENKDIVREFALKKPVSRMLVNTGGSL 401
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 872568246 411 GGIGDIYNgFIPSLTLGCGSYGKNSVSQNVTATHLLNIKRLA 452
Cdd:TIGR02518 402 GGIGATTN-LVPAFTLGCGAVGGSSTSDNITPENLINIRRVA 442
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
18-454 |
4.28e-153 |
|
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: 456.34 E-value: 4.28e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 18 IDTLVNNGRKALQALESFTQEQIDNIVHEMALAGVDQHMPLAKLAVEETGRGVYEDKCIKNIFATEYIWHSIKKDKTVGI 97
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIKNHFAAEYIYNVYKDEKTCGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 98 IHEDPHEEIIEIAEPVGVVAGVTPVTNPTSTTMFKALIAIKTRNPIIFAFHPSAQKCSIAAAKTVYDAAVKAGAPKHCIQ 177
Cdd:cd07081 81 LTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 178 WIEKPSVEATKQLMNHEGVALVLATGGAGMVKSAYSTGKPALGVGPGNVPCYIEKSAHVKRAVNDLILSKTFDNGMICAS 257
Cdd:cd07081 161 WIDNPSIELAQRLMKFPGIGLLLATGGPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 258 EQAIIVDKEIYDDVKTEMIANNCYFVTEEERRQLEKLVINENtcAVNSDIVGKSAQYIAELVGITVPENTKMLVAEIQGI 337
Cdd:cd07081 241 EQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQQVQPVILKNG--DVNRDIVGQDAYKIAAAAGLKVPQETRILIGEVTSL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 338 GAAYPLSREKLSPVLACVKANSLEEGFAYCEEMLNLGGLGHSAVIHSVN-KAVQK--QFGLRMKACRLIVNAPSSQGGIG 414
Cdd:cd07081 319 AEHEPFAHEKLSPVLAMYRAANFADADAKALALKLEGGCGHTSAMYSDNiKAIENmnQFANAMKTSRFVKNGPCSQGGLG 398
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 872568246 415 DIYNGFI-PSLTLGCGSYGKNSVSQNVTATHLLNIKRLANR 454
Cdd:cd07081 399 DLYNFRGwPSMTLGCGTWGGNSVSENVGPKHLVNLKTVALR 439
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
460-860 |
1.07e-145 |
|
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: 434.73 E-value: 1.07e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 460 WFKLPPKIYFEKHATAYLANMPNiSRAFIVTDPGMVEHGYVDTVTHYLRKHanDVKVEVFFEVEPDPSDETVFKGAEMMR 539
Cdd:cd14862 2 WYFSSPKIVFGEDALSHLEQLSG-KRALIVTDKVLVKLGLLKKVLKRLLQA--GFEVEVFDEVEPEPPLETVLKGAEAMR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 540 SFQPDVIIALGGGSAMDAAKGMWLFYEYPETTFYGIKqkFLDIRKrtckypeLGSKAQFVAIPTTSGTGSEVTPFAVITD 619
Cdd:cd14862 79 EFEPDLIIALGGGSVMDAAKAAWVLYERPDLDPEDIS--PLDLLG-------LRKKAKLIAIPTTSGTGSEATWAIVLTD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 620 KKNNIKYPLADYELTPDVAIVDPQFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLVFKYLPRAFKDG 699
Cdd:cd14862 150 TEEPRKIAVANPELVPDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLSTWSNDFSDALALKAIELIFKYLPRAYKDG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 700 NDEEAREKMHNASAIAGMAFANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVVRYNAIkprkhalfpkyehfVADERY 779
Cdd:cd14862 230 DDLEAREKMHNAATIAGLAFGNSQAGLAHALGHSLGAVFHVPHGIAVGLFLPYVIEFYAK--------------VTDERY 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 780 AHIARmLGLPASSAAEGVESLVQAIIELGKSLNINMSIAGQGVDKDQFEEVVGLLAERAFEDQCTTANPKLPLISELKEI 859
Cdd:cd14862 296 DLLKL-LGIEARDEEEALKKLVEAIRELYKEVGQPLSIKDLGISEEEFEEKLDELVEYAMEDSCTITSPRPPSEEDLKKL 374
|
.
gi 872568246 860 Y 860
Cdd:cd14862 375 F 375
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
464-860 |
1.60e-142 |
|
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: 426.48 E-value: 1.60e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 464 PPKIYFEKHATAYLANM---PNISRAFIVTDPGMVEHGYVDTVTHYLRKHanDVKVEVFFEVEPDPSDETVFKGAEMMRS 540
Cdd:cd08551 1 PTRIVFGAGALARLGEElkaLGGKKVLLVTDPGLVKAGLLDKVLESLKAA--GIEVEVFDDVEPNPTVETVEAAAELARE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 541 FQPDVIIALGGGSAMDAAKGMWLFYEYPETTFYgikqkFLDIRKRTCKypelgsKAQFVAIPTTSGTGSEVTPFAVITDK 620
Cdd:cd08551 79 EGADLVIAVGGGSVLDTAKAIAVLATNGGSIRD-----YEGIGKVPKP------GLPLIAIPTTAGTGSEVTPNAVITDP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 621 KNNIKYPLADYELTPDVAIVDPQFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLVFKYLPRAFKDGN 700
Cdd:cd08551 148 ETGRKMGIVSPYLLPDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANPISDALALEAIRLIGKNLRRAVADGS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 701 DEEAREKMHNASAIAGMAFANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVVRYNAIkprkhalfpkyehfVADERYA 780
Cdd:cd08551 228 DLEAREAMLLASLLAGIAFGNAGLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLP--------------ACPEKYA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 781 HIARMLGLPAS--SAAEGVESLVQAIIELGKSLNINMSIAGQGVDKDQFEEvvglLAERAFEDQCTTAN-PKLPLISELK 857
Cdd:cd08551 294 EIAEALGEDVEglSDEEAAEAAVEAVRELLRDLGIPTSLSELGVTEEDIPE----LAEDAMKSGRLLSNnPRPLTEEDIR 369
|
...
gi 872568246 858 EIY 860
Cdd:cd08551 370 EIY 372
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
464-856 |
3.67e-137 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 412.38 E-value: 3.67e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 464 PPKIYFEKHATAYLAN-MPNI-SRAFIVTDPGMVEHGYVDTVTHYLRkhANDVKVEVFFEVEPDPSDETVFKGAEMMRSF 541
Cdd:pfam00465 1 PTRIVFGAGALAELGEeLKRLgARALIVTDPGSLKSGLLDKVLASLE--EAGIEVVVFDGVEPEPTLEEVDEAAALAREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 542 QPDVIIALGGGSAMDAAKGMWLFYEYPETTFygikqKFLDIRKRTCKypelgsKAQFVAIPTTSGTGSEVTPFAVITDKK 621
Cdd:pfam00465 79 GADVIIAVGGGSVIDTAKAIALLLTNPGDVW-----DYLGGKPLTKP------ALPLIAIPTTAGTGSEVTPLAVITDTE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 622 NNIKYPLADYELTPDVAIVDPQFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLVFKYLPRAFKDGND 701
Cdd:pfam00465 148 TGEKLGIFSPKLLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDALALEAIRLIAENLPRAVADGED 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 702 EEAREKMHNASAIAGMAFANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVVRYNAIkprkhalfpkyehfVADERYAH 781
Cdd:pfam00465 228 LEARENMLLASTLAGLAFSNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNAP--------------AAPEKLAQ 293
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872568246 782 IARMLGLPasSAAEGVESLVQAIIELGKSLNINMSIAGQGVDKDQFEEvvglLAERAFEDQCTTANPKLPLISEL 856
Cdd:pfam00465 294 LARALGED--SDEEAAEEAIEALRELLRELGLPTTLSELGVTEEDLDA----LAEAALRDRSLANNPRPLTAEDI 362
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
464-864 |
4.77e-121 |
|
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: 371.09 E-value: 4.77e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 464 PPKIYF----EKHATAYLANMpNISRAFIVTDPGMVEHGYVDTVTHYLRKHanDVKVEVFFEVEPDPSDETVFKGAEMMR 539
Cdd:cd08194 1 PRTIIIgggaLEELGEEAASL-GGKRALIVTDKVMVKLGLVDKVTQLLAEA--GIAYAVFDDVVSEPTDEMVEEGLALYK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 540 SFQPDVIIALGGGSAMDAAKGMWLFYeypetTFYGikqkflDIRKRTCKYPELGSKAQFVAIPTTSGTGSEVTPFAVITD 619
Cdd:cd08194 78 EGGCDFIVALGGGSPIDTAKAIAVLA-----TNGG------PIRDYMGPRKVDKPGLPLIAIPTTAGTGSEVTRFTVITD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 620 KKNNIKYPLADYELTPDVAIVDPQFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLVFKYLPRAFKDG 699
Cdd:cd08194 147 TETDVKMLLKGPALLPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQPLTDTLALSAIKLIGRNLRRAYADG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 700 NDEEAREKMHNASAIAGMAFANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVVRYNAIkprkhalfpkyehfVADERY 779
Cdd:cd08194 227 DDLEAREAMMLAALEAGIAFSNSSVALVHGMSRPIGALFHVPHGLSNAMLLPAVTEFSLP--------------GAPERY 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 780 AHIARMLGLPAS--SAAEGVESLVQAIIELGKSLNINmSIAGQGVDKDQFEEVVGLLAERAFEDQCTTANPKLPLISELK 857
Cdd:cd08194 293 AEIARAMGIATEgdSDEEAAEKLVEALERLCADLEIP-TLREYGIDEEEFEAALDKMAEDALASGSPANNPRVPTKEEII 371
|
....*..
gi 872568246 858 EIYMKAY 864
Cdd:cd08194 372 ELYREAW 378
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
461-861 |
2.79e-117 |
|
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: 361.45 E-value: 2.79e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 461 FKLPPKIYFEKHATAYLANMP---NISRAFIVTDPGMVEHGYVDTVTHYLRKhaNDVKVEVFFEVEPDPSDETVFKGAEM 537
Cdd:cd08188 3 FYIPPVNLFGPGCLKEIGDELkklGGKKALIVTDKGLVKLGLVKKVTDVLEE--AGIEYVIFDGVQPNPTVTNVNEGLEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 538 MRSFQPDVIIALGGGSAMDAAKGMWLF---------YEypettfyGIkqkfldirkRTCKYPELgskaQFVAIPTTSGTG 608
Cdd:cd08188 81 FKENGCDFIISVGGGSAHDCAKAIGILatnggeiedYE-------GV---------DKSKKPGL----PLIAINTTAGTA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 609 SEVTPFAVITDKKNNIKYPLADYELTPDVAIVDPQFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLV 688
Cdd:cd08188 141 SEVTRFAVITDEERHVKMVIVDWNVTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVSTGATPLTDALALEAIRLI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 689 FKYLPRAFKDGNDEEAREKMHNASAIAGMAFANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVVRYNAIkprkhalfp 768
Cdd:cd08188 221 AENLPKAVANGKDLEARENMAYAQFLAGMAFNNAGLGYVHAMAHQLGGFYNLPHGVCNAILLPHVMEFNLP--------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 769 kyehfVADERYAHIARMLGLPAS--SAAEGVESLVQAIIELGKSLNINMSIAGQGVDKDQFEevvgLLAERAFEDQCTTA 846
Cdd:cd08188 292 -----ACPERFADIARALGENTEglSDEEAAEAAIEAIRKLSRRVGIPSGLKELGVKEEDFP----LLAENALKDACGPT 362
|
410
....*....|....*
gi 872568246 847 NPKLPLISELKEIYM 861
Cdd:cd08188 363 NPRQATKEDVIAIYR 377
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
461-860 |
1.37e-114 |
|
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: 354.16 E-value: 1.37e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 461 FKLPPKIYFEKHATAYLANMP---NISRAFIVTDPGMVEHGYVDTVTHYLRKhaNDVKVEVFFEVEPDPSDETVFKGAEM 537
Cdd:cd08176 3 FVLNPTSYFGWGAIEEIGEEAkkrGFKKALIVTDKGLVKFGIVDKVTDVLKE--AGIAYTVFDEVKPNPTIENVMAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 538 MRSFQPDVIIALGGGSAMDAAKGMWLfyeypettfyGIKQKFLDIRKRTCKYPelgSKAQFV---AIPTTSGTGSEVTPF 614
Cdd:cd08176 81 YKESGADGIIAVGGGSSIDTAKAIGI----------IVANPGADVRSLEGVAP---TKNPAVpiiAVPTTAGTGSEVTIN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 615 AVITDKKNNIKYPLADYELTPDVAIVDPQFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLVFKYLPR 694
Cdd:cd08176 148 YVITDTEKKRKFVCVDPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYITKGAWELSDMLALKAIELIAKNLRK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 695 AFKDGNDEEAREKMHNASAIAGMAFANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVVRYNAIkprkhalfpkyehfV 774
Cdd:cd08176 228 AVANPNNVEARENMALAQYIAGMAFSNVGLGIVHSMAHPLSAFYDTPHGVANAILLPYVMEFNAP--------------A 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 775 ADERYAHIARMLGLP--ASSAAEGVESLVQAIIELGKSLNINMSIAGQGVDKDQFEevvgLLAERAFEDQCTTANPKLPL 852
Cdd:cd08176 294 TGEKYRDIARAMGVDttGMSDEEAAEAAVDAVKKLSKDVGIPQKLSELGVKEEDIE----ALAEDALNDVCTPGNPREAT 369
|
....*...
gi 872568246 853 ISELKEIY 860
Cdd:cd08176 370 KEDIIALY 377
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
484-864 |
6.62e-113 |
|
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: 349.91 E-value: 6.62e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 484 SRAFIVTDPGMVEHGYVDTVTHYLRKhaNDVKVEVFFEVEPDPSDETVFKGAEMMRSFQPDVIIALGGGSAMDAAKG--M 561
Cdd:cd14863 28 KKVLLVTDKGLKKAGIVDKIIDLLEE--AGIEVVVFDDVEPDPPDEIVDEAAEIAREEGADGVIGIGGGSVLDTAKAiaV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 562 WLFYEYPETTFYGIKQKFLDIRKrtckyPelgskaqFVAIPTTSGTGSEVTPFAVITDKKNNIKYPLADYELTPDVAIVD 641
Cdd:cd14863 106 LLTNPGPIIDYALAGPPVPKPGI-----P-------LIAIPTTAGTGSEVTPIAVITDEENGVKKSLLGPFLVPDLAILD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 642 PQFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLVFKYLPRAFKDGNDEEAREKMHNASAIAGMAFAN 721
Cdd:cd14863 174 PELTVGLPPSLTAATGMDALSHAIEAYTSKLANPMTDALALQAIRLIVKNLPRAVKDGDNLEARENMLLASNLAGIAFNN 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 722 AFLGINHSLAHKIGPEFHIPHGRANAILMPHVVRYNAikprkhalfPKYEhfvadERYAHIARMLGL--PASSAAEGVES 799
Cdd:cd14863 254 AGTHIGHAIAHALGALYHIPHGLACALALPVVLEFNA---------EAYP-----EKVKKIAKALGVsfPGESDEELGEA 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872568246 800 LVQAIIELGKSLNINMSIAGQGVDKDQFEEvvglLAERAFEDQCTTANPKLPLISELKEIYMKAY 864
Cdd:cd14863 320 VADAIREFMKELGIPSLFEDYGIDKEDLDK----IAEAVLKDPFAMFNPRPITEEEVAEILEAIY 380
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
461-864 |
1.55e-112 |
|
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: 349.15 E-value: 1.55e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 461 FKLPPKIYFEKHAtayLANMP------NISRAFIVTDPGMVEHGYVDTVTHYLRKHANDVkvEVFFEVEPDPSDETVFKG 534
Cdd:cd14865 3 FFNPTKIVSGAGA---LENLPaelarlGARRPLIVTDKGLAAAGLLKKVEDALGDAIEIV--GVFDDVPPDSSVAVVNEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 535 AEMMRSFQPDVIIALGGGSAMDAAKGMWLFYEYpettfyGIK----QKFLDIRKRtckypelgSKAQFVAIPTTSGTGSE 610
Cdd:cd14865 78 AARAREAGADGIIAVGGGSVIDTAKGVNILLSE------GGDdlddYGGANRLTR--------PLKPLIAIPTTAGTGSE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 611 VTPFAVITDKKNNIKYPLADYELTPDVAIVDPQFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLVFK 690
Cdd:cd14865 144 VTLVAVIKDEEKKVKLLFVSPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDALALQAIRLISE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 691 YLPRAFKDGNDEEAREKMHNASAIAGMAFANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVVRYNAIkprkhalfpky 770
Cdd:cd14865 224 NLPKAVKNGKDLEARLALAIAATMAGIAFSNSMVGLVHAIAHAVGAVAGVPHGLANSILLPHVMRYNLD----------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 771 ehfVADERYAHIARMLGLPASSAAEGVESLVQAII----ELGKSLNINMSIAGQGVDKDQFEEvvglLAERAFEDQCTTA 846
Cdd:cd14865 293 ---AAAERYAELALALAYGVTPAGRRAEEAIEAAIdlvrRLHELCGLPTRLRDVGVPEEQLEA----IAELALNDGAILF 365
|
410
....*....|....*...
gi 872568246 847 NPKLPLISELKEIYMKAY 864
Cdd:cd14865 366 NPREVDPEDILAILEAAY 383
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
476-860 |
1.57e-106 |
|
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: 332.97 E-value: 1.57e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 476 YLANMpNISRAFIVTDPGMVEHGYVDTVTHYLRkhANDVKVEVFFEVEPDPSDETVFKGAEMMRSFQPDVIIALGGGSAM 555
Cdd:cd17814 20 YAKNL-GARKVLVVTDPGVIKAGWVDEVLDSLE--AEGLEYVVFSDVTPNPRDFEVMEGAELYREEGCDGIVAVGGGSPI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 556 DAAKGMWLFyeypeTTFYGIKQKFLDIRKRTCKYPELgskaqfVAIPTTSGTGSEVTPFAVITDKKNNIKYPLADYELTP 635
Cdd:cd17814 97 DCAKGIGIV-----VSNGGHILDYEGVDKVRRPLPPL------ICIPTTAGSSADVSQFAIITDTERRVKMAIISKTLVP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 636 DVAIVDPQFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLVFKYLPRAFKDGNDEEAREKMHNASAIA 715
Cdd:cd17814 166 DVSLIDPETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDLHALEAIRLISENLPKAVADPDDLEAREKMMLASLQA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 716 GMAFANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVVRYNAIkprkhalfpkyehfVADERYAHIARMLGLPA--SSA 793
Cdd:cd17814 246 GLAFSNASLGAVHAMAHSLGGLLDLPHGECNALLLPHVIRFNFP--------------AAPERYRKIAEAMGLDVdgLDD 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872568246 794 AEGVESLVQAIIELGKSLNINMSIAGQGVDkdqfEEVVGLLAERAFEDQCTTANPKLPLISELKEIY 860
Cdd:cd17814 312 EEVAERLIEAIRDLREDLGIPETLSELGVD----EEDIPELAKRAMKDPCLVTNPRRPTREDIEEIY 374
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
464-862 |
1.68e-106 |
|
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: 333.28 E-value: 1.68e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 464 PPKIYFEKHATAYLAN---MPNISRAFIVTDPGMVEHGYVDTVTHYLRKHanDVKVEVFFEVEPDPSDETVFKGAEMMRS 540
Cdd:cd08189 5 EPELFEGAGSLLQLPEalkKLGIKRVLIVTDKGLVKLGLLDPLLDALKKA--GIEYVVFDGVVPDPTIDNVEEGLALYKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 541 FQPDVIIALGGGSAMDAAKGMWLFYEYPETTFYGIKqKFLDIRKRTckypelgskAQFVAIPTTSGTGSEVTPFAVITDK 620
Cdd:cd08189 83 NGCDAIIAIGGGSVIDCAKVIAARAANPKKSVRKLK-GLLKVRKKL---------PPLIAVPTTAGTGSEATIAAVITDP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 621 KNNIKYPLADYELTPDVAIVDPQFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLVFKYLPRAFKDGN 700
Cdd:cd08189 153 ETHEKYAINDPKLIPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETDEYALEAVKLIFENLPKAYEDGS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 701 DEEAREKMHNASAIAGMAFANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVVRYNAIKprkhalfpkyehfvADERYA 780
Cdd:cd08189 233 DLEARENMLLASYYAGLAFTRAYVGYVHAIAHQLGGLYGVPHGLANAVVLPHVLEFYGPA--------------AEKRLA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 781 HIARMLGL--PASSAAEGVESLVQAIIELGKSLNINMSIAgqGVDKDQFEEvvglLAERAFEDqcttANPK--LPLI--- 853
Cdd:cd08189 299 ELADAAGLgdSGESDSEKAEAFIAAIRELNRRMGIPTTLE--ELKEEDIPE----IAKRALKE----ANPLypVPRImdr 368
|
....*....
gi 872568246 854 SELKEIYMK 862
Cdd:cd08189 369 KDCEELLRK 377
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
485-861 |
2.05e-101 |
|
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: 319.83 E-value: 2.05e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 485 RAFIVTDPG-MVEHGYVDTVTHYLRKhaNDVKVEVFFEVEPDPSDETVFKGAEMMRSFQPDVIIALGGGSAMDAAKGMWL 563
Cdd:cd08185 27 KALIVTGKGsSKKTGLLDRVKKLLEK--AGVEVVVFDKVEPNPLTTTVMEGAALAKEEGCDFVIGLGGGSSMDAAKAIAF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 564 FYEYPETTFYGIKQKFldirkrtcKYPELGSKA-QFVAIPTTSGTGSEVTPFAVITDKKNNIKYPLADYELTPDVAIVDP 642
Cdd:cd08185 105 MATNPGDIWDYIFGGT--------GKGPPPEKAlPIIAIPTTAGTGSEVDPWAVITNPETKEKKGIGHPALFPKVSIVDP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 643 QFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLVFKYLPRAFKDGNDEEAREKMHNASAIAGMAFANA 722
Cdd:cd08185 177 ELMLTVPPRVTAYTGFDALFHAFESYISKNANPFSDMLALEAIRLVAKYLPRAVKDGSDLEAREKMAWASTLAGIVIANS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 723 FLGINHSLAHKIGPEF-HIPHGRANAILMPHVVRYNAikpRKHAlfpkyehfvadERYAHIArMLGLPASSAAEGVESLV 801
Cdd:cd08185 257 GTTLPHGLEHPLSGYHpNIPHGAGLAALYPAYFEFTI---EKAP-----------EKFAFVA-RAEASGLSDAKAAEDFI 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872568246 802 QAIIELGKSLNINMSIAGQGVDKDQFEEvvglLAERAFE--DQCTTANPKLPLISELKEIYM 861
Cdd:cd08185 322 EALRKLLKDIGLDDLLSDLGVTEEDIPW----LAENAMEtmGGLFANNPVELTEEDIVEIYE 379
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
461-860 |
1.10e-99 |
|
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: 314.90 E-value: 1.10e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 461 FKLPPKIYFEKHATAYL---ANMPNISRAFIVTDPGMVEHGYVDTVthylRKHANDVKVEVFFEVEPDPSDETVFKGAEM 537
Cdd:cd08196 3 YYQPVKIIFGEGILKELpdiIKELGGKRGLLVTDPSFIKSGLAKRI----VESLKGRIVAVFSDVEPNPTVENVDKCARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 538 MRSFQPDVIIALGGGSAMDAAKGMWLFYEYPETTFYGIKQKFLDIRKRtckypelgskAQFVAIPTTSGTGSEVTPFAVI 617
Cdd:cd08196 79 ARENGADFVIAIGGGSVLDTAKAAACLAKTDGSIEDYLEGKKKIPKKG----------LPLIAIPTTAGTGSEVTPVAVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 618 TDKKNNIKYPLADYELTPDVAIVDPQFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLVFKYLPRAFK 697
Cdd:cd08196 149 TDKEKGKKAPLVSPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSINHQPISDALALEAAKLVLENLEKAYN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 698 DGNDEEAREKMHNASAIAGMAFANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVVRYNAIkprkhalfpkyehfVADE 777
Cdd:cd08196 229 NPNDKEAREKMALASLLAGLAFSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNAE--------------ALPG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 778 RYAHIARMLGLpassaaEGVESLVQAIIELGKSLNINMSIAGQGVDKDQFEEvvglLAERAFEDQCTTANPKLPLISELK 857
Cdd:cd08196 295 RLDELAKQLGF------KDAEELADKIEELKKRIGLRTRLSELGITEEDLEE----IVEESFHPNRANNNPVEVTKEDLE 364
|
...
gi 872568246 858 EIY 860
Cdd:cd08196 365 KLL 367
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
464-863 |
1.69e-98 |
|
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: 312.14 E-value: 1.69e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 464 PPKIYFEKHATAYLANM---PNISRAFIVTDPGMVEHGYVDTVTHYLRkhANDVKVEVFFEVEPDPSDETVFKGAEMMRS 540
Cdd:cd14861 3 PTRIRFGAGAIAELPEElkaLGIRRPLLVTDPGLAALGIVDRVLEALG--AAGLSPAVFSDVPPNPTEADVEAGVAAYRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 541 FQPDVIIALGGGSAMDAAKGMWLF--YEYPETTFYGIKQKFLDIRKRTckypelgskAQFVAIPTTSGTGSEVTPFAVIT 618
Cdd:cd14861 81 GGCDGIIALGGGSAIDAAKAIALMatHPGPLWDYEDGEGGPAAITPAV---------PPLIAIPTTAGTGSEVGRAAVIT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 619 DKKNNIKYPLADYELTPDVAIVDPQFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLVFKYLPRAFKD 698
Cdd:cd14861 152 DDDTGRKKIIFSPKLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGFHPMADGIALEGLRLISEWLPRAVAD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 699 GNDEEAREKMHNASAIAGMAFANAfLGINHSLAHKIGPEFHIPHGRANAILMPHVVRYNaikpRKHalfpkyehfvADER 778
Cdd:cd14861 232 GSDLEARGEMMMAALMGAVAFQKG-LGAVHALAHALGALYGLHHGLLNAILLPYVLRFN----RPA----------VEDK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 779 YAHIARMLGLPASSAaegvESLVQAIIELGKSLNINMSIAGQGVDKDQFEEvvglLAERAFEDQCTTANPKLPLISELKE 858
Cdd:cd14861 297 LARLARALGLGLGGF----DDFIAWVEDLNERLGLPATLSELGVTEDDLDE----LAELALADPCHATNPRPVTAEDYRA 368
|
....*
gi 872568246 859 IYMKA 863
Cdd:cd14861 369 LLREA 373
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
465-864 |
1.52e-92 |
|
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: 297.53 E-value: 1.52e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 465 PKIYFEKHATAY----LANMpNISRAFIVTDPGMVEHGYVDTVTHYLRKHanDVKVEVFFEVEPDPSDETVFKGAEMMRS 540
Cdd:cd08190 2 SNIRFGPGATRElgmdLKRL-GAKKVLVVTDPGLAKLGLVERVLESLEKA--GIEVVVYDGVRVEPTDESFEEAIEFAKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 541 FQPDVIIALGGGSAMDAAKGMWLFYEYPettfygikQKFLD-----IRKRTckyPELGSKAQFVAIPTTSGTGSEVTPFA 615
Cdd:cd08190 79 GDFDAFVAVGGGSVIDTAKAANLYATHP--------GDFLDyvnapIGKGK---PVPGPLKPLIAIPTTAGTGSETTGVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 616 VITDKKNNIKYPLADYELTPDVAIVDPQFVMTVPPHVTADTGMDVLTHAIEAYVSVL------------------ANDYT 677
Cdd:cd08190 148 IFDLEELKVKTGISSRYLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTARPynarprpanpderpayqgSNPIS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 678 DGLALKAIDLVFKYLPRAFKDGNDEEAREKMHNASAIAGMAFANAFLGINHSLAHKIG-------------PEFHIPHGR 744
Cdd:cd08190 228 DVWAEKAIELIGKYLRRAVNDGDDLEARSNMLLASTLAGIGFGNAGVHLPHAMAYPIAglvkdyrppgypvDHPHVPHGL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 745 ANAILMPHVVRYNAikPrkhalfpkyehfVADERYAHIARMLG--LPASSAAEGVESLVQAIIELGKSLNINMSIAGQGV 822
Cdd:cd08190 308 SVALTAPAVFRFTA--P------------ACPERHLEAAELLGadTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGY 373
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 872568246 823 DKDQFEEvvglLAERAFEDQCTTA-NPKLPLISELKEIYMKAY 864
Cdd:cd08190 374 SEDDIPA----LVEGTLPQQRLLKlNPRPVTEEDLEEIFEDAL 412
|
|
| lactal_redase |
TIGR02638 |
lactaldehyde reductase; This clade of genes encoding iron-containing alcohol dehydrogenase ... |
461-860 |
2.86e-90 |
|
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: 290.49 E-value: 2.86e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 461 FKLPPKIYFEK----HATAYLANMPnISRAFIVTDPGMVEHGYVDTVTHYLRKHAndVKVEVFFEVEPDPSDETVFKGAE 536
Cdd:TIGR02638 4 LILNETSYFGAgaieDIVDEVKRRG-FKKALVVTDKDLIKFGVADKVTDLLDEAG--IAYELFDEVKPNPTITVVKAGVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 537 MMRSFQPDVIIALGGGSAMDAAKGMWLFYEYPEttfygikqkFLDIRKRTCKYPELGSKAQFVAIPTTSGTGSEVTPFAV 616
Cdd:TIGR02638 81 AFKASGADYLIAIGGGSPIDTAKAIGIISNNPE---------FADVRSLEGVAPTKKPGVPIIAIPTTAGTAAEVTINYV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 617 ITDKKNNIKYPLADYELTPDVAIVDPQFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLVFKYLPRAF 696
Cdd:TIGR02638 152 ITDEENKRKFVCVDPHDIPDVAVIDAEMMYSMPKSLTAATGMDALTHAIEGYITKGAWELTDMLHLKAIEIIARWLRSAV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 697 KDGNDEEAREKMHNASAIAGMAFANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVVRYNAIKprkhalfpkyehfvAD 776
Cdd:TIGR02638 232 EGGKDLEAREQMALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEFNAEF--------------TG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 777 ERYAHIARMLGLPAS--SAAEGVESLVQAIIELGKSLNINMSIAGQGVDKDQFEEvvglLAERAFEDQCTTANPKLPLIS 854
Cdd:TIGR02638 298 EKYREIAKAMGVKTEgmSDEEARDAAVEAVKTLSKRVGIPEGLSELGVKEEDIPA----LAEAALADVCTGGNPRETTVE 373
|
....*.
gi 872568246 855 ELKEIY 860
Cdd:TIGR02638 374 EIEELY 379
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
464-859 |
2.83e-88 |
|
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: 285.16 E-value: 2.83e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 464 PPKIYFEKHATAYLANM--PNISRAFIVTDPGMVEHGYVDTVTHYLRkhANDVKVEVFfEVEPDPSDETVFKGAEMMRSF 541
Cdd:cd08183 1 PPRIVFGRGSLQELGELaaELGKRALLVTGRSSLRSGRLARLLEALE--AAGIEVALF-SVSGEPTVETVDAAVALAREA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 542 QPDVIIALGGGSAMDAAK---GMwlfyeypeTTFYGIKQKFLDIRKRTCKYPElgSKAQFVAIPTTSGTGSEVTPFAVIT 618
Cdd:cd08183 78 GCDVVIAIGGGSVIDAAKaiaAL--------LTNEGSVLDYLEVVGKGRPLTE--PPLPFIAIPTTAGTGSEVTKNAVLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 619 DKKNNIKYPLADYELTPDVAIVDPQFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLVFKYLPRAFKD 698
Cdd:cd08183 148 SPEHGVKVSLRSPSMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTDALAREGLRLAARSLRRAYED 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 699 GNDEEAREKMHNASAIAGMAFANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVVRYNAikprkHALFPKYEHFVADER 778
Cdd:cd08183 228 GEDLEAREDMALASLLGGLALANAGLGAVHGLAGPLGGMFGAPHGAICAALLPPVLEANL-----RALREREPDSPALAR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 779 YAHIARMLGLPASSAAEGvesLVQAIIELGKSLNINmSIAGQGVDKDQFEEVVgllaERAFEDQCTTANPKLPLISELKE 858
Cdd:cd08183 303 YRELAGILTGDPDAAAED---GVEWLEELCEELGIP-RLSEYGLTEEDFPEIV----EKARGSSSMKGNPIELSDEELLE 374
|
.
gi 872568246 859 I 859
Cdd:cd08183 375 I 375
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
484-864 |
3.37e-88 |
|
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: 285.66 E-value: 3.37e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 484 SRAFIVTDPGMVEHGYVDTVTHYLRkhANDVKVEVFFEVEPDPSDETVFKGAEMMRSFQPDVIIALGGGSAMDAAK--GM 561
Cdd:cd08191 26 SRVLIVTDPRLASTPLVAELLAALT--AAGVAVEVFDGGQPELPVSTVADAAAAARAFDPDVVIGLGGGSNMDLAKvvAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 562 WLFYEYPETTFYGikqkFLDIRKRTCKypelgskaqFVAIPTTSGTGSEVTPFAVITDKKNNIKYPLADYELTPDVAIVD 641
Cdd:cd08191 104 LLAHGGDPRDYYG----EDRVPGPVLP---------LIAVPTTAGTGSEVTPVAVLTDPARGMKVGVSSPYLRPAVAIVD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 642 PQFVMTVPPHVTADTGMDVLTHAIEAYVSVL---------------ANDYTDGLALKAIDLVFKYLPRAFKDGNDEEARE 706
Cdd:cd08191 171 PELTLTCPPGVTADSGIDALTHAIESYTARDfppfprldpdpvyvgKNPLTDLLALEAIRLIGRHLPRAVRDGDDLEARS 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 707 KMHNASAIAGMAFANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVVRYNaikpRKHALfpkyehfvadERYAHIARML 786
Cdd:cd08191 251 GMALAALLAGLAFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLPYVMRFN----RPARA----------AELAEIARAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 787 GLPASSA-AEGVESLVQAIIELGKSLNINMSIAGQGVDKDQFEEVV--GLLAERafedqCTTANPKLPLISELKEIYMKA 863
Cdd:cd08191 317 GVTTAGTsEEAADRAIERVEELLARIGIPTTLADLGVTEADLPGLAekALSVTR-----LIANNPRPPTEEDLLRILRAA 391
|
.
gi 872568246 864 Y 864
Cdd:cd08191 392 F 392
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
464-839 |
2.23e-87 |
|
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: 282.58 E-value: 2.23e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 464 PPKIYFEKHATAYLANM---PNISRAFIVTDPGMVEHGYVDTvthYLRKHANDVKVEVFFEVEPDPSDETVFKGAEMMRS 540
Cdd:cd08182 1 PVKIIFGPGALAELKDLlggLGARRVLLVTGPSAVRESGAAD---ILDALGGRIPVVVFSDFSPNPDLEDLERGIELFRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 541 FQPDVIIALGGGSAMDAAKGMWLFYEYPETTFYGIKQKfldIRKRTCKYPELgskaqfVAIPTTSGTGSEVTPFAVITDK 620
Cdd:cd08182 78 SGPDVIIAVGGGSVIDTAKAIAALLGSPGENLLLLRTG---EKAPEENALPL------IAIPTTAGTGSEVTPFATIWDE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 621 KNNIKYPLADYELTPDVAIVDPQFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLVFKYLPRAFKDGN 700
Cdd:cd08182 149 AEGKKYSLAHPSLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYALRAIRLILENLPLLLENLP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 701 DEEAREKMHNASAIAGMAFANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVVRYNAikprkhalfPKYEHFVADERYA 780
Cdd:cd08182 229 NLEAREAMAEASLLAGLAISITKTTAAHAISYPLTSRYGVPHGHACALTLPAVLRYNA---------GADDECDDDPRGR 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 872568246 781 HIARMLGlpASSAAEgvesLVQAIIELGKSLNINMSIAGQGVDKDQFEevvgLLAERAF 839
Cdd:cd08182 300 EILLALG--ASDPAE----AAERLRALLESLGLPTRLSEYGVTAEDLE----ALAASVN 348
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
461-864 |
2.85e-87 |
|
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: 282.48 E-value: 2.85e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 461 FKLPPKIYFEKHATAYLANM---PNISRAFIVTDPGMVEHGYVDTVTHYLRkhANDVKVEVFFEVEPDPSDETVFKGAEM 537
Cdd:cd08193 1 FQTVPRIICGAGAAARLGELlreLGARRVLLVTDPGLVKAGLADPALAALE--AAGIAVTVFDDVVADPPEAVVEAAVEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 538 MRSFQPDVIIALGGGSAMDAAKGMWLFYEYPET--TFYGIKQkfldIRkrtckypelGSKAQFVAIPTTSGTGSEVTPFA 615
Cdd:cd08193 79 AREAGADGVIGFGGGSSMDVAKLVALLAGSDQPldDIYGVGK----AT---------GPRLPLILVPTTAGTGSEVTPIS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 616 VITD---KKNNIKYPLadyeLTPDVAIVDPQFVMTVPPHVTADTGMDVLTHAIEAYVS-VLANDYTDGLALKAIDLVFKY 691
Cdd:cd08193 146 IVTTgetEKKGVVSPQ----LLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSrHKKNPISDALAREALRLLGAN 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 692 LPRAFKDGNDEEAREKMHNASAIAGMAFANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVVRYNAikPRKHALfpkye 771
Cdd:cd08193 222 LRRAVEDGSDLEAREAMLLGSMLAGQAFANAPVAAVHALAYPLGGHFHVPHGLSNALVLPHVLRFNL--PAAEAL----- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 772 hfvaderYAHIARML--GLPASSAAEGVESLVQAIIELGKSLNINMSIAGQGVDkdqfEEVVGLLAERAFEDQ-CTTANP 848
Cdd:cd08193 295 -------YAELARALlpGLAFGSDAAAAEAFIDALEELVEASGLPTRLRDVGVT----EEDLPMLAEDAMKQTrLLVNNP 363
|
410
....*....|....*.
gi 872568246 849 KLPLISELKEIYMKAY 864
Cdd:cd08193 364 REVTEEDALAIYQAAL 379
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
485-864 |
5.74e-82 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 268.40 E-value: 5.74e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 485 RAFIVTDPGMVEHGYVDTVTHYLrkHANDVKVEVFFEVEPDPSDETVFKGAEMMRSFQPDVIIALGGGSAMDAAKGMWLF 564
Cdd:PRK10624 32 KALIVTDKTLVKCGVVAKVTDVL--DAAGLAYEIYDGVKPNPTIEVVKEGVEVFKASGADYLIAIGGGSPQDTCKAIGII 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 565 YEYPEttfygikqkFLDIRKRTCKYPELGSKAQFVAIPTTSGTGSEVTPFAVITDKKNNIKYPLADYELTPDVAIVDPQF 644
Cdd:PRK10624 110 SNNPE---------FADVRSLEGVAPTKKPSVPIIAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIPQVAFVDADM 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 645 VMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLVFKYLPRAFKdgNDEEAREKMHNASAIAGMAFANAFL 724
Cdd:PRK10624 181 MDSMPPGLKAATGVDALTHAIEGYITRGAWALTDMLHLKAIEIIAGALRGAVA--GDKEAGEGMALGQYIAGMGFSNVGL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 725 GINHSLAHKIGPEFHIPHGRANAILMPHVVRYNAIkprkhalfpkyehfVADERYAHIARMLGLPAS--SAAEGVESLVQ 802
Cdd:PRK10624 259 GLVHGMAHPLGAFYNTPHGVANAILLPHVMEYNAD--------------FTGEKYRDIARAMGVKVEgmSLEEARNAAVE 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872568246 803 AIIELGKSLNINMSIAGQGVDkdqfEEVVGLLAERAFEDQCTTANPKLPLISELKEIYMKAY 864
Cdd:PRK10624 325 AVKALNRDVGIPPHLRDVGVK----EEDIPALAQAAFDDVCTGGNPREATLEDIVELYKKAW 382
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
18-414 |
1.95e-75 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 253.67 E-value: 1.95e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 18 IDTLVNNGRKALQALESFTQEQIDNIVHEMALAGVDQHMPLAKLAVEETGRGVYEDKCIKNIFATEyiwhsikkdKTVGI 97
Cdd:PRK15398 38 VDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGMGRVEDKIAKNVAAAE---------KTPGV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 98 ihEDPHEE---------IIEIAePVGVVAGVTPVTNPTSTTMFKALIAIKTRNPIIFAFHPSAQKCSIAAAKTVYDAAVK 168
Cdd:PRK15398 109 --EDLTTEaltgdngltLIEYA-PFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELLNEAIVA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 169 AGAPKHCIQWIEKPSVEATKQLMNHEGVALVLATGGAGMVKSAYSTGKPALGVGPGNVPCYIEKSAHVKRAVNDLILSKT 248
Cdd:PRK15398 186 AGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPAVVKAAMKSGKKAIGAGAGNPPVVVDETADIEKAARDIVKGAS 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 249 FDNGMICASEQAIIVDKEIYDDVKTEMIANNCYFVTEEERRQLEKLVINENTcAVNSDIVGKSAQYIAELVGITVPENTK 328
Cdd:PRK15398 266 FDNNLPCIAEKEVIVVDSVADELMRLMEKNGAVLLTAEQAEKLQKVVLKNGG-TVNKKWVGKDAAKILEAAGINVPKDTR 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 329 MLVAEiqgIGAAYPL-SREKLSPVLACVKANSLEEGFAYCEEMlnLGGLGHSAVIHSVNKAVQKQFGLRMKACRLIVNAP 407
Cdd:PRK15398 345 LLIVE---TDANHPFvVTELMMPVLPVVRVKDVDEAIALAVKL--EHGNRHTAIMHSRNVDNLNKMARAIQTSIFVKNGP 419
|
....*...
gi 872568246 408 SSQG-GIG 414
Cdd:PRK15398 420 SYAGlGLG 427
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
18-415 |
2.42e-75 |
|
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: 252.54 E-value: 2.42e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 18 IDTLVNNGRKALQALESFTQEQIDNIVHEMALAGVDQHMPLAKLAVEETGRGVYEDKCIKNIFAteyiwhsikKDKTVGI 97
Cdd:cd07121 6 VDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGMGRVEDKIAKNHLA---------AEKTPGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 98 ihEDPHEE---------IIEIAePVGVVAGVTPVTNPTSTTMFKALIAIKTRNPIIFAFHPSAQKCSIAAAKTVYDAAVK 168
Cdd:cd07121 77 --EDLTTTawsgdngltLVEYA-PFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 169 AGAPKHCIQWIEKPSVEATKQLMNHEGVALVLATGGAGMVKSAYSTGKPALGVGPGNVPCYIEKSAHVKRAVNDLILSKT 248
Cdd:cd07121 154 AGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVKAALSSGKKAIGAGAGNPPVVVDETADIEKAARDIVQGAS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 249 FDNGMICASEQAIIVDKEIYDDVKTEMIANNCYFVTEEE-RRQLEKLVINENTCAVNSDIVGKSAQYIAELVGITVPENT 327
Cdd:cd07121 234 FDNNLPCIAEKEVIAVDSVADYLIAAMQRNGAYVLNDEQaEQLLEVVLLTNKGATPNKKWVGKDASKILKAAGIEVPADI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 328 KMLVAEIQgigAAYPL-SREKLSPVLACVKANSLEEGFAYCEEMlnLGGLGHSAVIHSVNKAVQKQFGLRMKACRLIVNA 406
Cdd:cd07121 314 RLIIVETD---KDHPFvVEEQMMPILPVVRVKNFDEAIELAVEL--EHGNRHTAIIHSKNVENLTKMARAMQTTIFVKNG 388
|
410
....*....|
gi 872568246 407 PSSQG-GIGD 415
Cdd:cd07121 389 PSYAGlGVGG 398
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
461-758 |
6.25e-70 |
|
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: 235.17 E-value: 6.25e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 461 FKLPPKIYFEKHATAYLANmpNIS----RAFIVTdpGMV---EHGYVDTVTHYLRKhaNDVKVEVFFEVEPDPSDETVFK 533
Cdd:cd08181 1 FYMPTKVYFGKNCVEKHAD--ELAalgkKALIVT--GKHsakKNGSLDDVTEALEE--NGIEYFIFDEVEENPSIETVEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 534 GAEMMRSFQPDVIIALGGGSAMDAAKGMWLFY----EYPETTFYGIKQKFLDIrkrtckypelgskaqfVAIPTTSGTGS 609
Cdd:cd08181 75 GAELARKEGADFVIGIGGGSPLDAAKAIALLAankdGDEDLFQNGKYNPPLPI----------------VAIPTTAGTGS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 610 EVTPFAVITDKKNNIKYPLADYELTPDVAIVDPQFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLVF 689
Cdd:cd08181 139 EVTPYSILTDHEKGTKKSFGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSVKATPLSDALALEALRLIG 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872568246 690 KYLPRAFKDGNDEEAREKMHNASAIAGMAFANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVVRYNA 758
Cdd:cd08181 219 ECLPNLLGDELDEEDREKLMYASTLAGMVIAQTGTTLPHGLGYPLTYFKGIPHGRANGILLPAYLKLCE 287
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
26-452 |
8.62e-69 |
|
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: 233.65 E-value: 8.62e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 26 RKALQALESFTQEQIDNIVHEMALAGVDQHMPLAKLAVEETGR-------------GVYEDKCIKNIFATEYIWHSIkkD 92
Cdd:cd07077 4 KNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAyirslianwiammGCSESKLYKNIDTERGITASV--G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 93 KTVGIIHEDPHEEIIeIAEPVGVVAGVTPVTNPTSTtMFKALIAIKTRNPIIFAFHPSAqKCSIAAAKTVYDAAVKAGAP 172
Cdd:cd07077 82 HIQDVLLPDNGETYV-RAFPIGVTMHILPSTNPLSG-ITSALRGIATRNQCIFRPHPSA-PFTNRALALLFQAADAAHGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 173 KHCIQWIEKPSVEATKQLMNHEGVALVLATGGAGMVKSAY--STGKPALGVGPGNVPCYIEKSAHVKRAVNDLILSKTFD 250
Cdd:cd07077 159 KILVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAVkhSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 251 NgMICASEQAIIVDKEIYDDVKTEMIANNCYfvteeerrqleklvinentcavnsdivgksaqyiaelVGITVPENTKML 330
Cdd:cd07077 239 Q-NACASEQNLYVVDDVLDPLYEEFKLKLVV-------------------------------------EGLKVPQETKPL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 331 VAEIqgIGAAYPLSREKLSPVLACVKANSLEEGFAYCEEMLNLGGLGHSAVIHSVNKAVQKQFGLRMKACRLIVNAPSSQ 410
Cdd:cd07077 281 SKET--TPSFDDEALESMTPLECQFRVLDVISAVENAWMIIESGGGPHTRCVYTHKINKVDDFVQYIDTASFYPNESSKK 358
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 872568246 411 GGiGDIYN-GFIPSLTLGCGSYGKnsvsQNVTATHLLNIKRLA 452
Cdd:cd07077 359 GR-GAFAGkGVERIVTSGMNNIFG----AGVGHDALRPLKRLV 396
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
485-863 |
4.41e-67 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 228.69 E-value: 4.41e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 485 RAFIVTDPGMVEHGYVDTVTHYLRKhaNDVKVEVFFEVEPDPSDETVFKGAEMMRSFQPDVIIALGGGSAMDAAKGMWLf 564
Cdd:PRK09860 33 RTLIVTDNMLTKLGMAGDVQKALEE--RNIFSVIYDGTQPNPTTENVAAGLKLLKENNCDSVISLGGGSPHDCAKGIAL- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 565 yeypettfygIKQKFLDIRK-----RTCKyPELgskaQFVAIPTTSGTGSEVTPFAVITDKKNNIKYPLADYELTPDVAI 639
Cdd:PRK09860 110 ----------VAANGGDIRDyegvdRSAK-PQL----PMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTPLLSV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 640 VDPQFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLVFKYLPRAFKDGNDEEAREKMHNASAIAGMAF 719
Cdd:PRK09860 175 NDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMAYAQFLAGMAF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 720 ANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVVRYNAIkprkhalfpkyehfVADERYAHIARMLGLPAS--SAAEGV 797
Cdd:PRK09860 255 NNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSK--------------VAAARLRDCAAAMGVNVTgkNDAEGA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872568246 798 ESLVQAIIELGKSLNINMSIAGQGVDkdqfEEVVGLLAERAFEDQCTTANPKLPLISELKEIYMKA 863
Cdd:PRK09860 321 EACINAIRELAKKVDIPAGLRDLNVK----EEDFAVLATNALKDACGFTNPIQATHEEIVAIYRAA 382
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
525-863 |
8.43e-65 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 222.60 E-value: 8.43e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 525 DPSDETVFKGAEMMRSFQPDVIIALGGGSAMDAAKGMWLFYEYPETTFygikqkfLDIRKRTCKYPELgskaQFVAIPTT 604
Cdd:PRK15454 89 EPCITDVCAAVAQLRESGCDGVIAFGGGSVLDAAKAVALLVTNPDSTL-------AEMSETSVLQPRL----PLIAIPTT 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 605 SGTGSEVTPFAVITDKKNNIKYPLADYELTPDVAIVDPQFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKA 684
Cdd:PRK15454 158 AGTGSETTNVTVIIDAVSGRKQVLAHASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 685 IDLVFKYLPRAFKDGNDEEAREKMHNASAIAGMAFANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVVRYNaikprkh 764
Cdd:PRK15454 238 IAMIGKSLPKAVGYGHDLAARESMLLASCMAGMAFSSAGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEFN------- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 765 alfpkyeHFVADERYAHIARMLGLPASSAAEGVESLVQAIIELGkslnINMSIAGQGVDKDQFeevvGLLAERAFEDQCT 844
Cdd:PRK15454 311 -------RMVCRERFSQIGRALRTKKSDDRDAINAVSELIAEVG----IGKRLGDVGATSAHY----GAWAQAALEDICL 375
|
330
....*....|....*....
gi 872568246 845 TANPKLPLISELKEIYMKA 863
Cdd:PRK15454 376 RSNPRTASLEQIVGLYAAA 394
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
461-860 |
9.99e-59 |
|
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor NAD(P)H being oxidized in the process; The butanol dehydrogenase (BDH) is involved in the final step of the butanol formation pathway in anaerobic micro-organism. Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor NAD(P)H being oxidized in the process. Activity in the reverse direction is 50-fold lower than that in the forward direction. The NADH-BDH has higher activity with longer chained aldehydes and is inhibited by metabolites containing an adenine moiety. This protein family belongs to the so-called iron-containing alcohol dehydrogenase superfamily. Since members of this superfamily use different divalent ions, preferentially iron or zinc, it has been suggested to be renamed to family III metal-dependent polyol dehydrogenases. This family also includes E. coli YqhD enzyme, an NADP-dependent dehydrogenase whose activity measurements with several alcohols demonstrate preference for alcohols longer than C3. The active site of YqhD contains a Zn metal, and a modified NADPH cofactor bearing OH groups on the saturated C5 and C6 atoms, possibly due to oxygen stress on the enzyme, which would functionally work under anaerobic conditions.
Pssm-ID: 341466 [Multi-domain] Cd Length: 382 Bit Score: 205.36 E-value: 9.99e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 461 FKLPPKIYFEKHATAYLANM--PNISRAFIVTDPG-MVEHGYVDTVTHYLRKhaNDVKVEVFFEVEPDPSDETVFKGAEM 537
Cdd:cd08187 4 FYNPTKIIFGKGAIEELGEEikKYGKKVLLVYGGGsIKKNGLYDRVVASLKE--AGIEVVEFGGVEPNPRLETVREGIEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 538 MRSFQPDVIIALGGGSAMDAAKGM----------WLFYEYPETTfygikQKFLDIrkrtckypelgskaqfVAIPTTSGT 607
Cdd:cd08187 82 AREENVDFILAVGGGSVIDAAKAIaagakydgdvWDFFTGKAPP-----EKALPV----------------GTVLTLAAT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 608 GSEVTPFAVITDKKNNIKYPLADYELTPDVAIVDPQFVMTVPPHVTADTGMDVLTHAIEAYVS-VLANDYTDGLALKAID 686
Cdd:cd08187 141 GSEMNGGAVITNEETKEKLGFGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTgTEDAPLQDRLAEGLLR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 687 LVFKYLPRAFKDGNDEEAREKMHNASAIAgmafANAFLGI-------NHSLAHKIGPEFHIPHGRANAILMPHVVRYnaI 759
Cdd:cd08187 221 TVIENGPKALKDPDDYEARANLMWAATLA----LNGLLGAgrggdwaTHAIEHELSALYDITHGAGLAIVFPAWMRY--V 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 760 KPRKHALFpkyehfvadERYAHiaRMLGLPAS-SAAEGVESLVQAIIELGKSLNINMSIAGQGVDKDQFEEvvglLAERA 838
Cdd:cd08187 295 LKKKPERF---------AQFAR--RVFGIDPGgDDEETALEGIEALEEFFKSIGLPTTLSELGIDEEDIEE----MAEKA 359
|
410 420
....*....|....*....|...
gi 872568246 839 FE-DQCTTANPKLPLiSELKEIY 860
Cdd:cd08187 360 VRgGGLGGGFKPLTR-EDIEEIL 381
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
482-859 |
1.71e-57 |
|
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: 202.09 E-value: 1.71e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 482 NISRAFIVTDpgmvehGYVDTVTHY---LRKHANDVKVEVFFEVEPDPSDETVFKGAEMMRSFQPDVIIALGGGSAMDAA 558
Cdd:cd08192 22 GASRVFIVTS------KSLATKTDVikrLEEALGDRHVGVFSGVRQHTPREDVLEAARAVREAGADLLVSLGGGSPIDAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 559 KGMWLFYEYPETTFYGIKQKFLDIRKRTckyPELGSKAQFVAIPTT-SGtgSEVTPFAVITDKKNNIKYPLADYELTPDV 637
Cdd:cd08192 96 KAVALALAEDVTDVDQLDALEDGKRIDP---NVTGPTLPHIAIPTTlSG--AEFTAGAGATDDDTGHKQGFAHPELGPDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 638 AIVDPQFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLVFKYLPRAFKDGNDEEAREKMHNASAIAGM 717
Cdd:cd08192 171 VILDPELTLHTPERLWLSTGIRAVDHAVETLCSPQATPFVDALALKALRLLFEGLPRSKADPEDLEARLKCQLAAWLSLF 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 718 AFANAF-LGINHSLAHKIGPEFHIPHGRANAILMPHVVRYNAikprkhalfpkyehFVADERYAHIARMLGLPASSAAEG 796
Cdd:cd08192 251 GLGSGVpMGASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNA--------------PVNAERQRLIARALGLVTGGLGRE 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872568246 797 VESLVQAIIELGKSLNINMSIAGQGVDKDQFEEvvglLAERAFEDQCTTANP-KLPLISELKEI 859
Cdd:cd08192 317 AADAADAIDALIRELGLPRTLRDVGVGRDQLEK----IAENALTDVWCRTNPrPITDKDDVLEI 376
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
483-852 |
2.70e-50 |
|
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: 181.69 E-value: 2.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 483 ISRAFIVTDPG-MVEHGYVDTVTHYLRKHAndVKVEVFFEVEPDPSDETVFKGAEMMRSFQPDVIIALGGGSAMDAAKGM 561
Cdd:cd08186 23 IDKVIIVTGRSsYKKSGAWDDVEKALEENG--IEYVVYDKVTPNPTVDQADEAAKLARDFGADAVIAIGGGSPIDTAKSV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 562 WLFYEYPETTFYGIKQKfldiRKRTCKYPELgskaqfVAIPTTSGTGSEVTPFAVITDKKNNIKYPLADYELTPDVAIVD 641
Cdd:cd08186 101 AVLLAYGGKTARDLYGF----RFAPERALPL------VAINLTHGTGSEVDRFAVATIPEKGYKPGIAYDCIYPLYAIDD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 642 PQFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLVFKYLPRAFKDGNDEEAREKMHNASAIAGMAFAN 721
Cdd:cd08186 171 PRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAIRLIAEYLPRALANPKDLEARYWLLYASMIAGIAIDN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 722 AFLGINHSLAH---KIGPEfhIPHGRANAILMPHVVRYnaIKPRKHALFPK-YEHFVADERyahiarmlglPASSAAEGV 797
Cdd:cd08186 251 GLLHLTHALEHplsGLKPE--LPHGLGLALLGPAVVKY--IYKAVPETLADiLRPIVPGLK----------GTPDEAEKA 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 872568246 798 EslvQAIIELGKSLNINMSIAGQGVDKDQFEEVVgllaERAFedqcttANPKLPL 852
Cdd:cd08186 317 A---RGVEEFLFSVGFTEKLSDYGFTEDDVDRLV----ELAF------TTPSLDL 358
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
484-859 |
3.11e-50 |
|
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: 181.66 E-value: 3.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 484 SRAFIVTDPGMVEHGYV-DTVTHYL-RKHANdvkveVFFEVEPDPSDETVFKGAEMMRSFQPDVIIALGGGSAMDAAKGM 561
Cdd:cd14866 28 RRALVVCGSSVGANPDLmDPVRAALgDRLAG-----VFDGVRPHSPLETVEAAAEALREADADAVVAVGGGSAIVTARAA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 562 WLF------YEYPETTFYGikqkfldirKRTCKYPELGS-KAQFVAIPTTSGTGSEVTPFAViTDKKNNIKYPLADYELT 634
Cdd:cd14866 103 SILlaedrdVRELCTRRAE---------DGLMVSPRLDApKLPIFVVPTTPTTADVKAGSAV-TDPPAGQRLALFDPKTR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 635 PDVAIVDPQFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLVFKYLPRAfKDGNDEEAREKMHNASAI 714
Cdd:cd14866 173 PAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHADPLADATLMHALRLLADGLPRL-ADDDDPAARADLVLAAVL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 715 AGMAFANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVVRYNAIkprkhalfpkyehfVADERYAHIARMLGLPASSAA 794
Cdd:cd14866 252 AGYGTDHTGGGVIHALGHAIGARYGVQNGVVHAILLPHVLRFNAP--------------ATDGRLDRLAEALGVADAGDE 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872568246 795 EGVESLVQAIIELGKSLNINMSIAGQGVDKDQFEEvvglLAERAFEDQCTTANPK-LPLISELKEI 859
Cdd:cd14866 318 ASAAAVVDAVEALLDALGVPTRLRDLGVSREDLPA----IAEAAMDDWFMDNNPRpVPTAEELEAL 379
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
461-817 |
2.67e-46 |
|
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: 170.17 E-value: 2.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 461 FKLPPKIYFEKHAtayLANMPNI-----SRAFIVTDPGMVEHGYVDTVTHYLRKHAndVKVEVFFEVEPDPSDETVFKGA 535
Cdd:cd14864 1 FKIPPNIVFGADS---LERIGEEvkeygSRFLLITDPVLKESGLADKIVSSLEKAG--ISVIVFDEIPASATSDTIDEAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 536 EMMRSFQPDVIIALGGGSAMDAAKGMWLFYEYPETTFYgikqkFLDirKRTCKYPELgskaQFVAIPTTSGTGSEVTPFA 615
Cdd:cd14864 76 ELARKAGADGIIAVGGGKVLDTAKAVAILANNDGGAYD-----FLE--GAKPKKKPL----PLIAVPTTPRSGFEFSDRF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 616 VITDKKNNIKYPLADYELTPDVAIVDPQFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLVFKYLPRA 695
Cdd:cd14864 145 PVVDSRSREVKLLKAQPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNFFSDALALKAIELVSENLDGA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 696 FKDGNDEEAREKMHNASAIAGMAFANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVVRYNAIkprkhalfpkyehfVA 775
Cdd:cd14864 225 LADPKNTPAEELLAQAGCLAGLAASSSSPGLATALALAVNSRYKVSKSLVASILLPHVIEYAAT--------------SA 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 872568246 776 DERYAHIARMLGL------PASSAAEGVESLVQAIIELG-----KSLNINMSI 817
Cdd:cd14864 291 PDKYAKIARALGEdvegasPEEAAIAAVEGVRRLIAQLNlptrlKDLDLASSL 343
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
461-864 |
4.65e-44 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 164.09 E-value: 4.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 461 FKLPPKIYFEKHATAYLANM--PNISRAFIVTDPGMVE-HGYVDTVTHYLrkHANDVKVEVFFEVEPDPSDETVFKGAEM 537
Cdd:COG1979 6 FYNPTKIIFGKGQIAKLGEEipKYGKKVLLVYGGGSIKkNGLYDQVKAAL--KEAGIEVVEFGGVEPNPRLETVRKGVEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 538 MRSFQPDVIIALGGGSAMDAAKGM----------WLFYEypettfygikqkfldiRKRTCK--YPelgskaqFVAIPTTS 605
Cdd:COG1979 84 CKEEGIDFILAVGGGSVIDGAKAIaagakydgdpWDILT----------------GKAPVEkaLP-------LGTVLTLP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 606 GTGSEVTPFAVITDKKNNIKYPLADYELTPDVAIVDPQFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDY-TDGLA--- 681
Cdd:COG1979 141 ATGSEMNSGSVITNEETKEKLGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYFTYPVDAPlQDRFAegl 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 682 LKAidlVFKYLPRAFKDGNDEEAREKMHNASAIAgmafANAFLGI-------NHSLAHKIGPEFHIPHGRANAILMPHVV 754
Cdd:COG1979 221 LRT---LIEEGPKALKDPEDYDARANLMWAATLA----LNGLIGAgvpqdwaTHMIEHELSALYDIDHGAGLAIVLPAWM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 755 RYnaIKPRKHALFpkyehfvadERYAHiaRMLGLPASSAAEGVESLVQAIIELGKSLNINMSIAGQGVDKDQFEEvvglL 834
Cdd:COG1979 294 RY--VLEEKPEKF---------AQYAE--RVWGITEGDDEERALEGIEATEEFFESLGLPTRLSEYGIDEEDIEE----M 356
|
410 420 430
....*....|....*....|....*....|..
gi 872568246 835 AERAFEDQCTT--ANPKLPLiSELKEIYMKAY 864
Cdd:COG1979 357 AEKATAHGMTAlgEFKDLTP-EDVREILELAL 387
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
26-432 |
8.95e-41 |
|
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: 153.92 E-value: 8.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 26 RKALQALESFTQEQIDNIVHEMALAGVDQHMPLAKLAVEETG--RGVYEDKCIKNIFATEYIWHSIKKDKTVGIIHEDPH 103
Cdd:cd06534 4 RAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGkpIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 104 EEIIEIAEPVGVVAGVTPVTNPTSTTMFKALIAIKTRNPIIFAFHPSAQKCSIAAAKTVYDaavkAGAPKHCIQWIEKPS 183
Cdd:cd06534 84 GEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQE----AGLPPGVVNVVPGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 184 VEATKQLMNHEGVALVLATGGAGMVKSAY----STGKPALGVGPGNVPCYIEKSAHVKRAVNDLILSKTFDNGMICASEQ 259
Cdd:cd06534 160 DEVGAALLSHPRVDKISFTGSTAVGKAIMkaaaENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 260 AIIVDKEIYDdvktemianncyfvteeerrqleklvinentcavnsdivgksaQYIAELVGITVPENTKMLVA--EIQGi 337
Cdd:cd06534 240 RLLVHESIYD-------------------------------------------EFVEKLVTVLVDVDPDMPIAqeEIFG- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 338 gaayplsreklsPVLACVKANSLEEGFayceEMLNLGGLGHSAVIHSVNKAVQKQFGLRMKACRLIVNAPSSQGGIGDIY 417
Cdd:cd06534 276 ------------PVLPVIRFKDEEEAI----ALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEAPF 339
|
410
....*....|....*
gi 872568246 418 NGFIPSltlGCGSYG 432
Cdd:cd06534 340 GGVKNS---GIGREG 351
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
458-864 |
3.79e-39 |
|
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: 149.29 E-value: 3.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 458 MQWFKLPPKIYFEKHATAYLANMpNISRA-FIVTDPGMVEHgyvdtvthYLRKHANDVKVeVFFE--VEPDPSDETVFKG 534
Cdd:cd14860 1 MKEFRIKPEIYQFDTCKEFAEEF-KLGKDdLVLTNEYIYEP--------YFEPLNLDCAV-IFQEkyGTGEPSDEMVEAI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 535 AEMMRSFQPDVIIALGGGSAMDAAKGMWLFYEYPETTFYgikQKFLDIRKrtckypelgsKAQFVAIPTTSGTGSEVTPF 614
Cdd:cd14860 71 YKDIKKYGYKRVIAIGGGTVIDIAKLLALKGISPVLDLF---DGKIPLIK----------EKELIIVPTTCGTGSEVTNI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 615 AVITDKKNNIKYPLADYELTPDVAIVDPQFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLVFKYLPR 694
Cdd:cd14860 138 SIVELTSLGTKKGLAVDELYADKAVLIPELLKGLPYKVFATSSIDALIHAIESYLSPKATPYTEMFSYKAIEMILEGYQE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 695 AFKDGndEEAREKMHN----ASAIAGMAFANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVVR-YNAIKPrKHALfpk 769
Cdd:cd14860 218 IAEKG--EEARFPLLGdfliASNYAGIAFGNAGCAAVHALSYPLGGKYHVPHGEANYAVFTGVLKnYQEKNP-DGEI--- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 770 yehfvaDERYAHIARMLGLPASSAAEGVESLVQAIIELgKSLNinmsiaGQGVDKDQFEEvvglLAERAFEDQCT-TANP 848
Cdd:cd14860 292 ------KKLNEFLAKILGCDEEDVYDELEELLNKILPK-KPLH------EYGMKEEEIDE----FADSVMENQQRlLANN 354
|
410
....*....|....*..
gi 872568246 849 KLPL-ISELKEIYMKAY 864
Cdd:cd14860 355 YVPLdREDVAEIYKELY 371
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
464-797 |
1.06e-38 |
|
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: 145.20 E-value: 1.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 464 PPKIYFEKHATAYLANMP--NISRAFIVTDPGMVEhGYVDTVTHYLRKHANdvkVEVFFEVEPDPSDETVFKGAEMMRSF 541
Cdd:cd07766 1 PTRIVFGEGAIAKLGEIKrrGFDRALVVSDEGVVK-GVGEKVADSLKKGLA---VAIFDFVGENPTFEEVKNAVERARAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 542 QPDVIIALGGGSAMDAAKgmwlfyeypettFYGIKqkfldirkrtckypeLGSKAQFVAIPTTSGTGSEVTPFAVITDKK 621
Cdd:cd07766 77 EADAVIAVGGGSTLDTAK------------AVAAL---------------LNRGIPFIIVPTTASTDSEVSPKSVITDKG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 622 NNIKYplADYELTPDVAIVDPQFVMTVPPHVTADTGMDVLTHAIEayvsvlandytdglalkaidlvfkylprafkdgnd 701
Cdd:cd07766 130 GKNKQ--VGPHYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVE----------------------------------- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 702 eeaREKMHNASAIAGMAFANA-FLGINHSLAHKIGPEFHIPHGRANAILMPHVVRYNAikprkhALFPKYEHFVadERYA 780
Cdd:cd07766 173 ---LEKVVEAATLAGMGLFESpGLGLAHAIGHALTAFEGIPHGEAVAVGLPYVLKVAN------DMNPEPEAAI--EAVF 241
|
330
....*....|....*..
gi 872568246 781 HIARMLGLPASSAAEGV 797
Cdd:cd07766 242 KFLEDLGLPTHLADLGV 258
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
483-848 |
2.47e-38 |
|
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: 146.11 E-value: 2.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 483 ISRAFIVTDPGMVEHgyVDTVTHYLRkhanDVKVEVFFEVEPDPSDETVFKGAEMMRSFQPDVIIALGGGSAMDAAKGmw 562
Cdd:cd08177 23 ARRALVLSTPRQRAL--AERVAALLG----DRVAGVFDGAVMHVPVEVAERALAAAREAGADGLVAIGGGSAIGLAKA-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 563 lfyeypettfygikqkfldIRKRTckypelgsKAQFVAIPTTSgTGSEVTPFAVITdkKNNIKYPLADYELTPDVAIVDP 642
Cdd:cd08177 95 -------------------IALRT--------GLPIVAVPTTY-AGSEMTPIWGET--EDGVKTTGRDPRVLPRTVIYDP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 643 QFVMTVPPHVTADTGMDVLTHAIEAYVSVLANDYTDGLALKAIDLVFKYLPRAFKDGNDEEAREKMHNASAIAGMAFANA 722
Cdd:cd08177 145 DLTLGLPAALSVASGLNALAHAVEALYAPDANPITSLLAEEGIRALARALPRLVADPSDLEARSDALYGAWLAGVVLGSV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 723 FLGINHSLAHKIGPEFHIPHGRANAILMPHVVRYNAikprkhalfpkyeHFVADErYAHIARmlglpassaAEGVESLVQ 802
Cdd:cd08177 225 GMGLHHKLCHVLGGTFDLPHAETHAVVLPHVLAYNA-------------PAAPDA-MARLAR---------ALGGGDAAG 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 872568246 803 AIIELGKSLNINMSIAGQGVDKDQFEEVVGLLAERAFedqcttANP 848
Cdd:cd08177 282 GLYDLARRLGAPTSLRDLGMPEDDIDRAADLALANPY------PNP 321
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
507-770 |
9.61e-25 |
|
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: 106.58 E-value: 9.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 507 LRKHANDVKVevFFEVEPDPSDETVFKGAEMMRSFQ---PDVIIALGGGSAMDAAKGMWLFYEYPE--TTFYG---IKQK 578
Cdd:cd08184 46 LPLQNGDLLI--FVDTTDEPKTDQIDALRAQIRAENdklPAAVVGIGGGSTMDIAKAVSNMLTNPGsaADYQGwdlVKNP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 579 FLDIrkrtckypelgskaqfVAIPTTSGTGSEVTPFAVIT--DKKNNIKyplADYELtPDVAIVDPQFVMTVPPHVTADT 656
Cdd:cd08184 124 GIYK----------------IGVPTLSGTGAEASRTAVLTgpEKKLGIN---SDYTV-FDQVILDPELIATVPRDQYFYT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 657 GMDVLTHAIEAYVSVLANDYTDGLALKAIDL---VFkylpraFKDGND-EEAREKMHNASAIAGMAFANAFLGINHSLAH 732
Cdd:cd08184 184 GMDCYIHCVESLNGTYRNAFGDAYAEKALELcrdVF------LSDDMMsPENREKLMVASYLGGSSIANSQVGVCHALSY 257
|
250 260 270
....*....|....*....|....*....|....*...
gi 872568246 733 KIGPEFHIPHGRANAILMPHVVRYnaiKPRKHALFPKY 770
Cdd:cd08184 258 GLSVVLGTHHGVANCIVFNVLEEF---YPEGVKEFREM 292
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
458-836 |
3.81e-19 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 90.62 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 458 MQWFKL--PPKIYFEKHATAYLAN-MPNISRAFIVTDPGMVEH-GYVDTVTHYLRKHandvKVEVFFEVEPDPSDETVFK 533
Cdd:PRK15138 1 MNNFNLhtPTRILFGKGAIAGLREqIPADARVLITYGGGSVKKtGVLDQVLDALKGM----DVLEFGGIEPNPTYETLMK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 534 GAEMMRSFQPDVIIALGGGSAMDAAKGMWLFYEYPETT--FYGIKQKFLDIRKrtckypelgskaqfvAIP-----TTSG 606
Cdd:PRK15138 77 AVKLVREEKITFLLAVGGGSVLDGTKFIAAAANYPENIdpWHILETGGKEIKS---------------AIPmgsvlTLPA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 607 TGSEVTPFAVITDKKNNIKYPLADYELTPDVAIVDPQFVMTVPPHVTADTGMDVLTHAIEAYVSVLAN-----DYTDGLA 681
Cdd:PRK15138 142 TGSESNAGAVISRKTTGDKQAFHSPHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVDakiqdRFAEGIL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 682 LKAIDlvfkYLPRAFKDGNDEEAREkmhNASAIAGMAFaNAFLGI-------NHSLAHKIGPEFHIPHGRANAILMPHVv 754
Cdd:PRK15138 222 LTLIE----EGPKALKEPENYDVRA---NVMWAATQAL-NGLIGAgvpqdwaTHMLGHELTAMHGLDHAQTLAIVLPAL- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 755 rYNAIKPRKHALFPKYEHfvaderyahiaRMLGLPASSAAEGVESLVQAIIELGKSLNINMSIAGQGVDKDQFEEVVGLL 834
Cdd:PRK15138 293 -WNEKRDTKRAKLLQYAE-----------RVWNITEGSDDERIDAAIAATRNFFEQMGVPTRLSDYGLDGSSIPALLKKL 360
|
..
gi 872568246 835 AE 836
Cdd:PRK15138 361 EE 362
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
58-432 |
4.26e-17 |
|
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: 84.57 E-value: 4.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 58 LAKLAVEETGR----GVYE-DKCIKNI-FATEYIwHSIKKDKtvgIIHEDPHEEIIEIAEPVGVVAGVTPVTNPTSTTMF 131
Cdd:cd07078 40 LAALETLETGKpieeALGEvARAADTFrYYAGLA-RRLHGEV---IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAW 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 132 KALIAIKTRNPIIfaFHPSaQKCSIAAAKtVYDAAVKAGAPKHCIQWIEKPSVEATKQLMNHEGVALVLATG----GAGM 207
Cdd:cd07078 116 KLAPALAAGNTVV--LKPS-ELTPLTALL-LAELLAEAGLPPGVLNVVTGDGDEVGAALASHPRVDKISFTGstavGKAI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 208 VKSAYSTGKP---ALGvgpGNVPCYIEKSAHVKRAVNDLILSKTFDNGMICASEQAIIVDKEIYDDVKTEMIAnncyfvt 284
Cdd:cd07078 192 MRAAAENLKRvtlELG---GKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHESIYDEFVERLVE------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 285 eeerrQLEKLVI----NENTCA---VNSDIVGKSAQYIAE--------LVGITVPENTKMLVAE---IQGIGAAYPLSRE 346
Cdd:cd07078 262 -----RVKALKVgnplDPDTDMgplISAAQLDRVLAYIEDakaegaklLCGGKRLEGGKGYFVPptvLTDVDPDMPIAQE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 347 KL-SPVLACVKANSLEEGFAYCEEMlnLGGLghSAVIHSVNKAVQKQFGLRMKACRLIVNAPSSQGGIGDIYNGFIPSlt 425
Cdd:cd07078 337 EIfGPVLPVIPFKDEEEAIELANDT--EYGL--AAGVFTRDLERALRVAERLEAGTVWINDYSVGAEPSAPFGGVKQS-- 410
|
....*..
gi 872568246 426 lGCGSYG 432
Cdd:cd07078 411 -GIGREG 416
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
104-277 |
6.48e-16 |
|
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: 81.33 E-value: 6.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 104 EEIIEIAEPVGVVAGVTPVTNPTSTTMFKALIAIKTRNPIIFafHPSAQK--CSIAAAKTVydaaVKAGAPKHCIQWIEK 181
Cdd:cd07094 115 RLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVL--KPASKTplSALELAKIL----VEAGVPEGVLQVVTG 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 182 PSVEATKQLMNHEGVALVLATGGA--GMVKSAYSTGKP-ALGVGpGNVPCYIEKSAHVKRAVNDLILSKTFDNGMICASE 258
Cdd:cd07094 189 EREVLGDAFAADERVAMLSFTGSAavGEALRANAGGKRiALELG-GNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISV 267
|
170
....*....|....*....
gi 872568246 259 QAIIVDKEIYDDVKTEMIA 277
Cdd:cd07094 268 QRIYVHEELYDEFIEAFVA 286
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
13-362 |
6.20e-13 |
|
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: 72.00 E-value: 6.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 13 EVKEMIDTlvnnGRKALQALESFTQEQIDNIVHEMALAGVDQHMPLAKLAVEETGRGVYEDKCIKN----IF--ATEYIw 86
Cdd:cd07145 22 EVREAIEV----AEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVErtirLFklAAEEA- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 87 hSIKKDKTVGIIHEDPHEE--IIEIAEPVGVVAGVTPVTNPTSTTMFKALIAIKTRNPIIFafHPSAqKCSIAA---AKT 161
Cdd:cd07145 97 -KVLRGETIPVDAYEYNERriAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVV--KPSS-NTPLTAielAKI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 162 VYdaavKAGAPKHCIQWIEKPSVEATKQLMNHEGVALVLATG----GAGMVKSAYSTGKP-ALGVGpGNVPCYIEKSAHV 236
Cdd:cd07145 173 LE----EAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGstavGLLIASKAGGTGKKvALELG-GSDPMIVLKDADL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 237 KRAVNDLILSKtFDN-GMICASEQAIIVDKEIYDDvktemianncyfVTEEERRQLEKLVI----NENTcAVNSDIVGKS 311
Cdd:cd07145 248 ERAVSIAVRGR-FENaGQVCNAVKRILVEEEVYDK------------FLKLLVEKVKKLKVgdplDEST-DLGPLISPEA 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872568246 312 AQYIAELVGITVPENTKMLVAEIQGIGAAYP-------------LSREKLSPVLACVKANSLEE 362
Cdd:cd07145 314 VERMENLVNDAVEKGGKILYGGKRDEGSFFPptvlendtpdmivMKEEVFGPVLPIAKVKDDEE 377
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
459-743 |
1.28e-12 |
|
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: 70.20 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 459 QWFKLPPKIYFEKHAtayLANMPNI-----SRAFIVTDPGMVEHgYVDTVTHYLRKHANDVKVEVFfevEPDPSDETVFK 533
Cdd:COG0371 1 RVIILPRRYVQGEGA---LDELGEYladlgKRALIITGPTALKA-AGDRLEESLEDAGIEVEVEVF---GGECSEEEIER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 534 GAEMMRSFQPDVIIALGGGSAMDAAKGmwlfyeypettfygikqkfldIRKRTckypelgsKAQFVAIPTTSGTGSEVTP 613
Cdd:COG0371 74 LAEEAKEQGADVIIGVGGGKALDTAKA---------------------VAYRL--------GLPVVSVPTIASTDAPASP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 614 FAVI-TDKKNNIKY-PLADyelTPDVAIVDPQFVMTVPPHVTAdTGM-DVLTHAIEAYVSVLANDYTDG---------LA 681
Cdd:COG0371 125 LSVIyTEDGAFDGYsFLAK---NPDLVLVDTDIIAKAPVRLLA-AGIgDALAKWYEARDWSLAHRDLAGeyyteaavaLA 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872568246 682 LKAIDLVFKYLPRAFKD---GNDEEAREKMHNAS-AIAGMAFANAF----LGINHSLAH---KIGPEFHIPHG 743
Cdd:COG0371 201 RLCAETLLEYGEAAIKAveaGVVTPALERVVEANlLLSGLAMGIGSsrpgSGAAHAIHNgltALPETHHALHG 273
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
15-277 |
2.36e-12 |
|
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: 70.25 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 15 KEMIDTLVNNGRKALQALESFTQEQIDNIVHEMAlAGVDQHM-PLAKLAVEETGR----GVYE-DKCIKNI-FATEYIwh 87
Cdd:pfam00171 28 AEDVDAAIAAARAAFPAWRKTPAAERAAILRKAA-DLLEERKdELAELETLENGKplaeARGEvDRAIDVLrYYAGLA-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 88 sikkDKTVG-IIHEDPHEEIIEIAEPVGVVAGVTPVTNPTSTTMFKALIAIKTRNPIIFafHPSAQKCSIAAAktVYDAA 166
Cdd:pfam00171 105 ----RRLDGeTLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVL--KPSELTPLTALL--LAELF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 167 VKAGAPKHCIQWIEKPSVEATKQLMNHEGVALVLATG----GAGMVKSAYSTGKPA---LGvgpGNVPCYIEKSAHVKRA 239
Cdd:pfam00171 177 EEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGstavGRHIAEAAAQNLKRVtleLG---GKNPLIVLEDADLDAA 253
|
250 260 270
....*....|....*....|....*....|....*...
gi 872568246 240 VNDLILSKTFDNGMICASEQAIIVDKEIYDDVKTEMIA 277
Cdd:pfam00171 254 VEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVE 291
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
5-277 |
4.03e-12 |
|
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: 69.22 E-value: 4.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 5 EKVVNEMQE-VKEMIDTLVNNGRKALQALESFTQEQIDNIVHEMAlAGVDQHM-PLAKLAVEETGRGVyEDKCIKNIFAT 82
Cdd:cd07088 23 GEVVATVPAaTAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLA-DLIRENAdELAKLIVEEQGKTL-SLARVEVEFTA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 83 EYI-WHSIKKDKTVG-IIHED-PHEEIIEIAEPVGVVAGVTPVTNPTSTTMFKALIAIKTRNPIIFafHPSaQKCSIAAA 159
Cdd:cd07088 101 DYIdYMAEWARRIEGeIIPSDrPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVI--KPS-EETPLNAL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 160 KTVyDAAVKAGAPKHCIQWIEKPSVEATKQLMNHEGVALVLATG--GAG---MVKSAYSTGKPALGVGpGNVPCYIEKSA 234
Cdd:cd07088 178 EFA-ELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGstEAGqkiMEAAAENITKVSLELG-GKAPAIVMKDA 255
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 872568246 235 HVKRAVNDLILSKTFDNGMICASEQAIIVDKEIYDDVKTEMIA 277
Cdd:cd07088 256 DLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVE 298
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
100-277 |
8.12e-12 |
|
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: 68.61 E-value: 8.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 100 EDPHEEIIEIAEPVGVVAGVTPVTNPTSTTMFKALIAIKTRNPIIFafHPSAQKCSIAAAktVYDAAVKAGAPKHCIQWI 179
Cdd:COG1012 129 DAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVL--KPAEQTPLSALL--LAELLEEAGLPAGVLNVV 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 180 EKPSVEATKQLMNHEGVALVLATG----GAGMVKSAYSTGKPA---LGvgpGNVPCYIEKSAHVKRAVNDLILSKTFDNG 252
Cdd:COG1012 205 TGDGSEVGAALVAHPDVDKISFTGstavGRRIAAAAAENLKRVtleLG---GKNPAIVLDDADLDAAVEAAVRGAFGNAG 281
|
170 180
....*....|....*....|....*
gi 872568246 253 MICASEQAIIVDKEIYDDVKTEMIA 277
Cdd:COG1012 282 QRCTAASRLLVHESIYDEFVERLVA 306
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
106-270 |
1.65e-09 |
|
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: 61.22 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 106 IIEIAEPVGVVAGVTPVTNPTSTTMFKALIAIKTRNPIIfaFHPSaQKCSIAAAKTVyDAAVKAGAPKHCIQWIEKPSVE 185
Cdd:cd07146 114 IFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIV--LKPS-EKTPLSAIYLA-DLLYEAGLPPDMLSVVTGEPGE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 186 ATKQLMNHEGVALVLATGGAGMVKS-AYSTG--KPALGVGpGNVPCYIEKSAHVKRAVnDLILSKTFDN-GMICASEQAI 261
Cdd:cd07146 190 IGDELITHPDVDLVTFTGGVAVGKAiAATAGykRQLLELG-GNDPLIVMDDADLERAA-TLAVAGSYANsGQRCTAVKRI 267
|
....*....
gi 872568246 262 IVDKEIYDD 270
Cdd:cd07146 268 LVHESVADE 276
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
484-730 |
4.09e-08 |
|
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: 56.01 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 484 SRAFIVTDP---GMVEhgyvDTVTHYLRKHANDVKVEVFfevEPDPSDETVFKGAEMMRSFQPDVIIALGGGSAMDAAKG 560
Cdd:cd08550 23 KKALIIGGKtalEAVG----EKLEKSLEEAGIDYEVEVF---GGECTEENIERLAEKAKEEGADVIIGIGGGKVLDTAKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 561 mwlfyeypettfygikqkfldirkrtckypeLGSKAQ--FVAIPTTSGTGSEVTPFAVITDKKNNIKYPLAdYELTPDVA 638
Cdd:cd08550 96 -------------------------------VADRLGlpVVTVPTIAATCAAWSALSVLYDEEGEFLGYSL-LKRSPDLV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 639 IVDPQFVMTVPPHVTAdTGM-DVLT--HAIEAYVSVLANDYTDGLALK----AIDLVFKYLPRAFKD---GNDEEAREKM 708
Cdd:cd08550 144 LVDTDIIAAAPVRYLA-AGIgDTLAkwYEARPSSRGGPDDLALQAAVQlaklAYDLLLEYGVQAVEDvrqGKVTPALEDV 222
|
250 260
....*....|....*....|....*..
gi 872568246 709 HNAS-AIAGMAF----ANAFLGINHSL 730
Cdd:cd08550 223 VDAIiLLAGLVGslggGGCRTAAAHAI 249
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
100-277 |
4.77e-08 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 56.42 E-value: 4.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 100 EDPHEEIIEIAEPVGVVAGVTPVTNPTSTTMFKALIAIKTRNPIIFAFHPSAQKCSIAAAKTVYDAAVKAGAPKHCIQWI 179
Cdd:cd07086 121 ERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPGVVNLV 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 180 EKPSvEATKQLMNHEGVALVLATGGAGM-----VKSAYSTGKPALGVGpGNVPCYIEKSAHVKRAVNDLILSKTFDNGMI 254
Cdd:cd07086 201 TGGG-DGGELLVHDPRVPLVSFTGSTEVgrrvgETVARRFGRVLLELG-GNNAIIVMDDADLDLAVRAVLFAAVGTAGQR 278
|
170 180
....*....|....*....|...
gi 872568246 255 CASEQAIIVDKEIYDDVKTEMIA 277
Cdd:cd07086 279 CTTTRRLIVHESVYDEFLERLVK 301
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
109-270 |
8.22e-08 |
|
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: 55.68 E-value: 8.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 109 IAEPVGVVAGVTPVTNPTSTTMFKALIAIKTRNPIIfaFHPSAQKcSIAAAKTVyDAAVKAGAPKHCIQWIEKPSVEATK 188
Cdd:cd07149 120 IREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVV--LKPASQT-PLSALKLA-ELLLEAGLPKGALNVVTGSGETVGD 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 189 QLMNHEGVALVLATGG----------AGMVKSAYSTGkpalgvgpGNVPCYIEKSAHVKRAVNDLILSKTFDNGMICASE 258
Cdd:cd07149 196 ALVTDPRVRMISFTGSpavgeaiarkAGLKKVTLELG--------SNAAVIVDADADLEKAVERCVSGAFANAGQVCISV 267
|
170
....*....|..
gi 872568246 259 QAIIVDKEIYDD 270
Cdd:cd07149 268 QRIFVHEDIYDE 279
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
109-269 |
1.20e-07 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 55.03 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 109 IAEPVGVVAGVTPVTNPTSTTMFKALIAIKTRNPIIFAFHPSAQKCSIAAAKTVYDaavkAGAPKHCIQWIEKPSVEATK 188
Cdd:cd07150 116 VRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEE----AGLPKGVFNVVTGGGAEVGD 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 189 QLMNHEGVALVLATGGAGM-----VKSAYSTGKPALGVGpGNVPCYIEKSAHVKRAVNDLILSKTFDNGMICASEQAIIV 263
Cdd:cd07150 192 ELVDDPRVRMVTFTGSTAVgreiaEKAGRHLKKITLELG-GKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIV 270
|
....*.
gi 872568246 264 DKEIYD 269
Cdd:cd07150 271 EEPVYD 276
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
101-409 |
3.38e-07 |
|
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: 53.79 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 101 DPHEEIIEIAEPVGVVAGVTPVTNPTSTTMFKALIAIKTRNPIIFafHPSAQKCSIAAAKTvyDAAVKAGAPKHCIQWIE 180
Cdd:cd07097 124 RPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVF--KPAELTPASAWALV--EILEEAGLPAGVFNLVM 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 181 KPSVEATKQLMNHEGVALVLATG----GAGMVKSAYSTGKPA-LGVGPGNvPCYIEKSAHVKRAVNDLILSKTFDNGMIC 255
Cdd:cd07097 200 GSGSEVGQALVEHPDVDAVSFTGstavGRRIAAAAAARGARVqLEMGGKN-PLVVLDDADLDLAVECAVQGAFFSTGQRC 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 256 ASEQAIIVDKEIYDDVKTEMIAnncyfvteeerrQLEKLVI----NENTC---AVNSDIVGKSAQYI-------AELV-- 319
Cdd:cd07097 279 TASSRLIVTEGIHDRFVEALVE------------RTKALKVgdalDEGVDigpVVSERQLEKDLRYIeiarsegAKLVyg 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 320 GITVPENTK---MLVAEIQGIGAAYPLSREKL-SPVLACVKANSLEEGFAyceeMLNLGGLGHSAVIHSVNKAVQKQFGL 395
Cdd:cd07097 347 GERLKRPDEgyyLAPALFAGVTNDMRIAREEIfGPVAAVIRVRDYDEALA----IANDTEFGLSAGIVTTSLKHATHFKR 422
|
330
....*....|....
gi 872568246 396 RMKACRLIVNAPSS 409
Cdd:cd07097 423 RVEAGVVMVNLPTA 436
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
471-560 |
7.17e-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: 52.41 E-value: 7.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 471 KHATAYLANMPNisRAFIVTDPGmVEHGYVDTVTHYLRKHANDVKVEVFF-EVepdpSDETVFKGAEMMRSFQPDVIIAL 549
Cdd:cd08170 12 DRLGEYLAPLGK--KALVIADPF-VLDLVGERLEESLEKAGLEVVFEVFGgEC----SREEIERLAAIARANGADVVIGI 84
|
90
....*....|.
gi 872568246 550 GGGSAMDAAKG 560
Cdd:cd08170 85 GGGKTIDTAKA 95
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
102-277 |
7.22e-07 |
|
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: 52.43 E-value: 7.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 102 PHEEIIEIAEPVGVVAGVTPVTNPTSTTMFKALIAIKTRNPIIfaFHPSAQK--CSIAAAKtvydAAVKAGAPKHCIQWI 179
Cdd:cd07103 107 PGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVV--LKPAEETplSALALAE----LAEEAGLPAGVLNVV 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 180 EKPSVEATKQLMNHEGVALVLATG----GAGMVKSAYSTGKPA---LGvgpGNVPCYIEKSAHVKRAVNDLILSKtFDN- 251
Cdd:cd07103 181 TGSPAEIGEALCASPRVRKISFTGstavGKLLMAQAADTVKRVsleLG---GNAPFIVFDDADLDKAVDGAIASK-FRNa 256
|
170 180
....*....|....*....|....*.
gi 872568246 252 GMICASEQAIIVDKEIYDDVKTEMIA 277
Cdd:cd07103 257 GQTCVCANRIYVHESIYDEFVEKLVE 282
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
22-269 |
9.12e-07 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 52.22 E-value: 9.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 22 VNNGRKALQALESFTQEQIDNIVHEMALAGVDQHMPLAKLAVEETGRGVYEDKCiKNIFATEYI-WHSIKKDKTVG--II 98
Cdd:PRK11241 54 IDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKG-EISYAASFIeWFAEEGKRIYGdtIP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 99 HEDPHEEIIEIAEPVGVVAGVTPVTNPTSTTMFKALIAIKTRNPIIfaFHPSAQKCSIAAAktVYDAAVKAGAPKHCIQW 178
Cdd:PRK11241 133 GHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMV--LKPASQTPFSALA--LAELAIRAGIPAGVFNV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 179 IEKPSVEATKQLMNHEGVALVLATGGAG-----MVKSAYSTGKPALGVGpGNVPCYIEKSAHVKRAVNDLILSKTFDNGM 253
Cdd:PRK11241 209 VTGSAGAVGGELTSNPLVRKLSFTGSTEigrqlMEQCAKDIKKVSLELG-GNAPFIVFDDADLDKAVEGALASKFRNAGQ 287
|
250
....*....|....*.
gi 872568246 254 ICASEQAIIVDKEIYD 269
Cdd:PRK11241 288 TCVCANRLYVQDGVYD 303
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
12-367 |
3.26e-06 |
|
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: 50.65 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 12 QEVKEMIDTLVNNGRKALQALEsfTQEQIDnIVHEMALAGVDQHMPLAKLAVEETGRGvYEDKCIKNIFATEYIWHSI-- 89
Cdd:cd07082 38 LEILEAAETAYDAGRGWWPTMP--LEERID-CLHKFADLLKENKEEVANLLMWEIGKT-LKDALKEVDRTIDYIRDTIee 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 90 -KK---DKTVGIIHEDPHEEIIEIA-EPVGVVAGVTPVTNP---TSTTMFKALIAIKTrnpiiFAFHPSAQKcSIAAAKT 161
Cdd:cd07082 114 lKRldgDSLPGDWFPGTKGKIAQVRrEPLGVVLAIGPFNYPlnlTVSKLIPALIMGNT-----VVFKPATQG-VLLGIPL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 162 VyDAAVKAGAPKHCIQWIEKPSVEATKQLMNHEGVALVLATGG---AGMVKSAYSTGKPALGVGPGNvPCYIEKSAHVKR 238
Cdd:cd07082 188 A-EAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGStevGNRLKKQHPMKRLVLELGGKD-PAIVLPDADLEL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 239 AVNDLILSKTFDNGMICASEQAIIVDKEIYDDVKTEMIAnncyfvteeerrQLEKLVI---NENTCAVNSDIVGKSAQYI 315
Cdd:cd07082 266 AAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKE------------EVAKLKVgmpWDNGVDITPLIDPKSADFV 333
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872568246 316 AELV------GITV------------------PENTKMLVAeiqgigaayplSREKLSPVLACVKANSLEEGFAYC 367
Cdd:cd07082 334 EGLIddavakGATVlngggreggnliyptlldPVTPDMRLA-----------WEEPFGPVLPIIRVNDIEEAIELA 398
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
111-420 |
8.67e-06 |
|
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: 49.28 E-value: 8.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 111 EPVGVVAGVTPVTNPTSTTMFKALIAIKTRNPIIFafhpsaqKCSIAAAKTVYDAAVKAGA--PKHCIQWIEKPSVEATK 188
Cdd:cd07108 116 EPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVL-------KAAEDAPLAVLLLAEILAQvlPAGVLNVITGYGEECGA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 189 QLMNHEGVALVLATGGAGMVKSAYSTGKP-----ALGVGpGNVPCYIEKSAHVKRAVNDLILSKTFD-NGMICASEQAII 262
Cdd:cd07108 189 ALVDHPDVDKVTFTGSTEVGKIIYRAAADrlipvSLELG-GKSPMIVFPDADLDDAVDGAIAGMRFTrQGQSCTAGSRLF 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 263 VDKEIYDDvktemianncyFVtEEERRQLEKLVI----NENT---CAVNSDIVGKSAQYIAElvGITVPENTKMLVAE-- 333
Cdd:cd07108 268 VHEDIYDA-----------FL-EKLVAKLSKLKIgdplDEATdigAIISEKQFAKVCGYIDL--GLSTSGATVLRGGPlp 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 334 ---------------IQGIGAAYPLSREKL-SPVLACVKANSLEEGFAyceeMLNLGGLGHSAVIHSVNKAVQKQFGLRM 397
Cdd:cd07108 334 gegpladgffvqptiFSGVDNEWRLAREEIfGPVLCAIPWKDEDEVIA----MANDSHYGLAAYVWTRDLGRALRAAHAL 409
|
330 340
....*....|....*....|....*.
gi 872568246 398 KACRLIVNapssQGG---IGDIYNGF 420
Cdd:cd07108 410 EAGWVQVN----QGGgqqPGQSYGGF 431
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
112-420 |
1.16e-05 |
|
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: 48.88 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 112 PVGVVAGVTPVTNPTSTTMFKALIAIKTRNPIIFAFHPSAQKCSIAAAKTVYDaavkAGAPKHCIQWIEKPSVEATKQLM 191
Cdd:cd07131 135 PIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAE----AGLPPGVVNVVHGRGEEVGEALV 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 192 NHEGVALVLATG----GAGMVKSAYSTGKP-ALGVGPGNvPCYIEKSAHVKRAVNDLILSKTFDNGMICASEQAIIVDKE 266
Cdd:cd07131 211 EHPDVDVVSFTGstevGERIGETCARPNKRvALEMGGKN-PIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHES 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 267 IYDDVKTEMIANNCYFV----TEEE--------RRQLEKlVINENTCAVNSDIVGKSAQYIAE--------LVGITVPEN 326
Cdd:cd07131 290 VYDEFLKRFVERAKRLRvgdgLDEEtdmgplinEAQLEK-VLNYNEIGKEEGATLLLGGERLTgggyekgyFVEPTVFTD 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 327 T--KMLVA--EIQGigaayplsreklsPVLACVKANSLEEGFayceEMLNLGGLGHSAVIH--SVNKAVqkQFGLRMKAC 400
Cdd:cd07131 369 VtpDMRIAqeEIFG-------------PVVALIEVSSLEEAI----EIANDTEYGLSSAIYteDVNKAF--RARRDLEAG 429
|
330 340
....*....|....*....|....*..
gi 872568246 401 RLIVNAPSSQ-------GGIGDIYNGF 420
Cdd:cd07131 430 ITYVNAPTIGaevhlpfGGVKKSGNGH 456
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
111-270 |
1.21e-05 |
|
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: 48.78 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 111 EPVGVVAGVTPVTNPTSTTMFKALIAIKTRNPIIFafHPSAQKCSIAAAktVYDAAVKAGAPKHCIQWIEkPSVEATKQL 190
Cdd:cd07102 115 EPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVIL--KHSPQTPLCGER--FAAAFAEAGLPEGVFQVLH-LSHETSAAL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 191 MNHEGVALVLATGG-AGMVKSAYSTGKPALGVG---PGNVPCYIEKSAHVKRAVNDLILSKTFDNGMICASEQAIIVDKE 266
Cdd:cd07102 190 IADPRIDHVSFTGSvAGGRAIQRAAAGRFIKVGlelGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHES 269
|
....
gi 872568246 267 IYDD 270
Cdd:cd07102 270 IYDA 273
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
101-269 |
1.42e-05 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 48.53 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 101 DPHEEIIEIAEPVGVVAGVTPVTNPtsttmfkalIAIKTRN--PIIFA-----FHPSAQKCSIAAAKTVYdaAVKAGAPK 173
Cdd:PLN02278 149 FPDRRLLVLKQPVGVVGAITPWNFP---------LAMITRKvgPALAAgctvvVKPSELTPLTALAAAEL--ALQAGIPP 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 174 HCIQWIEKPSVEATKQLMNHEGVALVLATGGAG-----MVKSAYSTGKPALGVGpGNVPCYIEKSAHVKRAVNDLILSKT 248
Cdd:PLN02278 218 GVLNVVMGDAPEIGDALLASPKVRKITFTGSTAvgkklMAGAAATVKRVSLELG-GNAPFIVFDDADLDVAVKGALASKF 296
|
170 180
....*....|....*....|.
gi 872568246 249 FDNGMICASEQAIIVDKEIYD 269
Cdd:PLN02278 297 RNSGQTCVCANRILVQEGIYD 317
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
111-277 |
4.52e-05 |
|
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: 47.05 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 111 EPVGVVAGVTPVTNPTSTTMFKALIAIKTRNPIIFAfhpSAQKCSIAAAKtVYDAAVKAGAPKHCIQWIEKPSVEATKQL 190
Cdd:cd07115 116 EPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLK---PAELTPLSALR-IAELMAEAGFPAGVLNVVTGFGEVAGAAL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 191 MNHEGVALVLATG----GAGMVKSAYSTGKP-ALGVGpGNVPCYIEKSAHVKRAVNDLILSKTFDNGMICASEQAIIVDK 265
Cdd:cd07115 192 VEHPDVDKITFTGstavGRKIMQGAAGNLKRvSLELG-GKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHE 270
|
170
....*....|..
gi 872568246 266 EIYDDVKTEMIA 277
Cdd:cd07115 271 SIYDEFLERFTS 282
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
111-275 |
4.66e-05 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 47.05 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 111 EPVGVVAGVTPVTNPTSTTMFKALIAIKTRNPIIFafhpsaqKCSIAAAKT---VYDAAVKAGAPKHCIQWIEKpSVEAT 187
Cdd:cd07113 141 EPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVI-------KPSEFTPLTllrVAELAKEAGIPDGVLNVVNG-KGAVG 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 188 KQLMNHEGVALVLATG----GAGMVKSAYSTGKPA-LGVGPGNvPCYIEKSAHVKRAVNDLILSKTFDNGMICASEQAII 262
Cdd:cd07113 213 AQLISHPDVAKVSFTGsvatGKKIGRQAASDLTRVtLELGGKN-AAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFY 291
|
170
....*....|...
gi 872568246 263 VDKEIYDDVKTEM 275
Cdd:cd07113 292 VHRSKFDELVTKL 304
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
136-248 |
4.98e-05 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 46.60 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 136 AIKTRNPIIF-----AFHpsaqkCSIAAAKTVYDAAVKAGAPKHCIQWIEKPSVEATKQLMNHEG-VALVLATGGAGMVK 209
Cdd:PRK00197 137 CLKSGNAVILrggseAIH-----SNRALVAVIQEALEEAGLPADAVQLVETTDRAAVGELLKLDGyVDVIIPRGGAGLIR 211
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 872568246 210 --SAYSTgKPALGVGPGNVPCYIEKSAHVKRAVNDLILSKT 248
Cdd:PRK00197 212 rvVENAT-VPVIEHGDGICHIYVDESADLDKALKIVLNAKT 251
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
111-362 |
7.21e-05 |
|
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: 46.03 E-value: 7.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 111 EPVGVVAGVTPVTNPTSTTMFKALIAIKTRNPIIFAFHPSAQKCSIAAAKTVYDAavkaGAPKHCIQWIE-KP--SVEAT 187
Cdd:cd07105 97 EPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEA----GLPKGVLNVVThSPedAPEVV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 188 KQLMNHEGVALVLATGGAGMVKSAYSTG----KPA---LGvgpGNVPCYIEKSAHVKRAVNDLILSKTFDNGMICASEQA 260
Cdd:cd07105 173 EALIAHPAVRKVNFTGSTRVGRIIAETAakhlKPVlleLG---GKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTER 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 261 IIVDKEIYDDVKT-------EMIANNCY---FVTEEERRQLEKLVinentcavnSDIVGKSAQYIAELVGITVPENTKML 330
Cdd:cd07105 250 IIVHESIADEFVEklkaaaeKLFAGPVVlgsLVSAAAADRVKELV---------DDALSKGAKLVVGGLADESPSGTSMP 320
|
250 260 270
....*....|....*....|....*....|...
gi 872568246 331 VAEIQGIGAAYPL-SREKLSPVLACVKANSLEE 362
Cdd:cd07105 321 PTILDNVTPDMDIySEESFGPVVSIIRVKDEEE 353
|
|
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
471-558 |
8.86e-05 |
|
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: 45.47 E-value: 8.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 471 KHATAYLANMPNISRAFIVTDPGmVEHGYVDTVTHYLRKHANDVKVEVFFEVEPDPSDETVFK------GAEMMRSfqpD 544
Cdd:COG0337 23 DELGELLAELLKGRRVLVVTDEN-VAPLYGERLRAALEAAGFEVHLLVLPDGEASKTLETLERildallEAGLDRD---D 98
|
90
....*....|....
gi 872568246 545 VIIALGGGSAMDAA 558
Cdd:COG0337 99 LVVALGGGVVGDLA 112
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
484-561 |
9.64e-05 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 45.58 E-value: 9.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 484 SRAFIVTDP---GMVEhgyvDTVTHYLRKHANDVKVEVFfevEPDPSDETVFKGAEMMRSFQPDVIIALGGGSAMDAAKG 560
Cdd:PRK09423 30 KRALVIADEfvlGIVG----DRVEASLKEAGLTVVFEVF---NGECSDNEIDRLVAIAEENGCDVVIGIGGGKTLDTAKA 102
|
.
gi 872568246 561 M 561
Cdd:PRK09423 103 V 103
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
111-276 |
3.03e-04 |
|
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: 44.22 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 111 EPVGVVAGVTPVTNPTSTTMFKALIAIKTRNPIIFAFHPSAQKCSIAAAktvyDAAVKAGAPKHCIQWIekPSVEATKQL 190
Cdd:cd07090 115 EPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLA----EILTEAGLPDGVFNVV--QGGGETGQL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 191 M-NHEGVALVLATG----GAGMVKSAYSTGKPA---LGvgpGNVPCYIEKSAHVKRAVNDLILSKTFDNGMICASEQAII 262
Cdd:cd07090 189 LcEHPDVAKVSFTGsvptGKKVMSAAAKGIKHVtleLG---GKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVF 265
|
170
....*....|....
gi 872568246 263 VDKEIYDDVKTEMI 276
Cdd:cd07090 266 VQRSIKDEFTERLV 279
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
216-270 |
2.78e-03 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 41.14 E-value: 2.78e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 872568246 216 KPALGVGpGNVPCYIEKSAHVKRAVNDLILSKTFDNGMICASEQAIIVDKEIYDD 270
Cdd:cd07151 236 KVALELG-GNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDE 289
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
112-277 |
4.28e-03 |
|
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: 40.69 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 112 PVGVVAGVTPVTNPTSTTMFKALIAIKTRNPIIFAfhPsAQKCSIAAAKtVYDAAVKAGAPKhciqwiEKPSV-----EA 186
Cdd:cd07147 123 PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLK--P-ASRTPLSALI-LGEVLAETGLPK------GAFSVlpcsrDD 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 187 TKQLMNHEGVALVLATGGAG---MVKSAYSTGKPALGVGpGNVPCYIEKSAHVKRAVNDLILSKTFDNGMICASEQAIIV 263
Cdd:cd07147 193 ADLLVTDERIKLLSFTGSPAvgwDLKARAGKKKVVLELG-GNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLV 271
|
170
....*....|....
gi 872568246 264 DKEIYDDVKTEMIA 277
Cdd:cd07147 272 HRSVYDEFKSRLVA 285
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
482-559 |
7.29e-03 |
|
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like proteins have not been characterized. The protein sequences have high similarity with that of glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion.
Pssm-ID: 341453 [Multi-domain] Cd Length: 332 Bit Score: 39.43 E-value: 7.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872568246 482 NISRAFIVTDPGmVEHGYVDTVTHYLRKHANDVKVEVffevEPDPSDETVFKGAEMMRsfQPDVIIALGGGSAMDAAK 559
Cdd:cd08174 24 GFGKVAIVTGEG-IDELLGEDILESLEEAGEIVTVEE----NTDNSAEELAEKAFSLP--KVDAIVGIGGGKVLDVAK 94
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
111-277 |
7.69e-03 |
|
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: 39.52 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 111 EPVGVVAGVTPVTNPTSTTMFKALIAIKTRNPIIfaFHPSAQKCSIAAAktVYDAAVKAGAPKHCIQWIEKPSVEATKQL 190
Cdd:cd07109 116 EPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVV--VKPAEDAPLTALR--LAELAEEAGLPAGALNVVTGLGAEAGAAL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 191 MNHEGVALVLATG----GAGMVKSAystgkpalgvGPGNVPCYIE---KS-------AHVKRAVNDLILSKTFDNGMICA 256
Cdd:cd07109 192 VAHPGVDHISFTGsvetGIAVMRAA----------AENVVPVTLElggKSpqivfadADLEAALPVVVNAIIQNAGQTCS 261
|
170 180
....*....|....*....|.
gi 872568246 257 SEQAIIVDKEIYDDVKTEMIA 277
Cdd:cd07109 262 AGSRLLVHRSIYDEVLERLVE 282
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
111-277 |
7.86e-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: 39.75 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 111 EPVGVVAGVTP----------VTNPtsttmfkALIAiktRNPIIFAFHPSAQKCSIAAAKTVYDAavkaGAPKHCIQWIe 180
Cdd:cd07100 95 EPLGVVLGIMPwnfpfwqvfrFAAP-------NLMA---GNTVLLKHASNVPGCALAIEELFREA----GFPEGVFQNL- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872568246 181 KPSVEATKQLMNHEGVALVLATG----GAGMVKSAYSTGKPA---LGvgpGNVPCYIEKSAHVKRAVNDLILSKTFDNGM 253
Cdd:cd07100 160 LIDSDQVEAIIADPRVRGVTLTGseraGRAVAAEAGKNLKKSvleLG---GSDPFIVLDDADLDKAVKTAVKGRLQNAGQ 236
|
170 180
....*....|....*....|....
gi 872568246 254 ICASEQAIIVDKEIYDDVKTEMIA 277
Cdd:cd07100 237 SCIAAKRFIVHEDVYDEFLEKFVE 260
|
|
| |
