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Conserved domains on  [gi|37604163|gb|AAH59850|]
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Fasn protein, partial [Mus musculus]

Protein Classification

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List of domain hits

 Name Accession Description Interval E-value
KR_1_FAS_SDR_x cd08954
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ...
 222-458 8.61e-110

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; NADP-dependent KR domain of the multidomain type I FAS, a complex SDR family. This subfamily also includes proteins identified as polyketide synthase (PKS), a protein with related modular protein architecture and similar function. It includes the KR domains of mammalian and chicken FAS, and Dictyostelium discoideum putative polyketide synthases (PKSs). These KR domains contain two subdomains, each of which is related to SDR Rossmann fold domains. However, while the C-terminal subdomain has an active site similar to the other SDRs and a NADP-binding capability, the N-terminal SDR-like subdomain is truncated and lacks these functions, serving a supportive structural role. In some instances, such as porcine FAS, an enoyl reductase (a Rossman fold NAD-binding domain of the medium-chain dehydrogenase/reductase, MDR family) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER); this KR and ER are members of the SDR family. This KR subfamily has an active site tetrad with a similar 3D orientation compared to archetypical SDRs, but the active site Lys and Asn residue positions are swapped. The characteristic NADP-binding is typical of the multidomain complex SDRs, with a GGXGXXG NADP binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


:

Pssm-ID: 187657 [Multi-domain]  Cd Length: 452  Bit Score: 344.43  E-value: 8.61e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 222 ISKTFCPA--HKSYIITGGLGGFGLELARWLVLRGAQR-LVLTSRSGIRTGyQAKHIREWRRQ---GIQVLVSTSNVSSL 295
Cdd:cd08954 208 ILKTNYPInlGKSYLITGGSGGLGLEILKWLVKRGAVEnIIILSRSGMKWE-LELLIREWKSQnikFHFVSVDVSDVSSL 286

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 296 EGARALIAEATKLGPVGGVFNLAMVLRDAMLENQTPELFQDVNKPKYNGTLNLDRATREACPELDYFVAFSSVSCGRGNA 375
Cdd:cd08954 287 EKAINLILNAPKIGPIGGIFHLAFVLIDKVLEIDTESLFISVNKAKVMGAINLHNQSIKRCWKLDYFVLFSSVSSIRGSA 366

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 376 GQTNYGFANSTMERICEQRRHDGLPGLAVQWGAIGDVGIVlEAMGTNDTVIG--GTLPQRISSCMEVLDLFLN--QPHAV 451
Cdd:cd08954 367 GQCNYVCANSVLDSLSRYRKSIGLPSIAINWGAIGDVGFV-SRNESVDTLLGgqGLLPQSINSCLGTLDLFLQnpSPNLV 445


                ....*..
gi 37604163 452 LSSFVLA 458
Cdd:cd08954 446 LSSFNFA 452
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 1-200 4.14e-103

Enoylreductase; Enoylreductase in Polyketide synthases.


:

Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 320.49  E-value: 4.14e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163      1 AYYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLqaRFPQLDDTSFANSRDTSFEQHVLL 80
Cdd:smart00829  91 AYYALVDLARLRPGESVLIHAAAGGVGQAAIQLARHLGAEVFATAGSPEKRDFL--RALGIPDDHIFSSRDLSFADEILR 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163     81 HTGGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIGKFDLSNNHPLGMAIFLKNVTFHGILLDALFEEaNDSWREVAALL 160
Cdd:smart00829 169 ATGGRGVDVVLNSLSGEFLDASLRCLAPGGRFVEIGKRDIRDNSQLAMAPFRPNVSYHAVDLDALEEG-PDRIRELLAEV 247

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 37604163    161 KAGIRDGVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLV 200
Cdd:smart00829 248 LELFAEGVLRPLPVTVFPISDAEDAFRYMQQGKHIGKVVL 287
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 588-847 1.41e-46

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


:

Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 166.02  E-value: 1.41e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   588 RPLFLVHPIEGSTTVFHSLAAKLSVPT------YGLQCTQAAPLDSIPNLAAYYIDCIKQVQPEGPYRIAGYSFGACVAF 661
Cdd:pfam00975   1 RPLFCFPPAGGSASSFRSLARRLPPPAevlavqYPGRGRGEPPLNSIEALADEYAEALRQIQPEGPYALFGHSMGGMLAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   662 EMCSQLQaQQGPAPTHnnLFLFDGSHTYVLAYTQSYRAKMTPgceaeaeaealcfFIKQFLDVEHSkvLEALLP----LK 737
Cdd:pfam00975  81 EVARRLE-RQGEAVRS--LFLSDASAPHTVRYEASRAPDDDE-------------VVAEFTDEGGT--PEELLEdeelLS 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   738 SLEDRVAASVDLITKSHHSLDRRelsfaavsfyhkLRAADQYKPKAKYHGNVTLlraktggtygedlgaDYNLSQVCDGK 817
Cdd:pfam00975 143 MLLPALRADYRALESYSCPPLDA------------QSATLFYGSDDPLHDADDL---------------AEWVRDHTPGE 195

                         250       260       270
                  ....*....|....*....|....*....|
gi 37604163   818 VSVHIIEGDHRTLLEgsGLESIINIIHSSL 847
Cdd:pfam00975 196 FDVHVFDGDHFYLIE--HLEAVLEIIEAKL 223
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 471-526 2.16e-10

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


:

Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 57.65  E-value: 2.16e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 37604163    471 QRDLVKAVAHILGIRDLAGINLDSTLADLGLDSLMGVEVRQILEREHDLVLPMREV 526
Cdd:smart00823  14 LDLVREQVAAVLGHAAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLV 69
 
Name Accession Description Interval E-value
KR_1_FAS_SDR_x cd08954
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ...
 222-458 8.61e-110

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; NADP-dependent KR domain of the multidomain type I FAS, a complex SDR family. This subfamily also includes proteins identified as polyketide synthase (PKS), a protein with related modular protein architecture and similar function. It includes the KR domains of mammalian and chicken FAS, and Dictyostelium discoideum putative polyketide synthases (PKSs). These KR domains contain two subdomains, each of which is related to SDR Rossmann fold domains. However, while the C-terminal subdomain has an active site similar to the other SDRs and a NADP-binding capability, the N-terminal SDR-like subdomain is truncated and lacks these functions, serving a supportive structural role. In some instances, such as porcine FAS, an enoyl reductase (a Rossman fold NAD-binding domain of the medium-chain dehydrogenase/reductase, MDR family) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER); this KR and ER are members of the SDR family. This KR subfamily has an active site tetrad with a similar 3D orientation compared to archetypical SDRs, but the active site Lys and Asn residue positions are swapped. The characteristic NADP-binding is typical of the multidomain complex SDRs, with a GGXGXXG NADP binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187657 [Multi-domain]  Cd Length: 452  Bit Score: 344.43  E-value: 8.61e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 222 ISKTFCPA--HKSYIITGGLGGFGLELARWLVLRGAQR-LVLTSRSGIRTGyQAKHIREWRRQ---GIQVLVSTSNVSSL 295
Cdd:cd08954 208 ILKTNYPInlGKSYLITGGSGGLGLEILKWLVKRGAVEnIIILSRSGMKWE-LELLIREWKSQnikFHFVSVDVSDVSSL 286

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 296 EGARALIAEATKLGPVGGVFNLAMVLRDAMLENQTPELFQDVNKPKYNGTLNLDRATREACPELDYFVAFSSVSCGRGNA 375
Cdd:cd08954 287 EKAINLILNAPKIGPIGGIFHLAFVLIDKVLEIDTESLFISVNKAKVMGAINLHNQSIKRCWKLDYFVLFSSVSSIRGSA 366

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 376 GQTNYGFANSTMERICEQRRHDGLPGLAVQWGAIGDVGIVlEAMGTNDTVIG--GTLPQRISSCMEVLDLFLN--QPHAV 451
Cdd:cd08954 367 GQCNYVCANSVLDSLSRYRKSIGLPSIAINWGAIGDVGFV-SRNESVDTLLGgqGLLPQSINSCLGTLDLFLQnpSPNLV 445


                ....*..
gi 37604163 452 LSSFVLA 458
Cdd:cd08954 446 LSSFNFA 452
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 1-200 4.14e-103

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 320.49  E-value: 4.14e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163      1 AYYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLqaRFPQLDDTSFANSRDTSFEQHVLL 80
Cdd:smart00829  91 AYYALVDLARLRPGESVLIHAAAGGVGQAAIQLARHLGAEVFATAGSPEKRDFL--RALGIPDDHIFSSRDLSFADEILR 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163     81 HTGGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIGKFDLSNNHPLGMAIFLKNVTFHGILLDALFEEaNDSWREVAALL 160
Cdd:smart00829 169 ATGGRGVDVVLNSLSGEFLDASLRCLAPGGRFVEIGKRDIRDNSQLAMAPFRPNVSYHAVDLDALEEG-PDRIRELLAEV 247

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 37604163    161 KAGIRDGVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLV 200
Cdd:smart00829 248 LELFAEGVLRPLPVTVFPISDAEDAFRYMQQGKHIGKVVL 287
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
 1-200 2.05e-87

enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. Polyketide synthases produce polyketides in step by step mechanism that is similar to fatty acid synthesis. Enoyl reductase reduces a double to single bond. Erythromycin is one example of a polyketide generated by 3 complex enzymes (megasynthases). 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176179 [Multi-domain]  Cd Length: 293  Bit Score: 279.45  E-value: 2.05e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQARFPqlDDTSFANSRDTSFEQHVLL 80
Cdd:cd05195  96 AYYALVDLARLQKGESVLIHAAAGGVGQAAIQLAQHLGAEVFATVGSEEKREFLRELGG--PVDHIFSSRDLSFADGILR 173

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  81 HTGGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIGKFDLSNNHPLGMAIFLKNVTFHGILLDALFEEandSWREVAALL 160
Cdd:cd05195 174 ATGGRGVDVVLNSLSGELLRASWRCLAPFGRFVEIGKRDILSNSKLGMRPFLRNVSFSSVDLDQLARE---RPELLRELL 250

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 37604163 161 KAGIR---DGVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLV 200
Cdd:cd05195 251 REVLElleAGVLKPLPPTVVPSASEIDAFRLMQSGKHIGKVVL 293
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 231-411 3.12e-55

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 188.46  E-value: 3.12e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163    231 KSYIITGGLGGFGLELARWLVLRGAQRLVLTSRSGIRTGYQAKHIREWRRQGIQVLVSTSNVSSLEGARALIAEA-TKLG 309
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGARRLVLLSRSGPDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIpAVEG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163    310 PVGGVFNLAMVLRDAMLENQTPELFQDVNKPKYNGTLNLDRATReaCPELDYFVAFSSVSCGRGNAGQTNYGFANSTMER 389
Cdd:smart00822  81 PLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTA--DLPLDFFVLFSSIAGVLGSPGQANYAAANAFLDA 158

                          170       180
                   ....*....|....*....|..
gi 37604163    390 ICEQRRHDGLPGLAVQWGAIGD 411
Cdd:smart00822 159 LAEYRRARGLPALSIAWGAWAE 180
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 1-203 7.61e-48

NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 173.03  E-value: 7.61e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQArfpqLDDTSFANSRDTSFEQHVLL 80
Cdd:COG0604 127 AWQALFDRGRLKPGETVLVHGAAGGVGSAAVQLAKALGARVIATASSPEKAELLRA----LGADHVIDYREEDFAERVRA 202

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  81 HTGGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIGKFDLSNNHPLGMAIFLKNVTFHGILLDALFEEAN-DSWREVAAL 159
Cdd:COG0604 203 LTGGRGVDVVLDTVGGDTLARSLRALAPGGRLVSIGAASGAPPPLDLAPLLLKGLTLTGFTLFARDPAERrAALAELARL 282

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 37604163 160 lkagIRDGVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLVQVR 203
Cdd:COG0604 283 ----LAAGKLRPVIDRVFPLEEAAEAHRLLESGKHRGKVVLTVD 322
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 588-847 1.41e-46

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 166.02  E-value: 1.41e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   588 RPLFLVHPIEGSTTVFHSLAAKLSVPT------YGLQCTQAAPLDSIPNLAAYYIDCIKQVQPEGPYRIAGYSFGACVAF 661
Cdd:pfam00975   1 RPLFCFPPAGGSASSFRSLARRLPPPAevlavqYPGRGRGEPPLNSIEALADEYAEALRQIQPEGPYALFGHSMGGMLAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   662 EMCSQLQaQQGPAPTHnnLFLFDGSHTYVLAYTQSYRAKMTPgceaeaeaealcfFIKQFLDVEHSkvLEALLP----LK 737
Cdd:pfam00975  81 EVARRLE-RQGEAVRS--LFLSDASAPHTVRYEASRAPDDDE-------------VVAEFTDEGGT--PEELLEdeelLS 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   738 SLEDRVAASVDLITKSHHSLDRRelsfaavsfyhkLRAADQYKPKAKYHGNVTLlraktggtygedlgaDYNLSQVCDGK 817
Cdd:pfam00975 143 MLLPALRADYRALESYSCPPLDA------------QSATLFYGSDDPLHDADDL---------------AEWVRDHTPGE 195

                         250       260       270
                  ....*....|....*....|....*....|
gi 37604163   818 VSVHIIEGDHRTLLEgsGLESIINIIHSSL 847
Cdd:pfam00975 196 FDVHVFDGDHFYLIE--HLEAVLEIIEAKL 223
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 232-411 2.73e-45

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 160.81  E-value: 2.73e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   232 SYIITGGLGGFGLELARWLVLRGAQRLVLTSRSGIRTGYQAKHIREWRRQGIQVLVSTSNVSSLEGARALIAEA-TKLGP 310
Cdd:pfam08659   2 TYLITGGLGGLGRELARWLAERGARHLVLLSRSAAPRPDAQALIAELEARGVEVVVVACDVSDPDAVAALLAEIkAEGPP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   311 VGGVFNLAMVLRDAMLENQTPELFQDVNKPKYNGTLNLDRATREAcpELDYFVAFSSVSCGRGNAGQTNYGFANSTMERI 390
Cdd:pfam08659  82 IRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHEATPDE--PLDFFVLFSSIAGLLGSPGQANYAAANAFLDAL 159

                         170       180
                  ....*....|....*....|.
gi 37604163   391 CEQRRHDGLPGLAVQWGAIGD 411
Cdd:pfam08659 160 AEYRRSQGLPATSINWGPWAE 180
quinone_pig3 TIGR02824
putative NAD(P)H quinone oxidoreductase, PIG3 family; Members of this family are putative ...
 1-202 1.41e-35

putative NAD(P)H quinone oxidoreductase, PIG3 family; Members of this family are putative quinone oxidoreductases that belong to the broader superfamily (modeled by Pfam pfam00107) of zinc-dependent alcohol (of medium chain length) dehydrogenases and quinone oxiooreductases. The alignment shows no motif of conserved Cys residues as are found in zinc-binding members of the superfamily, and members are likely to be quinone oxidoreductases instead. A member of this family in Homo sapiens, PIG3, is induced by p53 but is otherwise uncharacterized. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274316 [Multi-domain]  Cd Length: 325  Bit Score: 137.78  E-value: 1.41e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163     1 AYYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQArfpqLDDTSFANSRDTSFEQHVLL 80
Cdd:TIGR02824 127 VWSNLFQRGGLKAGETVLIHGGASGIGTTAIQLAKAFGARVFTTAGSDEKCAACEA----LGADIAINYREEDFVEVVKA 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163    81 HTGGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIG-------KFDLsnnhplgMAIFLKNVTFHGILLDAlfeEANDSW 153
Cdd:TIGR02824 203 ETGGKGVDVILDIVGGSYLNRNIKALALDGRIVQIGfqggrkaELDL-------GPLLAKRLTITGSTLRA---RPVAEK 272

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 37604163   154 REVAALLKAG----IRDGVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLVQV 202
Cdd:TIGR02824 273 AAIAAELREHvwplLASGRVRPVIDKVFPLEDAAQAHALMESGDHIGKIVLTV 325
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
 585-851 1.33e-34

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 142.15  E-value: 1.33e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 585 SSERPLFLVHPIEGSTTVFHSLAAKLS--VPTYGLQC----TQAAPLDSIPNLAAYYIDCIKQVQPEGPYRIAGYSFGAC 658
Cdd:COG3319 599 GSGPPLFCVHPAGGNVLCYRPLARALGpdRPVYGLQApgldGGEPPPASVEEMAARYVEAIRAVQPEGPYHLLGWSFGGL 678

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 659 VAFEMCSQLQAQQGPAPThnnLFLFDgshtyvlaytqSYRAKMTPGCEAEAEAEALCFFIKQFLDVEHSkvLEALLPLkS 738
Cdd:COG3319 679 VAYEMARQLEAQGEEVAL---LVLLD-----------SYAPGALARLDEAELLAALLRDLARGVDLPLD--AEELRAL-D 741

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 739 LEDRVAASVDLITKSH--HSLDRRELSFAAVSFYHKLRAADQYKPKAkYHGNVTLLRAkTGGTYGEDLGADYNLSQVCDG 816
Cdd:COG3319 742 PEERLARLLERLREAGlpAGLDAERLRRLLRVFRANLRALRRYRPRP-YDGPVLLFRA-EEDPPGRADDPALGWRPLVAG 819

                       250       260       270
                ....*....|....*....|....*....|....*
gi 37604163 817 KVSVHIIEGDHRTLLEGSGLESIINIIHSSLAEPR 851
Cdd:COG3319 820 GLEVHDVPGDHFSMLREPHVAELAAALRAALAAAE 854
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
25-162 8.55e-19

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 83.04  E-value: 8.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163    25 GVGQAAISIALSLGCRVFTTVGSAEKRAYLQarfpQLDDTSFANSRDTSFEQHVLLHTGGKGVDLVLNSL-AEEKLQASV 103
Cdd:pfam00107   1 GVGLAAIQLAKAAGAKVIAVDGSEEKLELAK----ELGADHVINPKETDLVEEIKELTGGKGVDVVFDCVgSPATLEQAL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   104 RCLAQHGRFLEIGKFdlSNNHPLGMA-IFLKNVTFHGILLDalfeeANDSWREVAALLKA 162
Cdd:pfam00107  77 KLLRPGGRVVVVGLP--GGPLPLPLApLLLKELTILGSFLG-----SPEEFPEALDLLAS 129
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
 1-204 1.23e-14

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 76.22  E-value: 1.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163    1 AYYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQarfpQLDDTSFANSRDTSFEQHVLL 80
Cdd:PTZ00354 128 AWQLLKKHGDVKKGQSVLIHAGASGVGTAAAQLAEKYGAATIITTSSEEKVDFCK----KLAAIILIRYPDEEGFAPKVK 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   81 H-TGGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIGKFDLSNNHPLGMA-IFLKNVTFHGILL----DALFEEANDSW- 153
Cdd:PTZ00354 204 KlTGEKGVNLVLDCVGGSYLSETAEVLAVDGKWIVYGFMGGAKVEKFNLLpLLRKRASIIFSTLrsrsDEYKADLVASFe 283

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 37604163  154 REVAALlkagIRDGVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLVQVRE 204
Cdd:PTZ00354 284 REVLPY----MEEGEIKPIVDRTYPLEEVAEAHTFLEQNKNIGKVVLTVNE 330
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 471-526 2.16e-10

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 57.65  E-value: 2.16e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 37604163    471 QRDLVKAVAHILGIRDLAGINLDSTLADLGLDSLMGVEVRQILEREHDLVLPMREV 526
Cdd:smart00823  14 LDLVREQVAAVLGHAAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLV 69
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
470-670 7.60e-10

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 62.75  E-value: 7.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   470 TQRDLVKAVAHILGiRDLAGInlDSTLADLGLDSLMGVEVRQILEREhdlvlpMRevRQLTLRKLQEMSSKTDSATDTTA 549
Cdd:PRK10252  979 TETIIAAAFSSLLG-CDVVDA--DADFFALGGHSLLAMKLAAQLSRQ------FA--RQVTPGQVMVASTVAKLATLLDA 1047

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   550 PksrsdtSLKQNQLNLSTL--LVNPEGPTLtqlnsvqsserplFLVHPIEGSTTVFHSLAAKLS--VPTYGLQC------ 619
Cdd:PRK10252 1048 E------EDESRRLGFGTIlpLREGDGPTL-------------FCFHPASGFAWQFSVLSRYLDpqWSIYGIQSprpdgp 1108

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 37604163   620 -TQAAPLDSipnLAAYYIDCIKQVQPEGPYRIAGYSFGACVAFEMCSQLQAQ 670
Cdd:PRK10252 1109 mQTATSLDE---VCEAHLATLLEQQPHGPYHLLGYSLGGTLAQGIAARLRAR 1157
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 472-526 1.41e-08

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 51.80  E-value: 1.41e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 37604163   472 RDLVKAVAHILGIrDLAGINLDSTLADLGLDSLMGVEVRQILEREHDLVLPMREV 526
Cdd:pfam00550   1 ERLRELLAEVLGV-PAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDL 54
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
246-409 2.02e-08

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 56.03  E-value: 2.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 246 LARWLVLRGAqRLVLTSRSGIRTGYQAKHIREwrrQGIQVLVSTSNVSSLEGARALIAEAT-KLGPVGGVFNLAMVLRDA 324
Cdd:COG0300  21 LARALAARGA-RVVLVARDAERLEALAAELRA---AGARVEVVALDVTDPDAVAALAEAVLaRFGPIDVLVNNAGVGGGG 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 325 MLENQTPELFQ---DVNkpkYNGTLNLdraTREACPEL-----DYFVAFSSVSCGRGNAGQTNYGFANSTMERICEQRR- 395
Cdd:COG0300  97 PFEELDLEDLRrvfEVN---VFGPVRL---TRALLPLMrargrGRIVNVSSVAGLRGLPGMAAYAASKAALEGFSESLRa 170

                       170
                ....*....|....*..
gi 37604163 396 ---HDGLPGLAVQWGAI 409
Cdd:COG0300 171 elaPTGVRVTAVCPGPV 187
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 469-534 4.60e-08

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 51.01  E-value: 4.60e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37604163 469 DTQRDLVKAVAHILGIrDLAGINLDSTL-ADLGLDSLMGVEVRQILEREHDLVLPMREVRQL-TLRKL 534
Cdd:COG0236   5 ELEERLAEIIAEVLGV-DPEEITPDDSFfEDLGLDSLDAVELIAALEEEFGIELPDTELFEYpTVADL 71
 
Name Accession Description Interval E-value
KR_1_FAS_SDR_x cd08954
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ...
 222-458 8.61e-110

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; NADP-dependent KR domain of the multidomain type I FAS, a complex SDR family. This subfamily also includes proteins identified as polyketide synthase (PKS), a protein with related modular protein architecture and similar function. It includes the KR domains of mammalian and chicken FAS, and Dictyostelium discoideum putative polyketide synthases (PKSs). These KR domains contain two subdomains, each of which is related to SDR Rossmann fold domains. However, while the C-terminal subdomain has an active site similar to the other SDRs and a NADP-binding capability, the N-terminal SDR-like subdomain is truncated and lacks these functions, serving a supportive structural role. In some instances, such as porcine FAS, an enoyl reductase (a Rossman fold NAD-binding domain of the medium-chain dehydrogenase/reductase, MDR family) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER); this KR and ER are members of the SDR family. This KR subfamily has an active site tetrad with a similar 3D orientation compared to archetypical SDRs, but the active site Lys and Asn residue positions are swapped. The characteristic NADP-binding is typical of the multidomain complex SDRs, with a GGXGXXG NADP binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187657 [Multi-domain]  Cd Length: 452  Bit Score: 344.43  E-value: 8.61e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 222 ISKTFCPA--HKSYIITGGLGGFGLELARWLVLRGAQR-LVLTSRSGIRTGyQAKHIREWRRQ---GIQVLVSTSNVSSL 295
Cdd:cd08954 208 ILKTNYPInlGKSYLITGGSGGLGLEILKWLVKRGAVEnIIILSRSGMKWE-LELLIREWKSQnikFHFVSVDVSDVSSL 286

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 296 EGARALIAEATKLGPVGGVFNLAMVLRDAMLENQTPELFQDVNKPKYNGTLNLDRATREACPELDYFVAFSSVSCGRGNA 375
Cdd:cd08954 287 EKAINLILNAPKIGPIGGIFHLAFVLIDKVLEIDTESLFISVNKAKVMGAINLHNQSIKRCWKLDYFVLFSSVSSIRGSA 366

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 376 GQTNYGFANSTMERICEQRRHDGLPGLAVQWGAIGDVGIVlEAMGTNDTVIG--GTLPQRISSCMEVLDLFLN--QPHAV 451
Cdd:cd08954 367 GQCNYVCANSVLDSLSRYRKSIGLPSIAINWGAIGDVGFV-SRNESVDTLLGgqGLLPQSINSCLGTLDLFLQnpSPNLV 445


                ....*..
gi 37604163 452 LSSFVLA 458
Cdd:cd08954 446 LSSFNFA 452
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 1-200 4.14e-103

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 320.49  E-value: 4.14e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163      1 AYYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLqaRFPQLDDTSFANSRDTSFEQHVLL 80
Cdd:smart00829  91 AYYALVDLARLRPGESVLIHAAAGGVGQAAIQLARHLGAEVFATAGSPEKRDFL--RALGIPDDHIFSSRDLSFADEILR 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163     81 HTGGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIGKFDLSNNHPLGMAIFLKNVTFHGILLDALFEEaNDSWREVAALL 160
Cdd:smart00829 169 ATGGRGVDVVLNSLSGEFLDASLRCLAPGGRFVEIGKRDIRDNSQLAMAPFRPNVSYHAVDLDALEEG-PDRIRELLAEV 247

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 37604163    161 KAGIRDGVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLV 200
Cdd:smart00829 248 LELFAEGVLRPLPVTVFPISDAEDAFRYMQQGKHIGKVVL 287
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
 1-200 2.05e-87

enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. Polyketide synthases produce polyketides in step by step mechanism that is similar to fatty acid synthesis. Enoyl reductase reduces a double to single bond. Erythromycin is one example of a polyketide generated by 3 complex enzymes (megasynthases). 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176179 [Multi-domain]  Cd Length: 293  Bit Score: 279.45  E-value: 2.05e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQARFPqlDDTSFANSRDTSFEQHVLL 80
Cdd:cd05195  96 AYYALVDLARLQKGESVLIHAAAGGVGQAAIQLAQHLGAEVFATVGSEEKREFLRELGG--PVDHIFSSRDLSFADGILR 173

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  81 HTGGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIGKFDLSNNHPLGMAIFLKNVTFHGILLDALFEEandSWREVAALL 160
Cdd:cd05195 174 ATGGRGVDVVLNSLSGELLRASWRCLAPFGRFVEIGKRDILSNSKLGMRPFLRNVSFSSVDLDQLARE---RPELLRELL 250

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 37604163 161 KAGIR---DGVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLV 200
Cdd:cd05195 251 REVLElleAGVLKPLPPTVVPSASEIDAFRLMQSGKHIGKVVL 293
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 247-452 1.83e-57

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 201.46  E-value: 1.83e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 247 ARWLVLRGAQRLVLTSRSGIRTGYQAKhIREWRRQGIQVLVSTSNVSSLEGARALIAEATKLGPVGGVFNLAMVLRDAML 326
Cdd:cd05274 167 ARWLAARGARHLVLLSRRGPAPRAAAR-AALLRAGGARVSVVRCDVTDPAALAALLAELAAGGPLAGVIHAAGVLRDALL 245

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 327 ENQTPELFQDVNKPKYNGTLNLDRATREAcpELDYFVAFSSVSCGRGNAGQTNYGFANSTMERICEQRRHDGLPGLAVQW 406
Cdd:cd05274 246 AELTPAAFAAVLAAKVAGALNLHELTPDL--PLDFFVLFSSVAALLGGAGQAAYAAANAFLDALAAQRRRRGLPATSVQW 323

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 37604163 407 GAIGDVGIVLEAMGTNDTVIGGTLPQRISSCMEVLDLFLNQPHAVL 452
Cdd:cd05274 324 GAWAGGGMAAAAALRARLARSGLGPLAPAEALEALEALLASDAPQA 369
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 231-411 3.12e-55

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 188.46  E-value: 3.12e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163    231 KSYIITGGLGGFGLELARWLVLRGAQRLVLTSRSGIRTGYQAKHIREWRRQGIQVLVSTSNVSSLEGARALIAEA-TKLG 309
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGARRLVLLSRSGPDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIpAVEG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163    310 PVGGVFNLAMVLRDAMLENQTPELFQDVNKPKYNGTLNLDRATReaCPELDYFVAFSSVSCGRGNAGQTNYGFANSTMER 389
Cdd:smart00822  81 PLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTA--DLPLDFFVLFSSIAGVLGSPGQANYAAANAFLDA 158

                          170       180
                   ....*....|....*....|..
gi 37604163    390 ICEQRRHDGLPGLAVQWGAIGD 411
Cdd:smart00822 159 LAEYRRARGLPALSIAWGAWAE 180
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 1-203 7.61e-48

NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 173.03  E-value: 7.61e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQArfpqLDDTSFANSRDTSFEQHVLL 80
Cdd:COG0604 127 AWQALFDRGRLKPGETVLVHGAAGGVGSAAVQLAKALGARVIATASSPEKAELLRA----LGADHVIDYREEDFAERVRA 202

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  81 HTGGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIGKFDLSNNHPLGMAIFLKNVTFHGILLDALFEEAN-DSWREVAAL 159
Cdd:COG0604 203 LTGGRGVDVVLDTVGGDTLARSLRALAPGGRLVSIGAASGAPPPLDLAPLLLKGLTLTGFTLFARDPAERrAALAELARL 282

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 37604163 160 lkagIRDGVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLVQVR 203
Cdd:COG0604 283 ----LAAGKLRPVIDRVFPLEEAAEAHRLLESGKHRGKVVLTVD 322
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 588-847 1.41e-46

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 166.02  E-value: 1.41e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   588 RPLFLVHPIEGSTTVFHSLAAKLSVPT------YGLQCTQAAPLDSIPNLAAYYIDCIKQVQPEGPYRIAGYSFGACVAF 661
Cdd:pfam00975   1 RPLFCFPPAGGSASSFRSLARRLPPPAevlavqYPGRGRGEPPLNSIEALADEYAEALRQIQPEGPYALFGHSMGGMLAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   662 EMCSQLQaQQGPAPTHnnLFLFDGSHTYVLAYTQSYRAKMTPgceaeaeaealcfFIKQFLDVEHSkvLEALLP----LK 737
Cdd:pfam00975  81 EVARRLE-RQGEAVRS--LFLSDASAPHTVRYEASRAPDDDE-------------VVAEFTDEGGT--PEELLEdeelLS 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   738 SLEDRVAASVDLITKSHHSLDRRelsfaavsfyhkLRAADQYKPKAKYHGNVTLlraktggtygedlgaDYNLSQVCDGK 817
Cdd:pfam00975 143 MLLPALRADYRALESYSCPPLDA------------QSATLFYGSDDPLHDADDL---------------AEWVRDHTPGE 195

                         250       260       270
                  ....*....|....*....|....*....|
gi 37604163   818 VSVHIIEGDHRTLLEgsGLESIINIIHSSL 847
Cdd:pfam00975 196 FDVHVFDGDHFYLIE--HLEAVLEIIEAKL 223
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 232-411 2.73e-45

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 160.81  E-value: 2.73e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   232 SYIITGGLGGFGLELARWLVLRGAQRLVLTSRSGIRTGYQAKHIREWRRQGIQVLVSTSNVSSLEGARALIAEA-TKLGP 310
Cdd:pfam08659   2 TYLITGGLGGLGRELARWLAERGARHLVLLSRSAAPRPDAQALIAELEARGVEVVVVACDVSDPDAVAALLAEIkAEGPP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   311 VGGVFNLAMVLRDAMLENQTPELFQDVNKPKYNGTLNLDRATREAcpELDYFVAFSSVSCGRGNAGQTNYGFANSTMERI 390
Cdd:pfam08659  82 IRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHEATPDE--PLDFFVLFSSIAGLLGSPGQANYAAANAFLDAL 159

                         170       180
                  ....*....|....*....|.
gi 37604163   391 CEQRRHDGLPGLAVQWGAIGD 411
Cdd:pfam08659 160 AEYRRSQGLPATSINWGPWAE 180
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
 1-201 5.06e-40

Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176203 [Multi-domain]  Cd Length: 323  Bit Score: 150.73  E-value: 5.06e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQARfpQLDDTsfANSRDTSFEQHVLL 80
Cdd:cd08241 127 AYHALVRRARLQPGETVLVLGAAGGVGLAAVQLAKALGARVIAAASSEEKLALARAL--GADHV--IDYRDPDLRERVKA 202

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  81 HTGGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIGkF------DLSNNHPLgmaifLKNVTFHGILLDALFEEANDSWR 154
Cdd:cd08241 203 LTGGRGVDVVYDPVGGDVFEASLRSLAWGGRLLVIG-FasgeipQIPANLLL-----LKNISVVGVYWGAYARREPELLR 276

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 37604163 155 EVAALLKAGIRDGVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLVQ 201
Cdd:cd08241 277 ANLAELFDLLAEGKIRPHVSAVFPLEQAAEALRALADRKATGKVVLT 323
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
 232-420 1.76e-38

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); Ketoreductase, a module of the multidomain polyketide synthase, has 2 subdomains, each corresponding to a short-chain dehydrogenases/reductase (SDR) family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerizes but is composed of 2 subdomains, each resembling an SDR monomer. In some instances, as in porcine FAS, an enoyl reductase (a Rossman fold NAD binding domain of the MDR family) module is inserted between the sub-domains. The active site resembles that of typical SDRs, except that the usual positions of the catalytic asparagine and tyrosine are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular polyketide synthases are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) fatty acid synthase. In some instances, such as porcine FAS , an enoyl reductase module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER). Polyketide syntheses also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes the KR domain of the Lyngbya majuscule Jam J, -K, and #L which are encoded on the jam gene cluster and are involved in the synthesis of the Jamaicamides (neurotoxins); Lyngbya majuscule Jam P belongs to a different KR_FAS_SDR_x subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187658 [Multi-domain]  Cd Length: 376  Bit Score: 147.82  E-value: 1.76e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 232 SYIITGGLGGFGLELARWLVLRGAQRLVLTSRSGIRTGYQAKhIREWRRQGIQVLVSTSNVSSLEGARALIAE-ATKLGP 310
Cdd:cd08955 151 TYLITGGLGGLGLLVAEWLVERGARHLVLTGRRAPSAAARQA-IAALEEAGAEVVVLAADVSDRDALAAALAQiRASLPP 229

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 311 VGGVFNLAMVLRDAMLENQTPELFQDVNKPKYNGTLNLDRATREAcpELDYFVAFSSVSCGRGNAGQTNYGFANSTMERI 390
Cdd:cd08955 230 LRGVIHAAGVLDDGVLANQDWERFRKVLAPKVQGAWNLHQLTQDL--PLDFFVLFSSVASLLGSPGQANYAAANAFLDAL 307

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 37604163 391 CEQRRHDGLPGLAVQWGAIGDVGI--------VLEAMG 420
Cdd:cd08955 308 AHYRRARGLPALSINWGPWAEVGMaaslarqaRLEARG 345
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
 1-200 1.88e-37

PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium chain dehydrogenase/reductase family member, acts in the apoptotic pathway. PIG3 reduces ortho-quinones, but its apoptotic activity has been attributed to oxidative stress generation, since overexpression of PIG3 accumulates reactive oxygen species. PIG3 resembles the MDR family member quinone reductases, which catalyze the reduction of quinone to hydroxyquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176180 [Multi-domain]  Cd Length: 323  Bit Score: 142.97  E-value: 1.88e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQARFPqldDTSFaNSRDTSFEQHVLL 80
Cdd:cd05276 127 AWQNLFQLGGLKAGETVLIHGGASGVGTAAIQLAKALGARVIATAGSEEKLEACRALGA---DVAI-NYRTEDFAEEVKE 202

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  81 HTGGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIG-------KFDLsnnhplgMAIFLKNVTFHGILLDAL-FEEANDS 152
Cdd:cd05276 203 ATGGRGVDVILDMVGGDYLARNLRALAPDGRLVLIGllggakaELDL-------APLLRKRLTLTGSTLRSRsLEEKAAL 275

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 37604163 153 WREVAALLKAGIRDGVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLV 200
Cdd:cd05276 276 AAAFREHVWPLFASGRIRPVIDKVFPLEEAAEAHRRMESNEHIGKIVL 323
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
 1-200 2.09e-36

polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that is similar to fatty acid synthesis. Enoyl reductase reduces a double to single bond. Erythromycin is one example of a polyketide generated by 3 complex enzymes (megasynthases). 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176213 [Multi-domain]  Cd Length: 303  Bit Score: 139.48  E-value: 2.09e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVvRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQarfpQLDDTSFANSRDTSFEQHVLL 80
Cdd:cd08251 109 VIDAFA-RAGLAKGEHILIQTATGGTGLMAVQLARLKGAEIYATASSDDKLEYLK----QLGVPHVINYVEEDFEEEIMR 183

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  81 HTGGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIGKFDLSNNHPLGMAIFLKNVTFHGI-LLDALFEEANDSWREVAAL 159
Cdd:cd08251 184 LTGGRGVDVVINTLSGEAIQKGLNCLAPGGRYVEIAMTALKSAPSVDLSVLSNNQSFHSVdLRKLLLLDPEFIADYQAEM 263

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 37604163 160 LkAGIRDGVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLV 200
Cdd:cd08251 264 V-SLVEEGELRPTVSRIFPFDDIGEAYRYLSDRENIGKVVV 303
quinone_pig3 TIGR02824
putative NAD(P)H quinone oxidoreductase, PIG3 family; Members of this family are putative ...
 1-202 1.41e-35

putative NAD(P)H quinone oxidoreductase, PIG3 family; Members of this family are putative quinone oxidoreductases that belong to the broader superfamily (modeled by Pfam pfam00107) of zinc-dependent alcohol (of medium chain length) dehydrogenases and quinone oxiooreductases. The alignment shows no motif of conserved Cys residues as are found in zinc-binding members of the superfamily, and members are likely to be quinone oxidoreductases instead. A member of this family in Homo sapiens, PIG3, is induced by p53 but is otherwise uncharacterized. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274316 [Multi-domain]  Cd Length: 325  Bit Score: 137.78  E-value: 1.41e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163     1 AYYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQArfpqLDDTSFANSRDTSFEQHVLL 80
Cdd:TIGR02824 127 VWSNLFQRGGLKAGETVLIHGGASGIGTTAIQLAKAFGARVFTTAGSDEKCAACEA----LGADIAINYREEDFVEVVKA 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163    81 HTGGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIG-------KFDLsnnhplgMAIFLKNVTFHGILLDAlfeEANDSW 153
Cdd:TIGR02824 203 ETGGKGVDVILDIVGGSYLNRNIKALALDGRIVQIGfqggrkaELDL-------GPLLAKRLTITGSTLRA---RPVAEK 272

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 37604163   154 REVAALLKAG----IRDGVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLVQV 202
Cdd:TIGR02824 273 AAIAAELREHvwplLASGRVRPVIDKVFPLEDAAQAHALMESGDHIGKIVLTV 325
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-202 6.45e-35

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176233 [Multi-domain]  Cd Length: 326  Bit Score: 135.76  E-value: 6.45e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVgSAEKRAYLQarfpQLDDTsFANSRDTSFEQHVLL 80
Cdd:cd08272 132 AWEGLVDRAAVQAGQTVLIHGGAGGVGHVAVQLAKAAGARVYATA-SSEKAAFAR----SLGAD-PIIYYRETVVEYVAE 205

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  81 HTGGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIGKFDlsnNHPLGMAIFlKNVTFHGI--LLDALFEEANDSWREVAA 158
Cdd:cd08272 206 HTGGRGFDVVFDTVGGETLDASFEAVALYGRVVSILGGA---THDLAPLSF-RNATYSGVftLLPLLTGEGRAHHGEILR 281

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 37604163 159 LLKAGIRDGVVKP-LKCTVFPKAQVEDAFRYMAQGKHIGKVLVQV 202
Cdd:cd08272 282 EAARLVERGQLRPlLDPRTFPLEEAAAAHARLESGSARGKIVIDV 326
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
 585-851 1.33e-34

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 142.15  E-value: 1.33e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 585 SSERPLFLVHPIEGSTTVFHSLAAKLS--VPTYGLQC----TQAAPLDSIPNLAAYYIDCIKQVQPEGPYRIAGYSFGAC 658
Cdd:COG3319 599 GSGPPLFCVHPAGGNVLCYRPLARALGpdRPVYGLQApgldGGEPPPASVEEMAARYVEAIRAVQPEGPYHLLGWSFGGL 678

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 659 VAFEMCSQLQAQQGPAPThnnLFLFDgshtyvlaytqSYRAKMTPGCEAEAEAEALCFFIKQFLDVEHSkvLEALLPLkS 738
Cdd:COG3319 679 VAYEMARQLEAQGEEVAL---LVLLD-----------SYAPGALARLDEAELLAALLRDLARGVDLPLD--AEELRAL-D 741

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 739 LEDRVAASVDLITKSH--HSLDRRELSFAAVSFYHKLRAADQYKPKAkYHGNVTLLRAkTGGTYGEDLGADYNLSQVCDG 816
Cdd:COG3319 742 PEERLARLLERLREAGlpAGLDAERLRRLLRVFRANLRALRRYRPRP-YDGPVLLFRA-EEDPPGRADDPALGWRPLVAG 819

                       250       260       270
                ....*....|....*....|....*....|....*
gi 37604163 817 KVSVHIIEGDHRTLLEGSGLESIINIIHSSLAEPR 851
Cdd:COG3319 820 GLEVHDVPGDHFSMLREPHVAELAAALRAALAAAE 854
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 247-419 2.51e-31

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 127.87  E-value: 2.51e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 247 ARWLVLRGAQRLVLTSRSGI--RTGYQAKHIREWRRQGIQVLVSTSNVSSLEGARALIAEATK-LGPVGGVFNLAMVLRD 323
Cdd:cd08953 222 ARALARRYGARLVLLGRSPLppEEEWKAQTLAALEALGARVLYISADVTDAAAVRRLLEKVRErYGAIDGVIHAAGVLRD 301

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 324 AMLENQTPELFQDVNKPKYNGTLNLDRATREAcpELDYFVAFSSVSCGRGNAGQTNYGFANSTMERICEQRR--HDGLPG 401
Cdd:cd08953 302 ALLAQKTAEDFEAVLAPKVDGLLNLAQALADE--PLDFFVLFSSVSAFFGGAGQADYAAANAFLDAFAAYLRqrGPQGRV 379

                       170
                ....*....|....*...
gi 37604163 402 LAVQWGAIGDVGIVLEAM 419
Cdd:cd08953 380 LSINWPAWREGGMAADLG 397
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-202 1.32e-30

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 123.48  E-value: 1.32e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQArfpqLDDTSFANSRDTSFEQHVLL 80
Cdd:cd08268 132 AYGALVELAGLRPGDSVLITAASSSVGLAAIQIANAAGATVIATTRTSEKRDALLA----LGAAHVIVTDEEDLVAEVLR 207

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  81 HTGGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIGKFDLSNNhPLGM-AIFLKNVTFHGILLDA--LFEEANdswREVA 157
Cdd:cd08268 208 ITGGKGVDVVFDPVGGPQFAKLADALAPGGTLVVYGALSGEPT-PFPLkAALKKSLTFRGYSLDEitLDPEAR---RRAI 283

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 37604163 158 ALLKAGIRDGVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLVQV 202
Cdd:cd08268 284 AFILDGLASGALKPVVDRVFPFDDIVEAHRYLESGQQIGKIVVTP 328
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
 1-202 2.24e-30

Alcohol dehydrogenases of the MDR family; This group contains proteins related to the zinc-dependent alcohol dehydrogenases. However, while the group has structural zinc site characteristic of these enzymes, it lacks the consensus site for a catalytic zinc. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176227 [Multi-domain]  Cd Length: 342  Bit Score: 123.14  E-value: 2.24e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQArfpqLDDTSFANSRDTSFEQHVLL 80
Cdd:cd08266 154 AWHMLVTRARLRPGETVLVHGAGSGVGSAAIQIAKLFGATVIATAGSEDKLERAKE----LGADYVIDYRKEDFVREVRE 229

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  81 HTGGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIG-------KFDLsnnhplgMAIFLKNVTFHGILLdalfeeanDSW 153
Cdd:cd08266 230 LTGKRGVDVVVEHVGAATWEKSLKSLARGGRLVTCGattgyeaPIDL-------RHVFWRQLSILGSTM--------GTK 294

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 37604163 154 REVAALLKAgIRDGVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLVQV 202
Cdd:cd08266 295 AELDEALRL-VFRGKLKPVIDSVFPLEEAAEAHRRLESREQFGKIVLTP 342
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
 1-202 8.69e-29

Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye lens protein with NADP-dependent quinone reductase activity (QOR). It has been cited as a structural component in mammalian eyes, but also has homology to quinone reductases in unrelated species. QOR catalyzes the conversion of a quinone and NAD(P)H to a hydroquinone and NAD(P+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176215 [Multi-domain]  Cd Length: 325  Bit Score: 118.07  E-value: 8.69e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQARFPqldDTSFaNSRDTSFEQHVLL 80
Cdd:cd08253 132 AYRALFHRAGAKAGETVLVHGGSGAVGHAAVQLARWAGARVIATASSAEGAELVRQAGA---DAVF-NYRAEDLADRILA 207

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  81 HTGGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIGKFDLSNNHPLGmAIFLKNVTFHGILLDALFEEAndsWREVAALL 160
Cdd:cd08253 208 ATAGQGVDVIIEVLANVNLAKDLDVLAPGGRIVVYGSGGLRGTIPIN-PLMAKEASIRGVLLYTATPEE---RAAAAEAI 283

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 37604163 161 KAGIRDGVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLVQV 202
Cdd:cd08253 284 AAGLADGALRPVIAREYPLEEAAAAHEAVESGGAIGKVVLDP 325
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-202 8.37e-28

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176237 [Multi-domain]  Cd Length: 336  Bit Score: 115.33  E-value: 8.37e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVVRGRIQRGETVLIHsGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQArfpqLDDTSFANSRDTS-FEQHVL 79
Cdd:cd08276 148 AWNALFGLGPLKPGDTVLVQ-GTGGVSLFALQFAKAAGARVIATSSSDEKLERAKA----LGADHVINYRTTPdWGEEVL 222

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  80 LHTGGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIGKFDLSNNHPLGMAIFLKNVTFHGILLD--ALFEEANdswrevA 157
Cdd:cd08276 223 KLTGGRGVDHVVEVGGPGTLAQSIKAVAPGGVISLIGFLSGFEAPVLLLPLLTKGATLRGIAVGsrAQFEAMN------R 296

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 37604163 158 ALLKAGIRdgvvkPLKCTVFPKAQVEDAFRYMAQGKHIGKVLVQV 202
Cdd:cd08276 297 AIEAHRIR-----PVIDRVFPFEEAKEAYRYLESGSHFGKVVIRV 336
KR_1_SDR_x cd08952
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 247-418 8.65e-28

ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the single KR domain of SpiF, the first KR domains of SpiE,-G,H,-I,and #J, the third KR domain of SpiG, and the second KR domain of SpiH. The second KR domains of SpiE,-G, I, and #J, and the KR domains of SpiD, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187655 [Multi-domain]  Cd Length: 480  Bit Score: 118.04  E-value: 8.65e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 247 ARWLVLRGAQRLVLTSRSGIRTGYQAKHIREWRRQGIQVLVSTSNVSSLEGARALIAEATKLGPVGGVFNLAMVLRDAML 326
Cdd:cd08952 247 ARWLARRGAEHLVLTSRRGPDAPGAAELVAELTALGARVTVAACDVADRDALAALLAALPAGHPLTAVVHAAGVLDDGPL 326

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 327 ENQTPELFQDVNKPKYNGTLNLDRATREAcpELDYFVAFSSVSCGRGNAGQTNYGFANSTMERICEQRRHDGLPGLAVQW 406
Cdd:cd08952 327 DDLTPERLAEVLRAKVAGARHLDELTRDR--DLDAFVLFSSIAGVWGSGGQGAYAAANAYLDALAERRRARGLPATSVAW 404

                       170
                ....*....|..
gi 37604163 407 GAIGDVGIVLEA 418
Cdd:cd08952 405 GPWAGGGMAAGA 416
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-160 9.10e-24

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 102.01  E-value: 9.10e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVVRGRIQRGETVLIHsGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQarfpQLDDTSFANSRDTSFEQHVLL 80
Cdd:cd05188 122 AYHALRRAGVLKPGDTVLVL-GAGGVGLLAAQLAKAAGARVIVTDRSDEKLELAK----ELGADHVIDYKEEDLEEELRL 196

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  81 hTGGKGVDLVLNSL-AEEKLQASVRCLAQHGRFLEIGKFDLSNNHPLGMAIFLKNVTFHGILLDALFEeandsWREVAAL 159
Cdd:cd05188 197 -TGGGGADVVIDAVgGPETLAQALRLLRPGGRIVVVGGTSGGPPLDDLRRLLFKELTIIGSTGGTRED-----FEEALDL 270


                .
gi 37604163 160 L 160
Cdd:cd05188 271 L 271
KR_3_FAS_SDR_x cd08956
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); ...
 247-452 2.89e-23

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta- ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the second KR domains of SpiE,-G, I, and -J, both KR domains of SpiD, and the third KR domain of SpiH. The single KR domain of SpiF, the first and second KR domains of SpiH, the first KR domains of SpiE,-G,- I, and -J, and the third KR domain of SpiG, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187659 [Multi-domain]  Cd Length: 448  Bit Score: 103.89  E-value: 2.89e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 247 ARWLVLR-GAQRLVLTSRSGIRTGYQAKHIREWRRQGIQVLVSTSNVSSLEGARALIAEATKLGPVGGVFNLAMVLRDAM 325
Cdd:cd08956 210 ARHLVTEhGVRHLLLVSRRGPDAPGAAELVAELAALGAEVTVAACDVADRAALAALLAAVPADHPLTAVVHAAGVLDDGV 289

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 326 LENQTPELFQDVNKPKYNGTLNLDRATREAcpELDYFVAFSSVSCGRGNAGQTNYGFANSTMERICEQRRHDGLPGLAVQ 405
Cdd:cd08956 290 LTSLTPERLDAVLRPKVDAAWHLHELTRDL--DLAAFVLFSSAAGVLGSPGQANYAAANAFLDALAQHRRARGLPATSLA 367

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 37604163 406 WGAIGDVGIVLEAMGTND---TVIGGTLPQRISSCMEVLDLFLNQPHAVL 452
Cdd:cd08956 368 WGLWAQASGMTAHLSDADlarLARGGLRPLSAEEGLALFDAALAADEPVL 417
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
 1-200 2.55e-21

alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; Members identified as zinc-dependent alcohol dehydrogenases and quinone oxidoreductase. QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176191 [Multi-domain]  Cd Length: 309  Bit Score: 95.71  E-value: 2.55e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVgSAEKRAYLQArfpqLDDTSFANSRDTSFEQHVLL 80
Cdd:cd05289 132 AWQALFELGGLKAGQTVLIHGAAGGVGSFAVQLAKARGARVIATA-SAANADFLRS----LGADEVIDYTKGDFERAAAP 206

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  81 HtggkGVDLVLNSLAEEKLQASVRCLAQHGRFLEIgkfdlsnnhpLGMAIFLKNVTFHGILLDALFEEAN-DSWREVAAL 159
Cdd:cd05289 207 G----GVDAVLDTVGGETLARSLALVKPGGRLVSI----------AGPPPAEQAAKRRGVRAGFVFVEPDgEQLAELAEL 272

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 37604163 160 lkagIRDGVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLV 200
Cdd:cd05289 273 ----VEAGKLRPVVDRVFPLEDAAEAHERLESGHARGKVVL 309
PGDH cd05288
Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the ...
 1-200 3.76e-20

Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176190 [Multi-domain]  Cd Length: 329  Bit Score: 92.54  E-value: 3.76e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQARFPQldDTSFaNSRDTSFEQhVLL 80
Cdd:cd05288 133 AYFGLTEIGKPKPGETVVVSAAAGAVGSVVGQIAKLLGARVVGIAGSDEKCRWLVEELGF--DAAI-NYKTPDLAE-ALK 208

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  81 HTGGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIG------KFDLSNNHPLGMAIFlKNVTFHG-ILLD--ALFEEANd 151
Cdd:cd05288 209 EAAPDGIDVYFDNVGGEILDAALTLLNKGGRIALCGaisqynATEPPGPKNLGNIIT-KRLTMQGfIVSDyaDRFPEAL- 286

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 37604163 152 swREVAALLKAG---IRDGVVKPLKctvfpkaQVEDAFRYMAQGKHIGKVLV 200
Cdd:cd05288 287 --AELAKWLAEGklkYREDVVEGLE-------NAPEAFLGLFTGKNTGKLVV 329
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-200 5.89e-19

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176236 [Multi-domain]  Cd Length: 337  Bit Score: 89.18  E-value: 5.89e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLgcRVFTTVG--SAEKRAYLQARFpqlddtsFANSRDTSFEQHV 78
Cdd:cd08275 126 AYYALFELGNLRPGQSVLVHSAAGGVGLAAGQLCKTV--PNVTVVGtaSASKHEALKENG-------VTHVIDYRTQDYV 196

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  79 --LLHTGGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIGKFDLSNNHPLGMAIFLK----------------NVTFHGI 140
Cdd:cd08275 197 eeVKKISPEGVDIVLDALGGEDTRKSYDLLKPMGRLVVYGAANLVTGEKRSWFKLAKkwwnrpkvdpmkliseNKSVLGF 276

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 141 LLDALFEEANDSWREVAALLKAgIRDGVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLV 200
Cdd:cd08275 277 NLGWLFEERELLTEVMDKLLKL-YEEGKIKPKIDSVFPFEEVGEAMRRLQSRKNIGKVVL 335
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
25-162 8.55e-19

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 83.04  E-value: 8.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163    25 GVGQAAISIALSLGCRVFTTVGSAEKRAYLQarfpQLDDTSFANSRDTSFEQHVLLHTGGKGVDLVLNSL-AEEKLQASV 103
Cdd:pfam00107   1 GVGLAAIQLAKAAGAKVIAVDGSEEKLELAK----ELGADHVINPKETDLVEEIKELTGGKGVDVVFDCVgSPATLEQAL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   104 RCLAQHGRFLEIGKFdlSNNHPLGMA-IFLKNVTFHGILLDalfeeANDSWREVAALLKA 162
Cdd:pfam00107  77 KLLRPGGRVVVVGLP--GGPLPLPLApLLLKELTILGSFLG-----SPEEFPEALDLLAS 129
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-202 2.49e-18

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176232 [Multi-domain]  Cd Length: 325  Bit Score: 86.95  E-value: 2.49e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVgSAEKRAYLQarfpQLDDTSFANSRDTSFEQHVLL 80
Cdd:cd08271 129 AYQALFKKLRIEAGRTILITGGAGGVGSFAVQLAKRAGLRVITTC-SKRNFEYVK----SLGADHVIDYNDEDVCERIKE 203

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  81 HTGGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIGKFDLSNNHPLgmaiFLKNVTFHGILLDALFEEAND----SWREV 156
Cdd:cd08271 204 ITGGRGVDAVLDTVGGETAAALAPTLAFNGHLVCIQGRPDASPDPP----FTRALSVHEVALGAAHDHGDPaawqDLRYA 279

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 37604163 157 AALLKAGIRDGVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLVQV 202
Cdd:cd08271 280 GEELLELLAAGKLEPLVIEVLPFEQLPEALRALKDRHTRGKIVVTI 325
ADH_zinc_N_2 pfam13602
Zinc-binding dehydrogenase;
68-200 2.04e-17

Zinc-binding dehydrogenase;


Pssm-ID: 433341 [Multi-domain]  Cd Length: 131  Bit Score: 79.30  E-value: 2.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163    68 NSRDTSFEQHvllhTGGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIGKFDLSNNhPLGMAIFLKNVTFHGILLdalFE 147
Cdd:pfam13602   8 DYRTTDFVQA----TGGEGVDVVLDTVGGEAFEASLRVLPGGGRLVTIGGPPLSAG-LLLPARKRGGRGVKYLFL---FV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 37604163   148 EAN---DSWREVAALLKAGirdgVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLV 200
Cdd:pfam13602  80 RPNlgaDILQELADLIEEG----KLRPVIDRVFPLEEAAEAHRYLESGRARGKIVL 131
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
 10-202 1.23e-16

Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. 2-haloacrylate reductase, a member of this subgroup, catalyzes the NADPH-dependent reduction of a carbon-carbon double bond in organohalogen compounds. Although similar to QOR, Burkholderia 2-haloacrylate reductase does not act on the quinones 1,4-benzoquinone and 1,4-naphthoquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176189 [Multi-domain]  Cd Length: 320  Bit Score: 81.72  E-value: 1.23e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  10 RIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAylQARFPQLDDTsfANSRDTSFEQHVLLHTGGKGVDL 89
Cdd:cd05286 133 PVKPGDTVLVHAAAGGVGLLLTQWAKALGATVIGTVSSEEKAE--LARAAGADHV--INYRDEDFVERVREITGGRGVDV 208

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  90 VLNSLAEEKLQASVRCLAQHGRFLEIGK-------FDLSNnhpLGM-AIFLKNVTFHGILLDAlfEEandsWREVAALLK 161
Cdd:cd05286 209 VYDGVGKDTFEGSLDSLRPRGTLVSFGNasgpvppFDLLR---LSKgSLFLTRPSLFHYIATR--EE----LLARAAELF 279

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 37604163 162 AGIRDGVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLVQV 202
Cdd:cd05286 280 DAVASGKLKVEIGKRYPLADAAQAHRDLESRKTTGKLLLIP 320
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-200 1.97e-15

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 78.03  E-value: 1.97e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVfTTVGSAEKRAYLQarfpQL--DDTSfaNSRDTSFeqhV 78
Cdd:cd08267 131 ALQALRDAGKVKPGQRVLINGASGGVGTFAVQIAKALGAHV-TGVCSTRNAELVR----SLgaDEVI--DYTTEDF---V 200

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  79 LLHTGGKGVDLVLNSLAEEK--LQASVRCLAQHGRFLEIGkfdlSNNHPLGMAIFLKNVTFHGI---LLDALFEEANDSW 153
Cdd:cd08267 201 ALTAGGEKYDVIFDAVGNSPfsLYRASLALKPGGRYVSVG----GGPSGLLLVLLLLPLTLGGGgrrLKFFLAKPNAEDL 276

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 37604163 154 REVAALLKAGIrdgvVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLV 200
Cdd:cd08267 277 EQLAELVEEGK----LKPVIDSVYPLEDAPEAYRRLKSGRARGKVVI 319
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
 1-200 3.51e-15

Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of undetermined function. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176212 [Multi-domain]  Cd Length: 329  Bit Score: 77.68  E-value: 3.51e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQArfpqLDDTSFANSRDTSFEQhVLL 80
Cdd:cd08250 127 ASIALEEVGEMKSGETVLVTAAAGGTGQFAVQLAKLAGCHVIGTCSSDEKAEFLKS----LGCDRPINYKTEDLGE-VLK 201

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  81 HTGGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIG---------KFDLSNNHPLGMAIFLKNVTFHGILLDALFEEAND 151
Cdd:cd08250 202 KEYPKGVDVVYESVGGEMFDTCVDNLALKGRLIVIGfisgyqsgtGPSPVKGATLPPKLLAKSASVRGFFLPHYAKLIPQ 281

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 37604163 152 SWREVAALLKAGirdgvvkPLKCTVFPKA-----QVEDAFRYMAQGKHIGKVLV 200
Cdd:cd08250 282 HLDRLLQLYQRG-------KLVCEVDPTRfrgleSVADAVDYLYSGKNIGKVVV 328
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
 10-199 5.20e-15

2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176645 [Multi-domain]  Cd Length: 323  Bit Score: 76.93  E-value: 5.20e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  10 RIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQArfpqLDDTSFANSRDTSFEQHVLLHTGGKGVDL 89
Cdd:cd05282 135 KLPPGDWVIQNAANSAVGRMLIQLAKLLGFKTINVVRRDEQVEELKA----LGADEVIDSSPEDLAQRVKEATGGAGARL 210

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  90 VLNSLAEEKLQASVRCLAQHGRFLEIGKfdLSNNH-PLGMAIFL-KNVTFHGILLDALFEEANDS-WREVAALLKAGIRD 166
Cdd:cd05282 211 ALDAVGGESATRLARSLRPGGTLVNYGL--LSGEPvPFPRSVFIfKDITVRGFWLRQWLHSATKEaKQETFAEVIKLVEA 288

                       170       180       190
                ....*....|....*....|....*....|...
gi 37604163 167 GVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVL 199
Cdd:cd05282 289 GVLTTPVGAKFPLEDFEEAVAAAEQPGRGGKVL 321
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 3-200 6.28e-15

D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport and metabolism];


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 76.69  E-value: 6.28e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   3 YSLVVRGRIQRGETVLIHsGSGGVGQAAISIALSLGCRVFTTVGSAEKRAylQARfpQLDDTSFANSRDTSFEQhvlLHT 82
Cdd:COG1064 152 YRALRRAGVGPGDRVAVI-GAGGLGHLAVQIAKALGAEVIAVDRSPEKLE--LAR--ELGADHVVNSSDEDPVE---AVR 223

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  83 GGKGVDLVLNSL-AEEKLQASVRCLAQHGRFLEIGkfDLSNNHPLGM-AIFLKNVTFHGILldalfeeaNDSWREVAALL 160
Cdd:COG1064 224 ELTGADVVIDTVgAPATVNAALALLRRGGRLVLVG--LPGGPIPLPPfDLILKERSIRGSL--------IGTRADLQEML 293

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 37604163 161 KAgIRDGVVKPlKCTVFPKAQVEDAFRYMAQGKHIGKVLV 200
Cdd:COG1064 294 DL-AAEGKIKP-EVETIPLEEANEALERLRAGKVRGRAVL 331
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
 1-204 1.23e-14

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 76.22  E-value: 1.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163    1 AYYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQarfpQLDDTSFANSRDTSFEQHVLL 80
Cdd:PTZ00354 128 AWQLLKKHGDVKKGQSVLIHAGASGVGTAAAQLAEKYGAATIITTSSEEKVDFCK----KLAAIILIRYPDEEGFAPKVK 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   81 H-TGGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIGKFDLSNNHPLGMA-IFLKNVTFHGILL----DALFEEANDSW- 153
Cdd:PTZ00354 204 KlTGEKGVNLVLDCVGGSYLSETAEVLAVDGKWIVYGFMGGAKVEKFNLLpLLRKRASIIFSTLrsrsDEYKADLVASFe 283

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 37604163  154 REVAALlkagIRDGVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLVQVRE 204
Cdd:PTZ00354 284 REVLPY----MEEGEIKPIVDRTYPLEEVAEAHTFLEQNKNIGKVVLTVNE 330
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-201 7.86e-14

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176234 [Multi-domain]  Cd Length: 331  Bit Score: 73.45  E-value: 7.86e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVgSAEKRAYLQarfpQLDDTSFANSRDTSFEQHVLl 80
Cdd:cd08273 127 AYQMLHRAAKVLTGQRVLIHGASGGVGQALLELALLAGAEVYGTA-SERNHAALR----ELGATPIDYRTKDWLPAMLT- 200

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  81 htgGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIGK------FDLSNNHPLGMAIFL---------KNVTFHGIllDAL 145
Cdd:cd08273 201 ---PGGVDVVFDGVGGESYEESYAALAPGGTLVCYGGnssllqGRRSLAALGSLLARLaklkllptgRRATFYYV--WRD 275

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 37604163 146 FEEANDSWREVAALLKAGIRDGVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLVQ 201
Cdd:cd08273 276 RAEDPKLFRQDLTELLDLLAKGKIRPKIAKRLPLSEVAEAHRLLESGKVVGKIVLL 331
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 6-202 1.41e-13

Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440683 [Multi-domain]  Cd Length: 341  Bit Score: 72.86  E-value: 1.41e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   6 VVRGRIQRGETVLIhSGSGGVGQAAISIALSLGC-RVFTTVGSAEKRAylQARfpQLDDTSFANSRDTSFEQHVLLHTGG 84
Cdd:COG1063 154 VERAGVKPGDTVLV-IGAGPIGLLAALAARLAGAaRVIVVDRNPERLE--LAR--ELGADAVVNPREEDLVEAVRELTGG 228

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  85 KGVDLVLNSL-AEEKLQASVRCLAQHGRFLEIG------KFDLsnnhplgMAIFLKNVTFHGILLDALfeeanDSWREVA 157
Cdd:COG1063 229 RGADVVIEAVgAPAALEQALDLVRPGGTVVLVGvpggpvPIDL-------NALVRKELTLRGSRNYTR-----EDFPEAL 296

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 37604163 158 ALLKAGIRDgvVKPLKCTVFPKAQVEDAFRYMAQGK-HIGKVLVQV 202
Cdd:COG1063 297 ELLASGRID--LEPLITHRFPLDDAPEAFEAAADRAdGAIKVVLDP 340
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 1-200 5.00e-13

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group contains proteins that share the characteristic catalytic and structural zinc-binding sites of the zinc-dependent alcohol dehydrogenase family. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48), then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176220 [Multi-domain]  Cd Length: 332  Bit Score: 71.19  E-value: 5.00e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVvRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQARFpqLDDTSFANSRDTSFEQHVll 80
Cdd:cd08259 151 AVHALK-RAGVKKGDTVLVTGAGGGVGIHAIQLAKALGARVIAVTRSPEKLKILKELG--ADYVIDGSKFSEDVKKLG-- 225

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  81 htggkGVDLVLNSLAEEKLQASVRCLAQHGRFLEIGKFD-LSNNHPLGMAIfLKNVTFHGilldalfeEANDSWREVAAL 159
Cdd:cd08259 226 -----GADVVIELVGSPTIEESLRSLNKGGRLVLIGNVTpDPAPLRPGLLI-LKEIRIIG--------SISATKADVEEA 291

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 37604163 160 LKAgIRDGVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLV 200
Cdd:cd08259 292 LKL-VKEGKIKPVIDRVVSLEDINEALEDLKSGKVVGRIVL 331
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 3-200 9.61e-13

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176235 [Multi-domain]  Cd Length: 350  Bit Score: 70.40  E-value: 9.61e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   3 YSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFtTVGSAEKRAYLQArfpqLDDTSFANSRDTSFEQHVLlhT 82
Cdd:cd08274 167 ENMLERAGVGAGETVLVTGASGGVGSALVQLAKRRGAIVI-AVAGAAKEEAVRA----LGADTVILRDAPLLADAKA--L 239

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  83 GGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIG-------KFDLSNnhplgmaIFLKNVTFHGILLDAlfeeandswRE 155
Cdd:cd08274 240 GGEPVDVVADVVGGPLFPDLLRLLRPGGRYVTAGaiagpvvELDLRT-------LYLKDLTLFGSTLGT---------RE 303

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 37604163 156 VAALLKAGIRDGVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLV 200
Cdd:cd08274 304 VFRRLVRYIEEGEIRPVVAKTFPLSEIREAQAEFLEKRHVGKLVL 348
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 1-200 2.70e-11

Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176205 [Multi-domain]  Cd Length: 320  Bit Score: 65.71  E-value: 2.70e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQAR---FPQLDDTSFANSrdtsfeqh 77
Cdd:cd08243 130 AWGSLFRSLGLQPGDTLLIRGGTSSVGLAALKLAKALGATVTATTRSPERAALLKELgadEVVIDDGAIAEQ-------- 201

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  78 vlLHTGGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIG----KFDLSNNHPLgMAIFLKN-VTFHG--------ILLDA 144
Cdd:cd08243 202 --LRAAPGGFDKVLELVGTATLKDSLRHLRPGGIVCMTGllggQWTLEDFNPM-DDIPSGVnLTLTGsssgdvpqTPLQE 278

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 37604163 145 LFEEandswrevaallkagIRDGVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLV 200
Cdd:cd08243 279 LFDF---------------VAAGHLDIPPSKVFTFDEIVEAHAYMESNRAFGKVVV 319
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
 9-201 1.26e-10

Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. Formaldehyde dehydrogenase (aka ADH3) may be the ancestral form of alcohol dehydrogenase, which evolved to detoxify formaldehyde. This CD contains glutathione dependant FDH, glutathione independent FDH, and related alcohol dehydrogenases. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. Unlike typical FDH, Pseudomonas putida aldehyde-dismutating FDH (PFDH) is glutathione-independent. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176181 [Multi-domain]  Cd Length: 347  Bit Score: 63.83  E-value: 1.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   9 GRIQRGETVLIhSGSGGVGQAAISIALSLGC-RVFTTVGSAEKRAYLQARFPqlddTSFANSRDTSFEQHVLLHTGGKGV 87
Cdd:cd05278 163 AGIKPGSTVAV-IGAGPVGLCAVAGARLLGAaRIIAVDSNPERLDLAKEAGA----TDIINPKNGDIVEQILELTGGRGV 237

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  88 DLVLNSLA-EEKLQASVRCLAQHGRFLEIGKFDLS-NNHPLGMAiFLKNVTFHGILLDAlfeeANDSWRevaaLLKAgIR 165
Cdd:cd05278 238 DCVIEAVGfEETFEQAVKVVRPGGTIANVGVYGKPdPLPLLGEW-FGKNLTFKTGLVPV----RARMPE----LLDL-IE 307

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 37604163 166 DGVVKPLK-CT-VFPKAQVEDAFRYMAQGK-HIGKVLVQ 201
Cdd:cd05278 308 EGKIDPSKlIThRFPLDDILKAYRLFDNKPdGCIKVVIR 346
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 1-116 1.67e-10

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group has the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176221 [Multi-domain]  Cd Length: 345  Bit Score: 63.39  E-value: 1.67e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVVRGRIQRGETVLIHsGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYlqARfpQLDDTSFANSRDT-SFEQHVL 79
Cdd:cd08260 153 AFRALVHQARVKPGEWVAVH-GCGGVGLSAVMIASALGARVIAVDIDDDKLEL--AR--ELGAVATVNASEVeDVAAAVR 227

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 37604163  80 LHTGGkGVDLVLNSL-AEEKLQASVRCLAQHGRFLEIG 116
Cdd:cd08260 228 DLTGG-GAHVSVDALgIPETCRNSVASLRKRGRHVQVG 264
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 471-526 2.16e-10

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 57.65  E-value: 2.16e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 37604163    471 QRDLVKAVAHILGIRDLAGINLDSTLADLGLDSLMGVEVRQILEREHDLVLPMREV 526
Cdd:smart00823  14 LDLVREQVAAVLGHAAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLV 69
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
 4-200 5.06e-10

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 61.98  E-value: 5.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163    4 SLVVRG----RIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQarfpqlddtsfansrdtSFEQHVL 79
Cdd:PRK13771 149 GMVYRGlrraGVKKGETVLVTGAGGGVGIHAIQVAKALGAKVIAVTSSESKAKIVS-----------------KYADYVI 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   80 lhTGGK---------GVDLVLNSLAEEKLQASVRCLAQHGRFLEIGKFDLSNNH--PLGMAIfLKNVTFHGIlldalfee 148
Cdd:PRK13771 212 --VGSKfseevkkigGADIVIETVGTPTLEESLRSLNMGGKIIQIGNVDPSPTYslRLGYII-LKDIEIIGH-------- 280

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 37604163  149 ANDSWREVAALLKAgIRDGVVKPLkctVFPKAQVED---AFRYMAQGKHIGKVLV 200
Cdd:PRK13771 281 ISATKRDVEEALKL-VAEGKIKPV---IGAEVSLSEidkALEELKDKSRIGKILV 331
CurA COG2130
NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and ...
 1-202 6.95e-10

NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 441733 [Multi-domain]  Cd Length: 333  Bit Score: 61.61  E-value: 6.95e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLqarfpqLDDTSFA---NSRDTSFEQH 77
Cdd:COG2130 134 AYFGLLDIGKPKAGETVVVSAAAGAVGSVVGQIAKLKGCRVVGIAGGAEKCRYL------VEELGFDaaiDYKAGDLAAA 207

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  78 vLLHTGGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIGKFDLSNNH-----PLGMAIFLKN-VTFHG-ILLD--ALFEE 148
Cdd:COG2130 208 -LAAACPDGIDVYFDNVGGEILDAVLPLLNTFARIAVCGAISQYNATepppgPRNLGQLLVKrLRMQGfIVFDhaDRFPE 286

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37604163 149 AndsWREVAALLKAG-------IRDGVvkplkctvfpkAQVEDAFRYMAQGKHIGKVLVQV 202
Cdd:COG2130 287 F---LAELAGWVAEGklkyretVVEGL-----------ENAPEAFLGLFEGENFGKLLVKV 333
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
470-670 7.60e-10

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 62.75  E-value: 7.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   470 TQRDLVKAVAHILGiRDLAGInlDSTLADLGLDSLMGVEVRQILEREhdlvlpMRevRQLTLRKLQEMSSKTDSATDTTA 549
Cdd:PRK10252  979 TETIIAAAFSSLLG-CDVVDA--DADFFALGGHSLLAMKLAAQLSRQ------FA--RQVTPGQVMVASTVAKLATLLDA 1047

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   550 PksrsdtSLKQNQLNLSTL--LVNPEGPTLtqlnsvqsserplFLVHPIEGSTTVFHSLAAKLS--VPTYGLQC------ 619
Cdd:PRK10252 1048 E------EDESRRLGFGTIlpLREGDGPTL-------------FCFHPASGFAWQFSVLSRYLDpqWSIYGIQSprpdgp 1108

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 37604163   620 -TQAAPLDSipnLAAYYIDCIKQVQPEGPYRIAGYSFGACVAFEMCSQLQAQ 670
Cdd:PRK10252 1109 mQTATSLDE---VCEAHLATLLEQQPHGPYHLLGYSLGGTLAQGIAARLRAR 1157
PRK10754 PRK10754
NADPH:quinone reductase;
2-116 7.67e-10

NADPH:quinone reductase;


Pssm-ID: 182701 [Multi-domain]  Cd Length: 327  Bit Score: 61.29  E-value: 7.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163    2 YYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKraylQARFPQLDDTSFANSRDTSFEQHVLLH 81
Cdd:PRK10754 129 YYLLRKTYEIKPDEQFLFHAAAGGVGLIACQWAKALGAKLIGTVGSAQK----AQRAKKAGAWQVINYREENIVERVKEI 204

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 37604163   82 TGGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIG 116
Cdd:PRK10754 205 TGGKKVRVVYDSVGKDTWEASLDCLQRRGLMVSFG 239
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
 1-200 8.65e-10

Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member of the medium chain dehydrogenase/ reductase (MDR) family. Riticulons are endoplasmic reticulum associated proteins involved in membrane trafficking and neuroendocrine secretion. The MDR/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176210 [Multi-domain]  Cd Length: 350  Bit Score: 61.47  E-value: 8.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVVRGRIQRGET----VLIHSGSGGVGQAAISIALSLGCRVFTTVGS--AEKRAYLQArfpqlDDTSFANSrdTSF 74
Cdd:cd08248 146 AWSALVNVGGLNPKNAagkrVLILGGSGGVGTFAIQLLKAWGAHVTTTCSTdaIPLVKSLGA-----DDVIDYNN--EDF 218

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  75 EQHVLLHTggkGVDLVLNSLAEEKLQASVRCLAQHGRFLEIGKFDLSNNHPLGMAI-FLKN-VTFHGILLDALFEEANDS 152
Cdd:cd08248 219 EEELTERG---KFDVILDTVGGDTEKWALKLLKKGGTYVTLVSPLLKNTDKLGLVGgMLKSaVDLLKKNVKSLLKGSHYR 295

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 37604163 153 W----------REVAALLKagirDGVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLV 200
Cdd:cd08248 296 WgffspsgsalDELAKLVE----DGKIKPVIDKVFPFEEVPEAYEKVESGHARGKTVI 349
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 13-202 9.04e-10

Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)- dependent oxidation. THD is a member of the zinc-requiring, medium chain NAD(H)-dependent alcohol dehydrogenase family (MDR). MDRs have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria) and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose.


Pssm-ID: 176184 [Multi-domain]  Cd Length: 341  Bit Score: 61.10  E-value: 9.04e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  13 RGETVLIhSGSGGVGQAAISIALSLGC-RVFTTVGSaEKRAYLqARfpQLDDTSFANSRDTSFeQHVLLHTGGKGVDLVL 91
Cdd:cd05281 163 SGKSVLI-TGCGPIGLMAIAVAKAAGAsLVIASDPN-PYRLEL-AK--KMGADVVINPREEDV-VEVKSVTDGTGVDVVL 236

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  92 N-SLAEEKLQASVRCLAQHGRFLEIG------KFDLSNNhplgmAIFlKNVTFHGILLDALFEeandSWREVAALLKAGI 164
Cdd:cd05281 237 EmSGNPKAIEQGLKALTPGGRVSILGlppgpvDIDLNNL-----VIF-KGLTVQGITGRKMFE----TWYQVSALLKSGK 306

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 37604163 165 RDgvVKPLKCTVFPKAQVEDAFRYMAQGKhIGKVLVQV 202
Cdd:cd05281 307 VD--LSPVITHKLPLEDFEEAFELMRSGK-CGKVVLYP 341
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
 8-199 8.14e-09

Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176206 [Multi-domain]  Cd Length: 324  Bit Score: 58.15  E-value: 8.14e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   8 RGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYlqARfpQLDDTSFANSRDTSFEQHVLLHTGGKGV 87
Cdd:cd08244 137 LATLTPGDVVLVTAAAGGLGSLLVQLAKAAGATVVGAAGGPAKTAL--VR--ALGADVAVDYTRPDWPDQVREALGGGGV 212

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  88 DLVLNSLAEEKLQASVRCLAQHGRFLEIGKFDLSNNHPLGMAIFLKNVTFHGILLDALfeEANDsWREVAALLKAGIRDG 167
Cdd:cd08244 213 TVVLDGVGGAIGRAALALLAPGGRFLTYGWASGEWTALDEDDARRRGVTVVGLLGVQA--ERGG-LRALEARALAEAAAG 289

                       170       180       190
                ....*....|....*....|....*....|..
gi 37604163 168 VVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVL 199
Cdd:cd08244 290 RLVPVVGQTFPLERAAEAHAALEARSTVGKVL 321
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 472-526 1.41e-08

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 51.80  E-value: 1.41e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 37604163   472 RDLVKAVAHILGIrDLAGINLDSTLADLGLDSLMGVEVRQILEREHDLVLPMREV 526
Cdd:pfam00550   1 ERLRELLAEVLGV-PAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDL 54
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 247-380 1.98e-08

3-ketoacyl-(acyl-carrier-protein) reductase; Validated


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 55.97  E-value: 1.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  247 ARWLVLRGAqRLVLTSRSGIRTGYQAkhIREWRRQGIQVLVSTSNVSSLEGARALIAEAT-KLGPVGGVFNLAMVLRDAM 325
Cdd:PRK05557  22 AERLAAQGA-NVVINYASSEAGAEAL--VAEIGALGGKALAVQGDVSDAESVERAVDEAKaEFGGVDILVNNAGITRDNL 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  326 LENQTPELFQDVNKPKYNGTLNLdraTREACPEL-----DYFVAFSSVSCGRGNAGQTNY 380
Cdd:PRK05557  99 LMRMKEEDWDRVIDTNLTGVFNL---TKAVARPMmkqrsGRIINISSVVGLMGNPGQANY 155
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
246-409 2.02e-08

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 56.03  E-value: 2.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 246 LARWLVLRGAqRLVLTSRSGIRTGYQAKHIREwrrQGIQVLVSTSNVSSLEGARALIAEAT-KLGPVGGVFNLAMVLRDA 324
Cdd:COG0300  21 LARALAARGA-RVVLVARDAERLEALAAELRA---AGARVEVVALDVTDPDAVAALAEAVLaRFGPIDVLVNNAGVGGGG 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 325 MLENQTPELFQ---DVNkpkYNGTLNLdraTREACPEL-----DYFVAFSSVSCGRGNAGQTNYGFANSTMERICEQRR- 395
Cdd:COG0300  97 PFEELDLEDLRrvfEVN---VFGPVRL---TRALLPLMrargrGRIVNVSSVAGLRGLPGMAAYAASKAALEGFSESLRa 170

                       170
                ....*....|....*..
gi 37604163 396 ---HDGLPGLAVQWGAI 409
Cdd:COG0300 171 elaPTGVRVTAVCPGPV 187
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
 6-201 2.19e-08

L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some members in this subgroup. L-iditol 2-dehydrogenase catalyzes the NAD+-dependent conversion of L-iditol to L-sorbose in fructose and mannose metabolism. This enzyme is related to sorbitol dehydrogenase, alcohol dehydrogenase, and other medium chain dehydrogenase/reductases. The zinc-dependent alcohol dehydrogenase (ADH-Zn)-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) to highlight its broad range of activities and to distinguish from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal GroES-like catalytic domain. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176197 [Multi-domain]  Cd Length: 343  Bit Score: 56.83  E-value: 2.19e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   6 VVRGRIQRGETVLIhSGSGGVGQAAISIALSLGCR-VFTTVGSAEKRAylQARfpQLDDTSFANSRDTSFEQHVLLHTGG 84
Cdd:cd08235 158 QRKAGIKPGDTVLV-IGAGPIGLLHAMLAKASGARkVIVSDLNEFRLE--FAK--KLGADYTIDAAEEDLVEKVRELTDG 232

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  85 KGVDLVLNSLAEEKLQA-SVRCLAQHGRFLEIGKFDLSNNhplgMAIFLKNVTFHGILLDALFEEANDSWREVAALLKAG 163
Cdd:cd08235 233 RGADVVIVATGSPEAQAqALELVRKGGRILFFGGLPKGST----VNIDPNLIHYREITITGSYAASPEDYKEALELIASG 308

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 37604163 164 IRDgvVKPLKCTVFPKAQVEDAFRYMAQGKHIgKVLVQ 201
Cdd:cd08235 309 KID--VKDLITHRFPLEDIEEAFELAADGKSL-KIVIT 343
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 6-200 2.23e-08

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 56.81  E-value: 2.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   6 VVRGRIQRGETVLIHsGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYlqARFPQLDDTsfANSRDTSFEQHVLLHTGGK 85
Cdd:cd08261 152 VRRAGVTAGDTVLVV-GAGPIGLGVIQVAKARGARVIVVDIDDERLEF--ARELGADDT--INVGDEDVAARLRELTDGE 226

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  86 GVDLVLNSL-AEEKLQASVRCLAQHGR--FLEIGKFDLSNNHPLgmaIFLKNVTFHGILLdALfeeaNDSWREVAALLka 162
Cdd:cd08261 227 GADVVIDATgNPASMEEAVELVAHGGRvvLVGLSKGPVTFPDPE---FHKKELTILGSRN-AT----REDFPDVIDLL-- 296

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 37604163 163 giRDGVVKPLK-CT-VFPKAQVEDAFRYMAQ-GKHIGKVLV 200
Cdd:cd08261 297 --ESGKVDPEAlIThRFPFEDVPEAFDLWEApPGGVIKVLI 335
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 469-534 4.60e-08

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 51.01  E-value: 4.60e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37604163 469 DTQRDLVKAVAHILGIrDLAGINLDSTL-ADLGLDSLMGVEVRQILEREHDLVLPMREVRQL-TLRKL 534
Cdd:COG0236   5 ELEERLAEIIAEVLGV-DPEEITPDDSFfEDLGLDSLDAVELIAALEEEFGIELPDTELFEYpTVADL 71
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 247-380 5.91e-08

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187594 [Multi-domain]  Cd Length: 240  Bit Score: 54.48  E-value: 5.91e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 247 ARWLVLRGAqRLVLTSRSGIRTGYQAKHIREwrrQGIQVLVSTSNVSSLEGARALIAEAT-KLGPVGGVFNLAMVLRDAM 325
Cdd:cd05333  17 ALRLAAEGA-KVAVTDRSEEAAAETVEEIKA---LGGNAAALEADVSDREAVEALVEKVEaEFGPVDILVNNAGITRDNL 92

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 37604163 326 LENQTPELFQDVNKPKYNGTLNLDRATREACPELDY--FVAFSSVSCGRGNAGQTNY 380
Cdd:cd05333  93 LMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSgrIINISSVVGLIGNPGQANY 149
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 590-682 3.65e-07

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 52.16  E-value: 3.65e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 590 LFLVHPIEGSTTVFHSLAAKLSvPTYGLQCTQ---------AAPLDSIPNLAAyyiDCIKQVQP--EGPYRIAGYSFGAC 658
Cdd:COG3208   9 LFCFPYAGGSASAYRPWAAALP-PDIEVLAVQlpgrgdrlgEPPLTSLEELAD---DLAEELAPllDRPFALFGHSMGAL 84

                        90       100
                ....*....|....*....|....
gi 37604163 659 VAFEMCSQLQAQQGPAPTHnnLFL 682
Cdd:COG3208  85 LAFELARRLERRGRPLPAH--LFV 106
leukotriene_B4_DH_like cd08294
13-PGR is a bifunctional enzyme with delta-13 15-prostaglandin reductase and leukotriene B4 12 ...
 1-202 4.85e-07

13-PGR is a bifunctional enzyme with delta-13 15-prostaglandin reductase and leukotriene B4 12 hydroxydehydrogenase activity; Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto- 13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176254 [Multi-domain]  Cd Length: 329  Bit Score: 52.65  E-value: 4.85e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQarfpQLD-DTSFaNSRDTSFEQhVL 79
Cdd:cd08294 131 AYFGLLEICKPKAGETVVVNGAAGAVGSLVGQIAKIKGCKVIGCAGSDDKVAWLK----ELGfDAVF-NYKTVSLEE-AL 204

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  80 LHTGGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIGKFDLSNN------HPLGMAIFLKNVTFHGILLDALFEEANDSW 153
Cdd:cd08294 205 KEAAPDGIDCYFDNVGGEFSSTVLSHMNDFGRVAVCGSISTYNDkepkkgPYVQETIIFKQLKMEGFIVYRWQDRWPEAL 284

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 37604163 154 REVAALLKAG---IRDGVVKPLKctvfpkaQVEDAFRYMAQGKHIGKVLVQV 202
Cdd:cd08294 285 KQLLKWIKEGklkYREHVTEGFE-------NMPQAFIGMLKGENTGKAIVKV 329
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
 12-200 6.75e-07

enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176211 [Multi-domain]  Cd Length: 339  Bit Score: 52.20  E-value: 6.75e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  12 QRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVgSAEKRAYLQarfpQLDDTSFANSRDTSFEQHVLLHTGGKgVDLVL 91
Cdd:cd08249 153 SKGKPVLIWGGSSSVGTLAIQLAKLAGYKVITTA-SPKNFDLVK----SLGADAVFDYHDPDVVEDIRAATGGK-LRYAL 226

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  92 NSLAE-EKLQASVRCLAQHGRfleiGKFDLSNNHPLGmAIFLKNVTFHGILLDALFEEANDS-------WREVAALLKag 163
Cdd:cd08249 227 DCISTpESAQLCAEALGRSGG----GKLVSLLPVPEE-TEPRKGVKVKFVLGYTVFGEIPEDrefgevfWKYLPELLE-- 299

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 37604163 164 irDGVVKPLKCTVFPK--AQVEDAFRYMAQGKHIGKVLV 200
Cdd:cd08249 300 --EGKLKPHPVRVVEGglEGVQEGLDLLRKGKVSGEKLV 336
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
 9-116 2.93e-06

Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This group contains the hypothetical TM0436 alcohol dehydrogenase from Thermotoga maritima, proteins annotated as 5-exo-alcohol dehydrogenase, and other members of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. MDR, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176193 [Multi-domain]  Cd Length: 361  Bit Score: 50.34  E-value: 2.93e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   9 GRIQRGETVLIHsGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQARFPQLDDTSFANSRDTSFEQHVLLHTGGKGVD 88
Cdd:cd08231 173 GPVGAGDTVVVQ-GAGPLGLYAVAAAKLAGARRVIVIDGSPERLELAREFGADATIDIDELPDPQRRAIVRDITGGRGAD 251

                        90       100       110
                ....*....|....*....|....*....|..
gi 37604163  89 LVL----NSLAeekLQASVRCLAQHGRFLEIG 116
Cdd:cd08231 252 VVIeasgHPAA---VPEGLELLRRGGTYVLVG 280
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 8-200 3.50e-06

NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol dehydrogenases and other sugar dehydrogenases of the medium-chain dehydrogenase/reductase family (MDR), which includes zinc-dependent alcohol dehydrogenase and related proteins. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Related proteins include threonine dehydrogenase, formaldehyde dehydrogenase, and butanediol dehydrogenase. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Horse liver alcohol dehydrogenase is a dimeric enzyme and each subunit has two domains. The NAD binding domain is in a Rossmann fold and the catalytic domain contains a zinc ion to which substrates bind. There is a cleft between the domains that closes upon formation of the ternary complex.


Pssm-ID: 176198 [Multi-domain]  Cd Length: 343  Bit Score: 49.92  E-value: 3.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   8 RGRIQRGETVLIhSGSGGVGQAAISIALSLGC-RVFTTVGSAEKRAYlqARFPQLDDTsfANSRDTSFEQhVLLHTGGKG 86
Cdd:cd08236 154 LAGITLGDTVVV-IGAGTIGLLAIQWLKILGAkRVIAVDIDDEKLAV--ARELGADDT--INPKEEDVEK-VRELTEGRG 227

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  87 VDLVLNSL-AEEKLQASVRCLAQHGRFLEIGkfDLSNNHPLGMA----IFLKNVTFHGILLDALFEEANDSWREVAALLK 161
Cdd:cd08236 228 ADLVIEAAgSPATIEQALALARPGGKVVLVG--IPYGDVTLSEEafekILRKELTIQGSWNSYSAPFPGDEWRTALDLLA 305

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 37604163 162 AGIRDgvVKPLKCTVFPKAQVEDAFRYMAQGK-HIGKVLV 200
Cdd:cd08236 306 SGKIK--VEPLITHRLPLEDGPAAFERLADREeFSGKVLL 343
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 3-196 3.79e-06

2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family has members identified as 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase and alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176217 [Multi-domain]  Cd Length: 277  Bit Score: 49.58  E-value: 3.79e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   3 YSLVVRGRIQRGETVLIhSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQARFPQLDDTSfansrdtsfeQHVLLHT 82
Cdd:cd08255  87 LNGVRDAEPRLGERVAV-VGLGLVGLLAAQLAKAAGAREVVGVDPDAARRELAEALGPADPVA----------ADTADEI 155

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  83 GGKGVDLVLN-SLAEEKLQASVRCLAQHGRFLEIGKFDLSNNhPLGMAIFLKNVTF---HGILLDAlfEEANDSWREVAA 158
Cdd:cd08255 156 GGRGADVVIEaSGSPSALETALRLLRDRGRVVLVGWYGLKPL-LLGEEFHFKRLPIrssQVYGIGR--YDRPRRWTEARN 232

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 37604163 159 LLKAG--IRDGVVKPLKCTVFPKAQVEDAFRYMAQGKHIG 196
Cdd:cd08255 233 LEEALdlLAEGRLEALITHRVPFEDAPEAYRLLFEDPPEC 272
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 1-116 5.93e-06

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176224 [Multi-domain]  Cd Length: 367  Bit Score: 49.29  E-value: 5.93e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVVRGRIQRGETVLIhSGSGGVGQAAISIALSLGCRVFTTVG-SAEKRAylQARfpQLDDTSFANSRDTSFEQHVL 79
Cdd:cd08263 175 AYGALKHAADVRPGETVAV-IGVGGVGSSAIQLAKAFGASPIIAVDvRDEKLA--KAK--ELGATHTVNAAKEDAVAAIR 249

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 37604163  80 LHTGGKGVDLVLNSLA-EEKLQASVRCLAQHGRFLEIG 116
Cdd:cd08263 250 EITGGRGVDVVVEALGkPETFKLALDVVRDGGRAVVVG 287
B4_12hDH TIGR02825
leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 ...
 1-55 6.78e-06

leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 12-hydroxydehydrogenase is an NADP-dependent enzyme of arachidonic acid metabolism, responsible for converting leukotriene B4 to the much less active metabolite 12-oxo-leukotriene B4. The BRENDA database lists leukotriene B4 12-hydroxydehydrogenase as one of the synonyms of 2-alkenal reductase (EC 1.3.1.74), while 1.3.1.48 is 15-oxoprostaglandin 13-reductase.


Pssm-ID: 131872 [Multi-domain]  Cd Length: 325  Bit Score: 49.22  E-value: 6.78e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 37604163     1 AYYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQ 55
Cdd:TIGR02825 126 AYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAAGSDEKVAYLK 180
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 1-193 6.81e-06

6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, and other MDR family members; This group contains enzymes of the zinc-dependent alcohol dehydrogenase family, including members (aka MDR) identified as 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase and N-benzyl-3-pyrrolidinol dehydrogenase. 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase catalyzes the conversion of 6-Hydroxycyclohex-1-enecarbonyl-CoA and NAD+ to 6-Ketoxycyclohex-1-ene-1-carboxyl-CoA,NADH, and H+. This group displays the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176216 [Multi-domain]  Cd Length: 338  Bit Score: 49.17  E-value: 6.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVVRGRIQRGETVLIhSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAylQARfpQLDDTSFANSRDTSFeQHVLL 80
Cdd:cd08254 153 PYHAVVRAGEVKPGETVLV-IGLGGLGLNAVQIAKAMGAAVIAVDIKEEKLE--LAK--ELGADEVLNSLDDSP-KDKKA 226

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  81 HTGGKGVDLVLN-SLAEEKLQASVRCLAQHGRFLEIGKFDLSNNHPLGMAIFL-KNVTFHgilldalFEEANDSWREVAA 158
Cdd:cd08254 227 AGLGGGFDVIFDfVGTQPTFEDAQKAVKPGGRIVVVGLGRDKLTVDLSDLIAReLRIIGS-------FGGTPEDLPEVLD 299

                       170       180       190
                ....*....|....*....|....*....|....*
gi 37604163 159 LlkagIRDGVVKPlKCTVFPKAQVEDAFRYMAQGK 193
Cdd:cd08254 300 L----IAKGKLDP-QVETRPLDEIPEVLERLHKGK 329
crotonyl_coA_red cd08246
crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase ...
 11-202 7.01e-06

crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase/reductase family, catalyzes the NADPH-dependent conversion of crotonyl-CoA to butyryl-CoA, a step in (2S)-methylmalonyl-CoA production for straight-chain fatty acid biosynthesis. Like enoyl reductase, another enzyme in fatty acid synthesis, crotonyl-CoA reductase is a member of the zinc-dependent alcohol dehydrogenase-like medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176208 [Multi-domain]  Cd Length: 393  Bit Score: 49.34  E-value: 7.01e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  11 IQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAY---LQAR-------FP---QLDDT-SFANSRDT---- 72
Cdd:cd08246 191 VKPGDNVLIWGASGGLGSMAIQLARAAGANPVAVVSSEEKAEYcraLGAEgvinrrdFDhwgVLPDVnSEAYTAWTkear 270

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  73 SFEQHVLLHTGGK-GVDLVLNSLAEEKLQASVRcLAQHGrfleigkfdlsnnhplGMAIFLKNVTFHGILLDALF----- 146
Cdd:cd08246 271 RFGKAIWDILGGReDPDIVFEHPGRATFPTSVF-VCDRG----------------GMVVICAGTTGYNHTYDNRYlwmrq 333

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37604163 147 ------EEANdsWREVAALLKAgIRDGVVKPLKCTVFPKAQVEDAFRYMAQGKH-IGKVLVQV 202
Cdd:cd08246 334 kriqgsHFAN--DREAAEANRL-VMKGRIDPCLSKVFSLDETPDAHQLMHRNQHhVGNMAVLV 393
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 247-383 2.41e-05

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 46.79  E-value: 2.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  247 ARWLVLRGAqRLVLTSRSGiRTGYQAkHIREWRRQGIQVLVSTSNVSSLEGARALIAEATK-LGPVGGVFNLAMVLRDAM 325
Cdd:PRK12825  23 ALRLARAGA-DVVVHYRSD-EEAAEE-LVEAVEALGRRAQAVQADVTDKAALEAAVAAAVErFGRIDILVNNAGIFEDKP 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  326 LENQTPELFQDVNKPKYNGTLNLDRATREACPELDY--FVAFSSVSCGRGNAGQTNYGFA 383
Cdd:PRK12825 100 LADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGgrIVNISSVAGLPGWPGRSNYAAA 159
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 277-383 3.86e-05

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 46.70  E-value: 3.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  277 EWRRQGIQVLVSTSNVSSLEGARALIAEATKLGPVGGVFNLAMVLRDAMLENQTPELFQDVNKPKYNGTLNL-------- 348
Cdd:PRK07792  56 EIRAAGAKAVAVAGDISQRATADELVATAVGLGGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLtrnaaayw 135

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 37604163  349 -DRATREACPELDYFVAFSSVSCGRGNAGQTNYGFA 383
Cdd:PRK07792 136 rAKAKAAGGPVYGRIVNTSSEAGLVGPVGQANYGAA 171
AST1_like cd08247
AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group ...
 17-202 5.48e-05

AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group contains members identified in targeting of yeast membrane proteins ATPase. AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast, identified as a multicopy suppressor of pma1 mutants which cause temperature sensitive growth arrest due to the inability of ATPase to target to the cell surface. This family is homologous to the medium chain family of dehydrogenases and reductases. Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176209 [Multi-domain]  Cd Length: 352  Bit Score: 46.11  E-value: 5.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  17 VLIHSGSGGVGQAAISIALSLGcRVFTTVGSAEKRAYLQARFPQLDDtsFANSRDTSFEQH---VLLHTGGKG-VDLVLN 92
Cdd:cd08247 155 VLVLGGSTSVGRFAIQLAKNHY-NIGTVVGTCSSRSAELNKKLGADH--FIDYDAHSGVKLlkpVLENVKGQGkFDLILD 231

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  93 SLAEEKLQAS----VRCLAQHGRFLEI-G------KFDLSNNHP---------LGMAIFLK-NVTFhgILLDAlfeeaND 151
Cdd:cd08247 232 CVGGYDLFPHinsiLKPKSKNGHYVTIvGdykanyKKDTFNSWDnpsanarklFGSLGLWSyNYQF--FLLDP-----NA 304

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 37604163 152 SWREVAALLkagIRDGVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLVQV 202
Cdd:cd08247 305 DWIEKCAEL---IADGKVKPPIDSVYPFEDYKEAFERLKSNRAKGKVVIKV 352
double_bond_reductase_like cd08295
Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase; This ...
 1-92 7.80e-05

Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase; This group includes proteins identified as the Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase. The Arabidopsis enzyme, a member of the medium chain dehydrogenase/reductase family, catalyzes the reduction of 7-8-double bond of phenylpropanal substrates as a plant defense mechanism. Prostaglandins and related eicosanoids (lipid mediators involved in host defense and inflamation) are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. Leukotriene B4 (LTB4) can be metabolized by LTB4 20-hydroxylase in inflamatory cells, and in other cells by bifunctional LTB4 12-HD/PGR. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176255 [Multi-domain]  Cd Length: 338  Bit Score: 45.77  E-value: 7.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVVRGRIQRGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQARF-----------PQLDDT---SF 66
Cdd:cd08295 139 AYAGFYEVCKPKKGETVFVSAASGAVGQLVGQLAKLKGCYVVGSAGSDEKVDLLKNKLgfddafnykeePDLDAAlkrYF 218

                        90       100
                ....*....|....*....|....*.
gi 37604163  67 ANSRDTSFEqhvllHTGGKGVDLVLN 92
Cdd:cd08295 219 PNGIDIYFD-----NVGGKMLDAVLL 239
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 314-409 2.42e-04

Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase (KR) domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 42.89  E-value: 2.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 314 VFNLAMVLRDAMLENQTPELFQDVNKPKYNGTLNLDRATREACPE--LDYFVAFSSVSCGRGNAGQTNYGFANSTMERIC 391
Cdd:cd02266  35 VVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAkrLGRFILISSVAGLFGAPGLGGYAASKAALDGLA 114

                        90       100
                ....*....|....*....|..
gi 37604163 392 EQRRHD----GLPGLAVQWGAI 409
Cdd:cd02266 115 QQWASEgwgnGLPATAVACGTW 136
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 231-381 2.73e-04

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 43.62  E-value: 2.73e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163 231 KSYIITGGLGGFGLELARWLVLRGAqRLVLTSRSGIRTGYQAKHIREwrrQGIQVLVSTSNVSSLEGARALIAEAT-KLG 309
Cdd:COG1028   7 KVALVTGGSSGIGRAIARALAAEGA-RVVITDRDAEALEAAAAELRA---AGGRALAVAADVTDEAAVEALVAAAVaAFG 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37604163 310 PVGGVFNLAMVLRDAMLENQTPELFQDVNKPKYNGTLNLdraTREACPEL---DY--FVAFSSVSCGRGNAGQTNYG 381
Cdd:COG1028  83 RLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLL---TRAALPHMrerGGgrIVNISSIAGLRGSPGQAAYA 156
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 247-334 3.54e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 43.07  E-value: 3.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  247 ARWLVLRGAQRLVLTSRSGIRTGYQAKHIREwrrQGIQVLVSTSNVSSLEGARALIAEA-TKLGPVGGVFNLAMVLRDAM 325
Cdd:PRK06198  23 ARAFAERGAAGLVICGRNAEKGEAQAAELEA---LGAKAVFVQADLSDVEDCRRVVAAAdEAFGRLDALVNAAGLTDRGT 99


                 ....*....
gi 37604163  326 LENQTPELF 334
Cdd:PRK06198 100 ILDTSPELF 108
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
231-381 3.84e-04

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 42.84  E-value: 3.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  231 KSYIITGGLGGFGLELARWLVLRGAqRLVLTSRSgiRTGyqAKHI-REWRRQGIQVLVSTSNVSSLEGARALIAEATK-L 308
Cdd:PRK05653   6 KTALVTGASRGIGRAIALRLAADGA-KVVIYDSN--EEA--AEALaAELRAAGGEARVLVFDVSDEAAVRALIEAAVEaF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  309 GPVGGVFNLAMVLRDAMLENQTPELFQ---DVNkpkYNGTLNLdraTREACP---ELDY--FVAFSSVSCGRGNAGQTNY 380
Cdd:PRK05653  81 GALDILVNNAGITRDALLPRMSEEDWDrviDVN---LTGTFNV---VRAALPpmiKARYgrIVNISSVSGVTGNPGQTNY 154


                 .
gi 37604163  381 G 381
Cdd:PRK05653 155 S 155
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
 15-201 4.04e-04

6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the zinc-dependent alcohol dehydrogenase-like family of medium chain dehydrogenases/reductases catalyzes the conversion of 6-hydroxyhexanoate and NAD(+) to 6-oxohexanoate + NADH and H+. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176202 [Multi-domain]  Cd Length: 350  Bit Score: 43.37  E-value: 4.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  15 ETVLIhSGSGGVGQAAISIALSLGCRVFTTVG-SAEKRAYLQARFPqldDTSFaNSRDTSFEQHVLLHTGGkGVDLVLNS 93
Cdd:cd08240 177 EPVVI-IGAGGLGLMALALLKALGPANIIVVDiDEAKLEAAKAAGA---DVVV-NGSDPDAAKRIIKAAGG-GVDAVIDF 250

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  94 L-AEEKLQASVRCLAQHGRFLEIGKFDLSNNHPLGMaIFLKNVTFHGILLDALFEeandsWREVAALLKAGirdgVVKPL 172
Cdd:cd08240 251 VnNSATASLAFDILAKGGKLVLVGLFGGEATLPLPL-LPLRALTIQGSYVGSLEE-----LRELVALAKAG----KLKPI 320

                       170       180
                ....*....|....*....|....*....
gi 37604163 173 KCTVFPKAQVEDAFRYMAQGKHIGKVLVQ 201
Cdd:cd08240 321 PLTERPLSDVNDALDDLKAGKVVGRAVLK 349
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
 1-201 5.88e-04

Arginate lyase and other MDR family members; This group contains a structure identified as an arginate lyase. Other members are identified quinone reductases, alginate lyases, and other proteins related to the zinc-dependent dehydrogenases/reductases. QOR catalyzes the conversion of a quinone and NAD(P)H to a hydroquinone and NAD(P+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176214 [Multi-domain]  Cd Length: 336  Bit Score: 42.90  E-value: 5.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSLVVRGRIQR-----GETVLIHSGSGGVGQAAISIA-LSLGCRVFTTVGSAEKRAYLQarfpQLDDTSFANSRDTSF 74
Cdd:cd08252 132 AWEALFDRLGISEdaeneGKTLLIIGGAGGVGSIAIQLAkQLTGLTVIATASRPESIAWVK----ELGADHVINHHQDLA 207

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  75 EQhvLLHTGGKGVDLVLNSLA-EEKLQASVRCLAQHGRFLEIgkfdLSNNHPL-GMAIFLKNVTFHGILL--DALF---- 146
Cdd:cd08252 208 EQ--LEALGIEPVDYIFCLTDtDQHWDAMAELIAPQGHICLI----VDPQEPLdLGPLKSKSASFHWEFMftRSMFqtpd 281

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37604163 147 -EEANDSWREVAALLKAGIrdgvvkpLKCTVFPK------AQVEDAFRYMAQGKHIGKVLVQ 201
Cdd:cd08252 282 mIEQHEILNEVADLLDAGK-------LKTTLTETlgpinaENLREAHALLESGKTIGKIVLE 336
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
234-387 7.04e-04

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 42.06  E-value: 7.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  234 IITGGLGGFGLELARWLVLRGaQRLVLTSRSgirtGYQAKHirEW----RRQGIQVLVSTSNVSSLEGARALIAE-ATKL 308
Cdd:PRK12824   6 LVTGAKRGIGSAIARELLNDG-YRVIATYFS----GNDCAK--DWfeeyGFTEDQVRLKELDVTDTEECAEALAEiEEEE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  309 GPVGGVFNLAMVLRDAMLENQTPELFQDVNKPKYNGTLNLDRATREACPELDY--FVAFSSVSCGRGNAGQTNYGFANST 386
Cdd:PRK12824  79 GPVDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYgrIINISSVNGLKGQFGQTNYSAAKAG 158


                 .
gi 37604163  387 M 387
Cdd:PRK12824 159 M 159
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
 8-200 8.93e-04

L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as a threonine dehydrogenase. L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)-dependent oxidation. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Zinc-dependent ADHs are medium chain dehydrogenase/reductase type proteins (MDRs) and have a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. In addition to alcohol dehydrogenases, this group includes quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176201 [Multi-domain]  Cd Length: 339  Bit Score: 42.31  E-value: 8.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   8 RGRIQRGETVLIHsGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQARFpQLDDTsfANSRDTSFEQHVLLhTGGKGV 87
Cdd:cd08239 158 RVGVSGRDTVLVV-GAGPVGLGALMLARALGAEDVIGVDPSPERLELAKAL-GADFV--INSGQDDVQEIREL-TSGAGA 232

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  88 DLVLN-SLAEEKLQASVRCLAQHGRFLEIGK-----FDLSNnhplgmAIFLKNVTFHGilldalfeeandSW-------R 154
Cdd:cd08239 233 DVAIEcSGNTAARRLALEAVRPWGRLVLVGEggeltIEVSN------DLIRKQRTLIG------------SWyfsvpdmE 294

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 37604163 155 EVAALL-KAGIRdgvVKPLKCTVFPKAQVEDAFRYMAQGKhIGKVLV 200
Cdd:cd08239 295 ECAEFLaRHKLE---VDRLVTHRFGLDQAPEAYALFAQGE-SGKVVF 337
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
 1-199 9.95e-04

Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; Glutathione-dependent formaldehyde dehydrogenases (FDHs) are members of the zinc-dependent/medium chain alcohol dehydrogenase family. Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD to formate and NADH. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. These tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176244 [Multi-domain]  Cd Length: 344  Bit Score: 42.24  E-value: 9.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   1 AYYSlVVRGRIQRGETVLIhSGSGGVGQAAISIALSLGCRVFTTVGSAEKR---AYLQARFPqlddtsfANSRDTSFEQH 77
Cdd:cd08284 156 GYFG-AKRAQVRPGDTVAV-IGCGPVGLCAVLSAQVLGAARVFAVDPVPERlerAAALGAEP-------INFEDAEPVER 226

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  78 VLLHTGGKGVDLVLNSL-AEEKLQASVRCLAQHGRFLEIGkfdLSNNHPL---GMAIFLKNVTFHGILLDALFEeandsW 153
Cdd:cd08284 227 VREATEGRGADVVLEAVgGAAALDLAFDLVRPGGVISSVG---VHTAEEFpfpGLDAYNKNLTLRFGRCPVRSL-----F 298

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 37604163 154 REVAALLKAGiRDGVVKPLKCTVfPKAQVEDAFRYMAQGKhIGKVL 199
Cdd:cd08284 299 PELLPLLESG-RLDLEFLIDHRM-PLEEAPEAYRLFDKRK-VLKVV 341
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
 6-201 1.13e-03

(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent medium chain alcohol dehydrogenase, catalyzes the NAD(+)-dependent oxidation of (2R,3R)-2,3-butanediol and meso-butanediol to acetoin. BDH functions as a homodimer. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit.


Pssm-ID: 176195 [Multi-domain]  Cd Length: 351  Bit Score: 42.14  E-value: 1.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   6 VVRGRIQRGETVLIhSGSGGVGQAAISIALSLGC-RVFTTVGSAEKRAYLQARFpqlDDTSFaNSRDTSFEQHVLLHTGG 84
Cdd:cd08233 165 VRRSGFKPGDTALV-LGAGPIGLLTILALKAAGAsKIIVSEPSEARRELAEELG---ATIVL-DPTEVDVVAEVRKLTGG 239

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  85 KGVDLVLN-SLAEEKLQASVRCLAQHGRFLEIGKFDlsnnHPLgmAIFLKNVTFHGILLDALFEEANDSWREVAALLKAG 163
Cdd:cd08233 240 GGVDVSFDcAGVQATLDTAIDALRPRGTAVNVAIWE----KPI--SFNPNDLVLKEKTLTGSICYTREDFEEVIDLLASG 313

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 37604163 164 IRDgvVKPLKCTVFP-KAQVEDAFRYMAQGK--HIgKVLVQ 201
Cdd:cd08233 314 KID--AEPLITSRIPlEDIVEKGFEELINDKeqHV-KILVS 351
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
 8-200 1.45e-03

D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related alcohol dehydrogenases. AraDH is a member of the medium chain dehydrogenase/reductase family and catalyzes the NAD(P)-dependent oxidation of D-arabinose and other pentoses, the initial step in the metabolism of d-arabinose into 2-oxoglutarate. Like the alcohol dehydrogenases, AraDH binds a zinc in the catalytic cleft as well as a distal structural zinc. AraDH forms homotetramers as a dimer of dimers. AraDH replaces a conserved catalytic His with replace with Arg, compared to the canonical ADH site. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176187 [Multi-domain]  Cd Length: 340  Bit Score: 41.78  E-value: 1.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   8 RGRIQRGETVLIhSGSGGVGQAAISIALSL-GCRVFTTVGSAEKRAY---LQArfpqldDTSFANSRDTsfEQHVLLHTG 83
Cdd:cd05284 162 LPYLDPGSTVVV-IGVGGLGHIAVQILRALtPATVIAVDRSEEALKLaerLGA------DHVLNASDDV--VEEVRELTG 232

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  84 GKGVDLVLNSL-AEEKLQASVRCLAQHGRFLEIGKFDlSNNHPLGMAIFlKNVTFHGILLdalfeeanDSWREVAALLKA 162
Cdd:cd05284 233 GRGADAVIDFVgSDETLALAAKLLAKGGRYVIVGYGG-HGRLPTSDLVP-TEISVIGSLW--------GTRAELVEVVAL 302

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 37604163 163 gIRDGVVKPlKCTVFPKAQVEDAFRYMAQGKHIGK-VLV 200
Cdd:cd05284 303 -AESGKVKV-EITKFPLEDANEALDRLREGRVTGRaVLV 339
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 9-92 3.69e-03

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 38.64  E-value: 3.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163      9 GRIQRGETVLIhsGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQARFPQLDDTSFANSrdTSFEQHVllhtggKGVD 88
Cdd:smart01002  16 GGVPPAKVVVI--GAGVVGLGAAATAKGLGAEVTVLDVRPARLRQLESLLGARFTTLYSQA--ELLEEAV------KEAD 85


                   ....
gi 37604163     89 LVLN 92
Cdd:smart01002  86 LVIG 89
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 234-381 4.40e-03

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 39.13  E-value: 4.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   234 IITGGLGGFGLELARWLVLRGAqRLVLTSRSGIRTGYQAKHIREwrrQGIQVLVSTSNVSSLEGARALIAEATK-LGPVG 312
Cdd:pfam00106   4 LVTGASSGIGRAIAKRLAKEGA-KVVLVDRSEEKLEAVAKELGA---LGGKALFIQGDVTDRAQVKALVEQAVErLGRLD 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37604163   313 GVFNLAMVLRDAMLENQTPELFQDVNKPKYNGTLNLdraTREACPELDY-----FVAFSSVSCGRGNAGQTNYG 381
Cdd:pfam00106  80 ILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNL---TRAVLPAMIKgsggrIVNISSVAGLVPYPGGSAYS 150
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
 8-190 6.90e-03

NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol dehydrogenases; they exist as tetramers and exhibit specificity for NADP(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like other zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), tetrameric ADHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains; however, they do not have and a structural zinc in a lobe of the catalytic domain. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176245 [Multi-domain]  Cd Length: 351  Bit Score: 39.53  E-value: 6.90e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   8 RGRIQRGETVLIHsGSGGVGQAAISIALSLGC-RVFTtVGSAEKRAYLqARFPQLDDTsfANSRDTSFEQHVLLHTGGKG 86
Cdd:cd08285 161 LANIKLGDTVAVF-GIGPVGLMAVAGARLRGAgRIIA-VGSRPNRVEL-AKEYGATDI--VDYKNGDVVEQILKLTGGKG 235

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  87 VDLVLNSL-AEEKLQASVRCLAQHGRFLEIGKF--DLSNNHPL-----GMAiflknvtfHGILLDALFEEANDSWREVAA 158
Cdd:cd08285 236 VDAVIIAGgGQDTFEQALKVLKPGGTISNVNYYgeDDYLPIPReewgvGMG--------HKTINGGLCPGGRLRMERLAS 307

                       170       180       190
                ....*....|....*....|....*....|..
gi 37604163 159 LLKAGiRDGVVKPLKCTVFPKAQVEDAFRYMA 190
Cdd:cd08285 308 LIEYG-RVDPSKLLTHHFFGFDDIEEALMLMK 338
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 8-203 8.92e-03

Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176230 [Multi-domain]  Cd Length: 312  Bit Score: 39.26  E-value: 8.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163   8 RGRIQRGETVLIhSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQARFpQLDDTSFANSRDTSFEQHVLlhTGGKGV 87
Cdd:cd08269 124 RGWIRAGKTVAV-IGAGFIGLLFLQLAAAAGARRVIAIDRRPARLALAREL-GATEVVTDDSEAIVERVREL--TGGAGA 199

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37604163  88 DLVLNSLAEEKLQA-SVRCLAQHGRfLEIGKFDLSNNHPLGMAI-FLKNVTF-------HGILLDALfeeandswREVAA 158
Cdd:cd08269 200 DVVIEAVGHQWPLDlAGELVAERGR-LVIFGYHQDGPRPVPFQTwNWKGIDLinaverdPRIGLEGM--------REAVK 270

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 37604163 159 LLKAGIRDgvVKPLKCTVFPKAQVEDAFRYMAQGKHiGKVLVQVR 203
Cdd:cd08269 271 LIADGRLD--LGSLLTHEFPLEELGDAFEAARRRPD-GFIKGVIV 312
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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