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Conserved domains on  [gi|13938279|gb|AAH07267|]
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Unknown (protein for IMAGE:3138929), partial [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 18-273 8.38e-126

Enoylreductase; Enoylreductase in Polyketide synthases.


:

Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 381.74  E-value: 8.38e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279     18 LGMEFSGRD----------ASGKRVMGLVPAkGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPG 87
Cdd:smart00829  26 LGGECAGVVtrvgpgvtglAVGDRVMGLAPG-AFATRVVTDARLVVPIPDGWSFEEAATVPVVFLTAYYALVDLARLRPG 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279     88 ETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLqaRFPQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSL 167
Cdd:smart00829 105 ESVLIHAAAGGVGQAAIQLARHLGAEVFATAGSPEKRDFL--RALGIPDDHIFSSRDLSFADEILRATGGRGVDVVLNSL 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279    168 AEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLKNVTFHGVLLDAFFnESSADWREVWALVQAGIRDGVVRPLKC 247
Cdd:smart00829 183 SGEFLDASLRCLAPGGRFVEIGKRDIRDNSQLAMAPFRPNVSYHAVDLDALE-EGPDRIRELLAEVLELFAEGVLRPLPV 261

                          250       260
                   ....*....|....*....|....*.
gi 13938279    248 TVFHGAQVEDAFRYMAQGKHIGKVVV 273
Cdd:smart00829 262 TVFPISDAEDAFRYMQQGKHIGKVVL 287
KR_1_FAS_SDR_x cd08954
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ...
 295-531 8.37e-104

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: 330.18  E-value: 8.37e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 295 ISKTFCPA--HKSYIIAGGLGGFGLELAQWLIQRGVQK-LVLTSRSGIRTGyQAKQVRRWRRQ---GVQVQVSTSNISSL 368
Cdd:cd08954 208 ILKTNYPInlGKSYLITGGSGGLGLEILKWLVKRGAVEnIIILSRSGMKWE-LELLIREWKSQnikFHFVSVDVSDVSSL 286

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 369 EGARGLIAEAAQLGPVGGVFNLAVVLRDGLLENQTPEFFQDVCKPKYSGTLNLDRVTREACPELDYFVVFSSVSCGRGNA 448
Cdd:cd08954 287 EKAINLILNAPKIGPIGGIFHLAFVLIDKVLEIDTESLFISVNKAKVMGAINLHNQSIKRCWKLDYFVLFSSVSSIRGSA 366

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 449 GQSNYGFANSAMERICEKRRHEGLPGLAVQWGAIGDVGIlVETMSTNDTIVS--GTLPQRMASCLEVLDLFLN--QPHMV 524
Cdd:cd08954 367 GQCNYVCANSVLDSLSRYRKSIGLPSIAINWGAIGDVGF-VSRNESVDTLLGgqGLLPQSINSCLGTLDLFLQnpSPNLV 445


                ....*..
gi 13938279 525 LSSFVLA 531
Cdd:cd08954 446 LSSFNFA 452
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 661-907 2.27e-48

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: 171.42  E-value: 2.27e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   661 RPLFLVHPIEGSTTVFHSLASRLSIPTygLQCTRAAP--------LDSIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACV 732
Cdd:pfam00975   1 RPLFCFPPAGGSASSFRSLARRLPPPA--EVLAVQYPgrgrgeppLNSIEALADEYAEALRQIQPEGPYALFGHSMGGML 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   733 AFEMCSQLQAQqspAPTHNSLFLFDGSPTYVLAYTQSYRAKLTPgceaeaeteaicfFVQQFTDMEHNrvLEALLP---- 808
Cdd:pfam00975  79 AFEVARRLERQ---GEAVRSLFLSDASAPHTVRYEASRAPDDDE-------------VVAEFTDEGGT--PEELLEdeel 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   809 LKGLEERVAAAVDLIIK-SHQGLDRQelsfaarsfyyklRAAEQYTPKAKYHGNVMLlraktggaygedlgaDYNLSQVC 887
Cdd:pfam00975 141 LSMLLPALRADYRALESySCPPLDAQ-------------SATLFYGSDDPLHDADDL---------------AEWVRDHT 192

                         250       260
                  ....*....|....*....|
gi 13938279   888 DGKVSVHVIEGDHRTLLEGS 907
Cdd:pfam00975 193 PGEFDVHVFDGDHFYLIEHL 212
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 530-598 1.60e-14

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: 69.59  E-value: 1.60e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13938279    530 LAEKAAAYRDRDSQRDLVEAVAHILGIRDLAAVNLDSSLADLGLDSLMSVEVRQTLERELNLVLSVREV 598
Cdd:smart00823   1 LAALPPAERRRLLLDLVREQVAAVLGHAAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLV 69
 
Name Accession Description Interval E-value
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 18-273 8.38e-126

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 381.74  E-value: 8.38e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279     18 LGMEFSGRD----------ASGKRVMGLVPAkGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPG 87
Cdd:smart00829  26 LGGECAGVVtrvgpgvtglAVGDRVMGLAPG-AFATRVVTDARLVVPIPDGWSFEEAATVPVVFLTAYYALVDLARLRPG 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279     88 ETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLqaRFPQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSL 167
Cdd:smart00829 105 ESVLIHAAAGGVGQAAIQLARHLGAEVFATAGSPEKRDFL--RALGIPDDHIFSSRDLSFADEILRATGGRGVDVVLNSL 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279    168 AEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLKNVTFHGVLLDAFFnESSADWREVWALVQAGIRDGVVRPLKC 247
Cdd:smart00829 183 SGEFLDASLRCLAPGGRFVEIGKRDIRDNSQLAMAPFRPNVSYHAVDLDALE-EGPDRIRELLAEVLELFAEGVLRPLPV 261

                          250       260
                   ....*....|....*....|....*.
gi 13938279    248 TVFHGAQVEDAFRYMAQGKHIGKVVV 273
Cdd:smart00829 262 TVFPISDAEDAFRYMQQGKHIGKVVL 287
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
 9-273 4.18e-108

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: 335.69  E-value: 4.18e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   9 GKWTSQDSLLGMEFSGRD----------ASGKRVMGLVPaKGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYAL 78
Cdd:cd05195  22 GLLPGDETPLGLECSGIVtrvgsgvtglKVGDRVMGLAP-GAFATHVRVDARLVVKIPDSLSFEEAATLPVAYLTAYYAL 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  79 VVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQARFPqlDSTSFANSRDTSFEQHVLWHTGGK 158
Cdd:cd05195 101 VDLARLQKGESVLIHAAAGGVGQAAIQLAQHLGAEVFATVGSEEKREFLRELGG--PVDHIFSSRDLSFADGILRATGGR 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 159 GVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLKNVTFHGVLLDAFFNESSADWREVWALVQAGIR 238
Cdd:cd05195 179 GVDVVLNSLSGELLRASWRCLAPFGRFVEIGKRDILSNSKLGMRPFLRNVSFSSVDLDQLARERPELLRELLREVLELLE 258

                       250       260       270
                ....*....|....*....|....*....|....*
gi 13938279 239 DGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVV 273
Cdd:cd05195 259 AGVLKPLPPTVVPSASEIDAFRLMQSGKHIGKVVL 293
KR_1_FAS_SDR_x cd08954
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ...
 295-531 8.37e-104

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: 330.18  E-value: 8.37e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 295 ISKTFCPA--HKSYIIAGGLGGFGLELAQWLIQRGVQK-LVLTSRSGIRTGyQAKQVRRWRRQ---GVQVQVSTSNISSL 368
Cdd:cd08954 208 ILKTNYPInlGKSYLITGGSGGLGLEILKWLVKRGAVEnIIILSRSGMKWE-LELLIREWKSQnikFHFVSVDVSDVSSL 286

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 369 EGARGLIAEAAQLGPVGGVFNLAVVLRDGLLENQTPEFFQDVCKPKYSGTLNLDRVTREACPELDYFVVFSSVSCGRGNA 448
Cdd:cd08954 287 EKAINLILNAPKIGPIGGIFHLAFVLIDKVLEIDTESLFISVNKAKVMGAINLHNQSIKRCWKLDYFVLFSSVSSIRGSA 366

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 449 GQSNYGFANSAMERICEKRRHEGLPGLAVQWGAIGDVGIlVETMSTNDTIVS--GTLPQRMASCLEVLDLFLN--QPHMV 524
Cdd:cd08954 367 GQCNYVCANSVLDSLSRYRKSIGLPSIAINWGAIGDVGF-VSRNESVDTLLGgqGLLPQSINSCLGTLDLFLQnpSPNLV 445


                ....*..
gi 13938279 525 LSSFVLA 531
Cdd:cd08954 446 LSSFNFA 452
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 18-275 2.07e-63

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: 216.94  E-value: 2.07e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  18 LGMEFSG----------RDASGKRVMGLVPAKGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPG 87
Cdd:COG0604  61 PGSDAAGvvvavgegvtGFKVGDRVAGLGRGGGYAEYVVVPADQLVPLPDGLSFEEAAALPLAGLTAWQALFDRGRLKPG 140

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  88 ETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQArfpqLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSL 167
Cdd:COG0604 141 ETVLVHGAAGGVGSAAVQLAKALGARVIATASSPEKAELLRA----LGADHVIDYREEDFAERVRALTGGRGVDVVLDTV 216

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 168 AEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLKNVTFHGVLLDAFFNESS-ADWREVWALVQAgirdGVVRPLK 246
Cdd:COG0604 217 GGDTLARSLRALAPGGRLVSIGAASGAPPPLDLAPLLLKGLTLTGFTLFARDPAERrAALAELARLLAA----GKLRPVI 292

                       250       260
                ....*....|....*....|....*....
gi 13938279 247 CTVFHGAQVEDAFRYMAQGKHIGKVVVQV 275
Cdd:COG0604 293 DRVFPLEEAAEAHRLLESGKHRGKVVLTV 321
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 316-484 1.83e-52

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: 181.14  E-value: 1.83e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279    316 GLELAQWLIQRGVQKLVLTSRSGIRTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEA-AQLGPVGGVFNLAVVL 394
Cdd:smart00822  13 GRALARWLAERGARRLVLLSRSGPDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIpAVEGPLTGVIHAAGVL 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279    395 RDGLLENQTPEFFQDVCKPKYSGTLNLDRVTReaCPELDYFVVFSSVSCGRGNAGQSNYGFANSAMERICEKRRHEGLPG 474
Cdd:smart00822  93 DDGVLASLTPERFAAVLAPKAAGAWNLHELTA--DLPLDFFVLFSSIAGVLGSPGQANYAAANAFLDALAEYRRARGLPA 170

                          170
                   ....*....|
gi 13938279    475 LAVQWGAIGD 484
Cdd:smart00822 171 LSIAWGAWAE 180
quinone_pig3 TIGR02824
putative NAD(P)H quinone oxidoreductase, PIG3 family; Members of this family are putative ...
 17-275 1.85e-48

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: 175.14  E-value: 1.85e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279    17 LLGMEFSG----------RDASGKRVMGLVPAKGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRP 86
Cdd:TIGR02824  60 ILGLEVAGevvavgegvsRWKVGDRVCALVAGGGYAEYVAVPAGQVLPVPEGLSLVEAAALPETFFTVWSNLFQRGGLKA 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279    87 GETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQArfpqLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNS 166
Cdd:TIGR02824 140 GETVLIHGGASGIGTTAIQLAKAFGARVFTTAGSDEKCAACEA----LGADIAINYREEDFVEVVKAETGGKGVDVILDI 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   167 LAEEKLQASVRCLATHGRFLEIG-------KFDLsqnhplgMAIFLKNVTFHGVLL----DAFFNESSADWRE-VWALvq 234
Cdd:TIGR02824 216 VGGSYLNRNIKALALDGRIVQIGfqggrkaELDL-------GPLLAKRLTITGSTLrarpVAEKAAIAAELREhVWPL-- 286

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 13938279   235 agIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQV 275
Cdd:TIGR02824 287 --LASGRVRPVIDKVFPLEDAAQAHALMESGDHIGKIVLTV 325
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 661-907 2.27e-48

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: 171.42  E-value: 2.27e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   661 RPLFLVHPIEGSTTVFHSLASRLSIPTygLQCTRAAP--------LDSIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACV 732
Cdd:pfam00975   1 RPLFCFPPAGGSASSFRSLARRLPPPA--EVLAVQYPgrgrgeppLNSIEALADEYAEALRQIQPEGPYALFGHSMGGML 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   733 AFEMCSQLQAQqspAPTHNSLFLFDGSPTYVLAYTQSYRAKLTPgceaeaeteaicfFVQQFTDMEHNrvLEALLP---- 808
Cdd:pfam00975  79 AFEVARRLERQ---GEAVRSLFLSDASAPHTVRYEASRAPDDDE-------------VVAEFTDEGGT--PEELLEdeel 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   809 LKGLEERVAAAVDLIIK-SHQGLDRQelsfaarsfyyklRAAEQYTPKAKYHGNVMLlraktggaygedlgaDYNLSQVC 887
Cdd:pfam00975 141 LSMLLPALRADYRALESySCPPLDAQ-------------SATLFYGSDDPLHDADDL---------------AEWVRDHT 192

                         250       260
                  ....*....|....*....|
gi 13938279   888 DGKVSVHVIEGDHRTLLEGS 907
Cdd:pfam00975 193 PGEFDVHVFDGDHFYLIEHL 212
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 305-484 4.24e-41

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: 148.86  E-value: 4.24e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   305 SYIIAGGLGGFGLELAQWLIQRGVQKLVLTSRSGIRTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEA-AQLGP 383
Cdd:pfam08659   2 TYLITGGLGGLGRELARWLAERGARHLVLLSRSAAPRPDAQALIAELEARGVEVVVVACDVSDPDAVAALLAEIkAEGPP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   384 VGGVFNLAVVLRDGLLENQTPEFFQDVCKPKYSGTLNLDRVTREAcpELDYFVVFSSVSCGRGNAGQSNYGFANSAMERI 463
Cdd:pfam08659  82 IRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHEATPDE--PLDFFVLFSSIAGLLGSPGQANYAAANAFLDAL 159

                         170       180
                  ....*....|....*....|.
gi 13938279   464 CEKRRHEGLPGLAVQWGAIGD 484
Cdd:pfam08659 160 AEYRRSQGLPATSINWGPWAE 180
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
 461-910 5.89e-33

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: 137.53  E-value: 5.89e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 461 ERICEKRRHEGLPGLAVQWGAIGDVGILVETMSTNDTIVSGTLPQRMASCLEVLDLFLNQPHMVLSSFVLAEKAAAYRDR 540
Cdd:COG3319 410 LREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLLLLLLLLLLA 489

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 541 DSQRDLVEAVAHILGIRDLAAVNLDSSLADLGLDSLMSVEVRQTLERELNLVLSVREVRQLTLRKLQELSSKADEASELA 620
Cdd:COG3319 490 ALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRLLLLLALLL 569

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 621 CPTPKEDGLAQQQTQLNLRSLLVNPEGPTlmrlnsvqSSERPLFLVHPIEGSTTVFHSLASRLS--IPTYGLQC----TR 694
Cdd:COG3319 570 APTLAALAAALAAAAAAAALSPLVPLRAG--------GSGPPLFCVHPAGGNVLCYRPLARALGpdRPVYGLQApgldGG 641

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 695 AAPLDSIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACVAFEMCSQLQAQ-QSPApthnSLFLFDgspTYVLAYTqsyrak 773
Cdd:COG3319 642 EPPPASVEEMAARYVEAIRAVQPEGPYHLLGWSFGGLVAYEMARQLEAQgEEVA----LLVLLD---SYAPGAL------ 708

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 774 ltpgcEAEAETEAICFFVQQFTDMEHNRVLEALLPLKGLEERVAAAVDLIIKSH--QGLDRQELSFAARSFYYKLRAAEQ 851
Cdd:COG3319 709 -----ARLDEAELLAALLRDLARGVDLPLDAEELRALDPEERLARLLERLREAGlpAGLDAERLRRLLRVFRANLRALRR 783

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13938279 852 YTPKAkYHGNVMLLRAkTGGAYGEDLGADYNLSQVCDGKVSVHVIEGDHRTLLEGSGLE 910
Cdd:COG3319 784 YRPRP-YDGPVLLFRA-EEDPPGRADDPALGWRPLVAGGLEVHDVPGDHFSMLREPHVA 840
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
 16-275 1.90e-28

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 117.44  E-value: 1.90e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   16 SLLGMEFSG----------RDASGKRVMGLVPAKGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVR 85
Cdd:PTZ00354  60 EILGLEVAGyvedvgsdvkRFKEGDRVMALLPGGGYAEYAVAHKGHVMHIPQGYTFEEAAAIPEAFLTAWQLLKKHGDVK 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   86 PGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQarfpQLDSTSFANSRD-TSFEQHVLWHTGGKGVDLVL 164
Cdd:PTZ00354 140 KGQSVLIHAGASGVGTAAAQLAEKYGAATIITTSSEEKVDFCK----KLAAIILIRYPDeEGFAPKVKKLTGEKGVNLVL 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  165 NSLAEEKLQASVRCLATHGRFLEIG--------KFDLsqnhplgMAIFLKNVTFHGVLL----DAFFNESSADW-REVWA 231
Cdd:PTZ00354 216 DCVGGSYLSETAEVLAVDGKWIVYGfmggakveKFNL-------LPLLRKRASIIFSTLrsrsDEYKADLVASFeREVLP 288

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 13938279  232 LvqagIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQV 275
Cdd:PTZ00354 289 Y----MEEGEIKPIVDRTYPLEEVAEAHTFLEQNKNIGKVVLTV 328
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
98-235 7.47e-21

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 89.20  E-value: 7.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279    98 GVGQAAIAIALSLGCRVFTTVGSAEKRAYLQarfpQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSL-AEEKLQASV 176
Cdd:pfam00107   1 GVGLAAIQLAKAAGAKVIAVDGSEEKLELAK----ELGADHVINPKETDLVEEIKELTGGKGVDVVFDCVgSPATLEQAL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   177 RCLATHGRFLEIGKFdlSQNHPLGMA-IFLKNVTFHGVLLDaffneSSADWREVWALVQA 235
Cdd:pfam00107  77 KLLRPGGRVVVVGLP--GGPLPLPLApLLLKELTILGSFLG-----SPEEFPEALDLLAS 129
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 530-598 1.60e-14

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: 69.59  E-value: 1.60e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13938279    530 LAEKAAAYRDRDSQRDLVEAVAHILGIRDLAAVNLDSSLADLGLDSLMSVEVRQTLERELNLVLSVREV 598
Cdd:smart00823   1 LAALPPAERRRLLLDLVREQVAAVLGHAAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLV 69
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
545-828 4.81e-13

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 73.54  E-value: 4.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   545 DLVEAVAHILGirdLAAVNLDSSLADLGLDSLMSVEVRQTLERELNlvlsvrevRQLTLRKLQELSSKADEASELAcptp 624
Cdd:PRK10252  982 IIAAAFSSLLG---CDVVDADADFFALGGHSLLAMKLAAQLSRQFA--------RQVTPGQVMVASTVAKLATLLD---- 1046

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   625 kEDGLAQQQTQLNLRSLLVNPEGPTLmrlnsvqsserplFLVHPIEGSTTVFHSLASRLS--IPTYGLQCTR---AAPL- 698
Cdd:PRK10252 1047 -AEEDESRRLGFGTILPLREGDGPTL-------------FCFHPASGFAWQFSVLSRYLDpqWSIYGIQSPRpdgPMQTa 1112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   699 DSIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACVAFEMCSQLQAQqspAPTHNSLFLFDGSPtyvlAYTQSYRAKLTPGC 778
Cdd:PRK10252 1113 TSLDEVCEAHLATLLEQQPHGPYHLLGYSLGGTLAQGIAARLRAR---GEEVAFLGLLDTWP----PETQNWREKEANGL 1185

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 13938279   779 EAEAETEAicffvqqftDMEHNRVLEAL---LP---LKGLEERVAAAVDLIIKSHQ 828
Cdd:PRK10252 1186 DPEVLAEI---------DREREAFLAAQqgsLStelFTTIEGNYADAVRLLTTAHS 1232
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 544-598 1.28e-09

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: 54.88  E-value: 1.28e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 13938279   544 RDLVEAVAHILGIrDLAAVNLDSSLADLGLDSLMSVEVRQTLERELNLVLSVREV 598
Cdd:pfam00550   1 ERLRELLAEVLGV-PAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDL 54
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
319-482 1.24e-08

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 56.80  E-value: 1.24e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 319 LAQWLIQRGVQkLVLTSRSGIRTgyqAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEA-AQLGPVGGVFNLAVVLRDG 397
Cdd:COG0300  21 LARALAARGAR-VVLVARDAERL---EALAAELRAAGARVEVVALDVTDPDAVAALAEAVlARFGPIDVLVNNAGVGGGG 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 398 LLENQTPEFFQDVCKPKYSGTLNLdrvTREACPEL-----DYFVVFSSVSCGRGNAGQSNYGFANSAMERICEKRRHE-- 470
Cdd:COG0300  97 PFEELDLEDLRRVFEVNVFGPVRL---TRALLPLMrargrGRIVNVSSVAGLRGLPGMAAYAASKAALEGFSESLRAEla 173

                       170
                ....*....|....
gi 13938279 471 --GLPGLAVQWGAI 482
Cdd:COG0300 174 ptGVRVTAVCPGPV 187
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 546-606 4.11e-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: 4.11e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13938279 546 LVEAVAHILGIrDLAAVNLDSSL-ADLGLDSLMSVEVRQTLERELNLVLSVREVRQL-TLRKL 606
Cdd:COG0236  10 LAEIIAEVLGV-DPEEITPDDSFfEDLGLDSLDAVELIAALEEEFGIELPDTELFEYpTVADL 71
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 354-461 3.54e-07

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 52.50  E-value: 3.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  354 QGVQVQVSTSNISSLEGARGLIAEA-AQLGPVGGVFNLAVVLRDGLLENQTPEFFQDVCKPKYSGTLNldrVTREACPEL 432
Cdd:PRK05557  53 LGGKALAVQGDVSDAESVERAVDEAkAEFGGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFN---LTKAVARPM 129

                         90       100       110
                 ....*....|....*....|....*....|....
gi 13938279  433 -----DYFVVFSSVSCGRGNAGQSNYGFANSAME 461
Cdd:PRK05557 130 mkqrsGRIINISSVVGLMGNPGQANYAASKAGVI 163
 
Name Accession Description Interval E-value
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 18-273 8.38e-126

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 381.74  E-value: 8.38e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279     18 LGMEFSGRD----------ASGKRVMGLVPAkGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPG 87
Cdd:smart00829  26 LGGECAGVVtrvgpgvtglAVGDRVMGLAPG-AFATRVVTDARLVVPIPDGWSFEEAATVPVVFLTAYYALVDLARLRPG 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279     88 ETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLqaRFPQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSL 167
Cdd:smart00829 105 ESVLIHAAAGGVGQAAIQLARHLGAEVFATAGSPEKRDFL--RALGIPDDHIFSSRDLSFADEILRATGGRGVDVVLNSL 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279    168 AEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLKNVTFHGVLLDAFFnESSADWREVWALVQAGIRDGVVRPLKC 247
Cdd:smart00829 183 SGEFLDASLRCLAPGGRFVEIGKRDIRDNSQLAMAPFRPNVSYHAVDLDALE-EGPDRIRELLAEVLELFAEGVLRPLPV 261

                          250       260
                   ....*....|....*....|....*.
gi 13938279    248 TVFHGAQVEDAFRYMAQGKHIGKVVV 273
Cdd:smart00829 262 TVFPISDAEDAFRYMQQGKHIGKVVL 287
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
 9-273 4.18e-108

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: 335.69  E-value: 4.18e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   9 GKWTSQDSLLGMEFSGRD----------ASGKRVMGLVPaKGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYAL 78
Cdd:cd05195  22 GLLPGDETPLGLECSGIVtrvgsgvtglKVGDRVMGLAP-GAFATHVRVDARLVVKIPDSLSFEEAATLPVAYLTAYYAL 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  79 VVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQARFPqlDSTSFANSRDTSFEQHVLWHTGGK 158
Cdd:cd05195 101 VDLARLQKGESVLIHAAAGGVGQAAIQLAQHLGAEVFATVGSEEKREFLRELGG--PVDHIFSSRDLSFADGILRATGGR 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 159 GVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLKNVTFHGVLLDAFFNESSADWREVWALVQAGIR 238
Cdd:cd05195 179 GVDVVLNSLSGELLRASWRCLAPFGRFVEIGKRDILSNSKLGMRPFLRNVSFSSVDLDQLARERPELLRELLREVLELLE 258

                       250       260       270
                ....*....|....*....|....*....|....*
gi 13938279 239 DGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVV 273
Cdd:cd05195 259 AGVLKPLPPTVVPSASEIDAFRLMQSGKHIGKVVL 293
KR_1_FAS_SDR_x cd08954
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ...
 295-531 8.37e-104

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: 330.18  E-value: 8.37e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 295 ISKTFCPA--HKSYIIAGGLGGFGLELAQWLIQRGVQK-LVLTSRSGIRTGyQAKQVRRWRRQ---GVQVQVSTSNISSL 368
Cdd:cd08954 208 ILKTNYPInlGKSYLITGGSGGLGLEILKWLVKRGAVEnIIILSRSGMKWE-LELLIREWKSQnikFHFVSVDVSDVSSL 286

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 369 EGARGLIAEAAQLGPVGGVFNLAVVLRDGLLENQTPEFFQDVCKPKYSGTLNLDRVTREACPELDYFVVFSSVSCGRGNA 448
Cdd:cd08954 287 EKAINLILNAPKIGPIGGIFHLAFVLIDKVLEIDTESLFISVNKAKVMGAINLHNQSIKRCWKLDYFVLFSSVSSIRGSA 366

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 449 GQSNYGFANSAMERICEKRRHEGLPGLAVQWGAIGDVGIlVETMSTNDTIVS--GTLPQRMASCLEVLDLFLN--QPHMV 524
Cdd:cd08954 367 GQCNYVCANSVLDSLSRYRKSIGLPSIAINWGAIGDVGF-VSRNESVDTLLGgqGLLPQSINSCLGTLDLFLQnpSPNLV 445


                ....*..
gi 13938279 525 LSSFVLA 531
Cdd:cd08954 446 LSSFNFA 452
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 18-275 2.07e-63

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: 216.94  E-value: 2.07e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  18 LGMEFSG----------RDASGKRVMGLVPAKGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPG 87
Cdd:COG0604  61 PGSDAAGvvvavgegvtGFKVGDRVAGLGRGGGYAEYVVVPADQLVPLPDGLSFEEAAALPLAGLTAWQALFDRGRLKPG 140

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  88 ETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQArfpqLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSL 167
Cdd:COG0604 141 ETVLVHGAAGGVGSAAVQLAKALGARVIATASSPEKAELLRA----LGADHVIDYREEDFAERVRALTGGRGVDVVLDTV 216

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 168 AEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLKNVTFHGVLLDAFFNESS-ADWREVWALVQAgirdGVVRPLK 246
Cdd:COG0604 217 GGDTLARSLRALAPGGRLVSIGAASGAPPPLDLAPLLLKGLTLTGFTLFARDPAERrAALAELARLLAA----GKLRPVI 292

                       250       260
                ....*....|....*....|....*....
gi 13938279 247 CTVFHGAQVEDAFRYMAQGKHIGKVVVQV 275
Cdd:COG0604 293 DRVFPLEEAAEAHRLLESGKHRGKVVLTV 321
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
 18-274 7.67e-60

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: 206.97  E-value: 7.67e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  18 LGMEFSGRDAS----------GKRVMGLVPAKGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPG 87
Cdd:cd08241  61 PGSEVAGVVEAvgegvtgfkvGDRVVALTGQGGFAEEVVVPAAAVFPLPDGLSFEEAAALPVTYGTAYHALVRRARLQPG 140

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  88 ETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQArfpqLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSL 167
Cdd:cd08241 141 ETVLVLGAAGGVGLAAVQLAKALGARVIAAASSEEKLALARA----LGADHVIDYRDPDLRERVKALTGGRGVDVVYDPV 216

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 168 AEEKLQASVRCLATHGRFLEIGkF------DLSQNHPLgmaifLKNVTFHGVLLDAFFNESSADWREVWALVQAGIRDGV 241
Cdd:cd08241 217 GGDVFEASLRSLAWGGRLLVIG-FasgeipQIPANLLL-----LKNISVVGVYWGAYARREPELLRANLAELFDLLAEGK 290

                       250       260       270
                ....*....|....*....|....*....|...
gi 13938279 242 VRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQ 274
Cdd:cd08241 291 IRPHVSAVFPLEQAAEALRALADRKATGKVVLT 323
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 320-525 5.35e-54

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: 192.60  E-value: 5.35e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 320 AQWLIQRGVQKLVLTSRSGIRTGYQAkQVRRWRRQGVQVQVSTSNISSLEGARGLIAEAAQLGPVGGVFNLAVVLRDGLL 399
Cdd:cd05274 167 ARWLAARGARHLVLLSRRGPAPRAAA-RAALLRAGGARVSVVRCDVTDPAALAALLAELAAGGPLAGVIHAAGVLRDALL 245

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 400 ENQTPEFFQDVCKPKYSGTLNLDRVTREAcpELDYFVVFSSVSCGRGNAGQSNYGFANSAMERICEKRRHEGLPGLAVQW 479
Cdd:cd05274 246 AELTPAAFAAVLAAKVAGALNLHELTPDL--PLDFFVLFSSVAALLGGAGQAAYAAANAFLDALAAQRRRRGLPATSVQW 323

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 13938279 480 GAIGDVGILVETMSTNDTIVSGTLPQRMASCLEVLDLFLNQPHMVL 525
Cdd:cd05274 324 GAWAGGGMAAAAALRARLARSGLGPLAPAEALEALEALLASDAPQA 369
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 316-484 1.83e-52

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: 181.14  E-value: 1.83e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279    316 GLELAQWLIQRGVQKLVLTSRSGIRTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEA-AQLGPVGGVFNLAVVL 394
Cdd:smart00822  13 GRALARWLAERGARRLVLLSRSGPDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIpAVEGPLTGVIHAAGVL 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279    395 RDGLLENQTPEFFQDVCKPKYSGTLNLDRVTReaCPELDYFVVFSSVSCGRGNAGQSNYGFANSAMERICEKRRHEGLPG 474
Cdd:smart00822  93 DDGVLASLTPERFAAVLAPKAAGAWNLHELTA--DLPLDFFVLFSSIAGVLGSPGQANYAAANAFLDALAEYRRARGLPA 170

                          170
                   ....*....|
gi 13938279    475 LAVQWGAIGD 484
Cdd:smart00822 171 LSIAWGAWAE 180
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
 17-273 3.08e-52

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: 185.72  E-value: 3.08e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  17 LLGMEFSGRDAS----------GKRVMGLVPAKGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRP 86
Cdd:cd05276  60 ILGLEVAGVVVAvgpgvtgwkvGDRVCALLAGGGYAEYVVVPAGQLLPVPEGLSLVEAAALPEVFFTAWQNLFQLGGLKA 139

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  87 GETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQarfpQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNS 166
Cdd:cd05276 140 GETVLIHGGASGVGTAAIQLAKALGARVIATAGSEEKLEACR----ALGADVAINYRTEDFAEEVKEATGGRGVDVILDM 215

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 167 LAEEKLQASVRCLATHGRFLEIG-------KFDLsqnhplgMAIFLKNVTFHG------------VLLDAFfnessadWR 227
Cdd:cd05276 216 VGGDYLARNLRALAPDGRLVLIGllggakaELDL-------APLLRKRLTLTGstlrsrsleekaALAAAF-------RE 281

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 13938279 228 EVWALvqagIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVV 273
Cdd:cd05276 282 HVWPL----FASGRIRPVIDKVFPLEEAAEAHRRMESNEHIGKIVL 323
quinone_pig3 TIGR02824
putative NAD(P)H quinone oxidoreductase, PIG3 family; Members of this family are putative ...
 17-275 1.85e-48

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: 175.14  E-value: 1.85e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279    17 LLGMEFSG----------RDASGKRVMGLVPAKGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRP 86
Cdd:TIGR02824  60 ILGLEVAGevvavgegvsRWKVGDRVCALVAGGGYAEYVAVPAGQVLPVPEGLSLVEAAALPETFFTVWSNLFQRGGLKA 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279    87 GETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQArfpqLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNS 166
Cdd:TIGR02824 140 GETVLIHGGASGIGTTAIQLAKAFGARVFTTAGSDEKCAACEA----LGADIAINYREEDFVEVVKAETGGKGVDVILDI 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   167 LAEEKLQASVRCLATHGRFLEIG-------KFDLsqnhplgMAIFLKNVTFHGVLL----DAFFNESSADWRE-VWALvq 234
Cdd:TIGR02824 216 VGGSYLNRNIKALALDGRIVQIGfqggrkaELDL-------GPLLAKRLTITGSTLrarpVAEKAAIAAELREhVWPL-- 286

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 13938279   235 agIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQV 275
Cdd:TIGR02824 287 --LASGRVRPVIDKVFPLEDAAQAHALMESGDHIGKIVLTV 325
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 661-907 2.27e-48

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: 171.42  E-value: 2.27e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   661 RPLFLVHPIEGSTTVFHSLASRLSIPTygLQCTRAAP--------LDSIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACV 732
Cdd:pfam00975   1 RPLFCFPPAGGSASSFRSLARRLPPPA--EVLAVQYPgrgrgeppLNSIEALADEYAEALRQIQPEGPYALFGHSMGGML 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   733 AFEMCSQLQAQqspAPTHNSLFLFDGSPTYVLAYTQSYRAKLTPgceaeaeteaicfFVQQFTDMEHNrvLEALLP---- 808
Cdd:pfam00975  79 AFEVARRLERQ---GEAVRSLFLSDASAPHTVRYEASRAPDDDE-------------VVAEFTDEGGT--PEELLEdeel 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   809 LKGLEERVAAAVDLIIK-SHQGLDRQelsfaarsfyyklRAAEQYTPKAKYHGNVMLlraktggaygedlgaDYNLSQVC 887
Cdd:pfam00975 141 LSMLLPALRADYRALESySCPPLDAQ-------------SATLFYGSDDPLHDADDL---------------AEWVRDHT 192

                         250       260
                  ....*....|....*....|
gi 13938279   888 DGKVSVHVIEGDHRTLLEGS 907
Cdd:pfam00975 193 PGEFDVHVFDGDHFYLIEHL 212
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
 40-273 2.49e-44

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: 162.60  E-value: 2.49e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  40 GLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVvRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVG 119
Cdd:cd08251  75 GHATLVTVPEDQVVRKPASLSFEEACALPVVFLTVIDAFA-RAGLAKGEHILIQTATGGTGLMAVQLARLKGAEIYATAS 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 120 SAEKRAYLQarfpQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPL 199
Cdd:cd08251 154 SDDKLEYLK----QLGVPHVINYVEEDFEEEIMRLTGGRGVDVVINTLSGEAIQKGLNCLAPGGRYVEIAMTALKSAPSV 229

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13938279 200 GMAIFLKNVTFHGVLLDAFFNESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVV 273
Cdd:cd08251 230 DLSVLSNNQSFHSVDLRKLLLLDPEFIADYQAEMVSLVEEGELRPTVSRIFPFDDIGEAYRYLSDRENIGKVVV 303
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 56-275 7.57e-42

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: 156.18  E-value: 7.57e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  56 PSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVgSAEKRAYLQarfpQLD 135
Cdd:cd08272 114 PANLSMREAAALPLVGITAWEGLVDRAAVQAGQTVLIHGGAGGVGHVAVQLAKAAGARVYATA-SSEKAAFAR----SLG 188

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 136 STsFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRF---LEIGKFDLSQNHplgmaifLKNVTFHG 212
Cdd:cd08272 189 AD-PIIYYRETVVEYVAEHTGGRGFDVVFDTVGGETLDASFEAVALYGRVvsiLGGATHDLAPLS-------FRNATYSG 260

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13938279 213 V--LLDAFFNESSADWREVWALVQAGIRDGVVRP-LKCTVFHGAQVEDAFRYMAQGKHIGKVVVQV 275
Cdd:cd08272 261 VftLLPLLTGEGRAHHGEILREAARLVERGQLRPlLDPRTFPLEEAAAAHARLESGSARGKIVIDV 326
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 305-484 4.24e-41

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: 148.86  E-value: 4.24e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   305 SYIIAGGLGGFGLELAQWLIQRGVQKLVLTSRSGIRTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEA-AQLGP 383
Cdd:pfam08659   2 TYLITGGLGGLGRELARWLAERGARHLVLLSRSAAPRPDAQALIAELEARGVEVVVVACDVSDPDAVAALLAEIkAEGPP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   384 VGGVFNLAVVLRDGLLENQTPEFFQDVCKPKYSGTLNLDRVTREAcpELDYFVVFSSVSCGRGNAGQSNYGFANSAMERI 463
Cdd:pfam08659  82 IRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHEATPDE--PLDFFVLFSSIAGLLGSPGQANYAAANAFLDAL 159

                         170       180
                  ....*....|....*....|.
gi 13938279   464 CEKRRHEGLPGLAVQWGAIGD 484
Cdd:pfam08659 160 AEYRRSQGLPATSINWGPWAE 180
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
 23-275 1.14e-38

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: 147.40  E-value: 1.14e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  23 SGRDA--SGKRVMGLVPAKGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVG 100
Cdd:cd08266 101 AGRENlcAQYGILGEHVDGGYAEYVAVPARNLLPIPDNLSFEEAAAAPLTFLTAWHMLVTRARLRPGETVLVHGAGSGVG 180

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 101 QAAIAIALSLGCRVFTTVGSAEKRAYLQArfpqLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLA 180
Cdd:cd08266 181 SAAIQIAKLFGATVIATAGSEDKLERAKE----LGADYVIDYRKEDFVREVRELTGKRGVDVVVEHVGAATWEKSLKSLA 256

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 181 THGRFLEIG-------KFDLsqnhplgMAIFLKNVTFHGVlldafFNESSADWREVWALVQAgirdGVVRPLKCTVFHGA 253
Cdd:cd08266 257 RGGRLVTCGattgyeaPIDL-------RHVFWRQLSILGS-----TMGTKAELDEALRLVFR----GKLKPVIDSVFPLE 320

                       250       260
                ....*....|....*....|..
gi 13938279 254 QVEDAFRYMAQGKHIGKVVVQV 275
Cdd:cd08266 321 EAAEAHRRLESREQFGKIVLTP 342
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
 320-490 1.21e-36

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: 142.42  E-value: 1.21e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 320 AQWLIQRGVQKLVLTSRSGIrTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAE-AAQLGPVGGVFNLAVVLRDGL 398
Cdd:cd08955 166 AEWLVERGARHLVLTGRRAP-SAAARQAIAALEEAGAEVVVLAADVSDRDALAAALAQiRASLPPLRGVIHAAGVLDDGV 244

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 399 LENQTPEFFQDVCKPKYSGTLNLDRVTREAcpELDYFVVFSSVSCGRGNAGQSNYGFANSAMERICEKRRHEGLPGLAVQ 478
Cdd:cd08955 245 LANQDWERFRKVLAPKVQGAWNLHQLTQDL--PLDFFVLFSSVASLLGSPGQANYAAANAFLDALAHYRRARGLPALSIN 322

                       170
                ....*....|..
gi 13938279 479 WGAIGDVGILVE 490
Cdd:cd08955 323 WGPWAEVGMAAS 334
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
 45-275 7.36e-36

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: 138.87  E-value: 7.36e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  45 VLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKR 124
Cdd:cd08253 103 VVVPADQLVPLPDGVSFEQGAALGIPALTAYRALFHRAGAKAGETVLVHGGSGAVGHAAVQLARWAGARVIATASSAEGA 182

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 125 AYlqARfpQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGmAIF 204
Cdd:cd08253 183 EL--VR--QAGADAVFNYRAEDLADRILAATAGQGVDVIIEVLANVNLAKDLDVLAPGGRIVVYGSGGLRGTIPIN-PLM 257

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13938279 205 LKNVTFHGVLLdafFNESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQV 275
Cdd:cd08253 258 AKEASIRGVLL---YTATPEERAAAAEAIAAGLADGALRPVIAREYPLEEAAAAHEAVESGGAIGKVVLDP 325
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 56-275 1.42e-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: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 138.12  E-value: 1.42e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  56 PSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQArfpqLD 135
Cdd:cd08268 114 PDGLSFVEAAALWMQYLTAYGALVELAGLRPGDSVLITAASSSVGLAAIQIANAAGATVIATTRTSEKRDALLA----LG 189

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 136 STSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNhPLGM-AIFLKNVTFHGVL 214
Cdd:cd08268 190 AAHVIVTDEEDLVAEVLRITGGKGVDVVFDPVGGPQFAKLADALAPGGTLVVYGALSGEPT-PFPLkAALKKSLTFRGYS 268

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13938279 215 LDAFFNESSADwREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQV 275
Cdd:cd08268 269 LDEITLDPEAR-RRAIAFILDGLASGALKPVVDRVFPFDDIVEAHRYLESGQQIGKIVVTP 328
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 18-275 2.22e-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: 176236 [Multi-domain]  Cd Length: 337  Bit Score: 137.72  E-value: 2.22e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  18 LGMEFSG----------RDASGKRVMGLVPAKGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPG 87
Cdd:cd08275  60 PGFECAGtveavgegvkDFKVGDRVMGLTRFGGYAEVVNVPADQVFPLPDGMSFEEAAAFPVNYLTAYYALFELGNLRPG 139

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  88 ETLLIHSGSGGVGQAAIAIALSLgcRVFTTVG--SAEKRAYLQARFpqldstsFANSRDTSFEQHV--LWHTGGKGVDLV 163
Cdd:cd08275 140 QSVLVHSAAGGVGLAAGQLCKTV--PNVTVVGtaSASKHEALKENG-------VTHVIDYRTQDYVeeVKKISPEGVDIV 210

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 164 LNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLK----------------NVTFHGVLLDAFFNESSADwR 227
Cdd:cd08275 211 LDALGGEDTRKSYDLLKPMGRLVVYGAANLVTGEKRSWFKLAKkwwnrpkvdpmkliseNKSVLGFNLGWLFEERELL-T 289

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 13938279 228 EVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQV 275
Cdd:cd08275 290 EVMDKLLKLYEEGKIKPKIDSVFPFEEVGEAMRRLQSRKNIGKVVLTP 337
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 40-233 2.71e-35

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: 135.53  E-value: 2.71e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  40 GLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHsGSGGVGQAAIAIALSLGCRVFTTVG 119
Cdd:cd05188  88 GFAEYVVVPADNLVPLPDGLSLEEAALLPEPLATAYHALRRAGVLKPGDTVLVL-GAGGVGLLAAQLAKAAGARVIVTDR 166

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 120 SAEKRAYLQarfpQLDSTSFANSRDTSFEQHVLWhTGGKGVDLVLNSL-AEEKLQASVRCLATHGRFLEIGKFDLSQNHP 198
Cdd:cd05188 167 SDEKLELAK----ELGADHVIDYKEEDLEEELRL-TGGGGADVVIDAVgGPETLAQALRLLRPGGRIVVVGGTSGGPPLD 241

                       170       180       190
                ....*....|....*....|....*....|....*
gi 13938279 199 LGMAIFLKNVTFHGVLLDaffneSSADWREVWALV 233
Cdd:cd05188 242 DLRRLLFKELTIIGSTGG-----TREDFEEALDLL 271
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
 461-910 5.89e-33

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: 137.53  E-value: 5.89e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 461 ERICEKRRHEGLPGLAVQWGAIGDVGILVETMSTNDTIVSGTLPQRMASCLEVLDLFLNQPHMVLSSFVLAEKAAAYRDR 540
Cdd:COG3319 410 LREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLLLLLLLLLLA 489

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 541 DSQRDLVEAVAHILGIRDLAAVNLDSSLADLGLDSLMSVEVRQTLERELNLVLSVREVRQLTLRKLQELSSKADEASELA 620
Cdd:COG3319 490 ALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRLLLLLALLL 569

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 621 CPTPKEDGLAQQQTQLNLRSLLVNPEGPTlmrlnsvqSSERPLFLVHPIEGSTTVFHSLASRLS--IPTYGLQC----TR 694
Cdd:COG3319 570 APTLAALAAALAAAAAAAALSPLVPLRAG--------GSGPPLFCVHPAGGNVLCYRPLARALGpdRPVYGLQApgldGG 641

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 695 AAPLDSIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACVAFEMCSQLQAQ-QSPApthnSLFLFDgspTYVLAYTqsyrak 773
Cdd:COG3319 642 EPPPASVEEMAARYVEAIRAVQPEGPYHLLGWSFGGLVAYEMARQLEAQgEEVA----LLVLLD---SYAPGAL------ 708

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 774 ltpgcEAEAETEAICFFVQQFTDMEHNRVLEALLPLKGLEERVAAAVDLIIKSH--QGLDRQELSFAARSFYYKLRAAEQ 851
Cdd:COG3319 709 -----ARLDEAELLAALLRDLARGVDLPLDAEELRALDPEERLARLLERLREAGlpAGLDAERLRRLLRVFRANLRALRR 783

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13938279 852 YTPKAkYHGNVMLLRAkTGGAYGEDLGADYNLSQVCDGKVSVHVIEGDHRTLLEGSGLE 910
Cdd:COG3319 784 YRPRP-YDGPVLLFRA-EEDPPGRADDPALGWRPLVAGGLEVHDVPGDHFSMLREPHVA 840
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
 18-273 6.22e-33

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: 129.60  E-value: 6.22e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  18 LGMEFSGR-DASGK---------RVMGLVPAK---GLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRV 84
Cdd:cd05289  63 PGHDVAGVvVAVGPgvtgfkvgdEVFGMTPFTrggAYAEYVVVPADELALKPANLSFEEAAALPLAGLTAWQALFELGGL 142

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  85 RPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVgSAEKRAYLQArfpqLDSTSFANSRDTSFEQHVLWHtggkGVDLVL 164
Cdd:cd05289 143 KAGQTVLIHGAAGGVGSFAVQLAKARGARVIATA-SAANADFLRS----LGADEVIDYTKGDFERAAAPG----GVDAVL 213

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 165 NSLAEEKLQASVRCLATHGRFLEIgkfdlsqnhpLGMAIFLKNVTFHGVLLDAFF-NESSADWREVWALVqagiRDGVVR 243
Cdd:cd05289 214 DTVGGETLARSLALVKPGGRLVSI----------AGPPPAEQAAKRRGVRAGFVFvEPDGEQLAELAELV----EAGKLR 279

                       250       260       270
                ....*....|....*....|....*....|
gi 13938279 244 PLKCTVFHGAQVEDAFRYMAQGKHIGKVVV 273
Cdd:cd05289 280 PVVDRVFPLEDAAEAHERLESGHARGKVVL 309
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 41-275 1.33e-32

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: 129.58  E-value: 1.33e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  41 LATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHsGSGGVGQAAIAIALSLGCRVFTTVGS 120
Cdd:cd08276 115 LAEYVVLPEEGLVRAPDHLSFEEAATLPCAGLTAWNALFGLGPLKPGDTVLVQ-GTGGVSLFALQFAKAAGARVIATSSS 193

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 121 AEKRAYLQArfpqLDSTSFANSRDTS-FEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPL 199
Cdd:cd08276 194 DEKLERAKA----LGADHVINYRTTPdWGEEVLKLTGGRGVDHVVEVGGPGTLAQSIKAVAPGGVISLIGFLSGFEAPVL 269

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13938279 200 GMAIFLKNVTFHGVlldafFNESSADWRevwALVQAGIRDGvVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQV 275
Cdd:cd08276 270 LLPLLTKGATLRGI-----AVGSRAQFE---AMNRAIEAHR-IRPVIDRVFPFEEAKEAYRYLESGSHFGKVVIRV 336
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 18-273 3.95e-32

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: 127.72  E-value: 3.95e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  18 LGMEFSGR-DASGK---------RVMGLVPAKG---LATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRV 84
Cdd:cd08267  62 PGMDFAGEvVAVGSgvtrfkvgdEVFGRLPPKGggaLAEYVVAPESGLAKKPEGVSFEEAAALPVAGLTALQALRDAGKV 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  85 RPGETLLIHSGSGGVGQAAIAIALSLGCRVfTTVGSAEKRAYLQarfpQLDSTSFANSRDTSFeqhVLWHTGGKGVDLVL 164
Cdd:cd08267 142 KPGQRVLINGASGGVGTFAVQIAKALGAHV-TGVCSTRNAELVR----SLGADEVIDYTTEDF---VALTAGGEKYDVIF 213

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 165 NSLAEEK--LQASVRCLATHGRFLEIGkfdlSQNHPLGMAIFLKNVTFHGV---LLDAFFNESSADWREVWALVQAGIrd 239
Cdd:cd08267 214 DAVGNSPfsLYRASLALKPGGRYVSVG----GGPSGLLLVLLLLPLTLGGGgrrLKFFLAKPNAEDLEQLAELVEEGK-- 287

                       250       260       270
                ....*....|....*....|....*....|....
gi 13938279 240 gvVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVV 273
Cdd:cd08267 288 --LKPVIDSVYPLEDAPEAYRRLKSGRARGKVVI 319
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
 16-275 1.90e-28

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 117.44  E-value: 1.90e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   16 SLLGMEFSG----------RDASGKRVMGLVPAKGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVR 85
Cdd:PTZ00354  60 EILGLEVAGyvedvgsdvkRFKEGDRVMALLPGGGYAEYAVAHKGHVMHIPQGYTFEEAAAIPEAFLTAWQLLKKHGDVK 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   86 PGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQarfpQLDSTSFANSRD-TSFEQHVLWHTGGKGVDLVL 164
Cdd:PTZ00354 140 KGQSVLIHAGASGVGTAAAQLAEKYGAATIITTSSEEKVDFCK----KLAAIILIRYPDeEGFAPKVKKLTGEKGVNLVL 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  165 NSLAEEKLQASVRCLATHGRFLEIG--------KFDLsqnhplgMAIFLKNVTFHGVLL----DAFFNESSADW-REVWA 231
Cdd:PTZ00354 216 DCVGGSYLSETAEVLAVDGKWIVYGfmggakveKFNL-------LPLLRKRASIIFSTLrsrsDEYKADLVASFeREVLP 288

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 13938279  232 LvqagIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQV 275
Cdd:PTZ00354 289 Y----MEEGEIKPIVDRTYPLEEVAEAHTFLEQNKNIGKVVLTV 328
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 320-496 3.94e-28

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: 118.62  E-value: 3.94e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 320 AQWLIQRGVQKLVLTSRSGI--RTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEA-AQLGPVGGVFNLAVVLRD 396
Cdd:cd08953 222 ARALARRYGARLVLLGRSPLppEEEWKAQTLAALEALGARVLYISADVTDAAAVRRLLEKVrERYGAIDGVIHAAGVLRD 301

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 397 GLLENQTPEFFQDVCKPKYSGTLNLDRVTREAcpELDYFVVFSSVSCGRGNAGQSNYGFANSAMERICEKRR--HEGLPG 474
Cdd:cd08953 302 ALLAQKTAEDFEAVLAPKVDGLLNLAQALADE--PLDFFVLFSSVSAFFGGAGQADYAAANAFLDAFAAYLRqrGPQGRV 379

                       170       180
                ....*....|....*....|..
gi 13938279 475 LAVQWGAIGDVGilvetMSTND 496
Cdd:cd08953 380 LSINWPAWREGG-----MAADL 396
KR_1_SDR_x cd08952
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 320-486 4.55e-26

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: 113.03  E-value: 4.55e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 320 AQWLIQRGVQKLVLTSRSGIRTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEAAQLGPVGGVFNLAVVLRDGLL 399
Cdd:cd08952 247 ARWLARRGAEHLVLTSRRGPDAPGAAELVAELTALGARVTVAACDVADRDALAALLAALPAGHPLTAVVHAAGVLDDGPL 326

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 400 ENQTPEFFQDVCKPKYSGTLNLDRVTREAcpELDYFVVFSSVSCGRGNAGQSNYGFANSAMERICEKRRHEGLPGLAVQW 479
Cdd:cd08952 327 DDLTPERLAEVLRAKVAGARHLDELTRDR--DLDAFVLFSSIAGVWGSGGQGAYAAANAYLDALAERRRARGLPATSVAW 404


                ....*..
gi 13938279 480 GAIGDVG 486
Cdd:cd08952 405 GPWAGGG 411
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 8-274 3.92e-25

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: 107.35  E-value: 3.92e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   8 PGKWTSQDSL---LGMEFSGR------DAS----GKRVMGLVPAKGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTA 74
Cdd:cd08273  48 RGLYPDQPPLpftPGYDLVGRvdalgsGVTgfevGDRVAALTRVGGNAEYINLDAKYLVPVPEGVDAAEAVCLVLNYVTA 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  75 YYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVgSAEKRAYLQarfpQLDSTSFANSRDTSFEQHVLwh 154
Cdd:cd08273 128 YQMLHRAAKVLTGQRVLIHGASGGVGQALLELALLAGAEVYGTA-SERNHAALR----ELGATPIDYRTKDWLPAMLT-- 200

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 155 tgGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGK------FDLSQNHPLGMAIFL---------KNVTFHGVllDAFF 219
Cdd:cd08273 201 --PGGVDVVFDGVGGESYEESYAALAPGGTLVCYGGnssllqGRRSLAALGSLLARLaklkllptgRRATFYYV--WRDR 276

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 13938279 220 NESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQ 274
Cdd:cd08273 277 AEDPKLFRQDLTELLDLLAKGKIRPKIAKRLPLSEVAEAHRLLESGKVVGKIVLL 331
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 40-273 1.39e-23

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 102.88  E-value: 1.39e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  40 GLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVvRGRVRPGETLLIHsGSGGVGQAAIAIALSLGCRVFTTVG 119
Cdd:COG1064 117 GYAEYVVVPARFLVKLPDGLDPAEAAPLLCAGITAYRALR-RAGVGPGDRVAVI-GAGGLGHLAVQIAKALGAEVIAVDR 194

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 120 SAEKRAylQARfpQLDSTSFANSRDTSFEQhvlWHTGGKGVDLVLNSL-AEEKLQASVRCLATHGRFLEIGkfDLSQNHP 198
Cdd:COG1064 195 SPEKLE--LAR--ELGADHVVNSSDEDPVE---AVRELTGADVVIDTVgAPATVNAALALLRRGGRLVLVG--LPGGPIP 265

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13938279 199 LGM-AIFLKNVTFHGVLldaffNESSADWREVWALVQAG-IR-DGVVRPLkctvfhgAQVEDAFRYMAQGKHIGKVVV 273
Cdd:COG1064 266 LPPfDLILKERSIRGSL-----IGTRADLQEMLDLAAEGkIKpEVETIPL-------EEANEALERLRAGKVRGRAVL 331
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 54-275 7.69e-23

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: 100.43  E-value: 7.69e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  54 DVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVgSAEKRAYLQarfpQ 133
Cdd:cd08271 109 PLPDSLSFEEAAALPCAGLTAYQALFKKLRIEAGRTILITGGAGGVGSFAVQLAKRAGLRVITTC-SKRNFEYVK----S 183

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 134 LDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEI-GKFDLSQNHPlgmaiFLKNVTFHG 212
Cdd:cd08271 184 LGADHVIDYNDEDVCERIKEITGGRGVDAVLDTVGGETAAALAPTLAFNGHLVCIqGRPDASPDPP-----FTRALSVHE 258

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 213 VLLDAF-FNESSADWREvwaLVQAG------IRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQV 275
Cdd:cd08271 259 VALGAAhDHGDPAAWQD---LRYAGeellelLAAGKLEPLVIEVLPFEQLPEALRALKDRHTRGKIVVTI 325
KR_3_FAS_SDR_x cd08956
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); ...
 320-508 3.55e-22

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: 100.80  E-value: 3.55e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 320 AQWLIQR-GVQKLVLTSRSGIRTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEAAQLGPVGGVFNLAVVLRDGL 398
Cdd:cd08956 210 ARHLVTEhGVRHLLLVSRRGPDAPGAAELVAELAALGAEVTVAACDVADRAALAALLAAVPADHPLTAVVHAAGVLDDGV 289

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 399 LENQTPEFFQDVCKPKYSGTLNLDRVTREAcpELDYFVVFSSVSCGRGNAGQSNYGFANSAMERICEKRRHEGLPGLAVQ 478
Cdd:cd08956 290 LTSLTPERLDAVLRPKVDAAWHLHELTRDL--DLAAFVLFSSAAGVLGSPGQANYAAANAFLDALAQHRRARGLPATSLA 367

                       170       180       190
                ....*....|....*....|....*....|
gi 13938279 479 WGAIGDVGILVETMSTNDtivsgtlPQRMA 508
Cdd:cd08956 368 WGLWAQASGMTAHLSDAD-------LARLA 390
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
98-235 7.47e-21

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 89.20  E-value: 7.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279    98 GVGQAAIAIALSLGCRVFTTVGSAEKRAYLQarfpQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSL-AEEKLQASV 176
Cdd:pfam00107   1 GVGLAAIQLAKAAGAKVIAVDGSEEKLELAK----ELGADHVINPKETDLVEEIKELTGGKGVDVVFDCVgSPATLEQAL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   177 RCLATHGRFLEIGKFdlSQNHPLGMA-IFLKNVTFHGVLLDaffneSSADWREVWALVQA 235
Cdd:pfam00107  77 KLLRPGGRVVVVGLP--GGPLPLPLApLLLKELTILGSFLG-----SPEEFPEALDLLAS 129
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 54-273 5.04e-20

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: 92.75  E-value: 5.04e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  54 DVPSNWTLEEAASVPVVYSTAYYALVvRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFtTVGSAEKRAYLQArfpq 133
Cdd:cd08274 146 PVNSPLSDVELATFPCSYSTAENMLE-RAGVGAGETVLVTGASGGVGSALVQLAKRRGAIVI-AVAGAAKEEAVRA---- 219

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 134 LDSTSFANSRDTSFEQHVLwhTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIG-------KFDLSQnhplgmaIFLK 206
Cdd:cd08274 220 LGADTVILRDAPLLADAKA--LGGEPVDVVADVVGGPLFPDLLRLLRPGGRYVTAGaiagpvvELDLRT-------LYLK 290

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13938279 207 NVTFHGvlldaffneSSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVV 273
Cdd:cd08274 291 DLTLFG---------STLGTREVFRRLVRYIEEGEIRPVVAKTFPLSEIREAQAEFLEKRHVGKLVL 348
PGDH cd05288
Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the ...
 73-273 7.00e-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: 91.77  E-value: 7.00e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  73 TAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLqarfpqldsTSFA------NSRDTS 146
Cdd:cd05288 132 TAYFGLTEIGKPKPGETVVVSAAAGAVGSVVGQIAKLLGARVVGIAGSDEKCRWL---------VEELgfdaaiNYKTPD 202

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 147 FEQhVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIG------KFDLSQNHPLGMAIFlKNVTFHGVLLDAFFN 220
Cdd:cd05288 203 LAE-ALKEAAPDGIDVYFDNVGGEILDAALTLLNKGGRIALCGaisqynATEPPGPKNLGNIIT-KRLTMQGFIVSDYAD 280

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 13938279 221 EssadWREVWALVQAGIRDGVVRPlKCTVFHG-AQVEDAFRYMAQGKHIGKVVV 273
Cdd:cd05288 281 R----FPEALAELAKWLAEGKLKY-REDVVEGlENAPEAFLGLFTGKNTGKLVV 329
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
 29-275 8.36e-19

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: 88.27  E-value: 8.36e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  29 GKRVMGLVPAKGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIAL 108
Cdd:cd05286  79 GDRVAYAGPPGAYAEYRVVPASRLVKLPDGISDETAAALLLQGLTAHYLLRETYPVKPGDTVLVHAAAGGVGLLLTQWAK 158

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 109 SLGCRVFTTVGSAEKRAylQARfpQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEI 188
Cdd:cd05286 159 ALGATVIGTVSSEEKAE--LAR--AAGADHVINYRDEDFVERVREITGGRGVDVVYDGVGKDTFEGSLDSLRPRGTLVSF 234

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 189 GK-------FDLSQnhpLGMaiflKNVTF-HGVLLDafFNESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFR 260
Cdd:cd05286 235 GNasgpvppFDLLR---LSK----GSLFLtRPSLFH--YIATREELLARAAELFDAVASGKLKVEIGKRYPLADAAQAHR 305

                       250
                ....*....|....*
gi 13938279 261 YMAQGKHIGKVVVQV 275
Cdd:cd05286 306 DLESRKTTGKLLLIP 320
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
 9-275 1.08e-18

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: 88.41  E-value: 1.08e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   9 GKWTSQDSLLGMEFSGR------DAS----GKRVMGLV-------PAKG-LATSVLLSPDFLWDVPSNWTLEEAASVPVV 70
Cdd:cd08249  49 GFIPSYPAILGCDFAGTvvevgsGVTrfkvGDRVAGFVhggnpndPRNGaFQEYVVADADLTAKIPDNISFEEAATLPVG 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  71 YSTAYYALVVR----------GRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVgSAEKRAYLQarfpQLDSTSFA 140
Cdd:cd08249 129 LVTAALALFQKlglplpppkpSPASKGKPVLIWGGSSSVGTLAIQLAKLAGYKVITTA-SPKNFDLVK----SLGADAVF 203

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 141 NSRDTSFEQHVLWHTGGKgVDLVLNSLAE-EKLQASVRCLATHGRfleiGKFDLSQNHPLGmAIFLKNVTFHGVLLDAFF 219
Cdd:cd08249 204 DYHDPDVVEDIRAATGGK-LRYALDCISTpESAQLCAEALGRSGG----GKLVSLLPVPEE-TEPRKGVKVKFVLGYTVF 277

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13938279 220 NESSADW---REVWALVQAGIRDGVVRPLKCTVFHG--AQVEDAFRYMAQGKHIG-KVVVQV 275
Cdd:cd08249 278 GEIPEDRefgEVFWKYLPELLEEGKLKPHPVRVVEGglEGVQEGLDLLRKGKVSGeKLVVRL 339
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
 29-272 4.13e-18

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: 86.56  E-value: 4.13e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  29 GKRVMGLVPAKGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIAL 108
Cdd:cd05282  81 GQRVLPLGGEGTWQEYVVAPADDLIPVPDSISDEQAAMLYINPLTAWLMLTEYLKLPPGDWVIQNAANSAVGRMLIQLAK 160

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 109 SLGCRVFTTVGSAEKRAYLQArfpqLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEI 188
Cdd:cd05282 161 LLGFKTINVVRRDEQVEELKA----LGADEVIDSSPEDLAQRVKEATGGAGARLALDAVGGESATRLARSLRPGGTLVNY 236

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 189 GKFDLSQNHPLGMAIFLKNVTFHGVLLDAFFNESSAD-WREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKH 267
Cdd:cd05282 237 GLLSGEPVPFPRSVFIFKDITVRGFWLRQWLHSATKEaKQETFAEVIKLVEAGVLTTPVGAKFPLEDFEEAVAAAEQPGR 316


                ....*
gi 13938279 268 IGKVV 272
Cdd:cd05282 317 GGKVL 321
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 55-273 1.12e-17

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: 85.45  E-value: 1.12e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  55 VPSNWTLEEAASVPVVYSTAYYALVvRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQARFpql 134
Cdd:cd08259 132 LPDNVSDESAALAACVVGTAVHALK-RAGVKKGDTVLVTGAGGGVGIHAIQLAKALGARVIAVTRSPEKLKILKELG--- 207

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 135 dstSFANSRDTSFEQHVlWHTGgkGVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNH-PLGMAIfLKNVTFHGV 213
Cdd:cd08259 208 ---ADYVIDGSKFSEDV-KKLG--GADVVIELVGSPTIEESLRSLNKGGRLVLIGNVTPDPAPlRPGLLI-LKEIRIIGS 280

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 214 LldaffNESSADWREVWALVQAgirdGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVV 273
Cdd:cd08259 281 I-----SATKADVEEALKLVKE----GKIKPVIDRVVSLEDINEALEDLKSGKVVGRIVL 331
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 40-275 1.70e-17

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: 84.80  E-value: 1.70e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  40 GLATSVLLSPDFLWDVPSNWTLEEAASVPVVySTAYYAlVVRGRVRPGETLLIhSGSGGVGQAAIAIALSLGC-RVFTTV 118
Cdd:COG1063 117 GFAEYVRVPAANLVKVPDGLSDEAAALVEPL-AVALHA-VERAGVKPGDTVLV-IGAGPIGLLAALAARLAGAaRVIVVD 193

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 119 GSAEKRAylQARfpQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSL-AEEKLQASVRCLATHGRFLEIG------KF 191
Cdd:COG1063 194 RNPERLE--LAR--ELGADAVVNPREEDLVEAVRELTGGRGADVVIEAVgAPAALEQALDLVRPGGTVVLVGvpggpvPI 269

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 192 DLsqnhplgMAIFLKNVTFHGVlldafFNESSADWREVWALVQAGIRDgvVRPLKCTVFHGAQVEDAFRYMAQGK-HIGK 270
Cdd:COG1063 270 DL-------NALVRKELTLRGS-----RNYTREDFPEALELLASGRID--LEPLITHRFPLDDAPEAFEAAADRAdGAIK 335


                ....*
gi 13938279 271 VVVQV 275
Cdd:COG1063 336 VVLDP 340
ADH_zinc_N_2 pfam13602
Zinc-binding dehydrogenase;
141-273 1.76e-17

Zinc-binding dehydrogenase;


Pssm-ID: 433341 [Multi-domain]  Cd Length: 131  Bit Score: 79.68  E-value: 1.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   141 NSRDTSFEQHvlwhTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNhPLGMAIFLKNVTFHGVLLDAFFN 220
Cdd:pfam13602   8 DYRTTDFVQA----TGGEGVDVVLDTVGGEAFEASLRVLPGGGRLVTIGGPPLSAG-LLLPARKRGGRGVKYLFLFVRPN 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 13938279   221 ESSADWREVWALVQAGirdgVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVV 273
Cdd:pfam13602  83 LGADILQELADLIEEG----KLRPVIDRVFPLEEAAEAHRYLESGRARGKIVL 131
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
 19-273 1.71e-16

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: 81.89  E-value: 1.71e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  19 GMEFS---GRDASG---------KR------VMGLVPAKG---LATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYA 77
Cdd:cd08248  70 GIEFPltlGRDCSGvvvdigsgvKSfeigdeVWGAVPPWSqgtHAEYVVVPENEVSKKPKNLSHEEAASLPYAGLTAWSA 149

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  78 LVVRGRVRPGET----LLIHSGSGGVGQAAIAIALSLGCRVFTTVGS--AEKRAYLQARfpqlDSTSFANsrdTSFEQHV 151
Cdd:cd08248 150 LVNVGGLNPKNAagkrVLILGGSGGVGTFAIQLLKAWGAHVTTTCSTdaIPLVKSLGAD----DVIDYNN---EDFEEEL 222

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 152 LWHTggkGVDLVLNSLAEEKLQASVRCLATHGRFLEIG----KFDLSQNHPLGMA----IFLKNVTFH---GVLLD-AFF 219
Cdd:cd08248 223 TERG---KFDVILDTVGGDTEKWALKLLKKGGTYVTLVspllKNTDKLGLVGGMLksavDLLKKNVKSllkGSHYRwGFF 299

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 13938279 220 NESSADWREVWALVQagirDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVV 273
Cdd:cd08248 300 SPSGSALDELAKLVE----DGKIKPVIDKVFPFEEVPEAYEKVESGHARGKTVI 349
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
 73-273 1.99e-16

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: 81.53  E-value: 1.99e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  73 TAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQArfpqLDSTSFANSRDTSFEQhVL 152
Cdd:cd08250 126 TASIALEEVGEMKSGETVLVTAAAGGTGQFAVQLAKLAGCHVIGTCSSDEKAEFLKS----LGCDRPINYKTEDLGE-VL 200

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 153 WHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIG---------KFDLSQNHPLGMAIFLKNVTFHGVLLDAFfnesS 223
Cdd:cd08250 201 KKEYPKGVDVVYESVGGEMFDTCVDNLALKGRLIVIGfisgyqsgtGPSPVKGATLPPKLLAKSASVRGFFLPHY----A 276

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 13938279 224 ADWREVWALVQAGIRDGVVRP-LKCTVFHGAQ-VEDAFRYMAQGKHIGKVVV 273
Cdd:cd08250 277 KLIPQHLDRLLQLYQRGKLVCeVDPTRFRGLEsVADAVDYLYSGKNIGKVVV 328
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 55-236 1.89e-15

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: 78.80  E-value: 1.89e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  55 VPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHsGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYlqARfpQL 134
Cdd:cd08260 134 LPDDVDFVTAAGLGCRFATAFRALVHQARVKPGEWVAVH-GCGGVGLSAVMIASALGARVIAVDIDDDKLEL--AR--EL 208

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 135 DSTSFANSRDT-SFEQHVLWHTGGkGVDLVLNSL-AEEKLQASVRCLATHGRFLEIGKFDLSQNH-PLGMA-IFLKNVTF 210
Cdd:cd08260 209 GAVATVNASEVeDVAAAVRDLTGG-GAHVSVDALgIPETCRNSVASLRKRGRHVQVGLTLGEEAGvALPMDrVVARELEI 287

                       170       180
                ....*....|....*....|....*.
gi 13938279 211 HGVlldafFNESSADWREVWALVQAG 236
Cdd:cd08260 288 VGS-----HGMPAHRYDAMLALIASG 308
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
 55-273 4.81e-15

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 77.38  E-value: 4.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   55 VPSNWTLEEAASVPVVYSTAYYALVvRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQarfpql 134
Cdd:PRK13771 132 VPPNVSDEGAVIVPCVTGMVYRGLR-RAGVKKGETVLVTGAGGGVGIHAIQVAKALGAKVIAVTSSESKAKIVS------ 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  135 dstsfansrdtSFEQHVLwhTGGK---------GVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNH--PLGMAI 203
Cdd:PRK13771 205 -----------KYADYVI--VGSKfseevkkigGADIVIETVGTPTLEESLRSLNMGGKIIQIGNVDPSPTYslRLGYII 271

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  204 fLKNVTFHGVLldaffNESSADWREVWALVqagiRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVV 273
Cdd:PRK13771 272 -LKDIEIIGHI-----SATKRDVEEALKLV----AEGKIKPVIGAEVSLSEIDKALEELKDKSRIGKILV 331
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 23-273 5.91e-15

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: 76.88  E-value: 5.91e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  23 SGRDASGKRV------MGLVPAKGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGS 96
Cdd:cd08243  73 GGTFTPGQRVatamggMGRTFDGSYAEYTLVPNEQVYAIDSDLSWAELAALPETYYTAWGSLFRSLGLQPGDTLLIRGGT 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  97 GGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQAR---FPQLDstsfansrDTSFEQHVLwhTGGKGVDLVLNSLAEEKLQ 173
Cdd:cd08243 153 SSVGLAALKLAKALGATVTATTRSPERAALLKELgadEVVID--------DGAIAEQLR--AAPGGFDKVLELVGTATLK 222

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 174 ASVRCLATHGRFLEIG---------KFDLSQNHPLGMAIFLknvtFHGVLLDafFNESSADWrevwaLVQAgIRDGVVRP 244
Cdd:cd08243 223 DSLRHLRPGGIVCMTGllggqwtleDFNPMDDIPSGVNLTL----TGSSSGD--VPQTPLQE-----LFDF-VAAGHLDI 290

                       250       260
                ....*....|....*....|....*....
gi 13938279 245 LKCTVFHGAQVEDAFRYMAQGKHIGKVVV 273
Cdd:cd08243 291 PPSKVFTFDEIVEAHAYMESNRAFGKVVV 319
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
 55-274 1.01e-14

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: 76.54  E-value: 1.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  55 VPSNWTLEEAASVPVVYSTAYYAlVVRGRVRPGETLLIhSGSGGVGQAAIAIALSLGC-RVFTTVGSAEKRAYLQARFPq 133
Cdd:cd05278 137 IPDGLPDEDALMLSDILPTGFHG-AELAGIKPGSTVAV-IGAGPVGLCAVAGARLLGAaRIIAVDSNPERLDLAKEAGA- 213

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 134 ldsTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLA-EEKLQASVRCLATHGRFLEIGKFDLSQ-NHPLGMAiFLKNVTFH 211
Cdd:cd05278 214 ---TDIINPKNGDIVEQILELTGGRGVDCVIEAVGfEETFEQAVKVVRPGGTIANVGVYGKPDpLPLLGEW-FGKNLTFK 289

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13938279 212 GVLLDAffnessadWREVWALVQAgIRDGVVRPLK-CT-VFHGAQVEDAFRYMAQGK-HIGKVVVQ 274
Cdd:cd05278 290 TGLVPV--------RARMPELLDL-IEEGKIDPSKlIThRFPLDDILKAYRLFDNKPdGCIKVVIR 346
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 530-598 1.60e-14

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: 69.59  E-value: 1.60e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13938279    530 LAEKAAAYRDRDSQRDLVEAVAHILGIRDLAAVNLDSSLADLGLDSLMSVEVRQTLERELNLVLSVREV 598
Cdd:smart00823   1 LAALPPAERRRLLLDLVREQVAAVLGHAAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLV 69
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
545-828 4.81e-13

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 73.54  E-value: 4.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   545 DLVEAVAHILGirdLAAVNLDSSLADLGLDSLMSVEVRQTLERELNlvlsvrevRQLTLRKLQELSSKADEASELAcptp 624
Cdd:PRK10252  982 IIAAAFSSLLG---CDVVDADADFFALGGHSLLAMKLAAQLSRQFA--------RQVTPGQVMVASTVAKLATLLD---- 1046

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   625 kEDGLAQQQTQLNLRSLLVNPEGPTLmrlnsvqsserplFLVHPIEGSTTVFHSLASRLS--IPTYGLQCTR---AAPL- 698
Cdd:PRK10252 1047 -AEEDESRRLGFGTILPLREGDGPTL-------------FCFHPASGFAWQFSVLSRYLDpqWSIYGIQSPRpdgPMQTa 1112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   699 DSIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACVAFEMCSQLQAQqspAPTHNSLFLFDGSPtyvlAYTQSYRAKLTPGC 778
Cdd:PRK10252 1113 TSLDEVCEAHLATLLEQQPHGPYHLLGYSLGGTLAQGIAARLRAR---GEEVAFLGLLDTWP----PETQNWREKEANGL 1185

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 13938279   779 EAEAETEAicffvqqftDMEHNRVLEAL---LP---LKGLEERVAAAVDLIIKSHQ 828
Cdd:PRK10252 1186 DPEVLAEI---------DREREAFLAAQqgsLStelFTTIEGNYADAVRLLTTAHS 1232
PRK10754 PRK10754
NADPH:quinone reductase;
55-189 9.92e-13

NADPH:quinone reductase;


Pssm-ID: 182701 [Multi-domain]  Cd Length: 327  Bit Score: 70.15  E-value: 9.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   55 VPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKraylQARFPQL 134
Cdd:PRK10754 109 LPDAISFEQAAASFLKGLTVYYLLRKTYEIKPDEQFLFHAAAGGVGLIACQWAKALGAKLIGTVGSAQK----AQRAKKA 184

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 13938279  135 DSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIG 189
Cdd:PRK10754 185 GAWQVINYREENIVERVKEITGGKKVRVVYDSVGKDTWEASLDCLQRRGLMVSFG 239
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
 29-272 5.01e-12

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: 68.16  E-value: 5.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  29 GKRVMGLVPAK--GLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYyALVVRGRVRPGETLLIHSGSGGVGQAAIAI 106
Cdd:cd08244  84 GRRVVAHTGRAggGYAELAVADVDSLHPVPDGLDLEAAVAVVHDGRTAL-GLLDLATLTPGDVVLVTAAAGGLGSLLVQL 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 107 ALSLGCRVFTTVGSAEKRAYLQArfpqLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFL 186
Cdd:cd08244 163 AKAAGATVVGAAGGPAKTALVRA----LGADVAVDYTRPDWPDQVREALGGGGVTVVLDGVGGAIGRAALALLAPGGRFL 238

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 187 EIGKFDLSQNHPLGMAIFLKNVTFHGVLLDAFFnesSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGK 266
Cdd:cd08244 239 TYGWASGEWTALDEDDARRRGVTVVGLLGVQAE---RGGLRALEARALAEAAAGRLVPVVGQTFPLERAAEAHAALEARS 315


                ....*.
gi 13938279 267 HIGKVV 272
Cdd:cd08244 316 TVGKVL 321
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 40-273 8.94e-12

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: 67.66  E-value: 8.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  40 GLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIhSGSGGVGQAAIAIALSLGCRVFTTVG 119
Cdd:cd08254 119 GFAEYIVVPARALVPVPDGVPFAQAAVATDAVLTPYHAVVRAGEVKPGETVLV-IGLGGLGLNAVQIAKAMGAAVIAVDI 197

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 120 SAEKRAylQARfpQLDSTSFANSRDTSFEQHVLwHTGGKGVDLVLN-SLAEEKLQASVRCLATHGRFLEIGkfdlsqnhp 198
Cdd:cd08254 198 KEEKLE--LAK--ELGADEVLNSLDDSPKDKKA-AGLGGGFDVIFDfVGTQPTFEDAQKAVKPGGRIVVVG--------- 263

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 199 LGMaiflKNVTFHGVLLDAF-------FNESSADWREVWALVQAGIRDGVV--RPLKctvfhgaQVEDAFRYMAQGKHIG 269
Cdd:cd08254 264 LGR----DKLTVDLSDLIARelriigsFGGTPEDLPEVLDLIAKGKLDPQVetRPLD-------EIPEVLERLHKGKVKG 332


                ....
gi 13938279 270 KVVV 273
Cdd:cd08254 333 RVVL 336
CurA COG2130
NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and ...
 73-275 1.84e-11

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: 66.62  E-value: 1.84e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  73 TAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLqarfpqLDSTSFA---NSRDTSFEQ 149
Cdd:COG2130 133 TAYFGLLDIGKPKAGETVVVSAAAGAVGSVVGQIAKLKGCRVVGIAGGAEKCRYL------VEELGFDaaiDYKAGDLAA 206

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 150 HvLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRF-------------LEIGkfdlsqnhPLGMAIFLKN-VTFHGVLL 215
Cdd:COG2130 207 A-LAAACPDGIDVYFDNVGGEILDAVLPLLNTFARIavcgaisqynatePPPG--------PRNLGQLLVKrLRMQGFIV 277

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13938279 216 DAFFnessADWREVWALVQAGIRDGVVRPlKCTVFHG-AQVEDAFRYMAQGKHIGKVVVQV 275
Cdd:COG2130 278 FDHA----DRFPEFLAELAGWVAEGKLKY-RETVVEGlENAPEAFLGLFEGENFGKLLVKV 333
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
 35-274 1.96e-11

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: 66.46  E-value: 1.96e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  35 LVPAKGLATSVLLSpdflwdVPSNWTLEEAASV-PVvySTAYYAlVVRGRVRPGETLLIhSGSGGVGQAAIAIALSLGCR 113
Cdd:cd08235 122 RVPAWAVKRGGVLK------LPDNVSFEEAALVePL--ACCINA-QRKAGIKPGDTVLV-IGAGPIGLLHAMLAKASGAR 191

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 114 -VFTTVGSAEKRAylQARfpQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQA-SVRCLATHGRFLEIGKF 191
Cdd:cd08235 192 kVIVSDLNEFRLE--FAK--KLGADYTIDAAEEDLVEKVRELTDGRGADVVIVATGSPEAQAqALELVRKGGRILFFGGL 267

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 192 DLSQNHPLGMA-IFLKNVTFHGVlldafFNESSADWREVWALVQAGIRDgvVRPLKCTVFHGAQVEDAFRYMAQGKHIgK 270
Cdd:cd08235 268 PKGSTVNIDPNlIHYREITITGS-----YAASPEDYKEALELIASGKID--VKDLITHRFPLEDIEEAFELAADGKSL-K 339


                ....
gi 13938279 271 VVVQ 274
Cdd:cd08235 340 IVIT 343
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 36-189 5.54e-11

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: 65.47  E-value: 5.54e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  36 VPAKGLATsvllspdflwdVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIhSGSGGVGQAAIAIALSLGCRVF 115
Cdd:cd08263 148 VPATALAP-----------LPESLDYTESAVLGCAGFTAYGALKHAADVRPGETVAV-IGVGGVGSSAIQLAKAFGASPI 215

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13938279 116 TTVG-SAEKRAylQARfpQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLA-EEKLQASVRCLATHGRFLEIG 189
Cdd:cd08263 216 IAVDvRDEKLA--KAK--ELGATHTVNAAKEDAVAAIREITGGRGVDVVVEALGkPETFKLALDVVRDGGRAVVVG 287
crotonyl_coA_red cd08246
crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase ...
 42-275 1.80e-10

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: 63.97  E-value: 1.80e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  42 ATSVLLSPDFLwdvpsnwTLEEAASVPVVYSTAYYALVVR--GRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVG 119
Cdd:cd08246 154 ATQLMPKPKHL-------SWEEAAAYMLVGATAYRMLFGWnpNTVKPGDNVLIWGASGGLGSMAIQLARAAGANPVAVVS 226

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 120 SAEKRAYLQA--------------RFPQLDSTSFANSRDT----SFEQHVLWHTGGK-GVDLVLNSLAEEKLQASVRcLA 180
Cdd:cd08246 227 SEEKAEYCRAlgaegvinrrdfdhWGVLPDVNSEAYTAWTkearRFGKAIWDILGGReDPDIVFEHPGRATFPTSVF-VC 305

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 181 THGrfleigkfdlsqnhplGMAIFLKNVTFHGVLLDAFF---------NESSADWREVWALVQAgIRDGVVRPLKCTVFH 251
Cdd:cd08246 306 DRG----------------GMVVICAGTTGYNHTYDNRYlwmrqkriqGSHFANDREAAEANRL-VMKGRIDPCLSKVFS 368

                       250       260
                ....*....|....*....|....*
gi 13938279 252 GAQVEDAFRYMAQGKH-IGKVVVQV 275
Cdd:cd08246 369 LDETPDAHQLMHRNQHhVGNMAVLV 393
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 29-258 2.96e-10

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: 62.29  E-value: 2.96e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  29 GKRVMGLVPAkglATSVLLSPDFLWDVPSNWTLEEAASVPVVySTAYYAlVVRGRVRPGETLLIhSGSGGVGQAAIAIAL 108
Cdd:cd08255  45 GDRVFCFGPH---AERVVVPANLLVPLPDGLPPERAALTALA-ATALNG-VRDAEPRLGERVAV-VGLGLVGLLAAQLAK 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 109 SLGCRVFTTVGSAEKRAYLQARFPQLDSTSFANSRDtsfeqhvlwhTGGKGVDLVLN-SLAEEKLQASVRCLATHGRFLE 187
Cdd:cd08255 119 AAGAREVVGVDPDAARRELAEALGPADPVAADTADE----------IGGRGADVVIEaSGSPSALETALRLLRDRGRVVL 188

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 188 IGKFDLSQNhPLGMAiflknvtFHGVLLDAFFNESSA--------DWREVWALVQAG--IRDGVVRPLkctVFHGAQVED 257
Cdd:cd08255 189 VGWYGLKPL-LLGEE-------FHFKRLPIRSSQVYGigrydrprRWTEARNLEEALdlLAEGRLEAL---ITHRVPFED 257


                .
gi 13938279 258 A 258
Cdd:cd08255 258 A 258
MDR4 cd08270
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 27-129 6.86e-10

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: 176231 [Multi-domain]  Cd Length: 305  Bit Score: 61.23  E-value: 6.86e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  27 ASGKRVMGLVPAKGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRpGETLLIHSGSGGVGQAAIAI 106
Cdd:cd08270  74 AVGARVVGLGAMGAWAELVAVPTGWLAVLPDGVSFAQAATLPVAGVTALRALRRGGPLL-GRRVLVTGASGGVGRFAVQL 152

                        90       100
                ....*....|....*....|...
gi 13938279 107 ALSLGCRVFTTVGSAEKRAYLQA 129
Cdd:cd08270 153 AALAGAHVVAVVGSPARAEGLRE 175
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
 42-273 1.02e-09

2-enoyl thioester reductase (ETR); 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: 176250 [Multi-domain]  Cd Length: 341  Bit Score: 61.08  E-value: 1.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  42 ATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSA 121
Cdd:cd08290 102 RTHAVVPADDLIKVPNDVDPEQAATLSVNPCTAYRLLEDFVKLQPGDWVIQNGANSAVGQAVIQLAKLLGIKTINVVRDR 181

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 122 EKRAYLQARFPQLDSTSFAN---SRDTSFEQhVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGKfdLSQNH- 197
Cdd:cd08290 182 PDLEELKERLKALGADHVLTeeeLRSLLATE-LLKSAPGGRPKLALNCVGGKSATELARLLSPGGTMVTYGG--MSGQPv 258

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 198 --PLGMAIFlKNVTFHGVLLDAFF-NESSADWREVWALVQAGIRDGVVRPLKCTVFHGA---QVEDAF-RYMAQGKHiGK 270
Cdd:cd08290 259 tvPTSLLIF-KDITLRGFWLTRWLkRANPEEKEDMLEELAELIREGKLKAPPVEKVTDDpleEFKDALaNALKGGGG-GK 336


                ...
gi 13938279 271 VVV 273
Cdd:cd08290 337 QVL 339
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 544-598 1.28e-09

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: 54.88  E-value: 1.28e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 13938279   544 RDLVEAVAHILGIrDLAAVNLDSSLADLGLDSLMSVEVRQTLERELNLVLSVREV 598
Cdd:pfam00550   1 ERLRELLAEVLGV-PAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDL 54
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
 56-274 1.38e-09

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: 60.62  E-value: 1.38e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  56 PSNWTLEEAASVPVVYSTAYYALVVRGRVRP-----GETLLIHSGSGGVGQAAIAIA-LSLGCRVFTTVGSAEKRAYLQa 129
Cdd:cd08252 114 PKSLSFAEAAALPLTSLTAWEALFDRLGISEdaeneGKTLLIIGGAGGVGSIAIQLAkQLTGLTVIATASRPESIAWVK- 192

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 130 rfpQLDSTSFANSRDTSFEQhvLWHTGGKGVDLVLNSLA-EEKLQASVRCLATHGRFLEI----GKFDLsqnhplgMAIF 204
Cdd:cd08252 193 ---ELGADHVINHHQDLAEQ--LEALGIEPVDYIFCLTDtDQHWDAMAELIAPQGHICLIvdpqEPLDL-------GPLK 260

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 205 LKNVTFHGVLLdafFNES---SADWR-------EVWALVQAGIrdgvvrpLKCTV---FHG---AQVEDAFRYMAQGKHI 268
Cdd:cd08252 261 SKSASFHWEFM---FTRSmfqTPDMIeqheilnEVADLLDAGK-------LKTTLtetLGPinaENLREAHALLESGKTI 330


                ....*.
gi 13938279 269 GKVVVQ 274
Cdd:cd08252 331 GKIVLE 336
AST1_like cd08247
AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group ...
 18-275 1.84e-09

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: 60.36  E-value: 1.84e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  18 LGMEFSGRDAS-----------GKRVMGLVP----AKG-LATSVLLSP--DF--LWDVPSNWTLEEAASVPVVYSTAYYA 77
Cdd:cd08247  62 LGRDYSGVIVKvgsnvasewkvGDEVCGIYPhpygGQGtLSQYLLVDPkkDKksITRKPENISLEEAAAWPLVLGTAYQI 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  78 LVVRGRVR-PGETLLIHSGSGGVGQAAIAIALSLGcRVFTTVGSAEKRAYLQARFPQLDstSFANSRDTSFEQH---VLW 153
Cdd:cd08247 142 LEDLGQKLgPDSKVLVLGGSTSVGRFAIQLAKNHY-NIGTVVGTCSSRSAELNKKLGAD--HFIDYDAHSGVKLlkpVLE 218

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 154 HTGGKG-VDLVLNSLAEEKLQAS----VRCLATHGRFLEI-G------KFDLSQNHP---------LGMAIFLK-NVTFh 211
Cdd:cd08247 219 NVKGQGkFDLILDCVGGYDLFPHinsiLKPKSKNGHYVTIvGdykanyKKDTFNSWDnpsanarklFGSLGLWSyNYQF- 297

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13938279 212 gVLLDAffnesSADWREVWAlvqAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQV 275
Cdd:cd08247 298 -FLLDP-----NADWIEKCA---ELIADGKVKPPIDSVYPFEDYKEAFERLKSNRAKGKVVIKV 352
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 32-195 3.03e-09

Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase family. However, this subgroup does not contain the characteristic catalytic zinc site. Also, it contains an atypical structural zinc-binding pattern: DxxCxxCxxxxxxxC. 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: 176225 [Multi-domain]  Cd Length: 325  Bit Score: 59.67  E-value: 3.03e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  32 VMGLVPAKGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALvVRGRVRPGETLLIHSGSGGVGQAAIAIALSLG 111
Cdd:cd08264 109 IIGVVSNGGYAEYIVVPEKNLFKIPDSISDELAASLPVAALTAYHAL-KTAGLGPGETVVVFGASGNTGIFAVQLAKMMG 187

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 112 CRVFTTVGsaekRAYLQaRFPQLDSTSFANSRDTSFEqhvlwhtGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIG-- 189
Cdd:cd08264 188 AEVIAVSR----KDWLK-EFGADEVVDYDEVEEKVKE-------ITKMADVVINSLGSSFWDLSLSVLGRGGRLVTFGtl 255

                       170
                ....*....|.
gi 13938279 190 -----KFDLSQ 195
Cdd:cd08264 256 tggevKLDLSD 266
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 45-273 3.17e-09

Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Cinnamyl alcohol dehydrogenases (CAD) reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. 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: 176257 [Multi-domain]  Cd Length: 341  Bit Score: 59.47  E-value: 3.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  45 VLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVvRGRVRPGETLLIhSGSGG-VGQAAIAIALSLGCRVFTTVGSAEK 123
Cdd:cd08297 125 AIADARYVTPIPDGLSFEQAAPLLCAGVTVYKALK-KAGLKPGDWVVI-SGAGGgLGHLGVQYAKAMGLRVIAIDVGDEK 202

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 124 RAYlqARfpQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLN-SLAEEKLQASVRCLATHGRFLEIGkfdLSQNHPLGMA 202
Cdd:cd08297 203 LEL--AK--ELGADAFVDFKKSDDVEAVKELTGGGGAHAVVVtAVSAAAYEQALDYLRPGGTLVCVG---LPPGGFIPLD 275

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13938279 203 IF---LKNVTFHGVLLDaffneSSADWREVWALVqagiRDGVVRPlKCTVFHGAQVEDAFRYMAQGKHIGKVVV 273
Cdd:cd08297 276 PFdlvLRGITIVGSLVG-----TRQDLQEALEFA----ARGKVKP-HIQVVPLEDLNEVFEKMEEGKIAGRVVV 339
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 31-273 3.20e-09

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: 59.51  E-value: 3.20e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  31 RVMGLVPAKGLATSVLLsPDFLWDVPSNWTLEEAASV-PvvYSTAYYAlVVRGRVRPGETLLIHsGSGGVGQAAIAIALS 109
Cdd:cd08261 107 QVLGVHRDGGFAEYIVV-PADALLVPEGLSLDQAALVeP--LAIGAHA-VRRAGVTAGDTVLVV-GAGPIGLGVIQVAKA 181

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 110 LGCRVFTTVGSAEKRAYlqARfpQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSL-AEEKLQASVRCLATHGR--FL 186
Cdd:cd08261 182 RGARVIVVDIDDERLEF--AR--ELGADDTINVGDEDVAARLRELTDGEGADVVIDATgNPASMEEAVELVAHGGRvvLV 257

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 187 EIGKFDLSQNHPLgmaIFLKNVTFHGvlldaffneSSADWREVWALVQAGIRDGVVRPLK-CT-VFHGAQVEDAFRYMAQ 264
Cdd:cd08261 258 GLSKGPVTFPDPE---FHKKELTILG---------SRNATREDFPDVIDLLESGKVDPEAlIThRFPFEDVPEAFDLWEA 325

                       250
                ....*....|
gi 13938279 265 -GKHIGKVVV 273
Cdd:cd08261 326 pPGGVIKVLI 335
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 41-275 3.67e-09

Sorbitol dehydrogenase; 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. Aldose reductase catalyzes the NADP(H)-dependent conversion of glucose to sorbital, and SDH uses NAD(H) in the conversion of sorbitol to fructose. 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: 176188 [Multi-domain]  Cd Length: 343  Bit Score: 59.43  E-value: 3.67e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  41 LATSVLLSPDFLWDVPSNWTLEEAASV-PVvySTAYYAlVVRGRVRPGETLLIhSGSGGVGQAAIAIALSLGCRVFTTVG 119
Cdd:cd05285 119 LCRYVNHPADFCHKLPDNVSLEEGALVePL--SVGVHA-CRRAGVRPGDTVLV-FGAGPIGLLTAAVAKAFGATKVVVTD 194

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 120 SAEKRayLQ-ARfpQLDSTSFANSRDTSFEQHVLWH---TGGKGVDLVLN-SLAEEKLQASVRCLATHGRFLEIGKFDLS 194
Cdd:cd05285 195 IDPSR--LEfAK--ELGATHTVNVRTEDTPESAEKIaelLGGKGPDVVIEcTGAESCIQTAIYATRPGGTVVLVGMGKPE 270

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 195 QNHPLgMAIFLKNVTFHGVLLDAffNessaDWREVWALVQAGIRDgvVRPLKCTVFHGAQVEDAFRYMAQGKHIG-KVVV 273
Cdd:cd05285 271 VTLPL-SAASLREIDIRGVFRYA--N----TYPTAIELLASGKVD--VKPLITHRFPLEDAVEAFETAAKGKKGViKVVI 341


                ..
gi 13938279 274 QV 275
Cdd:cd05285 342 EG 343
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
319-482 1.24e-08

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 56.80  E-value: 1.24e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 319 LAQWLIQRGVQkLVLTSRSGIRTgyqAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEA-AQLGPVGGVFNLAVVLRDG 397
Cdd:COG0300  21 LARALAARGAR-VVLVARDAERL---EALAAELRAAGARVEVVALDVTDPDAVAALAEAVlARFGPIDVLVNNAGVGGGG 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 398 LLENQTPEFFQDVCKPKYSGTLNLdrvTREACPEL-----DYFVVFSSVSCGRGNAGQSNYGFANSAMERICEKRRHE-- 470
Cdd:COG0300  97 PFEELDLEDLRRVFEVNVFGPVRL---TRALLPLMrargrGRIVNVSSVAGLRGLPGMAAYAASKAALEGFSESLRAEla 173

                       170
                ....*....|....
gi 13938279 471 --GLPGLAVQWGAI 482
Cdd:COG0300 174 ptGVRVTAVCPGPV 187
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 546-606 4.11e-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: 4.11e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13938279 546 LVEAVAHILGIrDLAAVNLDSSL-ADLGLDSLMSVEVRQTLERELNLVLSVREVRQL-TLRKL 606
Cdd:COG0236  10 LAEIIAEVLGV-DPEEITPDDSFfEDLGLDSLDAVELIAALEEEFGIELPDTELFEYpTVADL 71
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 320-483 1.55e-07

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: 53.64  E-value: 1.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 320 AQWLIQRGVqKLVLTSRSGIRtgyqAKQVRRW-RRQGVQVQVSTSNISSLEGARGLIAEA-AQLGPVGGVFNLAVVLRDG 397
Cdd:COG1028  23 ARALAAEGA-RVVITDRDAEA----LEAAAAElRAAGGRALAVAADVTDEAAVEALVAAAvAAFGRLDILVNNAGITPPG 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 398 LLENQTPEFFQDVCKPKYSGTLNLdrvTREACPEL---DY--FVVFSSVSCGRGNAGQSNYGFANSAMERICEkrrhegl 472
Cdd:COG1028  98 PLEELTEEDWDRVLDVNLKGPFLL---TRAALPHMrerGGgrIVNISSIAGLRGSPGQAAYAASKAAVVGLTR------- 167

                       170
                ....*....|.
gi 13938279 473 pGLAVQWGAIG 483
Cdd:COG1028 168 -SLALELAPRG 177
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 354-461 3.54e-07

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 52.50  E-value: 3.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  354 QGVQVQVSTSNISSLEGARGLIAEA-AQLGPVGGVFNLAVVLRDGLLENQTPEFFQDVCKPKYSGTLNldrVTREACPEL 432
Cdd:PRK05557  53 LGGKALAVQGDVSDAESVERAVDEAkAEFGGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFN---LTKAVARPM 129

                         90       100       110
                 ....*....|....*....|....*....|....
gi 13938279  433 -----DYFVVFSSVSCGRGNAGQSNYGFANSAME 461
Cdd:PRK05557 130 mkqrsGRIINISSVVGLMGNPGQANYAASKAGVI 163
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
 52-272 3.78e-07

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: 53.03  E-value: 3.78e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  52 LWDVPSNWTLEEAASVPVVYSTAYYAlVVRGRVRPGETLLIhSGSGGVGQAAIAIALSLGCRVFTTVGSAEKR---AYLQ 128
Cdd:cd08284 134 LLKLPDGLSDEAALLLGDILPTGYFG-AKRAQVRPGDTVAV-IGCGPVGLCAVLSAQVLGAARVFAVDPVPERlerAAAL 211

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 129 ARFPqldstsfANSRDTSFEQHVLWHTGGKGVDLVLNSL-AEEKLQASVRCLATHGRFLEIGkfdLSQNHPL---GMAIF 204
Cdd:cd08284 212 GAEP-------INFEDAEPVERVREATEGRGADVVLEAVgGAAALDLAFDLVRPGGVISSVG---VHTAEEFpfpGLDAY 281

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13938279 205 LKNVTFHGVLLDAffnesSADWREVWALVQAGIRDGVV-----RPLkctvfhgAQVEDAFRYMAQGKhIGKVV 272
Cdd:cd08284 282 NKNLTLRFGRCPV-----RSLFPELLPLLESGRLDLEFlidhrMPL-------EEAPEAYRLFDKRK-VLKVV 341
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
 40-236 4.37e-07

(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: 52.93  E-value: 4.37e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  40 GLATSVLLSPDFLWDVPSNWTLEEAASV-PVvySTAYYAlVVRGRVRPGETLLIhSGSGGVGQAAIAIALSLGC-RVFTT 117
Cdd:cd08233 128 GFAEYVVVPAYHVHKLPDNVPLEEAALVePL--AVAWHA-VRRSGFKPGDTALV-LGAGPIGLLTILALKAAGAsKIIVS 203

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 118 VGSAEKRAYLQARFpqldSTSFANSRDTSFEQHVLWHTGGKGVDLVLN-SLAEEKLQASVRCLATHGRFLEIGKFDlsqn 196
Cdd:cd08233 204 EPSEARRELAEELG----ATIVLDPTEVDVVAEVRKLTGGGGVDVSFDcAGVQATLDTAIDALRPRGTAVNVAIWE---- 275

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 13938279 197 HPLgmAIFLKNVTFHGVLLDAFFNESSADWREVWALVQAG 236
Cdd:cd08233 276 KPI--SFNPNDLVLKEKTLTGSICYTREDFEEVIDLLASG 313
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
 40-236 4.82e-07

Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination 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 an 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: 176219 [Multi-domain]  Cd Length: 306  Bit Score: 52.70  E-value: 4.82e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  40 GLATSVLLSPDFLWDVPSNWTLEEAA-SVPVvySTAYYALVVRGRVRPGETLLIhSGSGGVGQAAIAIALSLGCRVfTTV 118
Cdd:cd08258 119 GFAEYVLVPEESLHELPENLSLEAAAlTEPL--AVAVHAVAERSGIRPGDTVVV-FGPGPIGLLAAQVAKLQGATV-VVV 194

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 119 GSAEKRAYLQ-ARFPQLDSTsfaNSRDTSFEQHVLWHTGGKGVDLVLN-SLAEEKLQASVRCLATHGRFLEIGKFdlsqn 196
Cdd:cd08258 195 GTEKDEVRLDvAKELGADAV---NGGEEDLAELVNEITDGDGADVVIEcSGAVPALEQALELLRKGGRIVQVGIF----- 266

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 13938279 197 HPLGMAIFLKNVTFHGVLLDAFFNESSADWREVWALVQAG 236
Cdd:cd08258 267 GPLAASIDVERIIQKELSVIGSRSSTPASWETALRLLASG 306
leukotriene_B4_DH_like cd08294
13-PGR is a bifunctional enzyme with delta-13 15-prostaglandin reductase and leukotriene B4 12 ...
 29-128 6.08e-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: 6.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  29 GKRVMGlvpAKGLATSVLLSPD---FLWDVPSNW--TLEEAASVPVVY---STAYYALVVRGRVRPGETLLIHSGSGGVG 100
Cdd:cd08294  81 GTIVVA---SFGWRTHTVSDGKdqpDLYKLPADLpdDLPPSLALGVLGmpgLTAYFGLLEICKPKAGETVVVNGAAGAVG 157

                        90       100
                ....*....|....*....|....*...
gi 13938279 101 QAAIAIALSLGCRVFTTVGSAEKRAYLQ 128
Cdd:cd08294 158 SLVGQIAKIKGCKVIGCAGSDDKVAWLK 185
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
 29-274 7.32e-07

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: 52.23  E-value: 7.32e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  29 GKRVMGLVPAKGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIhSGSGGVGQAAIAIAL 108
Cdd:cd08240 118 KGRALGIFQDGGYAEYVIVPHSRYLVDPGGLDPALAATLACSGLTAYSAVKKLMPLVADEPVVI-IGAGGLGLMALALLK 196

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 109 SLGCRVFTTVG-SAEKRAYLQARfpqlDSTSFANSRDTSFEQHVLWHTGGkGVDLVLNSL-AEEKLQASVRCLATHGRFL 186
Cdd:cd08240 197 ALGPANIIVVDiDEAKLEAAKAA----GADVVVNGSDPDAAKRIIKAAGG-GVDAVIDFVnNSATASLAFDILAKGGKLV 271

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 187 EIGKFDLSQNHPLGMaIFLKNVTFHGVLLDaffneSSADWREVWALVQAgirdGVVRPLKCTVFHGAQVEDAFRYMAQGK 266
Cdd:cd08240 272 LVGLFGGEATLPLPL-LPLRALTIQGSYVG-----SLEELRELVALAKA----GKLKPIPLTERPLSDVNDALDDLKAGK 341


                ....*...
gi 13938279 267 HIGKVVVQ 274
Cdd:cd08240 342 VVGRAVLK 349
B4_12hDH TIGR02825
leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 ...
 73-274 1.90e-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: 50.76  E-value: 1.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279    73 TAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQarfpQLDSTSFANSRDTSFEQHVL 152
Cdd:TIGR02825 125 TAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAAGSDEKVAYLK----KLGFDVAFNYKTVKSLEETL 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279   153 WHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDL-SQNHPLGMAIFLKNVTFHGVLLDAF-FNESSADWRE-- 228
Cdd:TIGR02825 201 KKASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICGAISTyNRTGPLPPGPPPEIVIYQELRMEGFiVNRWQGEVRQka 280

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 13938279   229 -----VWALvqagirDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQ 274
Cdd:TIGR02825 281 lkellKWVL------EGKIQYKEYVIEGFENMPAAFMGMLKGENLGKTIVK 325
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 663-755 2.31e-06

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


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 49.85  E-value: 2.31e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 663 LFLVHPIEGSTTVFHSLASRL--SIPTYGLQC------TRAAPLDSIHSLAAyyiDCIRQVQP--EGPYRVAGYSYGACV 732
Cdd:COG3208   9 LFCFPYAGGSASAYRPWAAALppDIEVLAVQLpgrgdrLGEPPLTSLEELAD---DLAEELAPllDRPFALFGHSMGALL 85

                        90       100
                ....*....|....*....|...
gi 13938279 733 AFEMCSQLQAQQSPAPTHnsLFL 755
Cdd:COG3208  86 AFELARRLERRGRPLPAH--LFV 106
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 348-461 2.91e-06

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 49.48  E-value: 2.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  348 VRRWRRQGVQVQVSTSNISSLEGARGLIAEAA-QLGPVGGVFNLAVVLRDGLLENQTPEFFQDVCKPKYSGTLNLDRVTR 426
Cdd:PRK12825  48 VEAVEALGRRAQAVQADVTDKAALEAAVAAAVeRFGRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVV 127

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 13938279  427 EACPELDY--FVVFSSVSCGRGNAGQSNYGFANSAME 461
Cdd:PRK12825 128 PPMRKQRGgrIVNISSVAGLPGWPGRSNYAAAKAGLV 164
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 387-482 6.65e-06

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: 47.51  E-value: 6.65e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 387 VFNLAVVLRDGLLENQTPEFFQDVCKPKYSGTLNLDRVTREACPE--LDYFVVFSSVSCGRGNAGQSNYGFANSAMERIC 464
Cdd:cd02266  35 VVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAkrLGRFILISSVAGLFGAPGLGGYAASKAALDGLA 114

                        90       100
                ....*....|....*....|..
gi 13938279 465 EKRRHE----GLPGLAVQWGAI 482
Cdd:cd02266 115 QQWASEgwgnGLPATAVACGTW 136
double_bond_reductase_like cd08295
Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase; This ...
 73-165 6.85e-06

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: 49.24  E-value: 6.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  73 TAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQARF-----------PQLDST---S 138
Cdd:cd08295 138 TAYAGFYEVCKPKKGETVFVSAASGAVGQLVGQLAKLKGCYVVGSAGSDEKVDLLKNKLgfddafnykeePDLDAAlkrY 217

                        90       100
                ....*....|....*....|....*..
gi 13938279 139 FANSRDTSFEqhvlwHTGGKGVDLVLN 165
Cdd:cd08295 218 FPNGIDIYFD-----NVGGKMLDAVLL 239
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
 55-275 7.44e-06

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: 49.16  E-value: 7.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  55 VPSNWTLEEAASVPVVYSTAYYAlVVRGRVRPGETLLIHsGSGGVGQAAIAIALSLGC-RVFTtVGSAEKRAYLQARFpq 133
Cdd:cd08285 136 LPDGLTDEQAVMLPDMMSTGFHG-AELANIKLGDTVAVF-GIGPVGLMAVAGARLRGAgRIIA-VGSRPNRVELAKEY-- 210

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 134 lDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSL-AEEKLQASVRCLATHGRFLEIGKF--DLSQNHPL-----GMAifl 205
Cdd:cd08285 211 -GATDIVDYKNGDVVEQILKLTGGKGVDAVIIAGgGQDTFEQALKVLKPGGTISNVNYYgeDDYLPIPReewgvGMG--- 286

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13938279 206 kNVTFHGVLLDAffneSSADWREVWALVQAGIRDgvVRPLKCTVFHG-AQVEDAFRYMA-QGKHIGKVVVQV 275
Cdd:cd08285 287 -HKTINGGLCPG----GRLRMERLASLIEYGRVD--PSKLLTHHFFGfDDIEEALMLMKdKPDDLIKPVIIF 351
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
 55-189 8.00e-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: 49.18  E-value: 8.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  55 VPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHsGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQARFPQL 134
Cdd:cd08231 146 VPDNVPDEVAAPANCALATVLAALDRAGPVGAGDTVVVQ-GAGPLGLYAVAAAKLAGARRVIVIDGSPERLELAREFGAD 224

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13938279 135 DSTSFANSRDTSFEQHVLWHTGGKGVDLVL----NSLAeekLQASVRCLATHGRFLEIG 189
Cdd:cd08231 225 ATIDIDELPDPQRRAIVRDITGGRGADVVIeasgHPAA---VPEGLELLRRGGTYVLVG 280
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 52-273 8.19e-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: 49.15  E-value: 8.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  52 LWDVPSNWTLEEAASV-PVvySTAYYAlVVRGRVRPGETLLIhSGSGGVGQAAIAIALSLGC-RVFTTVGSAEKRAYlqA 129
Cdd:cd08236 127 LIKIPDHVDYEEAAMIePA--AVALHA-VRLAGITLGDTVVV-IGAGTIGLLAIQWLKILGAkRVIAVDIDDEKLAV--A 200

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 130 RfpQLDSTSFANSRDTSFEQhVLWHTGGKGVDLVLNSL-AEEKLQASVRCLATHGRFLEIGkfDLSQNHPLGMA----IF 204
Cdd:cd08236 201 R--ELGADDTINPKEEDVEK-VRELTEGRGADLVIEAAgSPATIEQALALARPGGKVVLVG--IPYGDVTLSEEafekIL 275

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13938279 205 LKNVTFHGvlldaFFNESSA-----DWREVWALVQAGIRDgvVRPLKCTVFHGAQVEDAFRYMAQGK-HIGKVVV 273
Cdd:cd08236 276 RKELTIQG-----SWNSYSApfpgdEWRTALDLLASGKIK--VEPLITHRLPLEDGPAAFERLADREeFSGKVLL 343
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 352-459 1.64e-05

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: 47.16  E-value: 1.64e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 352 RRQGVQVQVSTSNISSLEGARGLIAEAAQ-LGPVGGVFNLAVVLRDGLLENQTPEFFQDVCKPKYSGTLNldrVTREACP 430
Cdd:cd05333  45 KALGGNAAALEADVSDREAVEALVEKVEAeFGPVDILVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFN---VTQAVIR 121

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 13938279 431 EL---DY--FVVFSSVSCGRGNAGQSNY--------GFANSA 459
Cdd:cd05333 122 AMikrRSgrIINISSVVGLIGNPGQANYaaskagviGFTKSL 163
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
 52-164 1.65e-05

formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase (FDH), which is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. This family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Another member is identified as a dihydroxyacetone reductase. Like the zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), 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. Unlike ADH, where NAD(P)(H) acts as a cofactor, NADH in FDH is a tightly bound redox cofactor (similar to nicotinamide proteins). 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: 176246 [Multi-domain]  Cd Length: 345  Bit Score: 48.02  E-value: 1.65e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  52 LWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIhSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRayLQ-AR 130
Cdd:cd08286 132 LYKLPEGVDEEAAVMLSDILPTGYECGVLNGKVKPGDTVAI-VGAGPVGLAALLTAQLYSPSKIIMVDLDDNR--LEvAK 208

                        90       100       110
                ....*....|....*....|....*....|....
gi 13938279 131 fpQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVL 164
Cdd:cd08286 209 --KLGATHTVNSAKGDAIEQVLELTDGRGVDVVI 240
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 82-165 4.83e-05

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: 44.42  E-value: 4.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279     82 GRVRPGETLLIhsGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQARFPQLDSTSFANSrdTSFEQHVlwhtggKGVD 161
Cdd:smart01002  16 GGVPPAKVVVI--GAGVVGLGAAATAKGLGAEVTVLDVRPARLRQLESLLGARFTTLYSQA--ELLEEAV------KEAD 85


                   ....
gi 13938279    162 LVLN 165
Cdd:smart01002  86 LVIG 89
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
348-454 6.32e-05

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 45.54  E-value: 6.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  348 VRRWRRQGVQVQVSTSNISSLEGARGLIAEA-AQLGPVGGVFNLAVVLRDGLLENQTPEFFQDVCkpkysgTLNLD---R 423
Cdd:PRK05653  46 AAELRAAGGEARVLVFDVSDEAAVRALIEAAvEAFGALDILVNNAGITRDALLPRMSEEDWDRVI------DVNLTgtfN 119

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 13938279  424 VTREACP---ELDY--FVVFSSVSCGRGNAGQSNYG 454
Cdd:PRK05653 120 VVRAALPpmiKARYgrIVNISSVSGVTGNPGQTNYS 155
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
 54-205 1.08e-03

Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, Class III ADH) are members of the zinc-dependent/medium chain alcohol dehydrogenase family. 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. 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. Class III ADH are also known as glutathione-dependent formaldehyde dehydrogenase (FDH), which convert aldehydes to corresponding carboxylic acid and alcohol. 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 an 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.


Pssm-ID: 176240 [Multi-domain]  Cd Length: 363  Bit Score: 42.53  E-value: 1.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  54 DVPsnwtLEEAA----SVPvvysTAYYALVVRGRVRPGETLLIhSGSGGVGQAAI---AIAlslGCRVFTTVG-SAEKRA 125
Cdd:cd08279 154 DIP----LDRAAllgcGVT----TGVGAVVNTARVRPGDTVAV-IGCGGVGLNAIqgaRIA---GASRIIAVDpVPEKLE 221

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 126 ylQARfpQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAE-EKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIF 204
Cdd:cd08279 222 --LAR--RFGATHTVNASEDDAVEAVRDLTDGRGADYAFEAVGRaATIRQALAMTRKGGTAVVVGMGPPGETVSLPALEL 297


                .
gi 13938279 205 L 205
Cdd:cd08279 298 F 298
MDR_yhdh_yhfp cd05280
Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone ...
 56-273 2.17e-03

Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone oxidoreductases (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 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: 176183 [Multi-domain]  Cd Length: 325  Bit Score: 41.37  E-value: 2.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  56 PSNWTLEEAAsvpvVYSTAYY--ALVV----RGRVRPGETLLIHSG-SGGVGQAAIAIALSLGCRVFTTVGSAEKRAYL- 127
Cdd:cd05280 113 PEGLSLREAM----ILGTAGFtaALSVhrleDNGQTPEDGPVLVTGaTGGVGSIAVAILAKLGYTVVALTGKEEQADYLk 188

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 128 -----QARFPQ---------LDSTSFANSRDTsfeqhvlwhTGGKGVDLVLNSLAEEKLQASVrclathGrflEIGKFDL 193
Cdd:cd05280 189 slgasEVLDREdlldeskkpLLKARWAGAIDT---------VGGDVLANLLKQTKYGGVVASC------G---NAAGPEL 250

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 194 SQNhplGMAIFLKNVTFHGVllDAffNESSADWRE-VWALV----QAGIRDGVVRplkctVFHGAQVEDAFRYMAQGKHI 268
Cdd:cd05280 251 TTT---VLPFILRGVSLLGI--DS--VNCPMELRKqVWQKLatewKPDLLEIVVR-----EISLEELPEAIDRLLAGKHR 318


                ....*
gi 13938279 269 GKVVV 273
Cdd:cd05280 319 GRTVV 323
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
 54-179 2.55e-03

Liver alcohol dehydrogenase and related 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. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. 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. 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 an 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.


Pssm-ID: 176182 [Multi-domain]  Cd Length: 365  Bit Score: 41.27  E-value: 2.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  54 DVPsnwtLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHsGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAylqARFPQ 133
Cdd:cd05279 155 DAP----LEKVCLIGCGFSTGYGAAVNTAKVTPGSTCAVF-GLGGVGLSVIMGCKAAGASRIIAVDINKDKF---EKAKQ 226

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 13938279 134 LDSTSFANSRDTSFE-QHVLWHTGGKGVDLVLNSLAE-EKLQASVRCL 179
Cdd:cd05279 227 LGATECINPRDQDKPiVEVLTEMTDGGVDYAFEVIGSaDTLKQALDAT 274
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 529-618 3.77e-03

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 40.50  E-value: 3.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 529 VLAEKAAAYRDRDSQRDLVEAVAHILGIrDLAAVNLDSSLADLGLDSLMSVEVRQTLeRELNLVLSVREV-RQLTLRKLQ 607
Cdd:COG3433 207 AAASPAPALETALTEEELRADVAELLGV-DPEEIDPDDNLFDLGLDSIRLMQLVERW-RKAGLDVSFADLaEHPTLAAWW 284

                        90
                ....*....|.
gi 13938279 608 ELSSKADEASE 618
Cdd:COG3433 285 ALLAAAQAAAA 295
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 84-163 4.37e-03

Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.


Pssm-ID: 240630 [Multi-domain]  Cd Length: 359  Bit Score: 40.47  E-value: 4.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  84 VRPGETLLIhsGSGGVGQAAIAIALSLGCRVftTV--GSAEKRAYLQARFPQLDSTSFANsrDTSFEQHVlwhtggKGVD 161
Cdd:cd05305 166 VPPAKVVIL--GAGVVGENAARVALGLGAEV--TVldINLERLRYLDDIFGGRVTTLYSN--PANLEEAL------KEAD 233


                ..
gi 13938279 162 LV 163
Cdd:cd05305 234 LV 235
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 63-162 4.64e-03

Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol dehydrogenase and has the catalytic and structural zinc-binding sites characteristic of this group. 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. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176226 [Multi-domain]  Cd Length: 384  Bit Score: 40.58  E-value: 4.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  63 EAASVPVVYSTAYYALVVR-GRVRPGETLLIHsGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQARFPQLDSTSFAN 141
Cdd:cd08265 179 EAGALVEPTSVAYNGLFIRgGGFRPGAYVVVY-GAGPIGLAAIALAKAAGASKVIAFEISEERRNLAKEMGADYVFNPTK 257

                        90       100
                ....*....|....*....|.
gi 13938279 142 SRDTSFEQHVLWHTGGKGVDL 162
Cdd:cd08265 258 MRDCLSGEKVMEVTKGWGADI 278
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 354-456 4.85e-03

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 40.04  E-value: 4.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  354 QGVQVQVSTSNISSLEGARGLIAEA-AQLGPVGGVFNLAVVLRDGLLENQTPEFFQDVCKPKYSG---TLNLD----RVT 425
Cdd:PRK07791  62 AGGEAVANGDDIADWDGAANLVDAAvETFGGLDVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGhfaTLRHAaaywRAE 141

                         90       100       110
                 ....*....|....*....|....*....|..
gi 13938279  426 REACPELDYFVVFSSVSCG-RGNAGQSNYGFA 456
Cdd:PRK07791 142 SKAGRAVDARIINTSSGAGlQGSVGQGNYSAA 173
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 320-473 5.16e-03

3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical SDRs. 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 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). 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) 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 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.


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 39.54  E-value: 5.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 320 AQWLIQRGVqKLVLTSRSGIRTGYQAKQVRRWR-RQGVQVQVSTSNISSLEGARGLIAEAA-QLGPVGGVFNLAVVLRDG 397
Cdd:cd08939  18 AKELVKEGA-NVIIVARSESKLEEAVEEIEAEAnASGQKVSYISADLSDYEEVEQAFAQAVeKGGPPDLVVNCAGISIPG 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279 398 LLENQTPEFFQDVCKPKYSGTLNldrVTREACPEL-----DYFVVFSSVSCGRGNAGQSNYGFANSAMERICEKRRHEGL 472
Cdd:cd08939  97 LFEDLTAEEFERGMDVNYFGSLN---VAHAVLPLMkeqrpGHIVFVSSQAALVGIYGYSAYCPSKFALRGLAESLRQELK 173


                .
gi 13938279 473 P 473
Cdd:cd08939 174 P 174
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
 83-189 6.75e-03

Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol dehydrogenase, but has some amino acid substitutions near the active site, which may determine the enzyme's specificity of oxidizing aromatic substrates. Also known as aryl-alcohol dehydrogenases, they catalyze the conversion of an aromatic alcohol + NAD+ to an aromatic aldehyde + NADH + 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: 176239 [Multi-domain]  Cd Length: 365  Bit Score: 39.79  E-value: 6.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  83 RVRPGETLLIhSGSGGVGQAAIAIALSLGCRvfTTVG---SAEKRAylQARfpQLDSTSFANSRDTSFEQHVLWHTGGkG 159
Cdd:cd08278 183 KPRPGSSIAV-FGAGAVGLAAVMAAKIAGCT--TIIAvdiVDSRLE--LAK--ELGATHVINPKEEDLVAAIREITGG-G 254

                        90       100       110
                ....*....|....*....|....*....|.
gi 13938279 160 VDLVLNSLAEEK-LQASVRCLATHGRFLEIG 189
Cdd:cd08278 255 VDYALDTTGVPAvIEQAVDALAPRGTLALVG 285
MDR_yhfp_like cd08289
Yhfp putative quinone oxidoreductases; yhfp putative quinone oxidoreductases (QOR). QOR ...
 55-127 8.42e-03

Yhfp putative quinone oxidoreductases; yhfp putative quinone oxidoreductases (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 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: 176249 [Multi-domain]  Cd Length: 326  Bit Score: 39.23  E-value: 8.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  55 VPSNW--------TLEEAasvpVVYSTAYY--ALVVRGRVRPGET-----LLIHSGSGGVGQAAIAIALSLGCRVFTTVG 119
Cdd:cd08289 104 VPAEWvvplpkglTLKEA----MILGTAGFtaALSIHRLEENGLTpeqgpVLVTGATGGVGSLAVSILAKLGYEVVASTG 179


                ....*...
gi 13938279 120 SAEKRAYL 127
Cdd:cd08289 180 KADAADYL 187
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 352-460 9.46e-03

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 38.99  E-value: 9.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938279  352 RRQGVQVQVSTSNISSLEGARGLIAEAAQLGPVGGVFNLAVVLRDGLLENQTPEFFQDVCKPKYSGTLNL---------D 422
Cdd:PRK07792  58 RAAGAKAVAVAGDISQRATADELVATAVGLGGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLtrnaaaywrA 137

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 13938279  423 RVTREACPELDYFVVFSSVSCGRGNAGQSNYGFANSAM 460
Cdd:PRK07792 138 KAKAAGGPVYGRIVNTSSEAGLVGPVGQANYGAAKAGI 175
 
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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