Uncharacterized conserved protein, related to short-chain dehydrogenases [Function unknown];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644140   1 MSGDRLDVIIFGASGFTGKYTVFEAVTvlRGLRWGIAGRNREKLEAVLKEMGAKakkdlsQVPIFIADVNDQASLLEMAK 80
Cdd:COG3268   1 MTEREFDIVVYGATGYTGRLVAEYLAR--RGLRPALAGRNAAKLEAVAAELGAA------DLPLRVADLDDPASLAALLA 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644140  81 KCRIVVNTAGPYRFHGENVVKCCIESGTHHVDVSGEPQYMETMQLRYDQLAREKGVYVVSACGFDSIPADMGVVFVEKNF 160
Cdd:COG3268  73 GTRVVLNTVGPFARTGEPLVEACLAAGTHYLDLTGEPDWVRRMIDRYDAAARAAGARIVPACGFDSVPSDLGAALLQERL 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644140 161 DGVVnSVETFLETGikeggsgggtAGLNYGTWESAVYGLAHSDELRGIRKQI-YPQRLPRFYPFlkPRPLVFRSTevdkV 239
Cdd:COG3268 153 PEAD-RLTLAVRAK----------GGFSGGTAASMLEALAAGGADRRNGRLVrVPYALRTREDF--PDGGPQQGA----W 215

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644140 240 CLPFPGSDRSVVMRSQRFL-YDqdkkrpvqmqAYVGFSSWLVAGGVIFFATIFGLLSKFKLGRTLLLnypglfSGGLASR 318
Cdd:COG3268 216 TAPWGDVNTAVVRRSNALLnYE----------EYMAVPKGAARALALAAGLGALLAAAVPPLRRLLK------RVLPKPG 279

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644140 319 SGPSEESMERTYFKMTFKAsgwlksdrlaessnqyTESPTKTLMVRVSGMNpGYGATCVAVLSAALTILRESdkmPSTGG 398
Cdd:COG3268 280 EGPSEEERERGRFVVWGEA----------------RTAGGRRVRARVRGPG-GYGLTAKMLAEAALRLLADD---PVRGG 339

                       410       420       430
                ....*....|....*....|....*....|..
gi 24644140 399 VLPPAAAFsktG--LISELEKHdHGIKFEILA 428
Cdd:COG3268 340 FLTPATAF---GaaLVLRLLAV-AGLTFEVEE 367

Uncharacterized conserved protein, related to short-chain dehydrogenases [Function unknown];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644140   1 MSGDRLDVIIFGASGFTGKYTVFEAVTvlRGLRWGIAGRNREKLEAVLKEMGAKakkdlsQVPIFIADVNDQASLLEMAK 80
Cdd:COG3268   1 MTEREFDIVVYGATGYTGRLVAEYLAR--RGLRPALAGRNAAKLEAVAAELGAA------DLPLRVADLDDPASLAALLA 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644140  81 KCRIVVNTAGPYRFHGENVVKCCIESGTHHVDVSGEPQYMETMQLRYDQLAREKGVYVVSACGFDSIPADMGVVFVEKNF 160
Cdd:COG3268  73 GTRVVLNTVGPFARTGEPLVEACLAAGTHYLDLTGEPDWVRRMIDRYDAAARAAGARIVPACGFDSVPSDLGAALLQERL 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644140 161 DGVVnSVETFLETGikeggsgggtAGLNYGTWESAVYGLAHSDELRGIRKQI-YPQRLPRFYPFlkPRPLVFRSTevdkV 239
Cdd:COG3268 153 PEAD-RLTLAVRAK----------GGFSGGTAASMLEALAAGGADRRNGRLVrVPYALRTREDF--PDGGPQQGA----W 215

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644140 240 CLPFPGSDRSVVMRSQRFL-YDqdkkrpvqmqAYVGFSSWLVAGGVIFFATIFGLLSKFKLGRTLLLnypglfSGGLASR 318
Cdd:COG3268 216 TAPWGDVNTAVVRRSNALLnYE----------EYMAVPKGAARALALAAGLGALLAAAVPPLRRLLK------RVLPKPG 279

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644140 319 SGPSEESMERTYFKMTFKAsgwlksdrlaessnqyTESPTKTLMVRVSGMNpGYGATCVAVLSAALTILRESdkmPSTGG 398
Cdd:COG3268 280 EGPSEEERERGRFVVWGEA----------------RTAGGRRVRARVRGPG-GYGLTAKMLAEAALRLLADD---PVRGG 339

                       410       420       430
                ....*....|....*....|....*....|..
gi 24644140 399 VLPPAAAFsktG--LISELEKHdHGIKFEILA 428
Cdd:COG3268 340 FLTPATAF---GaaLVLRLLAV-AGLTFEVEE 367

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644140   8 VIIFGASGFTGKYTVfeAVTVLRGLRWGIAGRnREKLEAVLKEMGakakkDLSQVPIFIADVNDQASLLEMAKKCRIVVN 87
Cdd:cd05271   3 VTVFGATGFIGRYVV--NRLAKRGSQVIVPYR-CEAYARRLLVMG-----DLGQVLFVEFDLRDDESIRKALEGSDVVIN 74

                        90       100       110
                ....*....|....*....|....*....|..
gi 24644140  88 TAG------PYRF-----HG-ENVVKCCIESG 107
Cdd:cd05271  75 LVGrlyetkNFSFedvhvEGpERLAKAAKEAG 106

Uncharacterized conserved protein, related to short-chain dehydrogenases [Function unknown];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644140   1 MSGDRLDVIIFGASGFTGKYTVFEAVTvlRGLRWGIAGRNREKLEAVLKEMGAKakkdlsQVPIFIADVNDQASLLEMAK 80
Cdd:COG3268   1 MTEREFDIVVYGATGYTGRLVAEYLAR--RGLRPALAGRNAAKLEAVAAELGAA------DLPLRVADLDDPASLAALLA 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644140  81 KCRIVVNTAGPYRFHGENVVKCCIESGTHHVDVSGEPQYMETMQLRYDQLAREKGVYVVSACGFDSIPADMGVVFVEKNF 160
Cdd:COG3268  73 GTRVVLNTVGPFARTGEPLVEACLAAGTHYLDLTGEPDWVRRMIDRYDAAARAAGARIVPACGFDSVPSDLGAALLQERL 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644140 161 DGVVnSVETFLETGikeggsgggtAGLNYGTWESAVYGLAHSDELRGIRKQI-YPQRLPRFYPFlkPRPLVFRSTevdkV 239
Cdd:COG3268 153 PEAD-RLTLAVRAK----------GGFSGGTAASMLEALAAGGADRRNGRLVrVPYALRTREDF--PDGGPQQGA----W 215

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644140 240 CLPFPGSDRSVVMRSQRFL-YDqdkkrpvqmqAYVGFSSWLVAGGVIFFATIFGLLSKFKLGRTLLLnypglfSGGLASR 318
Cdd:COG3268 216 TAPWGDVNTAVVRRSNALLnYE----------EYMAVPKGAARALALAAGLGALLAAAVPPLRRLLK------RVLPKPG 279

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644140 319 SGPSEESMERTYFKMTFKAsgwlksdrlaessnqyTESPTKTLMVRVSGMNpGYGATCVAVLSAALTILRESdkmPSTGG 398
Cdd:COG3268 280 EGPSEEERERGRFVVWGEA----------------RTAGGRRVRARVRGPG-GYGLTAKMLAEAALRLLADD---PVRGG 339

                       410       420       430
                ....*....|....*....|....*....|..
gi 24644140 399 VLPPAAAFsktG--LISELEKHdHGIKFEILA 428
Cdd:COG3268 340 FLTPATAF---GaaLVLRLLAV-AGLTFEVEE 367

Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine dehydrogenase, NADP-dependent is part of the Pathway/BioSystem: Lysine biosynthesis

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644140  36 IAGRNREKLEAVlkemgakaKKDLSQVPIFIADVNDQASLLEMAKKCRIVVNTAGPYRfhGENVVKCCIESGTHHVDVSG 115
Cdd:COG1748   5 LADRSLEKAEAL--------AASGPKVEAAQLDASDPEALAALIAGADLVINALPPYL--NLTVAEACIEAGVHYVDLSE 74

                        90       100       110
                ....*....|....*....|....*....|
gi 24644140 116 EPQYMEtMQLRYDQLAREKGVYVVSACGFD 145
Cdd:COG1748  75 DEPETE-AKLALDELAKEAGVTAIPGCGLA 103

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644140   8 VIIFGASGFTGKYTVFEAVTvlRGLRWGIAGRNREKLEAVLKEmgakakkdlsQVPIFIADVNDQASLLEMAKKCRIVVN 87
Cdd:COG0702   2 ILVTGATGFIGRRVVRALLA--RGHPVRALVRDPEKAAALAAA----------GVEVVQGDLDDPESLAAALAGVDAVFL 69

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 24644140  88 TAGP--------YRFHGENVVKCCIESG-THHVDVSG 115
Cdd:COG0702  70 LVPSgpggdfavDVEGARNLADAAKAAGvKRIVYLSA 106

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644140   8 VIIFGASGFTGKYTVfeAVTVLRGLRWGIAGRnREKLEAVLKEMGakakkDLSQVPIFIADVNDQASLLEMAKKCRIVVN 87
Cdd:cd05271   3 VTVFGATGFIGRYVV--NRLAKRGSQVIVPYR-CEAYARRLLVMG-----DLGQVLFVEFDLRDDESIRKALEGSDVVIN 74

                        90       100       110
                ....*....|....*....|....*....|..
gi 24644140  88 TAG------PYRF-----HG-ENVVKCCIESG 107
Cdd:cd05271  75 LVGrlyetkNFSFedvhvEGpERLAKAAKEAG 106

atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644140   8 VIIFGASGFTGKYTVFEAVTvlRGlRWGIAG-RNREKLEAvLKEMGAKakkdlsqvpIFIADVNDQASLLEMAKKCRIVV 86
Cdd:cd05243   2 VLVVGATGKVGRHVVRELLD--RG-YQVRALvRDPSQAEK-LEAAGAE---------VVVGDLTDAESLAAALEGIDAVI 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644140  87 NTAGPYRFHGE-----------NVVKCCIESG-THHVDVS------------GEPQYMEtMQLRYDQLAREKGV-Y-VVS 140
Cdd:cd05243  69 SAAGSGGKGGPrteavdydgniNLIDAAKKAGvKRFVLVSsigadkpshpleALGPYLD-AKRKAEDYLRASGLdYtIVR 147

                       170       180
                ....*....|....*....|....*..
gi 24644140 141 ACGFDSIPADMGVVFVEKNFDGVVNSV 167
Cdd:cd05243 148 PGGLTDDPAGTGRVVLGGDGTRLDGPI 174

putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-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 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644140   8 VIIFGASGFTGKYTVFEAVTvlRGLRWGIAGRNREKLEAVLKEM---GAKAKKdlsqvpiFIADVNDQASLLEMAKK--- 81
Cdd:cd08935   8 AVITGGTGVLGGAMARALAQ--AGAKVAALGRNQEKGDKVAKEItalGGRAIA-------LAADVLDRASLERAREEiva 78

                        90
                ....*....|...
gi 24644140  82 ----CRIVVNTAG 90
Cdd:cd08935  79 qfgtVDILINGAG 91