Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. 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, 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 512960259   6 RVALVTGANKGIGFAITRDLCRRFSGDVVLTARDEARGRAAVQQLQAEGLSPRFHQLDIDDLQSIRAVRDFLRKEYGGLD 85
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259  86 VLINNAGIAFKMADP-TPFHIQAEVTIKTNFYGTRDVCTELLPLIKP--GGRVVNVSSMTSLMalkgcspelqqkfrset 162
Cdd:cd05324   81 ILVNNAGIAFKGFDDsTPTREQARETMKTNFFGTVDVTQALLPLLKKspAGRIVNVSSGLGSL----------------- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259 163 iteeelvglmnkfvedtknkvhekegwpSSAYGVSKIGVTVLSRIHARKLSEerggDKILLNACCPGWVRTDMAGPSATK 242
Cdd:cd05324  144 ----------------------------TSAYGVSKAALNALTRILAKELKE----TGIKVNACCPGWVKTDMGGGKAPK 191

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 512960259 243 SPEEGAETPIYLALLPPDSrGPHGQFVQEKRVEQW 277
Cdd:cd05324  192 TPEEGAETPVYLALLPPDG-EPTGKFFSDKKVVPW 225

Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. 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, 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 512960259   6 RVALVTGANKGIGFAITRDLCRRFSGDVVLTARDEARGRAAVQQLQAEGLSPRFHQLDIDDLQSIRAVRDFLRKEYGGLD 85
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259  86 VLINNAGIAFKMADP-TPFHIQAEVTIKTNFYGTRDVCTELLPLIKP--GGRVVNVSSMTSLMalkgcspelqqkfrset 162
Cdd:cd05324   81 ILVNNAGIAFKGFDDsTPTREQARETMKTNFFGTVDVTQALLPLLKKspAGRIVNVSSGLGSL----------------- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259 163 iteeelvglmnkfvedtknkvhekegwpSSAYGVSKIGVTVLSRIHARKLSEerggDKILLNACCPGWVRTDMAGPSATK 242
Cdd:cd05324  144 ----------------------------TSAYGVSKAALNALTRILAKELKE----TGIKVNACCPGWVKTDMGGGKAPK 191

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 512960259 243 SPEEGAETPIYLALLPPDSrGPHGQFVQEKRVEQW 277
Cdd:cd05324  192 TPEEGAETPVYLALLPPDG-EPTGKFFSDKKVVPW 225

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259    6 RVALVTGANKGIGFAItrdlCRRFS---GDVVLTARDEARGRAAVQQLQAEGLSPRFHQLDIDDLQSIRAVRDFLRKEYG 82
Cdd:pfam00106   1 KVALVTGASSGIGRAI----AKRLAkegAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259   83 GLDVLINNAGIafkmADPTPFHIQAEV----TIKTNFYGTRDVCTELLPLIK--PGGRVVNVSSMTSLMalkgcspelqq 156
Cdd:pfam00106  77 RLDILVNNAGI----TGLGPFSELSDEdwerVIDVNLTGVFNLTRAVLPAMIkgSGGRIVNISSVAGLV----------- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259  157 kfrsetiteeelvglmnkfvedtknkvhekeGWPS-SAYGVSKIGVTVLSrihaRKLSEERGGDKILLNACCPGWVRTDM 235
Cdd:pfam00106 142 -------------------------------PYPGgSAYSASKAAVIGFT----RSLALELAPHGIRVNAVAPGGVDTDM 186

                  ...
gi 512960259  236 AGP 238
Cdd:pfam00106 187 TKE 189

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259     9 LVTGANKGIGFAITRDLCRRFSGDVVLTAR---DEARGRAAVQQLQAEGLSPRFHQLDIDDLQSIRAVRDFLRKEYGGLD 85
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGARRLVLLSRsgpDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLT 83

                   ....*...
gi 512960259    86 VLINNAGI 93
Cdd:smart00822  84 GVIHAAGV 91

Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. 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, 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 512960259   6 RVALVTGANKGIGFAITRDLCRRFSGDVVLTARDEARGRAAVQQLQAEGLSPRFHQLDIDDLQSIRAVRDFLRKEYGGLD 85
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259  86 VLINNAGIAFKMADP-TPFHIQAEVTIKTNFYGTRDVCTELLPLIKP--GGRVVNVSSMTSLMalkgcspelqqkfrset 162
Cdd:cd05324   81 ILVNNAGIAFKGFDDsTPTREQARETMKTNFFGTVDVTQALLPLLKKspAGRIVNVSSGLGSL----------------- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259 163 iteeelvglmnkfvedtknkvhekegwpSSAYGVSKIGVTVLSRIHARKLSEerggDKILLNACCPGWVRTDMAGPSATK 242
Cdd:cd05324  144 ----------------------------TSAYGVSKAALNALTRILAKELKE----TGIKVNACCPGWVKTDMGGGKAPK 191

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 512960259 243 SPEEGAETPIYLALLPPDSrGPHGQFVQEKRVEQW 277
Cdd:cd05324  192 TPEEGAETPVYLALLPPDG-EPTGKFFSDKKVVPW 225

classical (c) 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 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 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 512960259   8 ALVTGANKGIGFAITRDLCRRfSGDVVLTARDEARGRAAVQqLQAEGLSPRFHQLDIDDLQSIRAVRDFLRKEYGGLDVL 87
Cdd:cd05233    1 ALVTGASSGIGRAIARRLARE-GAKVVLADRNEEALAELAA-IEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDIL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259  88 INNAGIAFkmaDPTPFHIQAEV---TIKTNFYGTRDVCTELLPLIK--PGGRVVNVSSMTSLMALKGcspelqqkfrset 162
Cdd:cd05233   79 VNNAGIAR---PGPLEELTDEDwdrVLDVNLTGVFLLTRAALPHMKkqGGGRIVNISSVAGLRPLPG------------- 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259 163 iteeelvglmnkfvedtknkvhekegwpSSAYGVSKIGVTVLSRIharkLSEERGGDKILLNACCPGWVRTDMAGPSATK 242
Cdd:cd05233  143 ----------------------------QAAYAASKAALEGLTRS----LALELAPYGIRVNAVAPGLVDTPMLAKLGPE 190

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 512960259 243 ----------------SPEEGAETpiYLALLPPDSRGPHGQFV 269
Cdd:cd05233  191 eaekelaaaiplgrlgTPEEVAEA--VVFLASDEASYITGQVI 231

retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and related proteins, classical (c) SDRs; Classical SDR subgroup containing retinol-DHs, LPORs, and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Pchlide reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14, dehydrogenase/reductase SDR family member (DHRS)-12 , -13 and -X (a DHRS on chromosome X), and WWOX (WW domain-containing oxidoreductase), as well as a Neurospora crassa SDR encoded by the blue light inducible bli-4 gene. 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 512960259   6 RVALVTGANKGIGFAITRDLCRRfSGDVVLTARDEARGRAAVQQLQAEGLSPR--FHQLDIDDLQSIRAVRDFLRKEYGG 83
Cdd:cd05327    2 KVVVITGANSGIGKETARELAKR-GAHVIIACRNEEKGEEAAAEIKKETGNAKveVIQLDLSSLASVRQFAEEFLARFPR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259  84 LDVLINNAGIafkMAdpTPFHIQA---EVTIKTNFYGTRDVCTELLPLIK--PGGRVVNVSSMTSLMAlkgcspelqqkf 158
Cdd:cd05327   81 LDILINNAGI---MA--PPRRLTKdgfELQFAVNYLGHFLLTNLLLPVLKasAPSRIVNVSSIAHRAG------------ 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259 159 rsetiteeelvglmnKFVEDTKNKVHEKEGWPSSAYGVSKigvtvLSRI-HARKLSEERGGDKILLNACCPGWVRTDM-- 235
Cdd:cd05327  144 ---------------PIDFNDLDLENNKEYSPYKAYGQSK-----LANIlFTRELARRLEGTGVTVNALHPGVVRTELlr 203

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 512960259 236 -----------AGPSATKSPEEGAETPIYLALLPPDSRGPHGQFVQEKRVE 275
Cdd:cd05327  204 rngsffllyklLRPFLKKSPEQGAQTALYAATSPELEGVSGKYFSDCKIKM 254

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259   1 MSSCSRVALVTGANKGIGFAITRDLCRRfsG-DVVLTARDEARGRAAVQQLqaeGLSPRFHQLDIDDLQSIRAVRDFLRK 79
Cdd:COG4221    1 MSDKGKVALITGASSGIGAATARALAAA--GaRVVLAARRAERLEALAAEL---GGRALAVPLDVTDEAAVEAAVAAAVA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259  80 EYGGLDVLINNAGIA----FKMADPTPFHIQAEVTIKTNFYGTRdvctELLPLIKP--GGRVVNVSSMTSLMALKGcspe 153
Cdd:COG4221   76 EFGRLDVLVNNAGVAllgpLEELDPEDWDRMIDVNVKGVLYVTR----AALPAMRArgSGHIVNISSIAGLRPYPG---- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259 154 lqqkfrsetiteeelvglmnkfvedtknkvhekegwpSSAYGVSKIGVTVLSRIharkLSEERGGDKILLNACCPGWVRT 233
Cdd:COG4221  148 -------------------------------------GAVYAATKAAVRGLSES----LRAELRPTGIRVTVIEPGAVDT 186

                        250       260
                 ....*....|....*....|....*..
gi 512960259 234 DMAGPSATKSPEEGAETPIYLALLPPD 260
Cdd:COG4221  187 EFLDSVFDGDAEAAAAVYEGLEPLTPE 213

3-oxoacyl-ACP reductase FabG;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259   5 SRVALVTGANKGIGFAITRDLCRRfsG-DVVLTARDEARGRAAVQQLQAEGLSPRFHQLDIDDLQSIRAVRDFLRKEYGG 83
Cdd:PRK05653   5 GKTALVTGASRGIGRAIALRLAAD--GaKVVIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAVEAFGA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259  84 LDVLINNAGIafkmADPTPFH-IQAE---VTIKTNFYGTRDVCTELLP-LIKPG-GRVVNVSSMtslmalkgcspelqqk 157
Cdd:PRK05653  83 LDILVNNAGI----TRDALLPrMSEEdwdRVIDVNLTGTFNVVRAALPpMIKARyGRIVNISSV---------------- 142

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512960259 158 frsetiteeelVGLMnkfvedtknkvhekeGWP-SSAYGVSKIGVTVLSrihaRKLSEERGGDKILLNACCPGWVRTDM 235
Cdd:PRK05653 143 -----------SGVT---------------GNPgQTNYSAAKAGVIGFT----KALALELASRGITVNAVAPGFIDTDM 191

carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl reductase of the classical SDR family. Studies in Drosophila melanogaster implicate Sniffer in the prevention of neurodegeneration due to aging and oxidative-stress. This subgroup also includes Rhodococcus sp. AD45 IsoH, which is an NAD-dependent 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase involved in isoprene metabolism, Aspergillus nidulans StcE encoded by a gene which is part of a proposed sterigmatocystin biosynthesis gene cluster, Bacillus circulans SANK 72073 BtrF encoded by a gene found in the butirosin biosynthesis gene cluster, and Aspergillus parasiticus nor-1 involved in the biosynthesis of aflatoxins. 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 512960259   8 ALVTGANKGIGFAITRDLCRRFSGDVVLTARDeARGRAAVQQLQAEGLSPRFHQLDIDDL--QSIRAVRDFLRKeyGGLD 85
Cdd:cd05325    1 VLITGASRGIGLELVRQLLARGNNTVIATCRD-PSAATELAALGASHSRLHILELDVTDEiaESAEAVAERLGD--AGLD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259  86 VLINNAGIAFKM-ADPTPFHIQAEVTIKTNFYGTRDVCTELLPLIKPGGR--VVNVSS-MTSLmalkgcspelqqkfrse 161
Cdd:cd05325   78 VLINNAGILHSYgPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARakIINISSrVGSI----------------- 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259 162 titeeelvGLMNKFvedtknkvhekegwPSSAYGVSKIGVTVLSrihaRKLSEERGGDKILLNACCPGWVRTDMAGPSA- 240
Cdd:cd05325  141 --------GDNTSG--------------GWYSYRASKAALNMLT----KSLAVELKRDGITVVSLHPGWVRTDMGGPFAk 194

                        250
                 ....*....|..
gi 512960259 241 ---TKSPEEGAE 249
Cdd:cd05325  195 nkgPITPEESVA 206

SDR family oxidoreductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259   6 RVALVTGANKGIGFAITRDLCRRfSGDVVLTARDEARGRAAVQQLQAEGLSpRFHQLDIDDLQSIRAVRDFLRKEYGGLD 85
Cdd:PRK07231   6 KVAIVTGASSGIGEGIARRFAAE-GARVVVTDRNEEAAERVAAEILAGGRA-IAVAADVSDEADVEAAVAAALERFGSVD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259  86 VLINNAGIAFK---MADPTP--FHIQAEVTIKTNFYGTRdvctELLPLIKP--GGRVVNVSSMTSLMAlkgcSPELqqkf 158
Cdd:PRK07231  84 ILVNNAGTTHRngpLLDVDEaeFDRIFAVNVKSPYLWTQ----AAVPAMRGegGGAIVNVASTAGLRP----RPGL---- 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512960259 159 rsetiteeelvglmnkfvedtknkvhekeGWpssaYGVSKIGVTVLSRIHARKLseerGGDKILLNACCPGWVRTDMA 236
Cdd:PRK07231 152 -----------------------------GW----YNASKGAVITLTKALAAEL----GPDKIRVNAVAPVVVETGLL 192

SDR family oxidoreductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259   5 SRVALVTGANKGIGFAITRDLCRRfSGDVVLTARDEARGRAAVQQLQAEGLSPRFHQLDIDDLQSIRAVRDFLRKEYGGL 84
Cdd:PRK12826   6 GRVALVTGAARGIGRAIAVRLAAD-GAEVIVVDICGDDAAATAELVEAAGGKARARQVDVRDRAALKAAVAAGVEDFGRL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259  85 DVLINNAGIA----FKMADPTpfhiQAEVTIKTNFYGTRDVCTELLPLIKP--GGRVVNVSSMTSL-MALKGcspelqqk 157
Cdd:PRK12826  85 DILVANAGIFpltpFAEMDDE----QWERVIDVNLTGTFLLTQAALPALIRagGGRIVLTSSVAGPrVGYPG-------- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259 158 frsetiteeelvglmnkfvedtknkvhekegwpSSAYGVSKIGVTVLsrihARKLSEERGGDKILLNACCPGWVRTDMAG 237
Cdd:PRK12826 153 ---------------------------------LAHYAASKAGLVGF----TRALALELAARNITVNSVHPGGVDTPMAG 195

                 .
gi 512960259 238 P 238
Cdd:PRK12826 196 N 196

short chain dehydrogenase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259   1 MSSCSRVALVTGANKGIGFAITRDLCRRFSGDVVLTARDEARGRAAVQQLQAEGLSPRFHQLDIDDLQSIRAVRDFLRKE 80
Cdd:PRK12937   1 MTLSNKVAIVTGASRGIGAAIARRLAADGFAVAVNYAGSAAAADELVAEIEAAGGRAIAVQADVADAAAVTRLFDAAETA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259  81 YGGLDVLINNAGIaFKMADPTPFHIQA-EVTIKTNFYGTRDVCTELLPLIKPGGRVVNVSsmTSLMALKgcspelqqkfr 159
Cdd:PRK12937  81 FGRIDVLVNNAGV-MPLGTIADFDLEDfDRTIATNLRGAFVVLREAARHLGQGGRIINLS--TSVIALP----------- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259 160 setiteeelvglmnkfvedtknkvhekegWPS-SAYGVSKIGVTVLSRIharkLSEERGGDKILLNACCPGWVRTDM--A 236
Cdd:PRK12937 147 -----------------------------LPGyGPYAASKAAVEGLVHV----LANELRGRGITVNAVAPGPVATELffN 193

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 512960259 237 GPSATK--------------SPEEGAETPIYLAllppdsrGPHGQFV 269
Cdd:PRK12937 194 GKSAEQidqlaglaplerlgTPEEIAAAVAFLA-------GPDGAWV 233

d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, catalyzes the interconversion of D-3-hydroxybutyrate and acetoacetate. It is a classical SDR, with the canonical NAD-binding motif and active site tetrad. 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 512960259   6 RVALVTGANKGIGFAITRDLCRRfSGDVVLTA-RDEARGRAAVQQLQAE-GLSPRFHQLDIDDLQSIRAVRDFLRKEYGG 83
Cdd:cd08940    3 KVALVTGSTSGIGLGIARALAAA-GANIVLNGfGDAAEIEAVRAGLAAKhGVKVLYHGADLSKPAAIEDMVAYAQRQFGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259  84 LDVLINNAGIAFkMADPTPFHI-QAEVTIKTN----FYGTRDVctelLPLIKPG--GRVVNVSSMTSlmalkgcspelqq 156
Cdd:cd08940   82 VDILVNNAGIQH-VAPIEDFPTeKWDAIIALNlsavFHTTRLA----LPHMKKQgwGRIINIASVHG------------- 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512960259 157 kfrsetiteeeLVGLMNKfvedtknkvhekegwpsSAYGVSKIGVTVLSRIHARklseERGGDKILLNACCPGWVRTDM 235
Cdd:cd08940  144 -----------LVASANK-----------------SAYVAAKHGVVGLTKVVAL----ETAGTGVTCNAICPGWVLTPL 190

gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. 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 512960259   6 RVALVTGANKGIGFAITRDLcRRFSGDVVLTARDEARGRAAVQQLQAEGLSPRFHQLDIDDLQSIRAVRDFLRKEYGGLD 85
Cdd:cd05347    6 KVALVTGASRGIGFGIASGL-AEAGANIVINSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDFGKID 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259  86 VLINNAGIA-------FKMADptpFHIQAEVTIKTNFYGTRDVCTELLPliKPGGRVVNVSSMTSlmalkgcspelqqkf 158
Cdd:cd05347   85 ILVNNAGIIrrhpaeeFPEAE---WRDVIDVNLNGVFFVSQAVARHMIK--QGHGKIINICSLLS--------------- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259 159 rsetiteeELVGLmnkfvedtknkvhekegwPSSAYGVSKIGVTVLSRIharkLSEERGGDKILLNACCPGWVRTDMAGP 238
Cdd:cd05347  145 --------ELGGP------------------PVPAYAASKGGVAGLTKA----LATEWARHGIQVNAIAPGYFATEMTEA 194

                 .
gi 512960259 239 S 239
Cdd:cd05347  195 V 195

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259   6 RVALVTGANKGIGFAITRDLCRRfSGDVVLTARDEARGRAAVQQLQAEGLSPRFHQLDIDDLQSIRAVRDFLRKEYGGLD 85
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAE-GAKVAVTDRSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFGPVD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259  86 VLINNAGI-----AFKMADPtpfhiQAEVTIKTN----FYGTRDVcteLLPLIKPG-GRVVNVSSmtslmalkgcspelq 155
Cdd:cd05333   80 ILVNNAGItrdnlLMRMSEE-----DWDAVINVNltgvFNVTQAV---IRAMIKRRsGRIINISS--------------- 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512960259 156 qkfrsetiteeeLVGLMnkfvedtknkvhekeGWPSSA-YGVSKIGVTVLSRIHARKLSeERGgdkILLNACCPGWVRTD 234
Cdd:cd05333  137 ------------VVGLI---------------GNPGQAnYAASKAGVIGFTKSLAKELA-SRG---ITVNAVAPGFIDTD 185