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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A        5 HVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 84
Cdd:cd05324   1 KVALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A       85 VLVNNAGIAFKVADP-TPFHIQAEVTMKTNFFGTRDVCTELLPLIKP--QGRVVNVSSIMSVRalkscspelqqkfrset 161
Cdd:cd05324  81 ILVNNAGIAFKGFDDsTPTREQARETMKTNFFGTVDVTQALLPLLKKspAGRIVNVSSGLGSL----------------- 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A      162 iteeelvglmnkfvedtkkgvhqkegwpSSAYGVTKIGVTVLSRIHARKLSEqrkgDKILLNACCPGWVRTDMAGPKATK 241
Cdd:cd05324 144 ----------------------------TSAYGVSKAALNALTRILAKELKE----TGIKVNACCPGWVKTDMGGGKAPK 191

                       250       260       270
                ....*....|....*....|....*....|....*
3BHJ_A      242 SPEEGAETPVYLALLPPDAEgPHGQFVSEKRVEQW 276
Cdd:cd05324 192 TPEEGAETPVYLALLPPDGE-PTGKFFSDKKVVPW 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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A        5 HVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 84
Cdd:cd05324   1 KVALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A       85 VLVNNAGIAFKVADP-TPFHIQAEVTMKTNFFGTRDVCTELLPLIKP--QGRVVNVSSIMSVRalkscspelqqkfrset 161
Cdd:cd05324  81 ILVNNAGIAFKGFDDsTPTREQARETMKTNFFGTVDVTQALLPLLKKspAGRIVNVSSGLGSL----------------- 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A      162 iteeelvglmnkfvedtkkgvhqkegwpSSAYGVTKIGVTVLSRIHARKLSEqrkgDKILLNACCPGWVRTDMAGPKATK 241
Cdd:cd05324 144 ----------------------------TSAYGVSKAALNALTRILAKELKE----TGIKVNACCPGWVKTDMGGGKAPK 191

                       250       260       270
                ....*....|....*....|....*....|....*
3BHJ_A      242 SPEEGAETPVYLALLPPDAEgPHGQFVSEKRVEQW 276
Cdd:cd05324 192 TPEEGAETPVYLALLPPDGE-PTGKFFSDKKVVPW 225

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A          6 VALVTGGNKGIGLAIVRdlcRLFS--GDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 83
Cdd:pfam00106   2 VALVTGASSGIGRAIAK---RLAKegAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A         84 DVLVNNAGIafkvADPTPFHIQAEV----TMKTNFFGTRDVCTELLPLIK--PQGRVVNVSSImsvralkscspelqqkf 157
Cdd:pfam00106  79 DILVNNAGI----TGLGPFSELSDEdwerVIDVNLTGVFNLTRAVLPAMIkgSGGRIVNISSV----------------- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A        158 rsetiteeelVGLMnkfvedtkkgvhqkeGWPS-SAYGVTKIGVTVLSRIHARKLSEqrkgDKILLNACCPGWVRTDMAG 236
Cdd:pfam00106 138 ----------AGLV---------------PYPGgSAYSASKAAVIGFTRSLALELAP----HGIRVNAVAPGGVDTDMTK 188

                  ..
3BHJ_A        237 PK 238
Cdd:pfam00106 189 EL 190

3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, also called 3-ketoacyl-acyl carrier protein reductase, an enzyme of fatty acid biosynthesis. [Fatty acid and phospholipid metabolism, Biosynthesis]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A          7 ALVTGGNKGIGLAIVRDLCRLFSgDVVLT-ARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 85
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGA-KVIITyRSSEEGAEEVVEELKALGVKALGVVLDVSDREDVKAVVEEIEEELGTIDI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A         86 LVNNAGI-----AFKVADPtpfhiQAEVTMKTNFFGTRDVCTELL-PLIKP-QGRVVNVSSImsvralkscspelqqkfr 158
Cdd:TIGR01830  80 LVNNAGItrdnlLMRMKEE-----DWDAVIDTNLTGVFNLTQAVLrIMIKQrSGRIINISSV------------------ 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3BHJ_A        159 setiteeelVGLMnkfvedtkkgvhqkeGWPSSA-YGVTKIGVTVLSRIHARKLSeqRKGdkILLNACCPGWVRTDM 234
Cdd:TIGR01830 137 ---------VGLM---------------GNAGQAnYAASKAGVIGFTKSLAKELA--SRN--ITVNAVAPGFIDTDM 185

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A        5 HVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 84
Cdd:cd05324   1 KVALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A       85 VLVNNAGIAFKVADP-TPFHIQAEVTMKTNFFGTRDVCTELLPLIKP--QGRVVNVSSIMSVRalkscspelqqkfrset 161
Cdd:cd05324  81 ILVNNAGIAFKGFDDsTPTREQARETMKTNFFGTVDVTQALLPLLKKspAGRIVNVSSGLGSL----------------- 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A      162 iteeelvglmnkfvedtkkgvhqkegwpSSAYGVTKIGVTVLSRIHARKLSEqrkgDKILLNACCPGWVRTDMAGPKATK 241
Cdd:cd05324 144 ----------------------------TSAYGVSKAALNALTRILAKELKE----TGIKVNACCPGWVKTDMGGGKAPK 191

                       250       260       270
                ....*....|....*....|....*....|....*
3BHJ_A      242 SPEEGAETPVYLALLPPDAEgPHGQFVSEKRVEQW 276
Cdd:cd05324 192 TPEEGAETPVYLALLPPDGE-PTGKFFSDKKVVPW 225

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A        6 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 84
Cdd:COG1028   8 VALVTGGSSGIGRAIARALAA--EGaRVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAFGRLD 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A       85 VLVNNAGIafkvADPTPFH-IQAEV---TMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSIMSVRALKscspelqqkfr 158
Cdd:COG1028  86 ILVNNAGI----TPPGPLEeLTEEDwdrVLDVNLKGPFLLTRAALPHMRERggGRIVNISSIAGLRGSP----------- 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A      159 setiteeelvglmnkfvedtkkgvhqkeGWpsSAYGVTKIGVTVLSRIHARKLseqrKGDKILLNACCPGWVRTDMAGPK 238
Cdd:COG1028 151 ----------------------------GQ--AAYAASKAAVVGLTRSLALEL----APRGIRVNAVAPGPIDTPMTRAL 196

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
3BHJ_A      239 ATK-----------------SPEEGAEtpVYLALLPPDAEGPHGQFV 268
Cdd:COG1028 197 LGAeevrealaariplgrlgTPEEVAA--AVLFLASDAASYITGQVL 241

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A        6 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLSPR--FHQLDIDDLQSIRALRDFLRKEYGGL 83
Cdd:cd05327   3 VVVITGANSGIGKETARELAKR-GAHVIIACRNEEKGEEAAAEIKKETGNAKveVIQLDLSSLASVRQFAEEFLARFPRL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A       84 DVLVNNAGIAFKVADPTPFHIqaEVTMKTNFFGTRDVCTELLPLIK--PQGRVVNVSSIMSVRALKScspelqqkfrset 161
Cdd:cd05327  82 DILINNAGIMAPPRRLTKDGF--ELQFAVNYLGHFLLTNLLLPVLKasAPSRIVNVSSIAHRAGPID------------- 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A      162 iteeelvglmnkFVEDTKKGVHQKEGWPssAYGVTKigvtvLSRI-HARKLSEQRKGDKILLNACCPGWVRTDM------ 234
Cdd:cd05327 147 ------------FNDLDLENNKEYSPYK--AYGQSK-----LANIlFTRELARRLEGTGVTVNALHPGVVRTELlrrngs 207

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
3BHJ_A      235 -------AGPKATKSPEEGAETPVYLALLpPDAEGPHGQFVSEKRVEQW 276
Cdd:cd05327 208 ffllyklLRPFLKKSPEQGAQTALYAATS-PELEGVSGKYFSDCKIKMS 255

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A        6 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVTRGQAAVQQLqaeGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 84
Cdd:COG4221   7 VALITGASSGIGAATARALAA--AGaRVVLAARRAERLEALAAEL---GGRALAVPLDVTDEAAVEAAVAAAVAEFGRLD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A       85 VLVNNAGIAF--KVADPTPFHIQAevTMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSIMSVRALkscspelqqkfrse 160
Cdd:COG4221  82 VLVNNAGVALlgPLEELDPEDWDR--MIDVNVKGVLYVTRAALPAMRARgsGHIVNISSIAGLRPY-------------- 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A      161 titeeelvglmnkfvedtkkgvhqkEGWpsSAYGVTKIGVTVLSRIharkLSEQRKGDKILLNACCPGWVRTDMAG---- 236
Cdd:COG4221 146 -------------------------PGG--AVYAATKAAVRGLSES----LRAELRPTGIRVTVIEPGAVDTEFLDsvfd 194

                       250       260       270
                ....*....|....*....|....*....|....*
3BHJ_A      237 ---PKATK--------SPEEGAETPVYLALLPPDA 260
Cdd:COG4221 195 gdaEAAAAvyegleplTPEDVAEAVLFALTQPAHV 229

Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A        8 LVTGGNKGIGLAIVRDLCRLfsG-DVVLTARDvtrgQAAVQQLQAEglSPRFH--QLDIDDLQSIRALRDFLRKEYGGLD 84
Cdd:COG3967   9 LITGGTSGIGLALAKRLHAR--GnTVIITGRR----EEKLEEAAAA--NPGLHtiVLDVADPASIAALAEQVTAEFPDLN 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A       85 VLVNNAGI--AFKVADPTPFHIQAEVTMKTNFFGTRDVCTELLPLIK--PQGRVVNVSSI 140
Cdd:COG3967  81 VLINNAGImrAEDLLDEAEDLADAEREITTNLLGPIRLTAAFLPHLKaqPEAAIVNVSSG 140

SDR family oxidoreductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A         5 HVALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVTRGQAAVQQLQAEGLSpRFHQLDIDDLQSIRALRDFLRKEYGGL 83
Cdd:PRK07231   6 KVAIVTGASSGIGEGIARRFAA--EGaRVVVTDRNEEAAERVAAEILAGGRA-IAVAADVSDEADVEAAVAAALERFGSV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A        84 DVLVNNAGI--AFKV---ADPTPFHIQAEVTMKTNFFGTRdvctELLPLIKPQ--GRVVNVSSIMSVRAlkscSPELqqk 156
Cdd:PRK07231  83 DILVNNAGTthRNGPlldVDEAEFDRIFAVNVKSPYLWTQ----AAVPAMRGEggGAIVNVASTAGLRP----RPGL--- 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
3BHJ_A       157 frsetiteeelvglmnkfvedtkkgvhqkeGWpssaYGVTKIGVTVLSRIHARKLSEqrkgDKILLNACCPGWVRTDMA 235
Cdd:PRK07231 152 ------------------------------GW----YNASKGAVITLTKALAAELGP----DKIRVNAVAPVVVETGLL 192

Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) reductases.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A         13 NKGIGLAIVRDLCRlfSG-DVVLTARDvTRGQAAVQQLqAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVLVNNAG 91
Cdd:pfam13561   5 ESGIGWAIARALAE--EGaEVVLTDLN-EALAKRVEEL-AEELGAAVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A         92 IAFKVAdpTPFH-IQAE---VTMKTNFFGTRDVCTELLPLIKPQGRVVNVSSIMSVRAlkscspelqqkfrsetiteeel 167
Cdd:pfam13561  81 FAPKLK--GPFLdTSREdfdRALDVNLYSLFLLAKAALPLMKEGGSIVNLSSIGAERV---------------------- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A        168 vglmnkfvedtkkgvhqkegWP-SSAYGVTKIGVTVLSRIHARKLSEQrkgdKILLNACCPGWVRTDMA-----GPKATK 241
Cdd:pfam13561 137 --------------------VPnYNAYGAAKAALEALTRYLAVELGPR----GIRVNAISPGPIKTLAAsgipgFDELLA 192

                         250       260
                  ....*....|....*....|....*
3BHJ_A        242 ------------SPEEGAETPVYLA 254
Cdd:pfam13561 193 aaearaplgrlgTPEEVANAAAFLA 217

SDR family oxidoreductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A         6 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 84
Cdd:PRK12826   8 VALVTGAARGIGRAIAVRLAA--DGaEVIVVDICGDDAAATAELVEAAGGKARARQVDVRDRAALKAAVAAGVEDFGRLD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A        85 VLVNNAGIafkvADPTPFHI----QAEVTMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSIMSVRAlkscspelqqkfr 158
Cdd:PRK12826  86 ILVANAGI----FPLTPFAEmddeQWERVIDVNLTGTFLLTQAALPALIRAggGRIVLTSSVAGPRV------------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A       159 setiteeelvglmnkfvedtkkgvhqkeGWP-SSAYGVTKIGVTVLSRIHARKLSEqrkgDKILLNACCPGWVRTDMAGP 237
Cdd:PRK12826 149 ----------------------------GYPgLAHYAASKAGLVGFTRALALELAA----RNITVNSVHPGGVDTPMAGN 196

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A        6 VALVTGGNKGIGLAIVRDLCRlFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 85
Cdd:cd05347   7 VALVTGASRGIGFGIASGLAE-AGANIVINSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDFGKIDI 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A       86 LVNNAGIAfKVADPTPFHIQA-EVTMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSIMSvralkscspelqqkfrseti 162
Cdd:cd05347  86 LVNNAGII-RRHPAEEFPEAEwRDVIDVNLNGVFFVSQAVARHMIKQghGKIINICSLLS-------------------- 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A      163 teeELVGLmnkfvedtkkgvhqkegwPSSAYGVTKIGVTVLSRIHARKLSEqrkgDKILLNACCPGWVRTDMAgpKATKS 242
Cdd:cd05347 145 ---ELGGP------------------PVPAYAASKGGVAGLTKALATEWAR----HGIQVNAIAPGYFATEMT--EAVVA 197

                ....*.
3BHJ_A      243 PEEGAE 248
Cdd:cd05347 198 DPEFND 203

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) SDR; This subgroup includes Escherichia coli CFT073 FabG. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. 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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A        6 VALVTGGNKGIGLAIVRDLCRlfSGDVVLTARDVTRGQAA--VQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 83
Cdd:cd05337   3 VAIVTGASRGIGRAIATELAA--RGFDIAINDLPDDDQATevVAEVLAAGRRAIYFQADIGELSDHEALLDQAWEDFGRL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A       84 DVLVNNAGIAFKV------ADPTPFHIQAEVTMKTNFFGTRDVCTELL----PLIKPQGRVVNVSSIMSVRAlkscSPEl 153
Cdd:cd05337  81 DCLVNNAGIAVRPrgdlldLTEDSFDRLIAINLRGPFFLTQAVARRMVeqpdRFDGPHRSIIFVTSINAYLV----SPN- 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A      154 qqkfRSEtiteeelvglmnkfvedtkkgvhqkegwpssaYGVTKIGVTVLSRIHARKLSEqrkgDKILLNACCPGWVRTD 233
Cdd:cd05337 156 ----RGE--------------------------------YCISKAGLSMATRLLAYRLAD----EGIAVHEIRPGLIHTD 195

                ....
3BHJ_A      234 MAGP 237
Cdd:cd05337 196 MTAP 199

short chain dehydrogenase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A         6 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLT-ARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 83
Cdd:PRK12937   7 VAIVTGASRGIGAAIARRLAA--DGfAVAVNyAGSAAAADELVAEIEAAGGRAIAVQADVADAAAVTRLFDAAETAFGRI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A        84 DVLVNNAGIAF--KVADptpFHIQA-EVTMKTNFFGTRDVCTELLPLIKPQGRVVNVSSimSVRALKscspelqqkfrse 160
Cdd:PRK12937  85 DVLVNNAGVMPlgTIAD---FDLEDfDRTIATNLRGAFVVLREAARHLGQGGRIINLST--SVIALP------------- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A       161 titeeelvglmnkfvedtkkgvhqkegWPS-SAYGVTKIGVTVLSRIHARKLseqrKGDKILLNACCPGWVRTDM----- 234
Cdd:PRK12937 147 ---------------------------LPGyGPYAASKAAVEGLVHVLANEL----RGRGITVNAVAPGPVATELffngk 195

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
3BHJ_A       235 AGPKATK-----------SPEEGAETPVYLAllppdaeGPHGQFVS 269
Cdd:PRK12937 196 SAEQIDQlaglaplerlgTPEEIAAAVAFLA-------GPDGAWVN 234

3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes members identified as 3beta17beta hydroxysteroid dehydrogenase, 20beta hydroxysteroid dehydrogenase, and R-alcohol dehydrogenase. These proteins exhibit the canonical active site tetrad and glycine rich NAD(P)-binding motif of the classical SDRs. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. 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 have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. 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 and Lys, as well as Asn (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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A        6 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLqaeGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 85
Cdd:cd05341   7 VAIVTGGARGLGLAHARLLVAE-GAKVVLSDILDEEGQAAAAEL---GDAARFFHLDVTDEDGWTAVVDTAREAFGRLDV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A       86 LVNNAGIAfkvadpTPFHIQAEV------TMKTN----FFGTRDVctelLPLIKPQGR--VVNVSSImsvralkscspel 153
Cdd:cd05341  83 LVNNAGIL------TGGTVETTTleewrrLLDINltgvFLGTRAV----IPPMKEAGGgsIINMSSI------------- 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BHJ_A      154 qqkfrsetiteEELVGLMNkfvedtkkgvhqkegwpSSAYGVTKIGVTVLSRIHARKLSEQrkGDKILLNACCPGWVRTD 233
Cdd:cd05341 140 -----------EGLVGDPA-----------------LAAYNASKGAVRGLTKSAALECATQ--GYGIRVNSVHPGYIYTP 189

                       250
                ....*....|....*....
3BHJ_A      234 M--AGPKATKSPEEGAETP 250
Cdd:cd05341 190 MtdELLIAQGEMGNYPNTP 208

HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC 7120 HetN, a putative oxidoreductase involved in heterocyst differentiation, and related proteins. 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.