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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2252308999  11 EELLGKLEKQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGGLS 59
Cdd:pfam13561 188 DELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGYT 236

xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins identified as L-xylulose reductase (XR) and carbonyl reductase; they are members of the SDR family. XR, catalyzes the NADP-dependent reduction of L-xyulose and other sugars. Tetrameric mouse carbonyl reductase is involved in the metabolism of biogenic and xenobiotic carbonyl compounds. This subgroup also includes tetrameric chicken liver D-erythrulose reductase, which catalyzes the reduction of D-erythrulose to D-threitol. 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).

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2252308999  15 GKLEKQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGGLSA 60
Cdd:cd05351   198 KKMLNRIPLGKFAEVEDVVNAILFLLSDKSSMTTGSTLPVDGGFLA 243

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2252308999  11 EELLGKLEKQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGGLS 59
Cdd:pfam13561 188 DELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGYT 236

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2252308999   1 MMQAFFENasEELLGKLEKQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGGLSA 60
Cdd:COG1028   192 MTRALLGA--EEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQVLAVDGGLTA 249

short chain dehydrogenase; Provisional

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2252308999  17 LEKQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGGLSAQ 61
Cdd:PRK06841  211 AKKLIPAGRFAYPEEIAAAALFLASDAAAMITGENLVIDGGYTIQ 255

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) SDR; This subgroup includes the putative Brucella melitensis biovar Abortus 2308 BKR, FabG, Mesorhizobium loti MAFF303099 FabG, and other classical SDRs. BKR, a member of the SDR family, catalyzes the NADPH-dependent reduction of acyl carrier protein in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of 4 elongation steps, which are repeated to extend the fatty acid chain thru the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I Fas utilizes one or 2 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 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
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2252308999   1 MMQAFFENASEELLGKLEKQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGG 57
Cdd:cd05345   189 LLSMFMGEDTPENRAKFRATIPLGRLSTPDDIANAALYLASDEASFITGVALEVDGG 245

3-oxoacyl-ACP reductase FabG;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2252308999   7 ENASEELLGKLEKQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGGLS 59
Cdd:PRK05653  193 EGLPEEVKAEILKEIPLGRLGQPEEVANAVAFLASDAASYITGQVIPVNGGMY 245

SDR family oxidoreductase;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2252308999   7 ENASEELLGKLEKQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGGLS 59
Cdd:PRK06500  195 EATLDAVAAQIQALVPLGRFGTPEEIAKAVLYLASDESAFIVGSEIIVDGGMS 247

short chain dehydrogenase; Provisional

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2252308999  21 IPIRKFAESIDVANGILFLASDESKMITGTELVIDGG 57
Cdd:PRK06523  219 IPLGRPAEPEEVAELIAFLASDRAASITGTEYVIDGG 255

SDR family oxidoreductase;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2252308999   1 MMQAFFENASEELLGKlekQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGG 57
Cdd:PRK12826  193 MAGNLGDAQWAEAIAA---AIPLGRLGEPEDIAAAVLFLASDEARYITGQTLPVDGG 246

enoyl-[acyl-carrier-protein] reductase FabL;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2252308999   5 FFENAsEELLGKLEKQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGGLS 59
Cdd:PRK08063  194 HFPNR-EELLEDARAKTPAGRMVEPEDVANAVLFLCSPEADMIRGQTIIVDGGRS 247

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

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2252308999   6 FENASEELLGKLEKQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGGLSAQ 61
Cdd:PRK05557  193 TDALPEDVKEAILAQIPLGRLGQPEEIASAVAFLASDEAAYITGQTLHVNGGMVMG 248

SDR family oxidoreductase;

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2252308999  22 PIRKFAESIDVANGILFLASDESKMITGTELVIDGGLSAQ 61
Cdd:PRK06138  213 PMNRFGTAEEVAQAALFLASDESSFATGTTLVVDGGWLAA 252

putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) SDR; This subgroup includes Rhizobium sp. NGR234 FabG1. 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 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
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2252308999   7 ENASEELLGKLEKQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGGL 58
Cdd:cd05349   193 AATPKEVFDAIAQTTPLGKVTTPQDIADAVLFFASPWARAVTGQNLVVDGGL 244

SDR family oxidoreductase;

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2252308999  17 LEKQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGGLSA 60
Cdd:PRK07074  200 LKKWYPLQDFATPDDVANAVLFLASPAARAITGVCLPVDGGLTA 243

short chain dehydrogenase; Provisional

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2252308999   9 ASEELLGKLEKQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGGLS 59
Cdd:PRK07576  201 PSPELQAAVAQSVPLKRNGTKQDIANAALFLASDMASYITGVVLPVDGGWS 251

2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 dihydrozybenzoate dehydrogenase shares the characteristics of the classical SDRs. This subgroup includes Escherichai coli EntA which catalyzes the NAD+-dependent oxidation of 2,3-dihydro-2,3-dihydroxybenzoate to 2,3-dihydroxybenzoate during biosynthesis of the siderophore Enterobactin. 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
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2252308999   7 ENASEELL-GKLEK---QIPIRKFAESIDVANGILFLASDESKMITGTELVIDGG 57
Cdd:cd05331   185 EDGAAQVIaGVPEQfrlGIPLGKIAQPADIANAVLFLASDQAGHITMHDLVVDGG 239

classical (c) SDR, subgroup 11; 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
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2252308999   7 ENASEELLGKLEKQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGGLSA 60
Cdd:cd05364   199 EEQYIKFLSRAKETHPLGRPGTVDEVAEAIAFLASDASSFITGQLLPVDGGRHL 252

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
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2252308999   1 MMQAFFEnasEELLGKLEKQIPIRKFAESIDVANGILFLASDESKMITGTELVID 55
Cdd:cd05233   183 MLAKLGP---EEAEKELAAAIPLGRLGTPEEVAEAVVFLASDEASYITGQVIPVD 234

human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are classical SDRs, with a canonical active site tetrad and a close match to the typical Gly-rich NAD-binding motif. Human DHRS6 is a cytosolic type 2 (R)-hydroxybutyrate dehydrogenase, which catalyses the conversion of (R)-hydroxybutyrate to acetoacetate. Also included in this subgroup is Escherichia coli UcpA (upstream cys P). 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. Note: removed : needed to make this chiodl smaller when drew final trees: rmeoved text form description: Other proteins in this subgroup include Thermoplasma acidophilum aldohexose dehydrogenase, which has high dehydrogenase activity against D-mannose, Bacillus subtilis BacC involved in the biosynthesis of the dipeptide bacilysin and its antibiotic moiety anticapsin, Sphingomonas paucimobilis strain B90 LinC, involved in the degradation of hexachlorocyclohexane isomers...... P).

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2252308999  11 EELLGKLEKQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGGLS 59
Cdd:cd05368   192 EEALKAFAARQPLGRLATPEEVAALAVYLASDESAYVTGTAVVIDGGWS 240

secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; Podophyllum secoisolariciresinol-DH is a homo tetrameric, classical SDR that catalyzes the NAD-dependent conversion of (-)-secoisolariciresinol to (-)-matairesinol via a (-)-lactol intermediate. (-)-Matairesinol is an intermediate to various 8'-lignans, including the cancer-preventive mammalian lignan, and those involved in vascular plant defense. This subgroup also includes rice momilactone A synthase which catalyzes the conversion of 3beta-hydroxy-9betaH-pimara-7,15-dien-19,6beta-olide into momilactone A, Arabidopsis ABA2 which during abscisic acid (ABA) biosynthesis, catalyzes the conversion of xanthoxin to abscisic aldehyde and, maize Tasselseed2 which participate in the maize sex determination pathway. 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
                  ....*....|....*....|....*....
gi 2252308999  31 DVANGILFLASDESKMITGTELVIDGGLS 59
Cdd:cd05326   221 DIAAAVLYLASDDSRYVSGQNLVVDGGLT 249

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
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2252308999   6 FENASEELLgkLEKQiPIRKFAESIDVANGILFLASDESKMITGTELVIDGGLSAQ 61
Cdd:cd08940   206 QEQAARELL--LEKQ-PSKQFVTPEQLGDTAVFLASDAASQITGTAVSVDGGWTAQ 258

xanthoxin dehydrogenase

                          10        20        30
                  ....*....|....*....|....*....|
gi 2252308999  31 DVANGILFLASDESKMITGTELVIDGGLSA 60
Cdd:PLN02253  242 DVANAVLFLASDEARYISGLNLMIDGGFTC 271

aldose dehydrogenase; Validated

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2252308999  22 PIRKFAESIDVANGILFLASDESKMITGTELVIDGGLSA 60
Cdd:PRK06398  208 PMKRVGKPEEVAYVVAFLASDLASFITGECVTVDGGLRA 246

Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl-[acyl-carrier-protein] reductase FabI is part of the Pathway/BioSystem: Fatty acid biosynthesis

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2252308999  11 EELLGKLEKQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGGLSA 60
Cdd:COG0623   202 DKLLDYAEERAPLGRNVTIEEVGNAAAFLLSDLASGITGEIIYVDGGYHI 251

short chain dehydrogenase; Provisional

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2252308999   1 MMQAFFENAS-------EELLGKLEKQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGG 57
Cdd:PRK07890  191 PLKGYFRHQAgkygvtvEQIYAETAANSDLKRLPTDDEVASAVLFLASDLARAITGQTLDVNCG 254

(S)-acetoin forming diacetyl reductase;

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2252308999  19 KQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGGL 58
Cdd:PRK08643  214 KDITLGRLSEPEDVANCVSFLAGPDSDYITGQTIIVDGGM 253

short chain dehydrogenase; Validated

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2252308999  16 KLEKQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGGLSA 60
Cdd:PRK06484  465 SIRRRIPLGRLGDPEEVAEAIAFLASPAASYVNGATLTVDGGWTA 509

SDR family oxidoreductase;

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2252308999  22 PIRKFAESIDVANGILFLASDESKMITGTELVIDGGLSA 60
Cdd:PRK07063  218 PMKRIGRPEEVAMTAVFLASDEAPFINATCITIDGGRSV 256

alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, which catalyzes the NAD-dependent oxidoreduction of hydroxysteroids, is a dimeric member of the classical 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 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
                  ....*....|....*....|....*....|....*....
gi 2252308999  22 PIRKFAESIDVANGILFLASDESKMITGTELVIDGGLSA 60
Cdd:cd05328   209 PMGRRAEPDEIAPVIAFLASDAASWINGANLFVDGGLDA 247

Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, classical (c) SDRs; This subgroup includes a putative carbohydrate or polyalcohol metabolizing SDR (A3DFK9) from Clostridium thermocellum. Its members have a TGXXXGXG classical-SDR glycine-rich NAD-binding motif, and some have a canonical SDR active site tetrad (A3DFK9 lacks the upstream Asn). 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
                  ....*....|....*....|....*....|....*....|
gi 2252308999  20 QIPIRKFAESIDVANGILFLASDESKMITGTELVIDGGLS 59
Cdd:cd09761   198 QHPAGRVGTPKDIANLVLFLCQQDAGFITGETFIVDGGMT 237

Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ENRs includes Escherichia coli ENR. ENR catalyzes the NAD(P)H-dependent reduction of enoyl-ACP in the last step of fatty acid biosynthesis. De novo fatty acid biosynthesis is catalyzed by the fatty acid synthetase complex, through the serial addition of 2-carbon subunits. In bacteria and plants,ENR catalyzes one of six synthetic steps in this process. Oilseed rape ENR, and also apparently the NADH-specific form of Escherichia coli ENR, is tetrameric. Although similar to the classical SDRs, this group does not have the canonical catalytic tetrad, nor does it have the typical Gly-rich NAD-binding pattern. Such so-called divergent SDRs have a GXXXXXSXA NAD-binding motif and a YXXMXXXK (or YXXXMXXXK) active site 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
                  ....*....|....*....|....*....|....*....|....
gi 2252308999  18 EKQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGGLSAQ 61
Cdd:cd05372   206 EQRAPLGRNVTAEEVGNTAAFLLSDLSSGITGEIIYVDGGYHIM 249

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
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2252308999   9 ASEELLGKLEKQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGGLSA 60
Cdd:cd05347   197 ADPEFNDDILKRIPAGRWGQPEDLVGAAVFLASDASDYVNGQIIFVDGGWLA 248

SDR family oxidoreductase;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2252308999   1 MMQAFFEnASEELLGKLEKQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGGLSAQ 61
Cdd:PRK06172  194 MFRRAYE-ADPRKAEFAAAMHPVGRIGKVEEVASAVLYLCSDGASFTTGHALMVDGGATAQ 253

short chain dehydrogenase; Provisional

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2252308999   7 ENASEELLGKLekqiPIRKFAESIDVANGILFLASDESKMITGTELVIDGGLSA 60
Cdd:PRK06125  206 ESRWQELLAGL----PLGRPATPEEVADLVAFLASPRSGYTSGTVVTVDGGISA 255

SDR family oxidoreductase;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2252308999   9 ASEELLGKLEKQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGGLSAQ 61
Cdd:PRK06124  203 ADPAVGPWLAQRTPLGRWGRPEEIAGAAVFLASPAASYVNGHVLAVDGGYSVH 255

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2252308999   7 ENASEELLGKlekqIPIRKFAESIDVANGILFLASDESKMITGTELVIDGG 57
Cdd:PRK06935  208 KNRNDEILKR----IPAGRWGEPDDLMGAAVFLASRASDYVNGHILAVDGG 254

tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup includes TR-I and TR-II; these proteins are members of the SDR family. TRs catalyze the NADPH-dependent reductions of the 3-carbonyl group of tropinone, to a beta-hydroxyl group. TR-I and TR-II produce different stereoisomers from tropinone, TR-I produces tropine (3alpha-hydroxytropane), and TR-II, produces pseudotropine (sigma-tropine, 3beta-hydroxytropane). 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
                  ....*....|....*....|....*....|....*....|....*....
gi 2252308999  12 ELLGKLEKQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGGLSA 60
Cdd:cd05329   202 ENLDKVIERTPLKRFGEPEEVAALVAFLCMPAASYITGQIIAVDGGLTA 250

SDR family oxidoreductase;

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2252308999   2 MQAFFEN-ASEELLGKLEKQIPIRKFAESIDVANGILFLASDESKMITG 49
Cdd:PRK07831  204 MHPFLAKvTSAELLDELAAREAFGRAAEPWEVANVIAFLASDYSSYLTG 252

D-mannonate oxidoreductase; Provisional

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2252308999  20 QIPIRKFAESIDVANGILFLASDE-SKMITGTELVIDGGLSA 60
Cdd:PRK08277  233 HTPMGRFGKPEELLGTLLWLADEKaSSFVTGVVLPVDGGFSA 274

coniferyl-alcohol dehydrogenase;

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2252308999  22 PIRKFAESIDVANGILFLASDESKMITGTELVIDGGLSAQ 61
Cdd:PRK12428  194 RMGRPATADEQAAVLVFLCSDAARWINGVNLPVDGGLAAT 233

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional

                          10        20
                  ....*....|....*....|....*
gi 2252308999  33 ANGILFLASDESKMITGTELVIDGG 57
Cdd:PRK12823  233 VAAILFLASDEASYITGTVLPVGGG 257

short chain dehydrogenase; Provisional

                          10        20        30
                  ....*....|....*....|....*....|
gi 2252308999  31 DVANGILFLASDESKMITGTELVIDGGLSA 60
Cdd:PRK08265  217 EVAQVVAFLCSDAASFVTGADYAVDGGYSA 246

SDR family oxidoreductase;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2252308999  11 EELLGKLEKQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGGLSA 60
Cdd:PRK09242  205 PDYYEQVIERTPMRRVGEPEEVAAAVAFLCMPAASYITGQCIAVDGGFLR 254

pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including Trypanosoma cruzi and Leishmania major) to obtain reduced pteridines by salvage rather than biosynthetic pathways. Enzymes in T. cruzi described as pteridine reductase 1 (PTR1) and pteridine reductase 2 (PTR2) have different activity profiles. PTR1 is more active with with fully oxidized biopterin and folate than with reduced forms, while PTR2 reduces dihydrobiopterin and dihydrofolate but not oxidized pteridines. T. cruzi PTR1 and PTR2 are more similar to each other in sequence than either is to the pteridine reductase of Leishmania major, and all are included in this family.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2252308999  11 EELLGKLEKQIPI-RKFAESIDVANGILFLASDESKMITGTELVIDGGLS 59
Cdd:TIGR02685 214 FEVQEDYRRKVPLgQREASAEQIADVVIFLVSPKAKYITGTCIKVDGGLS 263

acetoacetyl-CoA reductase; Provisional

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2252308999  11 EELLGKLEKQIPIRKFAESIDVANGILFLASDESkMITGTELVIDGGL 58
Cdd:PRK12935  199 EEVRQKIVAKIPKKRFGQADEIAKGVVYLCRDGA-YITGQQLNINGGL 245

3-ketoacyl-ACP reductase;

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2252308999  11 EELLGKLEKQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGGL 58
Cdd:PRK12938  196 PDVLEKIVATIPVRRLGSPDEIGSIVAWLASEESGFSTGADFSLNGGL 243

short chain dehydrogenase; Provisional

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2252308999   5 FFENASEELLGKLEKQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGGL 58
Cdd:PRK12937  191 FFNGKSAEQIDQLAGLAPLERLGTPEEIAAAVAFLAGPDGAWVNGQVLRVNGGF 244

SDR family oxidoreductase;

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2252308999  22 PIRKFAESIDVANGILFLASDESKMITGTELVIDGGLSA 60
Cdd:PRK08589  216 PLGRLGKPEEVAKLVVFLASDDSSFITGETIRIDGGVMA 254

short chain dehydrogenase; Provisional

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2252308999  10 SEELLGKLEKQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGG 57
Cdd:PRK05875  203 SPELSADYRACTPLPRVGEVEDVANLAMFLLSDAASWITGQVINVDGG 250

short chain dehydrogenase; Provisional

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2252308999  17 LEKQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGGL 58
Cdd:PRK12827  207 LLNPVPVQRLGEPDEVAALVAFLVSDAASYVTGQVIPVDGGF 248

sorbitol-6-phosphate dehydrogenase; Provisional

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2252308999  19 KQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGG 57
Cdd:PRK12384  217 DKVPLKRGCDYQDVLNMLLFYASPKASYCTGQSINVTGG 255

enoyl-[acyl-carrier-protein] reductase FabI;

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2252308999  12 ELLGKLEKQIPIRKFAESIDVANGILFLASDESKMITGTELVIDGGLS 59
Cdd:PRK07370  207 DMIHHVEEKAPLRRTVTQTEVGNTAAFLLSDLASGITGQTIYVDAGYC 254