17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) SDRs; This subgroup includes various 17-beta-hydroxysteroid dehydrogenases and 3-ketoacyl-CoA reductase, these are members of the SDR family, and contain the canonical active site tetrad and glycine-rich NAD-binding motif of the classical SDRs. 3-ketoacyl-CoA reductase (KAR, aka 17beta-HSD type 12, encoded by HSD17B12) acts in fatty acid elongation; 17beta- hydroxysteroid dehydrogenases are isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. 17beta-estradiol dehydrogenase (aka 17beta-HSD type 1, encoded by HSD17B1) converts estrone to estradiol. Estradiol is the predominant female sex hormone. 17beta-HSD type 3 (aka testosterone 17-beta-dehydrogenase 3, encoded by HSD17B3) catalyses the reduction of androstenedione to testosterone, it also accepts estrogens as substrates. This subgroup also contains a putative steroid dehydrogenase let-767 from Caenorhabditis elegans, mutation in which results in hypersensitivity to cholesterol limitation. 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266  64 ASWAVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSsIEVRTAAFDFTnAAPSAYKDLLATLNQVE 143
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYG-VETKTIAADFS-AGDDIYERIEKELEGLD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266 144 IGVLINNVGMSYEYPDVLHKVDGgiERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATK 223
Cdd:cd05356   79 IGILVNNVGISHSIPEYFLETPE--DELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASK 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266 224 KYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKVKRTSFFTPDGAVFAKSALNTVGNTSDTTGYITHQLQLELMDLIP 303
Cdd:cd05356  157 AFLDFFSRALYEEYKSQGIDVQSLLPYLVATKMSKIRKSSLFVPSPEQFVRSALNTLGLSKRTTGYWSHALQGWVARLVP 236

                 ...
gi 392895266 304 TFI 306
Cdd:cd05356  237 EWI 239

17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) SDRs; This subgroup includes various 17-beta-hydroxysteroid dehydrogenases and 3-ketoacyl-CoA reductase, these are members of the SDR family, and contain the canonical active site tetrad and glycine-rich NAD-binding motif of the classical SDRs. 3-ketoacyl-CoA reductase (KAR, aka 17beta-HSD type 12, encoded by HSD17B12) acts in fatty acid elongation; 17beta- hydroxysteroid dehydrogenases are isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. 17beta-estradiol dehydrogenase (aka 17beta-HSD type 1, encoded by HSD17B1) converts estrone to estradiol. Estradiol is the predominant female sex hormone. 17beta-HSD type 3 (aka testosterone 17-beta-dehydrogenase 3, encoded by HSD17B3) catalyses the reduction of androstenedione to testosterone, it also accepts estrogens as substrates. This subgroup also contains a putative steroid dehydrogenase let-767 from Caenorhabditis elegans, mutation in which results in hypersensitivity to cholesterol limitation. 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266  64 ASWAVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSsIEVRTAAFDFTnAAPSAYKDLLATLNQVE 143
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYG-VETKTIAADFS-AGDDIYERIEKELEGLD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266 144 IGVLINNVGMSYEYPDVLHKVDGgiERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATK 223
Cdd:cd05356   79 IGILVNNVGISHSIPEYFLETPE--DELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASK 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266 224 KYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKVKRTSFFTPDGAVFAKSALNTVGNTSDTTGYITHQLQLELMDLIP 303
Cdd:cd05356  157 AFLDFFSRALYEEYKSQGIDVQSLLPYLVATKMSKIRKSSLFVPSPEQFVRSALNTLGLSKRTTGYWSHALQGWVARLVP 236

                 ...
gi 392895266 304 TFI 306
Cdd:cd05356  237 EWI 239

Short-chain dehydrogenase [General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266  66 WAVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKysSIEVRTAAFDFTN--AAPSAYKDLLATLNQVE 143
Cdd:COG0300    7 TVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAA--GARVEVVALDVTDpdAVAALAEAVLARFGPID 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266 144 igVLINNVGMSYeyPDVLHKVDggIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATK 223
Cdd:COG0300   85 --VLVNNAGVGG--GGPFEELD--LEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASK 158

                        170       180       190
                 ....*....|....*....|....*....|...
gi 392895266 224 KYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 256
Cdd:COG0300  159 AALEGFSESLRAELAPTGVRVTAVCPGPVDTPF 191

sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain dehydrogenase/reductase family. The enzyme catalyzes the last step in the biosynthesis of tetrahydrobiopterin. A similar enzyme in Bacillus cereus was isolated for its ability to convert benzil to (S)-benzoin, a property sepiapterin reductase also shares. Cutoff scores for this model are set such that benzil reductase scores between trusted and noise cutoffs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266   67 AVVTGATDGIGKAYAFELARR----GFNVLLVSRTQSKLDETKKEILEKYSSIEVRTAAFDFTNAAPSA--YKDLLATL- 139
Cdd:TIGR01500   3 CLVTGASRGFGRTIAQELAKClkspGSVLVLSARNDEALRQLKAEIGAERSGLRVVRVSLDLGAEAGLEqlLKALRELPr 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266  140 -NQVEIGVLINNVGMSYEypdvLHKVDGGIERLANITTINTLppTLLSAGILPQMVARK-------AGVIVNVGSSAGAN 211
Cdd:TIGR01500  83 pKGLQRLLLINNAGTLGD----VSKGFVDLSDSTQVQNYWAL--NLTSMLCLTSSVLKAfkdspglNRTVVNISSLCAIQ 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 392895266  212 QMALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM-SKVKRTS 263
Cdd:TIGR01500 157 PFKGWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMqQQVREES 209

17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) SDRs; This subgroup includes various 17-beta-hydroxysteroid dehydrogenases and 3-ketoacyl-CoA reductase, these are members of the SDR family, and contain the canonical active site tetrad and glycine-rich NAD-binding motif of the classical SDRs. 3-ketoacyl-CoA reductase (KAR, aka 17beta-HSD type 12, encoded by HSD17B12) acts in fatty acid elongation; 17beta- hydroxysteroid dehydrogenases are isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. 17beta-estradiol dehydrogenase (aka 17beta-HSD type 1, encoded by HSD17B1) converts estrone to estradiol. Estradiol is the predominant female sex hormone. 17beta-HSD type 3 (aka testosterone 17-beta-dehydrogenase 3, encoded by HSD17B3) catalyses the reduction of androstenedione to testosterone, it also accepts estrogens as substrates. This subgroup also contains a putative steroid dehydrogenase let-767 from Caenorhabditis elegans, mutation in which results in hypersensitivity to cholesterol limitation. 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266  64 ASWAVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSsIEVRTAAFDFTnAAPSAYKDLLATLNQVE 143
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYG-VETKTIAADFS-AGDDIYERIEKELEGLD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266 144 IGVLINNVGMSYEYPDVLHKVDGgiERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATK 223
Cdd:cd05356   79 IGILVNNVGISHSIPEYFLETPE--DELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASK 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266 224 KYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKVKRTSFFTPDGAVFAKSALNTVGNTSDTTGYITHQLQLELMDLIP 303
Cdd:cd05356  157 AFLDFFSRALYEEYKSQGIDVQSLLPYLVATKMSKIRKSSLFVPSPEQFVRSALNTLGLSKRTTGYWSHALQGWVARLVP 236

                 ...
gi 392895266 304 TFI 306
Cdd:cd05356  237 EWI 239

Short-chain dehydrogenase [General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266  66 WAVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKysSIEVRTAAFDFTN--AAPSAYKDLLATLNQVE 143
Cdd:COG0300    7 TVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAA--GARVEVVALDVTDpdAVAALAEAVLARFGPID 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266 144 igVLINNVGMSYeyPDVLHKVDggIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATK 223
Cdd:COG0300   85 --VLVNNAGVGG--GGPFEELD--LEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASK 158

                        170       180       190
                 ....*....|....*....|....*....|...
gi 392895266 224 KYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 256
Cdd:COG0300  159 AALEGFSESLRAELAPTGVRVTAVCPGPVDTPF 191

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266  67 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEIlekysSIEVRTAAFDFTNAA--PSAYKDLLATLNQVEi 144
Cdd:COG4221    8 ALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAEL-----GGRALAVPLDVTDEAavEAAVAAAVAEFGRLD- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266 145 gVLINNVGMSyeYPDVLHKVDggIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKK 224
Cdd:COG4221   82 -VLVNNAGVA--LLGPLEELD--PEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKA 156

                        170       180       190
                 ....*....|....*....|....*....|...
gi 392895266 225 YVSWLTAILRKEYEHQGITVQTIAPMMVATKMS 257
Cdd:COG4221  157 AVRGLSESLRAELRPTGIRVTVIEPGAVDTEFL 189

classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266  67 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTaafDFTNAApsaykDLLATLNQVE--- 143
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAIEALGGNAVAVQA---DVSDEE-----DVEALVEEALeef 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266 144 --IGVLINNVGMSYEYPdvlhKVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSA 221
Cdd:cd05233   73 grLDILVNNAGIARPGP----LEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAA 148

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 392895266 222 TKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSK 258
Cdd:cd05233  149 SKAALEGLTRSLALELAPYGIRVNAVAPGLVDTPMLA 185

SDR family oxidoreductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266  67 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKysSIEVRTAAFDFTN--AAPSAYKDLLAtlNQVEI 144
Cdd:PRK07454   9 ALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRST--GVKAAAYSIDLSNpeAIAPGIAELLE--QFGCP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266 145 GVLINNVGMSYEYPdvlhKVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKK 224
Cdd:PRK07454  85 DVLINNAGMAYTGP----LLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQWGAYCVSKA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 392895266 225 YVSWLTAILRKEYEHQGITVQTIAPMMVATKM-------SKVKRTSFFTPD 268
Cdd:PRK07454 161 ALAAFTKCLAEEERSHGIRVCTITLGAVNTPLwdtetvqADFDRSAMLSPE 211

11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human 11beta_HSD1 catalyzes the NADP(H)-dependent interconversion of cortisone and cortisol. This subgroup also includes human dehydrogenase/reductase SDR family member 7C (DHRS7C) and DHRS7B. These proteins have the GxxxGxG nucleotide binding motif and S-Y-K catalytic triad characteristic of the SDRs, but have an atypical C-terminal domain that contributes to homodimerization contacts. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266  68 VVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEkYSSIEVRTAAFDFTN--AAPSAYKDLLATLNQVEIg 145
Cdd:cd05332    7 IITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLE-LGAPSPHVVPLDMSDleDAEQVVEEALKLFGGLDI- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266 146 vLINNVGMSyeYPDVLHKVDggIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKKY 225
Cdd:cd05332   85 -LINNAGIS--MRSLFHDTS--IDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAASKHA 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 392895266 226 VSWLTAILRKEYEHQGITVQTIAPMMVATKMS 257
Cdd:cd05332  160 LQGFFDSLRAELSEPNISVTVVCPGLIDTNIA 191

SDR family oxidoreductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266  51 VLLSPIDLK-KRAgaswaVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEkySSIEVRTAAFDFTNaaP 129
Cdd:PRK05866  31 PPRQPVDLTgKRI-----LLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITR--AGGDAMAVPCDLSD--L 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266 130 SAYKDLLATLNQvEIG---VLINNVGMSYEYP-----DVLHKVdggiERlanITTINTLPPTLLSAGILPQMVARKAGVI 201
Cdd:PRK05866 102 DAVDALVADVEK-RIGgvdILINNAGRSIRRPlaeslDRWHDV----ER---TMVLNYYAPLRLIRGLAPGMLERGDGHI 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 392895266 202 VNVGS-SAGANQMALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 256
Cdd:PRK05866 174 INVATwGVLSEASPLFSVYNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVATPM 229

gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107,15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266  67 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEIlEKYsSIEVRTAAFDFTNaaPSAYKDLLAtlnQVE--- 143
Cdd:cd05347    8 ALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLI-EKE-GVEATAFTCDVSD--EEAIKAAVE---AIEedf 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266 144 --IGVLINNVGMSYEYPdvlhKVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSA 221
Cdd:cd05347   81 gkIDILVNNAGIIRRHP----AEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAA 156

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 392895266 222 TKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSK 258
Cdd:cd05347  157 SKGGVAGLTKALATEWARHGIQVNAIAPGYFATEMTE 193

classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a canonical active site tetrad and a fairly well conserved typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266  67 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVrtAAFDFTNAA--PSAYKDLLATLNQVEI 144
Cdd:cd05350    1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNPSVEV--EILDVTDEErnQLVIAELEAELGGLDL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266 145 GVLINNVGMSYEYPDVLHKVDGGIERLANITTINTLPPtllsagILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKK 224
Cdd:cd05350   79 VIINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEA------ALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266 225 YVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKVKRTSFFTPDGAVFAKSALNTVgNTSDTTGYITHQL--QLELMDLI 302
Cdd:cd05350  153 ALSSLAESLRYDVKKRGIRVTVINPGFIDTPLTANMFTMPFLMSVEQAAKRIYKAI-KKGAAEPTFPWRLavPLRLLKLL 231

                 ....*...
gi 392895266 303 PTFIRDKI 310
Cdd:cd05350  232 PERLRRRL 239

3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266  67 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKY--SSIEVRTAAFDFTNaapsaYKDLLATLNQVE- 143
Cdd:cd08939    4 VLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEAEAnaSGQKVSYISADLSD-----YEEVEQAFAQAVe 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266 144 ----IGVLINNVGMSyeYPDVLHKVDGG-IERLANI---TTINtlpptlLSAGILPQMVARKAGVIVNVGSSAGANQMAL 215
Cdd:cd08939   79 kggpPDLVVNCAGIS--IPGLFEDLTAEeFERGMDVnyfGSLN------VAHAVLPLMKEQRPGHIVFVSSQAALVGIYG 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 392895266 216 WAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 256
Cdd:cd08939  151 YSAYCPSKFALRGLAESLRQELKPYNIRVSVVYPPDTDTPG 191

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; DHB DH (aka 1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase) catalyzes the NAD-dependent conversion of 1,2-dihydroxycyclohexa-3,4-diene carboxylate to a catechol. This subgroup also contains Pseudomonas putida F1 CmtB, 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase, the second enzyme in the pathway for catabolism of p-cumate catabolism. This subgroup shares the glycine-rich NAD-binding motif of the classical SDRs and shares the same catalytic triad; however, the upstream Asn implicated in cofactor binding or catalysis in other SDRs is generally substituted by a Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266  67 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLdETKKEILEKYSSIEVRTAAFDFTNAAPSAYKDLLATLNQVEIgv 146
Cdd:cd08937    7 VVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVH-EVLAEILAAGDAAHVHTADLETYAGAQGVVRAAVERFGRVDV-- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266 147 LINNVGMSYEYPDVLHKVDGGIErlANITtiNTLPPTL-LSAGILPQMVARKAGVIVNVGSSAGANqmALWAVYSATKKY 225
Cdd:cd08937   84 LINNVGGTIWAKPYEHYEEEQIE--AEIR--RSLFPTLwCCRAVLPHMLERQQGVIVNVSSIATRG--IYRIPYSAAKGG 157

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 392895266 226 VSWLTAILRKEYEHQGITVQTIAPMMVATKMSKVKRTS 263
Cdd:cd08937  158 VNALTASLAFEHARDGIRVNAVAPGGTEAPPRKIPRNA 195

SDR family oxidoreductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266  68 VVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEIleKYSSiEVRTAAFDFTnaAPSAYKDLLATLNQVE-IGV 146
Cdd:PRK09072   9 LLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARL--PYPG-RHRWVVADLT--SEAGREAVLARAREMGgINV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266 147 LINNVGMSYEypDVL-HKVDGGIERL--ANITTintlpPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATK 223
Cdd:PRK09072  84 LINNAGVNHF--ALLeDQDPEAIERLlaLNLTA-----PMQLTRALLPLLRAQPSAMVVNVGSTFGSIGYPGYASYCASK 156

                        170       180       190
                 ....*....|....*....|....*....|...
gi 392895266 224 KYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 256
Cdd:PRK09072 157 FALRGFSEALRRELADTGVRVLYLAPRATRTAM 189

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266  67 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEIleKYSSIEVRTAAFDFTN--AAPSAYKDLLATLNQVEI 144
Cdd:cd05333    3 ALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEI--KALGGNAAALEADVSDreAVEALVEKVEAEFGPVDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895266 145 gvLINNVG---------MSYE-YPDVLHkvdggierlANITTIntlppTLLSAGILPQMVARKAGVIVNVGSSAG----A 210
Cdd:cd05333   81 --LVNNAGitrdnllmrMSEEdWDAVIN---------VNLTGV-----FNVTQAVIRAMIKRRSGRIINISSVVGlignP 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 392895266 211 NQmalwAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKV 259
Cdd:cd05333  145 GQ----ANYAASKAGVIGFTKSLAKELASRGITVNAVAPGFIDTDMTDA 189