位置:首页 > 蛋白库 > AK1C1_MACFA
AK1C1_MACFA
ID   AK1C1_MACFA             Reviewed;         323 AA.
AC   Q95JH7;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Aldo-keto reductase family 1 member C1 {ECO:0000250|UniProtKB:Q04828};
DE            EC=1.1.1.- {ECO:0000269|PubMed:15618685};
DE            EC=1.1.1.112 {ECO:0000269|PubMed:15618685};
DE            EC=1.1.1.209 {ECO:0000250|UniProtKB:Q04828};
DE            EC=1.1.1.210 {ECO:0000250|UniProtKB:Q04828};
DE            EC=1.1.1.357 {ECO:0000250|UniProtKB:Q04828};
DE            EC=1.1.1.51 {ECO:0000250|UniProtKB:Q04828};
DE            EC=1.1.1.53 {ECO:0000250|UniProtKB:Q04828};
DE            EC=1.1.1.62 {ECO:0000250|UniProtKB:Q04828};
DE            EC=1.3.1.20 {ECO:0000250|UniProtKB:Q04828};
DE   AltName: Full=20-alpha-hydroxysteroid dehydrogenase;
DE            Short=20-alpha-HSD;
DE            EC=1.1.1.149 {ECO:0000250|UniProtKB:Q04828};
DE   AltName: Full=Dihydrodiol dehydrogenase 1;
DE            Short=DD-1;
DE            Short=DD1;
GN   Name=AKR1C1;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, AND PROTEIN SEQUENCE OF 2-26; 40-123; 137-172; 271-282 AND
RP   295-323.
RC   TISSUE=Liver;
RX   PubMed=15618685; DOI=10.2133/dmpk.17.348;
RA   Higaki Y., Kamiya T., Usami N., Shintani S., Shiraishi H., Ishikura S.,
RA   Yamamoto I., Hara A.;
RT   "Molecular characterization of two monkey dihydrodiol dehydrogenases.";
RL   Drug Metab. Pharmacokinet. 17:348-356(2002).
CC   -!- FUNCTION: Cytosolic aldo-keto reductase that catalyzes the NADH and
CC       NADPH-dependent reduction of ketosteroids to hydroxysteroids
CC       (PubMed:15618685). Most probably acts as a reductase in vivo since the
CC       oxidase activity measured in vitro is inhibited by physiological
CC       concentrations of NADPH (By similarity). Displays a broad positional
CC       specificity acting on positions 3, 17 and 20 of steroids and regulates
CC       the metabolism of hormones like estrogens and androgens
CC       (PubMed:15618685). May also reduce conjugated steroids such as 5alpha-
CC       dihydrotestosterone sulfate. Displays affinity for bile acids (By
CC       similarity). Can also act on non-steroidal substrates such as S-indan-
CC       1-ol, S-tetralol and 4-chromanol (PubMed:15618685).
CC       {ECO:0000250|UniProtKB:Q04828, ECO:0000269|PubMed:15618685}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3alpha-hydroxysteroid + NADP(+) = a 3-oxosteroid + H(+) +
CC         NADPH; Xref=Rhea:RHEA:34783, ChEBI:CHEBI:15378, ChEBI:CHEBI:36835,
CC         ChEBI:CHEBI:47788, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.357; Evidence={ECO:0000250|UniProtKB:Q04828};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3alpha-hydroxysteroid + NAD(+) = a 3-oxosteroid + H(+) +
CC         NADH; Xref=Rhea:RHEA:34779, ChEBI:CHEBI:15378, ChEBI:CHEBI:36835,
CC         ChEBI:CHEBI:47788, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.357; Evidence={ECO:0000250|UniProtKB:Q04828};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(17R,20S)-17,20-dihydroxypregn-4-en-3-one + NADP(+) = 17alpha-
CC         hydroxyprogesterone + H(+) + NADPH; Xref=Rhea:RHEA:15857,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16418, ChEBI:CHEBI:17252,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.149;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15859;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(17R,20S)-17,20-dihydroxypregn-4-en-3-one + NAD(+) = 17alpha-
CC         hydroxyprogesterone + H(+) + NADH; Xref=Rhea:RHEA:15853,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16418, ChEBI:CHEBI:17252,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.149;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15855;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(20S)-hydroxypregn-4-en-3-one + NADP(+) = H(+) + NADPH +
CC         progesterone; Xref=Rhea:RHEA:42112, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17026, ChEBI:CHEBI:28453, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; Evidence={ECO:0000250|UniProtKB:Q04828};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42113;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42114;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(20S)-hydroxypregn-4-en-3-one + NAD(+) = H(+) + NADH +
CC         progesterone; Xref=Rhea:RHEA:42108, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17026, ChEBI:CHEBI:28453, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:Q04828};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42109;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42110;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1R,2R)-1,2-dihydrobenzene-1,2-diol + NADP(+) = catechol +
CC         H(+) + NADPH; Xref=Rhea:RHEA:16729, ChEBI:CHEBI:10702,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:18135, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.3.1.20;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-indan-1-ol + NAD(+) = H(+) + indan-1-one + NADH;
CC         Xref=Rhea:RHEA:16317, ChEBI:CHEBI:15378, ChEBI:CHEBI:17404,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:156384;
CC         EC=1.1.1.112; Evidence={ECO:0000250|UniProtKB:Q04828};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-indan-1-ol + NADP(+) = H(+) + indan-1-one + NADPH;
CC         Xref=Rhea:RHEA:16321, ChEBI:CHEBI:15378, ChEBI:CHEBI:17404,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:156384;
CC         EC=1.1.1.112; Evidence={ECO:0000269|PubMed:15618685};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5alpha-androstane-3alpha,17beta-diol + NADP(+) = 17beta-
CC         hydroxy-5alpha-androstan-3-one + H(+) + NADPH; Xref=Rhea:RHEA:42116,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:36713,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42118;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5alpha-androstane-3beta,17beta-diol + NADP(+) = 17beta-
CC         hydroxy-5alpha-androstan-3-one + H(+) + NADPH; Xref=Rhea:RHEA:16297,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:18329,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.210;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16299;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5alpha-androstane-3alpha,17beta-diol + NAD(+) = 17beta-
CC         hydroxy-5alpha-androstan-3-one + H(+) + NADH; Xref=Rhea:RHEA:42004,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:36713,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.53;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42006;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17beta-hydroxy-5alpha-androstan-3-one + NADP(+) = 5alpha-
CC         androstan-3,17-dione + H(+) + NADPH; Xref=Rhea:RHEA:42120,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:16330,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42121;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3alpha-hydroxy-5alpha-androstan-17-one + NADP(+) = 5alpha-
CC         androstan-3,17-dione + H(+) + NADPH; Xref=Rhea:RHEA:20377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:16032,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.209;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20378;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3alpha-hydroxy-5alpha-androstan-17-one + H(+) + NADPH =
CC         5alpha-androstane-3alpha,17beta-diol + NADP(+); Xref=Rhea:RHEA:42156,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16032, ChEBI:CHEBI:36713,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42157;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42158;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5alpha-androstane-3alpha,17beta-diol + NAD(+) = 3alpha-
CC         hydroxy-5alpha-androstan-17-one + H(+) + NADH; Xref=Rhea:RHEA:42124,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16032, ChEBI:CHEBI:36713,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42125;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17beta-estradiol + NADP(+) = estrone + H(+) + NADPH;
CC         Xref=Rhea:RHEA:24616, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469,
CC         ChEBI:CHEBI:17263, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.62;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24617;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:24618;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17beta-estradiol + NAD(+) = estrone + H(+) + NADH;
CC         Xref=Rhea:RHEA:24612, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469,
CC         ChEBI:CHEBI:17263, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.62;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24613;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:24614;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + testosterone = androst-4-ene-3,17-dione + H(+) +
CC         NADPH; Xref=Rhea:RHEA:14981, ChEBI:CHEBI:15378, ChEBI:CHEBI:16422,
CC         ChEBI:CHEBI:17347, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.51;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14982;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=20alpha-hydroxy-5beta-pregnan-3-one + NADP(+) = 5beta-pregnan-
CC         3,20-dione + H(+) + NADPH; Xref=Rhea:RHEA:42168, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30154, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78666; Evidence={ECO:0000250|UniProtKB:Q04828};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42169;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3beta-hydroxy-5beta-pregnane-20-one + NADP(+) = 5beta-pregnan-
CC         3,20-dione + H(+) + NADPH; Xref=Rhea:RHEA:22944, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16229, ChEBI:CHEBI:30154, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; Evidence={ECO:0000250|UniProtKB:Q04828};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3beta-hydroxy-5beta-pregnane-20-one + H(+) + NADPH =
CC         3beta,20alpha-dihydroxy-5beta-pregnane + NADP(+);
CC         Xref=Rhea:RHEA:65496, ChEBI:CHEBI:15378, ChEBI:CHEBI:16229,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:156526;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65497;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3beta,5alpha,17beta)-3-hydroxyandrostan-17-yl sulfate +
CC         NADP(+) = 5alpha-dihydrotestosterone sulfate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:53120, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:136982, ChEBI:CHEBI:136983;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53122;
CC         Evidence={ECO:0000250|UniProtKB:Q04828};
CC   -!- ACTIVITY REGULATION: Potently inhibited by benzbromarone and
CC       3',3'',5',5''-tetrabromophenolphthalein (TBPP).
CC       {ECO:0000269|PubMed:15618685}.
CC   -!- PATHWAY: Steroid metabolism. {ECO:0000250|UniProtKB:Q04828}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q04828}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q04828}.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB070209; BAB63206.1; -; mRNA.
DR   AlphaFoldDB; Q95JH7; -.
DR   SMR; Q95JH7; -.
DR   STRING; 9541.XP_005564594.1; -.
DR   eggNOG; KOG1577; Eukaryota.
DR   BRENDA; 1.3.1.20; 1793.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0047006; F:17-alpha,20-alpha-dihydroxypregn-4-en-3-one dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044594; F:17-beta-hydroxysteroid dehydrogenase (NAD+) activity; IEA:RHEA.
DR   GO; GO:0033703; F:3beta-hydroxy-5beta-steroid dehydrogenase activity; IEA:RHEA.
DR   GO; GO:0047024; F:5alpha-androstane-3beta,17beta-diol dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047044; F:androstan-3-alpha,17-beta-diol dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047042; F:androsterone dehydrogenase (B-specific) activity; ISS:UniProtKB.
DR   GO; GO:0032052; F:bile acid binding; ISS:UniProtKB.
DR   GO; GO:0031406; F:carboxylic acid binding; ISS:UniProtKB.
DR   GO; GO:0035410; F:dihydrotestosterone 17-beta-dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047718; F:indanol dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047045; F:testosterone 17-beta-dehydrogenase (NADP+) activity; IEA:RHEA.
DR   GO; GO:0030283; F:testosterone dehydrogenase [NAD(P)] activity; IEA:UniProtKB-EC.
DR   GO; GO:0047115; F:trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0008206; P:bile acid metabolic process; ISS:UniProtKB.
DR   GO; GO:0007586; P:digestion; ISS:UniProtKB.
DR   CDD; cd19108; AKR_AKR1C1-35; 1.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR044482; AKR1C.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PIRSF; PIRSF000097; AKR; 1.
DR   PRINTS; PR00069; ALDKETRDTASE.
DR   SUPFAM; SSF51430; SSF51430; 1.
DR   PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR   PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR   PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Lipid metabolism; NADP;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..323
FT                   /note="Aldo-keto reductase family 1 member C1"
FT                   /id="PRO_0000124634"
FT   ACT_SITE        55
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         20..24
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         24
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         50
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         166..167
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         190
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         216..222
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         227
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         270..280
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   SITE            54
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000250"
FT   SITE            84
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   323 AA;  36947 MW;  D632ACC1C65D3744 CRC64;
     MDSKHQCVKL NDGHFMPVLG FGTYAPAEVP KNKALEATKL AIEAGFRHID SAHLYNNEEY
     VGLAIRSKIA DGTVKREDIF YTSKLWCNSH RPEFVRPALE RSLKNLQLDY VDLYLIHFPV
     SLKPGEELIP KDENGKLLFD TVDLCATWEA MEKCKDAGLA KSIGVSNFNR RQLEMILNKP
     GLKYKPVCNQ VECHPYLNQR KLLDFCKSKD IVLVAFSALG SHREKPWVDQ NSPVLLEDPV
     LCALAKKHKR TPALIALRYQ LQRGVVVLAK SYNEQRIREN MKVFEFQLTS EDMKAIDGLD
     RNIRYLTLDI FAGPPNYPFS DEY
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025