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XYL1_CANTR
ID   XYL1_CANTR              Reviewed;         324 AA.
AC   O13283;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=NAD(P)H-dependent D-xylose reductase I,II;
DE            Short=XR;
DE            EC=1.1.1.307;
GN   Name=xyrA;
OS   Candida tropicalis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96745 / CBS 4913 / NBRC 0618 / NRRL Y-5716;
RA   Yokoyama S., Kinoshita Y., Suzuki T., Kawai K., Horitsu H., Takamizawa K.;
RT   "Cloning and sequencing of two D-xylose reductase genes (xyrA and xyrB)
RT   from Candida tropicalis.";
RL   J. Ferment. Bioeng. 80:603-605(1995).
CC   -!- FUNCTION: Reduces D-xylose into xylitol. Has a preference for NADPH,
CC       but can also utilize NADH as cosubstrate (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + xylitol = D-xylose + H(+) + NADH;
CC         Xref=Rhea:RHEA:27441, ChEBI:CHEBI:15378, ChEBI:CHEBI:17151,
CC         ChEBI:CHEBI:53455, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.307;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + xylitol = D-xylose + H(+) + NADPH;
CC         Xref=Rhea:RHEA:27445, ChEBI:CHEBI:15378, ChEBI:CHEBI:17151,
CC         ChEBI:CHEBI:53455, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.307;
CC   -!- PATHWAY: Carbohydrate metabolism; D-xylose degradation.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR   EMBL; AB002105; BAA19476.1; -; Genomic_DNA.
DR   AlphaFoldDB; O13283; -.
DR   SMR; O13283; -.
DR   PRIDE; O13283; -.
DR   VEuPathDB; FungiDB:CTMYA2_054230; -.
DR   VEuPathDB; FungiDB:CTRG_05993; -.
DR   UniPathway; UPA00810; -.
DR   GO; GO:0032866; F:D-xylose:NADP reductase activity; IEA:InterPro.
DR   GO; GO:0042843; P:D-xylose catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd19113; AKR_AKR2B1-10; 1.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR044486; AKR2B1.
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   3: Inferred from homology;
KW   Carbohydrate metabolism; NAD; NADP; Oxidoreductase; Xylose metabolism.
FT   CHAIN           1..324
FT                   /note="NAD(P)H-dependent D-xylose reductase I,II"
FT                   /id="PRO_0000124662"
FT   ACT_SITE        54
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         171..172
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         220..229
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         276..286
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            83
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   324 AA;  36575 MW;  3002FFBDA21FA3E0 CRC64;
     MSTTPTIPTI KLNSGYEMPL VGFGCWKVTN ATAADQIYNA IKTGYRLFDG AEDYGNEKEV
     GEGINRAIKE GLVKREELFI TSKLWNNFHD PKNVETALNK TLSDLNLDYV DLFLIHFPIA
     FKFVPIEEKY PPGFYCGDGD NFHYEDVPLL DTWKALEKLV EAGKIKSIGI SNFTGALIYD
     LIRGATIKPA VLQIEHHPYL QQPKLIEYVQ KAGIAITGYS SFGPQSFLEL ESKRALNTPT
     LFEHETIKLI ADKHGKSPAQ VLLRWATQRN IAVIPKSNNP ERLAQNLSVV DFDLTKDDLD
     NIAKLDIGLR FNDPWDWDNI PIFV
 
 
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