XYL2_CANTR
ID XYL2_CANTR Reviewed; 324 AA.
AC P87039;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=NADPH-dependent D-xylose reductase II,III;
DE Short=XR;
DE EC=1.1.1.307;
GN Name=xyrB;
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).
RN [2]
RP CHARACTERIZATION.
RC STRAIN=ATCC 96745 / CBS 4913 / NBRC 0618 / NRRL Y-5716;
RA Yokoyama S., Suzuki T., Kawai K., Horitsu H., Takamizawa K.;
RT "Purification, characterization and structure analysis of NADPH-dependent
RT D-xylose reductase from Candida tropicalis.";
RL J. Ferment. Bioeng. 79:217-223(1997).
CC -!- FUNCTION: Reduces D-xylose into xylitol. Preferentially utilizes NADPH
CC as a cosubstrate.
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}.
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; AB002106; BAA19477.1; -; Genomic_DNA.
DR AlphaFoldDB; P87039; -.
DR SMR; P87039; -.
DR VEuPathDB; FungiDB:CTMYA2_054080; -.
DR VEuPathDB; FungiDB:CTMYA2_054230; -.
DR VEuPathDB; FungiDB:CTRG_05993; -.
DR BRENDA; 1.1.1.307; 1146.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; NADP; Oxidoreductase; Xylose metabolism.
FT CHAIN 1..324
FT /note="NADPH-dependent D-xylose reductase II,III"
FT /id="PRO_0000124663"
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="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 220..229
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 276..286
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 83
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250"
SQ SEQUENCE 324 AA; 36620 MW; CA2769CA1655A239 CRC64;
MSTTPTIPTI KLNSGYEMPL VGFGCWKVNN ETAADQIYNA IKTGYRLFDG AEDYGNEKEV
GEGINRAIKE GLVKREELFI TSKLWNNFHD PKNVETALNK TLSDLNLDYV DLFLIHFPIA
FKFVPIEEKY PPGFYCGDGD NFHYEDVPLL DTWKALEKLV EAGKIKSIGI SNFTGALIYD
LIRGATIKPA VLQIEHHPYL QQPKLIEYVQ KAGIAITGYS SFGPQSFLEL ESKRALNTPT
LFEHETIKSI ADKHGKSPAQ VLLRWATQRN IAVIPKSNNP ERLAQNLSVV DFDLTKDDLD
NIAKLDIGLR FNDPWDWDNI PIFV
