ID U1GUL2_ENDPU Unreviewed; 417 AA.
AC U1GUL2;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=D-xylose reductase [NAD(P)H] {ECO:0000256|ARBA:ARBA00012845};
DE EC=1.1.1.307 {ECO:0000256|ARBA:ARBA00012845};
GN ORFNames=EPUS_01461 {ECO:0000313|EMBL:ERF76128.1};
OS Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF76128.1, ECO:0000313|Proteomes:UP000019373};
RN [1] {ECO:0000313|Proteomes:UP000019373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT "Genome characteristics reveal the impact of lichenization on lichen-
RT forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL BMC Genomics 15:34-34(2014).
CC -!- FUNCTION: Catalyzes the initial reaction in the xylose utilization
CC pathway by reducing D-xylose into xylitol. Xylose is a major component
CC of hemicelluloses such as xylan. Most fungi utilize D-xylose via three
CC enzymatic reactions, xylose reductase (XR), xylitol dehydrogenase
CC (XDH), and xylulokinase, to form xylulose 5-phosphate, which enters
CC pentose phosphate pathway. {ECO:0000256|ARBA:ARBA00025065}.
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; Evidence={ECO:0000256|ARBA:ARBA00000578};
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; Evidence={ECO:0000256|ARBA:ARBA00001334};
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DR EMBL; KE720780; ERF76128.1; -; Genomic_DNA.
DR RefSeq; XP_007786594.1; XM_007788404.1.
DR AlphaFoldDB; U1GUL2; -.
DR GeneID; 19236518; -.
DR eggNOG; KOG1577; Eukaryota.
DR HOGENOM; CLU_658938_0_0_1; -.
DR OrthoDB; 5305445at2759; -.
DR Proteomes; UP000019373; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd19071; AKR_AKR1-5-like; 1.
DR Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR019257; MeTrfase_dom.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR PANTHER; PTHR43827; 2,5-DIKETO-D-GLUCONIC ACID REDUCTASE; 1.
DR PANTHER; PTHR43827:SF3; ALDO-KETO REDUCTASE; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR Pfam; PF10017; Methyltransf_33; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000019373}.
FT DOMAIN 16..169
FT /note="Histidine-specific methyltransferase SAM-dependent"
FT /evidence="ECO:0000259|Pfam:PF10017"
FT DOMAIN 180..404
FT /note="NADP-dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00248"
SQ SEQUENCE 417 AA; 46724 MW; 7160A9A6A7E6F971 CRC64;
MGLSPICKPR RLRIYGLVLR NSFANASPAS SVAFLSKPPA SNHEHPSRIC HQGRALVTID
GCRDSKRVLE AYGTHSSVHH KFLFHALHHT NQVLGQNVFF EDHLGLNTHF DEPSGLSLQN
VVAKTSLDLL IDGKYLKILC GEEVHMCQSG KWHQQQVHVL VETGGLQIVG MAGRRWRLCV
DSAQMYHNER EVGSAILQFL SGPTNSNGLK REDIFFTSKL ASNSSYEAAR KSIRQSVKTC
GLGYIDLFLL HSPYGGKTKR LECWRAVEDA IQDGDVKTGG VSNFGVKHLE ELMASKPRIM
PAVNQIEVHP FNTRTSITSF CQKHGIIVEA YAPLVRALRM KHPVIQSFSK KYGCTPAQLM
IRWSLQHGFI PLPKSVTKHR IQENANIGGF HIEEQDMKKL DTLDEYLVTD WDPVDAD
//
