ID B8BME8_ORYSI Unreviewed; 477 AA.
AC B8BME8;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Xylose isomerase {ECO:0000256|RuleBase:RU000609};
DE EC=5.3.1.5 {ECO:0000256|RuleBase:RU000609};
GN ORFNames=OsI_38664 {ECO:0000313|EMBL:EEC69468.1};
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946 {ECO:0000313|EMBL:EEC69468.1, ECO:0000313|Proteomes:UP000007015};
RN [1] {ECO:0000313|EMBL:EEC69468.1, ECO:0000313|Proteomes:UP000007015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11 {ECO:0000313|Proteomes:UP000007015};
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C., Chen H., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA Zheng W., Hao B., Liu S., Wang W., Yuan L., Cao M., McDermott J.,
RA Samudrala R., Wang J., Wong G.K., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
CC -!- FUNCTION: Possesses non-specific lipolytic acyl hydrolase (LAH)
CC activity. Hydrolyzes phospholipids as well as galactolipids. May play a
CC role in disease resistance. {ECO:0000256|ARBA:ARBA00025642}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-xylose = alpha-D-xylulofuranose; Xref=Rhea:RHEA:22816,
CC ChEBI:CHEBI:28518, ChEBI:CHEBI:188998; EC=5.3.1.5;
CC Evidence={ECO:0000256|RuleBase:RU000609};
CC -!- SIMILARITY: Belongs to the patatin family.
CC {ECO:0000256|ARBA:ARBA00010240}.
CC -!- SIMILARITY: Belongs to the xylose isomerase family.
CC {ECO:0000256|ARBA:ARBA00005765, ECO:0000256|RuleBase:RU000609}.
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DR EMBL; CM000137; EEC69468.1; -; Genomic_DNA.
DR AlphaFoldDB; B8BME8; -.
DR STRING; 39946.B8BME8; -.
DR EnsemblPlants; BGIOSGA037558-TA; BGIOSGA037558-PA; BGIOSGA037558.
DR Gramene; BGIOSGA037558-TA; BGIOSGA037558-PA; BGIOSGA037558.
DR HOGENOM; CLU_572912_0_0_1; -.
DR Proteomes; UP000007015; Chromosome 12.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009045; F:xylose isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002641; PNPLA_dom.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR InterPro; IPR001998; Xylose_isomerase.
DR PANTHER; PTHR32176:SF45; PATATIN; 1.
DR PANTHER; PTHR32176; XYLOSE ISOMERASE; 1.
DR Pfam; PF01734; Patatin; 1.
DR PRINTS; PR00688; XYLOSISMRASE.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51658; Xylose isomerase-like; 1.
DR PROSITE; PS51635; PNPLA; 1.
DR PROSITE; PS51415; XYLOSE_ISOMERASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU000609};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU000609};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000609};
KW Reference proteome {ECO:0000313|Proteomes:UP000007015};
KW Xylose metabolism {ECO:0000256|RuleBase:RU000609}.
FT DOMAIN 38..245
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
SQ SEQUENCE 477 AA; 52768 MW; AE5999ACDC69302A CRC64;
MLRFTTARLL RPRCRRLYHG CSDGAAACSV VGERVTVLTI DGGGIRGIIP GKVLEFLENE
LQQLDGPEAR LADYFDYIAG TSTGGLITAM LAAPGAGRDG RRRPMFAAGE ICPFYQEHGP
RIFPQRWCKL ASTVAVVWGP KYNGRYLRDM VRRVLGETTV GDTLTKVVIP TFDVRLLQPV
IFSTYDAKHS PLKNALLSDV CIGTSAAPTY LPAHCFRTHD GAGETREYNL IDGGVAANNP
TMVAMTMITE EMIAEEKARL FLAKPPEECG RFLEPTKHQY DYDVATVYGF LKQFGLEKEI
KVNIEAHHAT LAGHSFHHEI ASAIALGIFG SVDAHRGDAQ LGWDTDQFPN SVEENALVMY
EIIKAGGFTT GGLNFDAKVR RQSTDKYDLF YGHIGAMDTM ALALKVAARM IEDGELDKRV
AKRYSGWNSE LGQQILKGQL SLAEIAKYAE QQQLAPQHQS GHQELLENLV NYYLFDK
//
