ID G7JD38_MEDTR Unreviewed; 480 AA. AC G7JD38; A0A0C3X802; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 2. DT 04-NOV-2026, entry version 86. DE RecName: Full=Xylose isomerase {ECO:0000256|ARBA:ARBA00011958, ECO:0000256|RuleBase:RU000609}; DE EC=5.3.1.5 {ECO:0000256|ARBA:ARBA00011958, ECO:0000256|RuleBase:RU000609}; GN OrderedLocusNames=MTR_4g128840 {ECO:0000313|EMBL:AES92376.2}; OS Medicago truncatula (Barrel medic) (Medicago tribuloides). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago. OX NCBI_TaxID=3880 {ECO:0000313|EMBL:AES92376.2, ECO:0000313|Proteomes:UP000002051}; RN [1] {ECO:0000313|EMBL:AES92376.2, ECO:0000313|Proteomes:UP000002051} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Jemalong A17 {ECO:0000313|Proteomes:UP000002051}; RX PubMed=22089132; DOI=10.1038/nature10625; RA Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K., RA Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S., RA Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S., RA Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D., RA Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S., RA Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A., RA Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R., RA Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S., RA Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J., RA Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y., RA Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S., RA Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L., RA Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R., RA Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E., RA Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T., RA Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R., RA Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X., RA Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B., RA Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A., RA Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F., RA Town C.D., Roe B.A.; RT "The Medicago genome provides insight into the evolution of rhizobial RT symbioses."; RL Nature 480:520-524(2011). RN [2] {ECO:0000313|EMBL:AES92376.2, ECO:0000313|Proteomes:UP000002051} RP GENOME REANNOTATION. RC STRAIN=cv. Jemalong A17 {ECO:0000313|Proteomes:UP000002051}; RX PubMed=24767513; DOI=10.1186/1471-2164-15-312; RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S., RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F., RA Schwartz D.C., Town C.D.; RT "An improved genome release (version Mt4.0) for the model legume Medicago RT truncatula."; RL BMC Genomics 15:312-312(2014). 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|ARBA:ARBA00033659, ECO:0000256|PROSITE- CC ProRule:PRU00748, ECO:0000256|RuleBase:RU000609}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|PROSITE- CC ProRule:PRU00748}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000256|PROSITE- CC ProRule:PRU00748}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PROSITE-ProRule:PRU00748}. CC -!- SIMILARITY: Belongs to the xylose isomerase family. CC {ECO:0000256|ARBA:ARBA00005765, ECO:0000256|PROSITE-ProRule:PRU00748, CC ECO:0000256|RuleBase:RU000609}. 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; CM001220; AES92376.2; -; Genomic_DNA. DR STRING; 3880.G7JD38; -. DR PaxDb; 3880-G7JD38; -. DR Gramene; rna27643; RHN64786.1; gene27643. DR KEGG; mtr:11445818; -. DR eggNOG; ENOG502QRMS; Eukaryota. DR HOGENOM; CLU_037261_1_0_1; -. DR OMA; AMEATHF; -. DR OrthoDB; 1730074at2759; -. DR FunFam; 3.20.20.150:FF:000002; Xylose isomerase; 1. DR Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 1. DR HAMAP; MF_00455; Xylose_isom_A; 1. DR InterPro; IPR036237; Xyl_isomerase-like_sf. DR InterPro; IPR013452; XylA_bac. DR InterPro; IPR001998; Xylose_isomerase. DR PANTHER; PTHR48408; -; 1. DR PANTHER; PTHR48408:SF1; XYLOSE ISOMERASE; 1. DR Pfam; PF27526; XylA2_C; 1. DR PRINTS; PR00688; XYLOSISMRASE. DR SUPFAM; SSF51658; Xylose isomerase-like; 1. DR NCBIfam; NF003998; PRK05474.1; 1. DR NCBIfam; TIGR02630; xylose_isom_A; 1. DR PROSITE; PS51415; XYLOSE_ISOMERASE; 1. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0009045; F:xylose isomerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniRule. DR Proteomes; UP000002051; Unassembled WGS sequence. DR AlphaFoldDB; G7JD38; -. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, KW ECO:0000256|PROSITE-ProRule:PRU00748}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PROSITE- KW ProRule:PRU00748}; Magnesium {ECO:0000256|PROSITE-ProRule:PRU00748}; KW Manganese {ECO:0000256|PROSITE-ProRule:PRU00748}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE- KW ProRule:PRU00748}; Pentose shunt {ECO:0000256|PROSITE-ProRule:PRU00748}; KW Reference proteome {ECO:0000313|Proteomes:UP000002051}; KW Signal {ECO:0000256|SAM:SignalP}; KW Xylose metabolism {ECO:0000256|ARBA:ARBA00022629, ECO:0000256|PROSITE- KW ProRule:PRU00748}. FT SIGNAL 1..25 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 26..480 FT /note="Xylose isomerase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5014572852" FT ACT_SITE 145 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00748" FT BINDING 276 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00748" FT BINDING 312 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00748" FT BINDING 312 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00748" FT BINDING 315 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00748" FT BINDING 340 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00748" FT BINDING 351 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00748" FT BINDING 353 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00748" FT BINDING 383 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00748" SQ SEQUENCE 480 AA; 54247 MW; 41CEB607627D688B CRC64; MIMKSGKLLL LLLSFNVFYY AAVNCAPQTC PATKDAKCGD SDDWKAEFFP GISKIKYEGP SSKNPLSFKW YNPEEEILGK KMKDWFRFSV AFWHTFRGTG VDPFGAPTKY WPWEDGTNSL SMAKRRMRAN FEFINKLGVD FWCFHDRDIA PDGKTIEESN ENLDEVVALA HELQRQSKKR VLWGTAQLFV HPRYMHGAAT SSELAVYAYA AAQVKKALEV THYLGGENYV FWGGREGYQS LLNTDMEREL NHLARFFEAA VAHKKKIGFN GTFLIEPKPQ EPTKHQYDWD AATAANFLRK YGLIGEFKLN IECNHATLSG HSCHHELETA RINGLLGNID ANTGDPQVGW DTDQFLVDIQ EATMIMLSVI RNGGIAPGGF NFDAKLRRES TDVEDLFIAH IVGMDTMARG LRNAAKLVED GSLAELVRKR YQSFDTEIGA QIEAGKADFD FLEKKVKEWG EPKVASAKQE LAEMIFQNAM //