ID F7X9L1_SINMM Unreviewed; 436 AA. AC F7X9L1; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAR-2024, entry version 69. DE RecName: Full=Xylose isomerase {ECO:0000256|ARBA:ARBA00011958, ECO:0000256|HAMAP-Rule:MF_00455}; DE EC=5.3.1.5 {ECO:0000256|ARBA:ARBA00011958, ECO:0000256|HAMAP-Rule:MF_00455}; GN Name=xylA {ECO:0000256|HAMAP-Rule:MF_00455, GN ECO:0000313|EMBL:AEH80310.1}; GN OrderedLocusNames=SM11_chr3066 {ECO:0000313|EMBL:AEH80310.1}; OS Sinorhizobium meliloti (strain SM11). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=707241 {ECO:0000313|EMBL:AEH80310.1, ECO:0000313|Proteomes:UP000009045}; RN [1] {ECO:0000313|EMBL:AEH80310.1, ECO:0000313|Proteomes:UP000009045} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM11 {ECO:0000313|EMBL:AEH80310.1, RC ECO:0000313|Proteomes:UP000009045}; RX PubMed=21396969; DOI=10.1016/j.jbiotec.2010.12.018; RA Schneiker-Bekel S., Wibberg D., Bekel T., Blom J., Linke B., Neuweger H., RA Stiens M., Vorholter F.J., Weidner S., Goesmann A., Puhler A., Schluter A.; RT "The complete genome sequence of the dominant Sinorhizobium meliloti field RT isolate SM11 extends the S. meliloti pan-genome."; RL J. Biotechnol. 155:20-33(2011). 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|HAMAP- CC Rule:MF_00455, ECO:0000256|RuleBase:RU000609}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00455}; CC Note=Binds 2 magnesium ions per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00455}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00455, CC ECO:0000256|RuleBase:RU000610}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00455, CC ECO:0000256|RuleBase:RU000610}. CC -!- SIMILARITY: Belongs to the xylose isomerase family. CC {ECO:0000256|ARBA:ARBA00005765, ECO:0000256|HAMAP-Rule:MF_00455, 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; CP001830; AEH80310.1; -; Genomic_DNA. DR RefSeq; WP_013844860.1; NZ_JAJJBH010000001.1. DR AlphaFoldDB; F7X9L1; -. DR KEGG; smx:SM11_chr3066; -. DR PATRIC; fig|707241.3.peg.3199; -. DR HOGENOM; CLU_037261_1_0_5; -. DR Proteomes; UP000009045; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium 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 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; Xylose_isom_bac. DR InterPro; IPR001998; Xylose_isomerase. DR NCBIfam; TIGR02630; xylose_isom_A; 1. DR PANTHER; PTHR48320; -; 1. DR PANTHER; PTHR48320:SF1; XYLOSE ISOMERASE; 1. DR PRINTS; PR00688; XYLOSISMRASE. DR SUPFAM; SSF51658; Xylose isomerase-like; 1. DR PROSITE; PS51415; XYLOSE_ISOMERASE; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP- KW Rule:MF_00455}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00455}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00455}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00455}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00455}; KW Xylose metabolism {ECO:0000256|ARBA:ARBA00022629, ECO:0000256|HAMAP- KW Rule:MF_00455}. FT ACT_SITE 100 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT ACT_SITE 103 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 231 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 267 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 267 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 270 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 295 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 306 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 308 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 338 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" SQ SEQUENCE 436 AA; 48928 MW; 91CEF4BD1BC686CA CRC64; MSTGFFGDIA KIKYEGPEST NPLAFRHYNP DDVVLGKRME DHLRFAVAYW HTFVWPGGDP FGGQTFERPW FKDSMEAAKL KADVAFEFFQ LLGVPYYCFH DADVRPEGRN FAENTSNLNA IVDYFAGKQE ETGVKLLWGT ANLFSNRRFM AGAATNPDPD VFAFAAATVK TCIDATQRLD GENYVLWGGR EGYETLLNTD LKRELDQLGR FLNLVVEYKH RIGFKGTILI EPKPQEPTKH QYDYDVATVY GFLKRYGLEN EVKVNIEQGH AILAGHSFEH ELALANALGI FGSIDMNRND YQSGWDTDQF PNNVPEMALA YYHVLAGGGF KTGGTNFDAK LRRQSIDPED LLIGHIGGMD CCARGLKAAA KMIEDKALSA PLEARYAGWN VPEAKKMLDG GFSLEEIEAW VLKSDVNPQP KSGRQELLEN VVNRYV //