ID M5B7B2_9MICO Unreviewed; 397 AA. AC M5B7B2; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 27-MAR-2024, entry version 62. DE RecName: Full=Xylose isomerase {ECO:0000256|ARBA:ARBA00018232, 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:CCE74800.1}; GN ORFNames=CMN_00844 {ECO:0000313|EMBL:CCE74800.1}; OS Clavibacter nebraskensis NCPPB 2581. OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae; OC Clavibacter. OX NCBI_TaxID=1097677 {ECO:0000313|EMBL:CCE74800.1, ECO:0000313|Proteomes:UP000012170}; RN [1] {ECO:0000313|EMBL:CCE74800.1, ECO:0000313|Proteomes:UP000012170} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCPPB 2581 {ECO:0000313|Proteomes:UP000012170}; RA Gartemann K.; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CCE74800.1, ECO:0000313|Proteomes:UP000012170} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCPPB 2581 {ECO:0000313|Proteomes:UP000012170}; RA Gartemann K.H., Blom J., Dreiseikelmann B., Fluegel M., Jaenicke S., RA Linke B., Sczcepanowski R., Wittmann J., Goesmann A., Puehler A., RA Eichenlaub R., Rueckert C.; RT "The genome sequence of the maize-pathogen Clavibacter michiganensis subsp. RT nebraskensis."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. 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|ARBA:ARBA00011881, CC ECO:0000256|HAMAP-Rule:MF_00455, ECO:0000256|RuleBase:RU000610}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_00455, 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00455}. 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; HE614873; CCE74800.1; -; Genomic_DNA. DR RefSeq; WP_015489588.1; NC_020891.1. DR AlphaFoldDB; M5B7B2; -. DR KEGG; cmc:CMN_00844; -. DR HOGENOM; CLU_060750_0_0_11; -. DR Proteomes; UP000012170; 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; IPR013022; Xyl_isomerase-like_TIM-brl. DR InterPro; IPR013453; XylA_actinobac. DR InterPro; IPR001998; Xylose_isomerase. DR NCBIfam; TIGR02631; xylA_Arthro; 1. DR PANTHER; PTHR48320; -; 1. DR PANTHER; PTHR48320:SF1; XYLOSE ISOMERASE; 1. DR Pfam; PF01261; AP_endonuc_2; 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}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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 DOMAIN 41..279 FT /note="Xylose isomerase-like TIM barrel" FT /evidence="ECO:0000259|Pfam:PF01261" FT ACT_SITE 54 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT ACT_SITE 57 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 181 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 217 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 217 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 220 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 245 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 293 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" SQ SEQUENCE 397 AA; 43821 MW; B5A72A571A9E3A16 CRC64; MALTPTREDK FSFGLWTIGY TGADPFGGPT RSDLDVVEGV ERISELGAYG LTFHDDDLFA FGSTDAERQT QIDRLKGALS DTGIVVPMVT TNLFSAPVFK DGGFTSNDRA VRRFAIHKVL RNIDLAAELG AQTFVMWGGR EGAEYDSAKD VRGALERYRE AVNLLGDYVT DKGYDIRFAI EPKPNEPRGD ILLPTLGHAL AFIETLERPE LVGVNPEVGH EQMAGLNFTA GIMQALYQGK LFHIDLNGQR GIKYDQDLVF GHGDLQNAFS LVDLLENGGV GGGRSYDGPR HFDYKPSRTE DITGVWDSAA ANMRMYLLLK ERAQAFRADP EVQEALAAAK VQDIYTPTLD EGESYDDILA DRSSYEDFAA DEYFDAKGFG FVRLNQLALE HLMGARS //