ID I0K3J0_9BACT Unreviewed; 446 AA. AC I0K3J0; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAR-2024, entry version 65. 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 ORFNames=FAES_0682 {ECO:0000313|EMBL:CCG98693.1}; OS Fibrella aestuarina BUZ 2. OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae; OC Fibrella. OX NCBI_TaxID=1166018 {ECO:0000313|EMBL:CCG98693.1, ECO:0000313|Proteomes:UP000011058}; RN [1] {ECO:0000313|EMBL:CCG98693.1, ECO:0000313|Proteomes:UP000011058} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BUZ 2T {ECO:0000313|Proteomes:UP000011058}; RX PubMed=22689241; DOI=10.1128/JB.00550-12; RA Filippini M., Qi W., Blom J., Goesmann A., Smits T.H., Bagheri H.C.; RT "Genome Sequence of Fibrella aestuarina BUZ 2T, a Filamentous Marine RT Bacterium."; RL J. Bacteriol. 194:3555-3555(2012). 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; HE796683; CCG98693.1; -; Genomic_DNA. DR RefSeq; WP_015329793.1; NC_020054.1. DR AlphaFoldDB; I0K3J0; -. DR STRING; 1166018.FAES_0682; -. DR KEGG; fae:FAES_0682; -. DR PATRIC; fig|1166018.3.peg.694; -. DR eggNOG; COG2115; Bacteria. DR HOGENOM; CLU_037261_1_0_10; -. DR OrthoDB; 9763981at2; -. DR Proteomes; UP000011058; 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}; Reference proteome {ECO:0000313|Proteomes:UP000011058}; KW Xylose metabolism {ECO:0000256|ARBA:ARBA00022629, ECO:0000256|HAMAP- KW Rule:MF_00455}. FT ACT_SITE 111 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT ACT_SITE 114 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 242 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 278 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 278 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 281 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 306 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 317 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 319 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 349 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" SQ SEQUENCE 446 AA; 50093 MW; 51479EE2B97EF29C CRC64; MAQINLTLGD KAYFPFVEKP IAYEGRDSDN PLAFKFYNPA QTIMGMPMKD LFRFAVAYWH TFCGTGADPF GPGVKHFPWD AGKDPLGAAF QKADAAFEFI TKMGIEYYCF HDVDVAPEGD SNHDFESNFR KVVDYLKQKQ QASGVNLLWG TANLFSHERY MNGASTNPDF HVLAHGAWQV KNAIDATIEL GGRGYTFWGG REGYMSLLNT NMKREQEHLG RFLQVSRDYA RKQGFKGAFY IEPKPMEPTK HQYDFDAATV VGFLNKYGLQ DDFELNLETN HATLANHTFA HELQVAVDNN MLGSIDANRG DYQNGWDTDQ FPVDVYELTE AMLVILEAGG FKSGGVNFDA KTRRNSTDLD DIFIAHIGGM DTFARAAIAA EAILTKSKYK QLRTDRYASY DSGAGADFEA GKLTLEDLRQ YAIDNGEAKQ VSGKQELYEM IVNQYI //