ID XYLA_CERSK Reviewed; 433 AA. AC B9KPP8; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 24-MAR-2009, sequence version 1. DT 27-MAR-2024, entry version 76. DE RecName: Full=Xylose isomerase {ECO:0000255|HAMAP-Rule:MF_00455}; DE EC=5.3.1.5 {ECO:0000255|HAMAP-Rule:MF_00455}; GN Name=xylA {ECO:0000255|HAMAP-Rule:MF_00455}; GN OrderedLocusNames=RSKD131_2573; OS Cereibacter sphaeroides (strain KD131 / KCTC 12085) (Rhodobacter OS sphaeroides). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; OC Paracoccaceae; Cereibacter. OX NCBI_TaxID=557760; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KD131 / KCTC 12085; RX PubMed=19028901; DOI=10.1128/jb.01565-08; RA Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K.; RT "Complete genome sequence of Rhodobacter sphaeroides KD131."; RL J. Bacteriol. 191:1118-1119(2009). 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:0000255|HAMAP-Rule:MF_00455}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00455}; CC Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00455}; CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00455}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00455}. CC -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000255|HAMAP- CC 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; CP001150; ACM02433.1; -; Genomic_DNA. DR RefSeq; WP_015921510.1; NC_011963.1. DR AlphaFoldDB; B9KPP8; -. DR SMR; B9KPP8; -. DR GeneID; 67447950; -. DR KEGG; rsk:RSKD131_2573; -. DR HOGENOM; CLU_037261_1_0_5; -. DR Proteomes; UP000001597; Chromosome 1. 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; Cytoplasm; Isomerase; Magnesium; Metal-binding; KW Xylose metabolism. FT CHAIN 1..433 FT /note="Xylose isomerase" FT /id="PRO_1000200302" FT BINDING 305 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" FT BINDING 307 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" SQ SEQUENCE 433 AA; 48551 MW; 4AADF98C974FF905 CRC64; MTDFFAGIPQ IRYEGEGSSN EFAFRHYNPD EVILGKRMED HLRFAVAWWH SFAWPGGDPF GGQTFDRPWF GDTLDLAKLK ADVAFEMFDI LGAPFFCFHD ADIRPEGATF AESKRNLEEI VDHIGTRMEG SKTKLLWGTA NLFSHRRFMS GAATNPDPDV FAWSAATVKG CMDATMKLGG ANYVLWGGRE GYETLLNTDL TREAENAGRF LQMVVDYKHK IGFQGTILIE PKPQEPSKHQ YDYDVATVYG FLKRFGLEKE VKLNIEQGHA ILAGHSFEHE LALAASLGIL GSIDMNRNDY QSGWDTDQFP HNHPEMALAY YEILRAGGFT TGGTNFDAKI RRQSLDPEDL VLAHVGGMDT CARALKAAAR LYEDGSLETA RAARYAGWET PEAQAMLASS LEEIEARVLA EGINPKPRSG RQERLENLWN RFV //