XYLA_CERSK
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 03-AUG-2022, entry version 70.
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; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; 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;
CC Evidence={ECO:0000255|HAMAP-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}.
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DR EMBL; CP001150; ACM02433.1; -; Genomic_DNA.
DR RefSeq; WP_015921510.1; NC_011963.1.
DR AlphaFoldDB; B9KPP8; -.
DR SMR; B9KPP8; -.
DR EnsemblBacteria; ACM02433; ACM02433; RSKD131_2573.
DR GeneID; 67447950; -.
DR KEGG; rsk:RSKD131_2573; -.
DR HOGENOM; CLU_037261_1_0_5; -.
DR OMA; TLAMYEI; -.
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 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 PRINTS; PR00688; XYLOSISMRASE.
DR SUPFAM; SSF51658; SSF51658; 1.
DR TIGRFAMs; TIGR02630; xylose_isom_A; 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
