XYLA_PECCP
ID XYLA_PECCP Reviewed; 440 AA.
AC C6DIH5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
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}; OrderedLocusNames=PC1_4155;
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-2009) 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: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; CP001657; ACT15169.1; -; Genomic_DNA.
DR RefSeq; WP_015842241.1; NC_012917.1.
DR AlphaFoldDB; C6DIH5; -.
DR SMR; C6DIH5; -.
DR STRING; 561230.PC1_4155; -.
DR EnsemblBacteria; ACT15169; ACT15169; PC1_4155.
DR KEGG; pct:PC1_4155; -.
DR eggNOG; COG2115; Bacteria.
DR HOGENOM; CLU_037261_1_0_6; -.
DR OMA; TLAMYEI; -.
DR OrthoDB; 481478at2; -.
DR Proteomes; UP000002736; 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 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..440
FT /note="Xylose isomerase"
FT /id="PRO_1000206266"
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"
FT BINDING 309
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
SQ SEQUENCE 440 AA; 49687 MW; 1CF4F4615285D3EA CRC64;
MQAYFEQIEK VRYEGSQSDN PFAFRHYNPD QEILGKRMAD HLRFAVAYWH TFCWNGADMF
GVGSFARPWQ QSGDALELAK RKADIAFEFF QKLSVPYYCF HDVDIAPEGN SLKEYLHNFA
VITDVLAEKQ QDSGVKLLWG TANCFTHPRY GAGAATNPDP DVFAWAATQV FTAMNATKKL
GGENYVLWGG REGYETLLNT DLRQEREQIG RFMQMVVEHK HKIGFQGTLL IEPKPQEPTK
HQYDYDVATV YGFLKQFGLE KEIKVNVEAN HATLAGHSFH HEIATAVALG VFGSVDANRG
DPQLGWDTDQ FPNSVEENTL IMYEILKAGG FTTGGLNFDA KVRRQSTDRY DLFHAHIGAM
DTMALALKAA ARMIEDDKLN QLVAKRYAGW NGELGQQILQ GKASLESLAH YAESHQLAPQ
HQSGQQELLE NLVNRHLYPK
