XYLA_STAXY
ID XYLA_STAXY Reviewed; 439 AA.
AC P27157;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Xylose isomerase;
DE EC=5.3.1.5;
GN Name=xylA;
OS Staphylococcus xylosus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1288;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 20267 / Isolate C2A;
RX PubMed=1714034; DOI=10.1007/bf00273926;
RA Sizemore C., Buchner E., Rygus T., Witke C., Goetz F., Hillen W.;
RT "Organization, promoter analysis and transcriptional regulation of the
RT Staphylococcus xylosus xylose utilization operon.";
RL Mol. Gen. Genet. 227:377-384(1991).
CC -!- FUNCTION: Involved in D-xylose catabolism.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000305}.
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DR EMBL; X57599; CAA40824.1; -; Genomic_DNA.
DR PIR; S16530; S16530.
DR AlphaFoldDB; P27157; -.
DR SMR; P27157; -.
DR STRING; 1288.SXYLSMQ121_0142; -.
DR eggNOG; COG2115; Bacteria.
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; IPR013022; Xyl_isomerase-like_TIM-brl.
DR InterPro; IPR013452; Xylose_isom_bac.
DR InterPro; IPR001998; Xylose_isomerase.
DR Pfam; PF01261; AP_endonuc_2; 1.
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..439
FT /note="Xylose isomerase"
FT /id="PRO_0000195794"
FT ACT_SITE 98
FT /evidence="ECO:0000250"
FT ACT_SITE 101
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 439 AA; 50140 MW; 4D3CC56A3BFA4E7E CRC64;
MSYFDINKVN YEGPKSNNAF SFKYYNPEEK LGNHSMSELL RFSVAYWHTF TADLSDPFGV
GVAERDWDSL DEMEKAKARV EAIFEFMEKT RIDYFCFHDV DISPEGASLK ESNENLDIIV
ELIKEKMDQT GKKLLWNTTN NFTHERFVHG AATSSNAEVF AYAAAKVKKS LEIAKKLGSE
NFVFWGGREG YESLLNTNMK LELDNLATFF KMAKSYADEI GYTGQFLIEP KPKEPTTHQY
DTDVATAHAF LQKYDLDKDF KFNIEANHAT LAGHTFQHEL RYARDNNMLG SVDANQGHPL
LGWDTDESTD VYDTTLAMYE ILKNGGLAPG GLNFDAKPRR TSFKQEDLIL THIAGMDTFA
LGLRVAYKMI EDNFFENIMD EKYKSFNEGI GKKIVEGETS LKELEDYAFN INTINNTSDH
LEVIKSQINQ YILNINNKD