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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
 
 
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