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Database: UniProt/TrEMBL
Entry: F8A4T4_CELGA
LinkDB: F8A4T4_CELGA
Original site: F8A4T4_CELGA 
ID   F8A4T4_CELGA            Unreviewed;       396 AA.
AC   F8A4T4;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 73.
DE   RecName: Full=Xylose isomerase {ECO:0000256|ARBA:ARBA00018232, ECO:0000256|HAMAP-Rule:MF_00455};
DE            EC=5.3.1.5 {ECO:0000256|ARBA:ARBA00011958, ECO:0000256|HAMAP-Rule:MF_00455};
GN   Name=xylA {ECO:0000256|HAMAP-Rule:MF_00455};
GN   OrderedLocusNames=Celgi_0378 {ECO:0000313|EMBL:AEI10900.1};
OS   Cellulomonas gilvus (strain ATCC 13127 / NRRL B-14078) (Cellvibrio gilvus).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=593907 {ECO:0000313|EMBL:AEI10900.1, ECO:0000313|Proteomes:UP000000485};
RN   [1] {ECO:0000313|Proteomes:UP000000485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13127 / NRRL B-14078 {ECO:0000313|Proteomes:UP000000485};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Munk A., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D., Brumm P.,
RA   Woyke T.;
RT   "Complete sequence of Cellvibrio gilvus ATCC 13127.";
RL   Submitted (APR-2011) 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:0000256|ARBA:ARBA00033659, ECO:0000256|HAMAP-
CC         Rule:MF_00455, ECO:0000256|RuleBase:RU000609};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00455};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00455};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC       ECO:0000256|HAMAP-Rule:MF_00455, ECO:0000256|RuleBase:RU000610}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00455, ECO:0000256|RuleBase:RU000610}.
CC   -!- SIMILARITY: Belongs to the xylose isomerase family.
CC       {ECO:0000256|ARBA:ARBA00005765, ECO:0000256|HAMAP-Rule:MF_00455,
CC       ECO:0000256|RuleBase:RU000609}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00455}.
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DR   EMBL; CP002665; AEI10900.1; -; Genomic_DNA.
DR   RefSeq; WP_013882425.1; NC_015671.1.
DR   AlphaFoldDB; F8A4T4; -.
DR   STRING; 593907.Celgi_0378; -.
DR   KEGG; cga:Celgi_0378; -.
DR   eggNOG; COG2115; Bacteria.
DR   HOGENOM; CLU_060750_0_0_11; -.
DR   OMA; TLAMYEI; -.
DR   OrthoDB; 9763981at2; -.
DR   Proteomes; UP000000485; 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   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; IPR013022; Xyl_isomerase-like_TIM-brl.
DR   InterPro; IPR013453; XylA_actinobac.
DR   InterPro; IPR013452; Xylose_isom_bac.
DR   InterPro; IPR001998; Xylose_isomerase.
DR   NCBIfam; TIGR02631; xylA_Arthro; 1.
DR   PANTHER; PTHR48306; XYLOSE ISOMERASE; 1.
DR   PANTHER; PTHR48306:SF1; XYLOSE ISOMERASE; 1.
DR   Pfam; PF01261; AP_endonuc_2; 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 {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW   Rule:MF_00455};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00455};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00455};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00455};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00455}; Reference proteome {ECO:0000313|Proteomes:UP000000485};
KW   Xylose metabolism {ECO:0000256|ARBA:ARBA00022629, ECO:0000256|HAMAP-
KW   Rule:MF_00455}.
FT   DOMAIN          41..279
FT                   /note="Xylose isomerase-like TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01261"
FT   ACT_SITE        54
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   ACT_SITE        57
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   BINDING         181
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   BINDING         217
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   BINDING         217
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   BINDING         220
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   BINDING         245
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   BINDING         293
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
SQ   SEQUENCE   396 AA;  43513 MW;  D3BB49828610C5E3 CRC64;
     MVRKPTPADK FSFGLWTVGW NAQDPFGSAT RPWLDPVESV HKLAELGAAH VTFHDDDVVP
     FGSSDAEREK ILDRFKGALA ETGITVEMVT TNTFSHPIFK DGAFTSNDRR VRRYALRKIL
     RNVDLAASLD ADTFVMWGGR EGAEYDSAKD LYAAHQAYAD GIDTVAAYIK EKGYKLRIAL
     EPKPNEPRGD ILLPTIGHAL GLIAKLENGD IVGLNPETGH EQMAGLNYTT GLAQALWAEK
     LFHIDLNGQR GIKYDQDLVF GHGDLFSAFA TVDLLENGFP GGGPKYTGPV HFDYKPSRTE
     DFDGVWESAR ANMATYLLLK ERAIAFREDP EVKEALEAAG VLELAKPTLN EGETLADFLA
     DRSAFEDFDV EGVAKHGFGF VRLNQLALEH ALGARG
//
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