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
//