ID A0A0D3LM91_9BACT Unreviewed; 443 AA.
AC A0A0D3LM91;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Xylose isomerase {ECO:0000256|ARBA:ARBA00011958, 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 ORFNames=D770_24450 {ECO:0000313|EMBL:AHM63135.1};
OS Flammeovirgaceae bacterium 311.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae.
OX NCBI_TaxID=1257021 {ECO:0000313|EMBL:AHM63135.1, ECO:0000313|Proteomes:UP000064112};
RN [1] {ECO:0000313|EMBL:AHM63135.1, ECO:0000313|Proteomes:UP000064112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=311 {ECO:0000313|EMBL:AHM63135.1,
RC ECO:0000313|Proteomes:UP000064112};
RA Fang C.;
RT "Complete bacteria genome obtained just from illumina data.";
RL Submitted (NOV-2012) 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|HAMAP-Rule:MF_00455,
CC ECO:0000256|RuleBase:RU000610}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00455,
CC 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}.
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DR EMBL; CP004371; AHM63135.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D3LM91; -.
DR STRING; 1257021.D770_24450; -.
DR KEGG; fbt:D770_24450; -.
DR PATRIC; fig|1257021.3.peg.5542; -.
DR OrthoDB; 9763981at2; -.
DR Proteomes; UP000064112; 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; IPR013452; Xylose_isom_bac.
DR InterPro; IPR001998; Xylose_isomerase.
DR NCBIfam; TIGR02630; xylose_isom_A; 1.
DR PANTHER; PTHR48320; -; 1.
DR PANTHER; PTHR48320:SF1; XYLOSE ISOMERASE; 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}; Cytoplasm {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:UP000064112};
KW Xylose metabolism {ECO:0000256|ARBA:ARBA00022629, ECO:0000256|HAMAP-
KW Rule:MF_00455}.
FT ACT_SITE 108
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT ACT_SITE 111
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT BINDING 239
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT BINDING 275
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT BINDING 275
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT BINDING 278
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT BINDING 314
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT BINDING 316
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT BINDING 346
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
SQ SEQUENCE 443 AA; 50396 MW; A5E70F7C5EB87573 CRC64;
MSKVVLGDKE YFKGVGQIKY EGRESDNPLA YRWYDENKMV AGKSMKDHFR FAIAYWHSFV
GDGADPFGSP THNYPWNEKK DPIERAKDKM DAAFEFITKM NMPYYCFHDV DVVDYGNDIK
ENDRRLQAMV EYAKQKQAES GVKLLWGTAN LFSHTRYMNG ASTNPDFHVL AHGAAQVKAA
LDATIALGGE NYVFWGGREG YMTLLNTDMK REQEHFARFL HTARDYARKQ GFKGTFFIEP
KPMEPTKHQY DYDAATVAGF LRQYDLMDDF KLNIEVNHAT LAGHTFQHEL QVAADQGLLG
SIDANRGDYQ NGWDTDQFPN DIYELTEAML VFLEAGGLQG GGVNFDAKIR RNSTDPKDLF
YAHVGGADIF ARALLTADAI LQKSDYKKIR QERYASFDSG KGKAFEEGQL SLEDLRAYAI
ENGEPATISG RQEYLENLIN RYI
//
