XYLA_PARP8
ID XYLA_PARP8 Reviewed; 441 AA.
AC B2JFE9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Xylose isomerase {ECO:0000255|HAMAP-Rule:MF_00455};
DE EC=5.3.1.5 {ECO:0000255|HAMAP-Rule:MF_00455};
GN Name=xylA {ECO:0000255|HAMAP-Rule:MF_00455}; OrderedLocusNames=Bphy_2342;
OS Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS STM815) (Burkholderia phymatum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=391038;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815;
RX PubMed=25197461; DOI=10.4056/sigs.4861021;
RA Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA Bristow J., Riley M.;
RT "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL Stand. Genomic Sci. 9:763-774(2014).
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:0000255|HAMAP-Rule:MF_00455};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00455};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00455};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00455}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00455}.
CC -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000255|HAMAP-
CC Rule:MF_00455}.
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DR EMBL; CP001043; ACC71517.1; -; Genomic_DNA.
DR RefSeq; WP_012401722.1; NZ_CADFGH010000002.1.
DR AlphaFoldDB; B2JFE9; -.
DR SMR; B2JFE9; -.
DR STRING; 391038.Bphy_2342; -.
DR PRIDE; B2JFE9; -.
DR EnsemblBacteria; ACC71517; ACC71517; Bphy_2342.
DR KEGG; bph:Bphy_2342; -.
DR eggNOG; COG2115; Bacteria.
DR HOGENOM; CLU_037261_1_0_4; -.
DR OMA; TLAMYEI; -.
DR OrthoDB; 481478at2; -.
DR Proteomes; UP000001192; Chromosome 1.
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; IPR013452; Xylose_isom_bac.
DR InterPro; IPR001998; Xylose_isomerase.
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 Reference proteome; Xylose metabolism.
FT CHAIN 1..441
FT /note="Xylose isomerase"
FT /id="PRO_1000200285"
FT ACT_SITE 100
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT ACT_SITE 103
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT BINDING 267
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT BINDING 267
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT BINDING 270
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT BINDING 338
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
SQ SEQUENCE 441 AA; 49397 MW; B32BC893B92CED35 CRC64;
MSYFEHLPAV RYEGPQTDNP FAYRHYDKDK LVLGKRMEDH LRVAVCYWHT FVWPGADMFG
PGTFERPWHH AGDALEMAHA KADHAFELFS KLGTPFYTFH DLDVAPEGDS IKSYVNNFKA
MTDVLARKQE QTGIKLLWGT ANLFSHPRYA AGAATNPNPD VFAFAATQVL NALEATQRLG
GANYVLWGGR EGYETLLNTD LKREREQLGR FMSMVVEHKH KTGFKGALLI EPKPQEPTKH
QYDYDVATVH GFLTQFGLQD EIRVNIEANH ATLAGHSFHH EIANAFALGI FGSVDANRGD
AQNGWDTDQF PNSVEELTLA FYEILRNGGF TTGGMNFDAK VRRQSIDPED IVHGHIGAID
VLAVALERAA HLIEHDRLAA FKQQRYAGWD SDFGRKILAG GYSLESLASD AVQRNIAPRH
VSGQQERLEN IVNQAIFSSA K
