XYLA_PRIM3
ID XYLA_PRIM3 Reviewed; 445 AA.
AC O08325; D5DF38;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Xylose isomerase;
DE EC=5.3.1.5;
GN Name=xylA; OrderedLocusNames=BMD_1858;
OS Priestia megaterium (strain DSM 319 / IMG 1521) (Bacillus megaterium).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=592022;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1719948; DOI=10.1007/bf00245346;
RA Rygus T., Scheler A., Allmansberger R., Hillen W.;
RT "Molecular cloning, structure, promoters and regulatory elements for
RT transcription of the Bacillus megaterium encoded regulon for xylose
RT utilization.";
RL Arch. Microbiol. 155:535-542(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9076741; DOI=10.1046/j.1365-2958.1997.2881654.x;
RA Schmiedel D., Kintrup M., Kuster E., Hillen W.;
RT "Regulation of expression, genetic organization and substrate specificity
RT of xylose uptake in Bacillus megaterium.";
RL Mol. Microbiol. 23:1053-1062(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 319 / IMG 1521;
RX PubMed=21705586; DOI=10.1128/jb.00449-11;
RA Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K.,
RA Koenig S.S., Creasy H.H., Rosovitz M.J., Riley D.R., Daugherty S.,
RA Martin M., Elbourne L.D., Paulsen I., Biedendieck R., Braun C.,
RA Grayburn S., Dhingra S., Lukyanchuk V., Ball B., Ul-Qamar R., Seibel J.,
RA Bremer E., Jahn D., Ravel J., Vary P.S.;
RT "Genome sequences of the biotechnologically important Bacillus megaterium
RT strains QM B1551 and DSM319.";
RL J. Bacteriol. 193:4199-4213(2011).
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.
CC -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000305}.
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DR EMBL; X57598; CAA40821.1; -; Genomic_DNA.
DR EMBL; Z71474; CAA96094.1; -; Genomic_DNA.
DR EMBL; CP001982; ADF38711.1; -; Genomic_DNA.
DR RefSeq; WP_013082761.1; NC_014103.1.
DR AlphaFoldDB; O08325; -.
DR SMR; O08325; -.
DR EnsemblBacteria; ADF38711; ADF38711; BMD_1858.
DR KEGG; bmd:BMD_1858; -.
DR PATRIC; fig|592022.4.peg.1800; -.
DR HOGENOM; CLU_037261_1_0_9; -.
DR OMA; TLAMYEI; -.
DR Proteomes; UP000002365; 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 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 Xylose metabolism.
FT CHAIN 1..445
FT /note="Xylose isomerase"
FT /id="PRO_0000195764"
FT ACT_SITE 107
FT /evidence="ECO:0000250"
FT ACT_SITE 110
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 313
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 315
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CONFLICT 58
FT /note="T -> Q (in Ref. 1; CAA40821 and 2; CAA96094)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="A -> R (in Ref. 1; CAA40821 and 2; CAA96094)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 445 AA; 50167 MW; 39CB7340E7403622 CRC64;
MVQTSTNKIN HFESANKVLY EGKDSKNPLA FKYYNPEEVV GGKTMKDQLR FSVAYWHTFT
ADGTDPFGAA TMQRSWDRYD GMDLAKARVE AAFQLFETLN VPFFAFHDRD IAPEGSTLQE
TNKNLDVIVT MIKEYMQTSN VKLLWNTANM FTNPRFVHGA ATSCNADVFA YAAAQVKKGL
ETAKELGAEN YVFWGGREGY ETLLNTNLQL ELDNLARFMH MAVDYATEIG YTGQFLIEPK
PKEPTTHQYD TDAATTISFL RQYGLDKYFK LNLEANHATL AGHTFEHELR VARVQGLLGS
VDANQGDPLL GWDTDEFPTD LYSTTLAMYE ILQNGGLGSG GLNFDAKVRR GSFEQDDLLY
AHVAGMDAFA RGLKVAHKLV EDRVFENVIN ERYSSFKEGI GLEIVEGKAN FHTLEQYAFK
NPNIANKSGR QERLKSILNQ YILEV
