XYLA_ECOLI
ID XYLA_ECOLI Reviewed; 440 AA.
AC P00944; P00945; Q2M7M8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Xylose isomerase;
DE EC=5.3.1.5 {ECO:0000269|PubMed:2405386, ECO:0000269|PubMed:6325179};
DE AltName: Full=D-xylulose keto-isomerase;
GN Name=xylA; OrderedLocusNames=b3565, JW3537;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MM294 / ATCC 33625 / DSM 5208;
RX PubMed=6320721; DOI=10.1128/aem.47.1.15-21.1984;
RA Lawlis V.B., Dennis M.S., Chen E.Y., Smith D.H., Henner D.J.;
RT "Cloning and sequencing of the xylose isomerase and xylulose kinase genes
RT of Escherichia coli.";
RL Appl. Environ. Microbiol. 47:15-21(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6327696; DOI=10.1016/s0021-9258(17)39802-2;
RA Schellenberg G.D., Sarthy A., Larson A.E., Backer M.P., Crabb J.W.,
RA Lidstrom M., Hall B.D., Furlong C.E.;
RT "Xylose isomerase from Escherichia coli. Characterization of the protein
RT and the structural gene.";
RL J. Biol. Chem. 259:6826-6832(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RX PubMed=6325179; DOI=10.1002/j.1460-2075.1984.tb01856.x;
RA Briggs K.A., Lancashire W.E., Hartley B.S.;
RT "Molecular cloning, DNA structure and expression of the Escherichia coli D-
RT xylose isomerase.";
RL EMBO J. 3:611-616(1984).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2132127;
RA Hou Y.M., Zhang Q.J., Wang S.J.;
RT "Sequence analysis of D-xylose isomerase gene from Escherichia coli.";
RL Chin. J. Biotechnol. 6:269-277(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [8]
RP ACTIVE SITE, AND CATALYTIC ACTIVITY.
RX PubMed=2405386; DOI=10.1073/pnas.87.2.618;
RA Batt C.A., Jamieson A.C., Vandeyar M.A.;
RT "Identification of essential histidine residues in the active site of
RT Escherichia coli xylose (glucose) isomerase.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:618-622(1990).
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:0000269|PubMed:2405386, ECO:0000269|PubMed:6325179};
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA25347.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA28394.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; K01996; AAA24768.1; -; Genomic_DNA.
DR EMBL; X04691; CAA28394.1; ALT_INIT; Genomic_DNA.
DR EMBL; X00772; CAA25346.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X00772; CAA25347.1; ALT_FRAME; Genomic_DNA.
DR EMBL; S68257; AAB20471.2; -; Genomic_DNA.
DR EMBL; U00039; AAB18542.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76589.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77728.1; -; Genomic_DNA.
DR PIR; A30252; ISECX1.
DR RefSeq; NP_418022.1; NC_000913.3.
DR RefSeq; WP_001149591.1; NZ_SSZK01000041.1.
DR AlphaFoldDB; P00944; -.
DR SMR; P00944; -.
DR BioGRID; 4262540; 18.
DR DIP; DIP-11149N; -.
DR IntAct; P00944; 9.
DR MINT; P00944; -.
DR STRING; 511145.b3565; -.
DR jPOST; P00944; -.
DR PaxDb; P00944; -.
DR PRIDE; P00944; -.
DR DNASU; 948141; -.
DR EnsemblBacteria; AAC76589; AAC76589; b3565.
DR EnsemblBacteria; BAE77728; BAE77728; BAE77728.
DR GeneID; 948141; -.
DR KEGG; ecj:JW3537; -.
DR KEGG; eco:b3565; -.
DR PATRIC; fig|1411691.4.peg.3147; -.
DR EchoBASE; EB1067; -.
DR eggNOG; COG2115; Bacteria.
DR HOGENOM; CLU_037261_1_0_6; -.
DR InParanoid; P00944; -.
DR OMA; TLAMYEI; -.
DR PhylomeDB; P00944; -.
DR BioCyc; EcoCyc:XYLISOM-MON; -.
DR BioCyc; MetaCyc:XYLISOM-MON; -.
DR PRO; PR:P00944; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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; IDA:EcoCyc.
DR GO; GO:0042843; P:D-xylose catabolic process; IMP:EcoCyc.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Cytoplasm; Isomerase; Magnesium; Metal-binding;
KW Reference proteome; Xylose metabolism.
FT CHAIN 1..440
FT /note="Xylose isomerase"
FT /id="PRO_0000195774"
FT ACT_SITE 101
FT /evidence="ECO:0000269|PubMed:2405386"
FT ACT_SITE 104
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 271
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CONFLICT 169
FT /note="Q -> E (in Ref. 4; AAB20471)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="R -> L (in Ref. 4; AAB20471)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="V -> D (in Ref. 4; AAB20471)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="E -> D (in Ref. 4; AAB20471)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 440 AA; 49742 MW; 6841659B6EC0561F CRC64;
MQAYFDQLDR VRYEGSKSSN PLAFRHYNPD ELVLGKRMEE HLRFAACYWH TFCWNGADMF
GVGAFNRPWQ QPGEALALAK RKADVAFEFF HKLHVPFYCF HDVDVSPEGA SLKEYINNFA
QMVDVLAGKQ EESGVKLLWG TANCFTNPRY GAGAATNPDP EVFSWAATQV VTAMEATHKL
GGENYVLWGG REGYETLLNT DLRQEREQLG RFMQMVVEHK HKIGFQGTLL IEPKPQEPTK
HQYDYDAATV YGFLKQFGLE KEIKLNIEAN HATLAGHSFH HEIATAIALG LFGSVDANRG
DAQLGWDTDQ FPNSVEENAL VMYEILKAGG FTTGGLNFDA KVRRQSTDKY DLFYGHIGAM
DTMALALKIA ARMIEDGELD KRIAQRYSGW NSELGQQILK GQMSLADLAK YAQEHHLSPV
HQSGRQEQLE NLVNHYLFDK
