XYLA_KLEPN
ID XYLA_KLEPN Reviewed; 440 AA.
AC P29442;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Xylose isomerase;
DE Short=XI;
DE EC=5.3.1.5;
GN Name=xylA;
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1033-5P14 / KAY2026;
RX PubMed=1324398; DOI=10.1007/bf00283840;
RA Feldmann S.D., Sahm H., Sprenger G.A.;
RT "Cloning and expression of the genes for xylose isomerase and xylulokinase
RT from Klebsiella pneumoniae 1033 in Escherichia coli K12.";
RL Mol. Gen. Genet. 234:201-210(1992).
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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000305}.
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DR EMBL; X61059; CAA43389.1; -; Genomic_DNA.
DR PIR; S25069; ISKBX.
DR AlphaFoldDB; P29442; -.
DR SMR; P29442; -.
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..440
FT /note="Xylose isomerase"
FT /id="PRO_0000195780"
FT ACT_SITE 101
FT /evidence="ECO:0000250"
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"
SQ SEQUENCE 440 AA; 49919 MW; 7F6D98831F4774C3 CRC64;
MQTYFDQLDR VRYEGPKSTN PLAFRHYNPD ELVLGKRMED HLRFAACYWH TFCWNGADMF
GVGSFDRPWQ QPGDALEMAK RKADVAFEFF HKLNVPYYCF HDVDVSPEGA SLKEYSNNFA
RMVEVLAEKQ QQSGVKLLWG TANCFTNPRY GAGAATNPDP EVFSWAATQV VTAMNATHQL
GGENYVLWGG REGYETLLNT DLRQEREQLG RLLQLVVEHK HKIGFKGTLL IEPKPQEPTK
HQYDYDASTV YGFLKQFGLE KEIKLNIEAN HATLAGHSFH HEIATAIALG LFGSVDANRG
DPQLGWDTDQ FPNRVEEDAL VMYEIFKAGG FTTGGLNFDA KVRRQSTDKY DLFYGHIGAM
DTMAVSLKVA ARMIEDGELD KRVARRYAGW NGELGQQILN GQMTLSDIAQ YAAQHQLAPQ
HRSGQQEQLE NLVNHYLFDK
