XYLA_LACLA
ID XYLA_LACLA Reviewed; 439 AA.
AC Q9CFG7; Q93K17; Q9RAV8; Q9X416; Q9X422;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Xylose isomerase;
DE EC=5.3.1.5;
GN Name=xylA; OrderedLocusNames=LL1509; ORFNames=L0230;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=210, ATCC 15577 / DSM 20175 / JCM 1158 / NRRL B-4449 / NCFB 2738,
RC and IO-1;
RA Erlandson K.A., Park J.-H., Delamarre S.C., El Khal W., Kao H.-H.,
RA Basaran P., Brydges S.D., Batt C.A.;
RT "The xylose and xylan loci of Lactococcus lactis.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Basaran P.;
RT "Lactococcus lactis xylose isomerase.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
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; AF092040; AAD20243.1; -; Genomic_DNA.
DR EMBL; AF092041; AAD20249.1; -; Genomic_DNA.
DR EMBL; AF092042; AAD20255.1; -; Genomic_DNA.
DR EMBL; AJ344090; CAC51082.1; -; Genomic_DNA.
DR EMBL; AE005176; AAK05607.1; -; Genomic_DNA.
DR PIR; E86813; E86813.
DR RefSeq; NP_267665.1; NC_002662.1.
DR RefSeq; WP_010906012.1; NC_002662.1.
DR AlphaFoldDB; Q9CFG7; -.
DR SMR; Q9CFG7; -.
DR STRING; 272623.L0230; -.
DR PaxDb; Q9CFG7; -.
DR EnsemblBacteria; AAK05607; AAK05607; L0230.
DR KEGG; lla:L0230; -.
DR PATRIC; fig|272623.7.peg.1619; -.
DR eggNOG; COG2115; Bacteria.
DR HOGENOM; CLU_037261_1_0_9; -.
DR OMA; TLAMYEI; -.
DR SABIO-RK; Q9CFG7; -.
DR Proteomes; UP000002196; 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; IPR013022; Xyl_isomerase-like_TIM-brl.
DR InterPro; IPR013452; Xylose_isom_bac.
DR InterPro; IPR001998; Xylose_isomerase.
DR Pfam; PF01261; AP_endonuc_2; 1.
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..439
FT /note="Xylose isomerase"
FT /id="PRO_0000195782"
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"
FT VARIANT 202
FT /note="R -> M (in strain: NRRL B-4449 and IO-1)"
FT VARIANT 218
FT /note="D -> Y (in strain: 210)"
FT VARIANT 247
FT /note="A -> S (in strain: NRRL B-4449 and IO-1)"
FT VARIANT 275
FT /note="V -> A (in strain: NRRL B-4449 and IO-1)"
FT VARIANT 388
FT /note="T -> S (in strain: NRRL B-4449 and IO-1)"
FT VARIANT 407
FT /note="E -> K (in strain: IO-1)"
FT VARIANT 416
FT /note="H -> Y (in strain: NRRL B-4449)"
FT CONFLICT 112
FT /note="L -> S (in Ref. 2; CAC51082)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="L -> I (in Ref. 2; CAC51082)"
FT /evidence="ECO:0000305"
FT CONFLICT 289..290
FT /note="FN -> IY (in Ref. 2; CAC51082)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="A -> P (in Ref. 2; CAC51082)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="N -> R (in Ref. 2; CAC51082)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="L -> H (in Ref. 2; CAC51082)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="H -> N (in Ref. 2; CAC51082)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="E -> G (in Ref. 2; CAC51082)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 439 AA; 49618 MW; 7744A3655B81B759 CRC64;
MAYFNDIAPI KYEGTKTKNM FAFRHYNPEE VVAGKTMEEQ LHFALAFWHT ITMDGSDPFG
GATMERPWDL EGGSELDRAH RRVDAFFEIA EKLGVKYYCF HDIDIAPTGN SLKEFYANLD
EITDHLLEKQ KATGIKLLWN TANMFSNPRY MNGVSTSNRA EVFAYGAAQV KKGLELSKKL
GGENYVFWGG REGYESLLNT DRGLEMDHMA KFFHLAIDYA KSINHLPIFL IEPKPKEPMT
HQYDFDAATA LAFLQKYDLD KYFKLNLETN HAWLVGHTFE HELNTARTFN ALGSIDANQG
NYLLGWDTDE FPTLVIDITL AMHQILLNGG LGKGGINFDA KVRRTSFKAE DLILAHIAGM
DTYARALKGA AAIIEDKFLS DIVDERYTSY KNTEVGQSIE NGTATFESLA AFALEHGDDI
ELDSNHLEYI KSVLNDYLV
