HIS7_LACLA
ID HIS7_LACLA Reviewed; 200 AA.
AC Q02134; Q9CG93;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 3.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Imidazoleglycerol-phosphate dehydratase;
DE Short=IGPD;
DE EC=4.2.1.19 {ECO:0000250|UniProtKB:P9WML9};
GN Name=hisB; OrderedLocusNames=LL1210; ORFNames=L0068;
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=NCDO 2118;
RX PubMed=1400209; DOI=10.1128/jb.174.20.6571-6579.1992;
RA Delorme C., Ehrlich S.D., Renault P.;
RT "Histidine biosynthesis genes in Lactococcus lactis subsp. lactis.";
RL J. Bacteriol. 174:6571-6579(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=7687248; DOI=10.1128/jb.175.14.4391-4399.1993;
RA Delorme C., Godon J.-J., Ehrlich S.D., Renault P.;
RT "Gene inactivation in Lactococcus lactis: histidine biosynthesis.";
RL J. Bacteriol. 175:4391-4399(1993).
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=D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-
CC 4-yl)-2-oxopropyl phosphate + H2O; Xref=Rhea:RHEA:11040,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57766, ChEBI:CHEBI:58278; EC=4.2.1.19;
CC Evidence={ECO:0000250|UniProtKB:P9WML9};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:O23346};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000250|UniProtKB:O23346};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
CC {ECO:0000250|UniProtKB:P9WML9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase
CC family. {ECO:0000305}.
CC -!- CAUTION: This protein is inactive in the dairy strain IL1403. The
CC histidine biosynthesis pathway is not functional in the dairy strain
CC IL1403. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U92974; AAB81905.1; -; Genomic_DNA.
DR EMBL; AE005176; AAK05308.1; -; Genomic_DNA.
DR PIR; B86776; B86776.
DR PIR; G45734; G45734.
DR RefSeq; NP_267366.1; NC_002662.1.
DR AlphaFoldDB; Q02134; -.
DR SMR; Q02134; -.
DR STRING; 272623.L0068; -.
DR PaxDb; Q02134; -.
DR EnsemblBacteria; AAK05308; AAK05308; L0068.
DR KEGG; lla:L0068; -.
DR PATRIC; fig|272623.7.peg.1307; -.
DR eggNOG; COG0131; Bacteria.
DR HOGENOM; CLU_044308_2_0_9; -.
DR UniPathway; UPA00031; UER00011.
DR Proteomes; UP000002196; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004424; F:imidazoleglycerol-phosphate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd07914; IGPD; 1.
DR Gene3D; 3.30.230.40; -; 2.
DR HAMAP; MF_00076; HisB; 1.
DR InterPro; IPR038494; IGPD_sf.
DR InterPro; IPR000807; ImidazoleglycerolP_deHydtase.
DR InterPro; IPR020565; ImidazoleglycerP_deHydtase_CS.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR23133; PTHR23133; 1.
DR Pfam; PF00475; IGPD; 1.
DR SUPFAM; SSF54211; SSF54211; 2.
DR PROSITE; PS00954; IGP_DEHYDRATASE_1; 1.
DR PROSITE; PS00955; IGP_DEHYDRATASE_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Lyase;
KW Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..200
FT /note="Imidazoleglycerol-phosphate dehydratase"
FT /id="PRO_0000158134"
FT BINDING 13
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 39..47
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 39
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 68..72
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 68
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 69
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 72
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 141
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 165..173
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 165
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 166
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 169
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 195..197
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT VARIANT 145
FT /note="A -> V (in strain: IL1403)"
FT VARIANT 159
FT /note="H -> N (in strain: IL1403)"
FT VARIANT 188
FT /note="S -> A (in strain: IL1403)"
FT CONFLICT 85
FT /note="A -> D (in Ref. 1; AAB81905)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 200 AA; 21963 MW; CA551A3E2ADC1587 CRC64;
MTRISHITRN TKETQIELSI NLDGTGQADI STGIGFLDHM LTLLTFHSDF DLKIIGHGDH
ETVGMDPHHL IEDVAIALGK CISEALGNKL GIRRYGSFTI PMDEALVTCD LDISGRPYLV
FHADLSGNQK LGGYDTEMTE EFFRALAFNA GITLHLNEHY GQNTHHIIEG MFKSTARALK
QAVSIDESKV GEIPSSKGVL
