ID   HIS6_LACLA              Reviewed;         259 AA.
AC   Q02133; Q9CG91;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 3.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=Imidazole glycerol phosphate synthase subunit HisF;
DE            EC=4.3.2.10;
DE   AltName: Full=IGP synthase cyclase subunit;
DE   AltName: Full=IGP synthase subunit HisF;
DE   AltName: Full=ImGP synthase subunit HisF;
DE            Short=IGPS subunit HisF;
GN   Name=hisF; OrderedLocusNames=LL1214; ORFNames=L0071;
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 [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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-83.
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).
CC   -!- FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to IGP,
CC       AICAR and glutamate. The HisF subunit catalyzes the cyclization
CC       activity that produces IGP and AICAR from PRFAR using the ammonia
CC       provided by the HisH subunit (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-
CC         phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-
CC         amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-
CC         erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate;
CC         Xref=Rhea:RHEA:24793, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:58278, ChEBI:CHEBI:58359, ChEBI:CHEBI:58475,
CC         ChEBI:CHEBI:58525; EC=4.3.2.10;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
CC   -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}.
CC   -!- CAUTION: The histidine biosynthesis pathway is not functional in the
CC       dairy strain IL1403. {ECO:0000305}.
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DR   EMBL; U92974; AAB81909.1; -; Genomic_DNA.
DR   EMBL; AE005176; AAK05312.1; -; Genomic_DNA.
DR   PIR; B47754; B47754.
DR   PIR; F86776; F86776.
DR   RefSeq; NP_267370.1; NC_002662.1.
DR   AlphaFoldDB; Q02133; -.
DR   SMR; Q02133; -.
DR   STRING; 272623.L0071; -.
DR   PaxDb; Q02133; -.
DR   EnsemblBacteria; AAK05312; AAK05312; L0071.
DR   KEGG; lla:L0071; -.
DR   PATRIC; fig|272623.7.peg.1311; -.
DR   eggNOG; COG0107; Bacteria.
DR   HOGENOM; CLU_048577_4_0_9; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000002196; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd04731; HisF; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01013; HisF; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006062; His_biosynth.
DR   InterPro; IPR004651; HisF.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   Pfam; PF00977; His_biosynth; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
DR   TIGRFAMs; TIGR00735; hisF; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Lyase;
KW   Reference proteome.
FT   CHAIN           1..259
FT                   /note="Imidazole glycerol phosphate synthase subunit HisF"
FT                   /id="PRO_0000142170"
FT   ACT_SITE        11
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        130
FT                   /evidence="ECO:0000255"
FT   VARIANT         25
FT                   /note="G -> S (in strain: IL1403)"
FT   VARIANT         32
FT                   /note="P -> S (in strain: IL1403)"
FT   VARIANT         79
FT                   /note="V -> F (in strain: IL1403)"
FT   VARIANT         120
FT                   /note="F -> L (in strain: IL1403)"
FT   VARIANT         226
FT                   /note="F -> V (in strain: IL1403)"
FT   CONFLICT        235..258
FT                   /note="ATVDEVKDELIKNNIPARIIKKET -> EQLMKLKTN (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   259 AA;  28296 MW;  62E79FEF4A82B9A9 CRC64;
     MLTKRIIPCL DIKNGKVVKG INFVGLREIG DPVELAKIYE EQCADEIVFL DITASFEERE
     IIGELIGRAA RELSIPLTVG GGIRSIDDFR RILARGADKV SVNSAAIENP ELIRQAANEF
     GVQCVVVAID AKKRADHRGY DVYIKGGREN AGLDLVDWAK KCERLGAGEI LLTSMDKDGT
     KTGYDLEMLN DVCTAVNIPV VASGGCGKIS DIVEVFQNTR SDAALFASLF HYGEATVDEV
     KDELIKNNIP ARIIKKETL