ID   HIS61_PROMM             Reviewed;         256 AA.
AC   Q7V8Q8;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Imidazole glycerol phosphate synthase subunit hisF1;
DE            EC=4.3.2.10;
DE   AltName: Full=IGP synthase cyclase subunit;
DE   AltName: Full=IGP synthase subunit hisF1;
DE   AltName: Full=ImGP synthase subunit hisF1;
DE            Short=IGPS subunit hisF1;
GN   Name=hisF1; OrderedLocusNames=PMT_0274;
OS   Prochlorococcus marinus (strain MIT 9313).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9313;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(2003).
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}.
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DR   EMBL; BX548175; CAE20449.1; -; Genomic_DNA.
DR   RefSeq; WP_011129653.1; NC_005071.1.
DR   AlphaFoldDB; Q7V8Q8; -.
DR   SMR; Q7V8Q8; -.
DR   STRING; 74547.PMT_0274; -.
DR   EnsemblBacteria; CAE20449; CAE20449; PMT_0274.
DR   KEGG; pmt:PMT_0274; -.
DR   eggNOG; COG0107; Bacteria.
DR   HOGENOM; CLU_048577_4_0_3; -.
DR   OMA; IFHYKET; -.
DR   OrthoDB; 1522718at2; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000001423; 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..256
FT                   /note="Imidazole glycerol phosphate synthase subunit hisF1"
FT                   /id="PRO_0000142200"
FT   ACT_SITE        11
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        130
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   256 AA;  26637 MW;  B835225029D606A6 CRC64;
     MVALRLIPCL DVADGRVVKG VNFVGLRDAG DPVELACRYS QAGADELVFL DIAASHEGRA
     TLVALVRRTA EAVTIPFTVG GGISSLDGIT ELLRAGADKV SLNSSAVRDP DLVAQGADRF
     GCQCIVVAID ARRRPECSGW DVFVKGGRQN TGLDAVSWAR QAAELGAGEI LLTSMDGDGT
     QAGYDLELTQ AVVEAVPVPV IASGGAGCLD HIAEAFTIGK ASAALLASLL HDGVLSVEQI
     KTDLLMRGLS IRPLEF