ID   HIS62_PROMM             Reviewed;         261 AA.
AC   Q7V958;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Putative imidazole glycerol phosphate synthase subunit hisF2;
DE            EC=4.3.2.10;
DE   AltName: Full=IGP synthase cyclase subunit;
DE   AltName: Full=IGP synthase subunit hisF2;
DE   AltName: Full=ImGP synthase subunit hisF2;
DE            Short=IGPS subunit hisF2;
GN   Name=hisF2; OrderedLocusNames=PMT_0100;
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}.
CC   -!- CAUTION: The potential active site Asp residue in position 11 is
CC       replaced by a Gln. {ECO:0000305}.
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DR   EMBL; BX548175; CAE20275.1; -; Genomic_DNA.
DR   RefSeq; WP_011129479.1; NC_005071.1.
DR   AlphaFoldDB; Q7V958; -.
DR   SMR; Q7V958; -.
DR   STRING; 74547.PMT_0100; -.
DR   EnsemblBacteria; CAE20275; CAE20275; PMT_0100.
DR   KEGG; pmt:PMT_0100; -.
DR   eggNOG; COG0107; Bacteria.
DR   HOGENOM; CLU_048577_4_0_3; -.
DR   OMA; PKYVGDP; -.
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:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04731; HisF; 1.
DR   Gene3D; 3.20.20.70; -; 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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Lyase;
KW   Reference proteome.
FT   CHAIN           1..261
FT                   /note="Putative imidazole glycerol phosphate synthase
FT                   subunit hisF2"
FT                   /id="PRO_0000142201"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   261 AA;  28166 MW;  C9D56A5B1AFCF249 CRC64;
     MLKKRLIPKL QFSIKPSYRG PKPVLVITRQ FDSKRAIGDP VSQAKIYEAQ LADELVLVDL
     EGTSDSWPIL LDTLSNMSES LATPLSVGGG ITSFEQVQQL LDRGADKVVL NSGAVNNPQL
     IDLVANSYGS QCVVISIDIR KESDLSRHVY IDGGSTATDW SLFSWANDCA SRGAGELLIT
     SIDNDGTGTG LDLDSIRQLR YEVNLPLIAS GGCGLAQHFV AGYEVGASAV AAGTFFSQRD
     QNPMQCRSHI RNAGLPIRLE Q