ID   HIS6_NEIMB              Reviewed;         255 AA.
AC   Q9K0H4;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 111.
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=NMB0628;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
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; AE002098; AAF41053.1; -; Genomic_DNA.
DR   PIR; H81176; H81176.
DR   RefSeq; NP_273671.1; NC_003112.2.
DR   RefSeq; WP_002222827.1; NC_003112.2.
DR   AlphaFoldDB; Q9K0H4; -.
DR   SMR; Q9K0H4; -.
DR   STRING; 122586.NMB0628; -.
DR   PaxDb; Q9K0H4; -.
DR   EnsemblBacteria; AAF41053; AAF41053; NMB0628.
DR   GeneID; 61223645; -.
DR   KEGG; nme:NMB0628; -.
DR   PATRIC; fig|122586.8.peg.796; -.
DR   HOGENOM; CLU_048577_4_0_4; -.
DR   OMA; IFHYKET; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000000425; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IBA:GO_Central.
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..255
FT                   /note="Imidazole glycerol phosphate synthase subunit HisF"
FT                   /id="PRO_0000142188"
FT   ACT_SITE        12
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        131
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   255 AA;  27001 MW;  EAABB234BF30E23C CRC64;
     MALAKRIIPC LDVKDGRVVK GVNFIGLRDA GDPVEAAKRY NGEGADELTF LDITASSDNR
     DTILHIIEEV AGQVFIPLTV GGGVRTVADI RRLLNAGADK VSINTAAVTR PDLIDEAAGF
     FGSQAIVAAV DAKAANPENT RWEIFTHGGR NPTGLDAVEW AVEMQKRGAG EILLTGMDRD
     GTKQGFNLPL TRAVAEAVDI PVIASGGVGN VRHLIEGITE GKADAVLAAG IFHFGEIAIR
     EAKRAMREAG IEVRL