ID   HIS62_PARMW             Reviewed;         269 AA.
AC   Q7U923;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=SYNW0436;
OS   Parasynechococcus marenigrum (strain WH8102).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Parasynechococcus; Parasynechococcus marenigrum.
OX   NCBI_TaxID=84588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH8102;
RX   PubMed=12917641; DOI=10.1038/nature01943;
RA   Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA   Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA   Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT   "The genome of a motile marine Synechococcus.";
RL   Nature 424:1037-1042(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 Leu. {ECO:0000305}.
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DR   EMBL; BX569690; CAE06951.1; -; Genomic_DNA.
DR   RefSeq; WP_011127310.1; NC_005070.1.
DR   AlphaFoldDB; Q7U923; -.
DR   SMR; Q7U923; -.
DR   STRING; 84588.SYNW0436; -.
DR   EnsemblBacteria; CAE06951; CAE06951; SYNW0436.
DR   KEGG; syw:SYNW0436; -.
DR   eggNOG; COG0107; Bacteria.
DR   HOGENOM; CLU_048577_4_0_3; -.
DR   OMA; CNTVRIF; -.
DR   OrthoDB; 1522718at2; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000001422; 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.
FT   CHAIN           1..269
FT                   /note="Putative imidazole glycerol phosphate synthase
FT                   subunit hisF2"
FT                   /id="PRO_0000142248"
FT   ACT_SITE        133
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   269 AA;  30317 MW;  72D4CA4B347BF3FE CRC64;
     MSKKRIIFVL LYCDGFFCLS RNFKLQRIGD FRWLQRNYNF NYSATFIDEL IILDISRKSR
     DINKFATLLY NLSENIFVPI TAGGGIRSFE DAKVLFENGA DKVCLNTSLI QCPHVSEKIS
     SVYGQQSLVA SIDFKHDHGD FKFFIDNGLI EVQYNIQELI SFLDPLPFCE ILLQSVDRDG
     TGTGFDLTLA NTFRDQLSKP IILLGGAGHS DHLVEGLLHQ STDAVATAHL LNFVGDGLKL
     SREQAQRHSE VSLARWPLLS STSFSTTKH