ID A0A0A7EK55_9GAMM Unreviewed; 257 AA.
AC A0A0A7EK55;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=imidazole glycerol-phosphate synthase {ECO:0000256|ARBA:ARBA00012809};
DE EC=4.3.2.10 {ECO:0000256|ARBA:ARBA00012809};
DE AltName: Full=IGP synthase cyclase subunit {ECO:0000256|ARBA:ARBA00030264};
GN ORFNames=OM33_18400 {ECO:0000313|EMBL:AIY67045.1};
OS Pseudoalteromonas piratica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1348114 {ECO:0000313|EMBL:AIY67045.1, ECO:0000313|Proteomes:UP000030341};
RN [1] {ECO:0000313|EMBL:AIY67045.1, ECO:0000313|Proteomes:UP000030341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OCN003 {ECO:0000313|EMBL:AIY67045.1,
RC ECO:0000313|Proteomes:UP000030341};
RA Beurmann S., Videau P., Ushijima B., Smith A.M., Aeby G.S., Callahan S.M.,
RA Belcaid M.;
RT "Complete Genome Sequence of Pseudoalteromonas sp. Strain OCN003 Isolated
RT from Kaneohe Bay, Oahu, Hawaii.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00025475}.
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 Evidence={ECO:0000256|ARBA:ARBA00000619};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
CC {ECO:0000256|ARBA:ARBA00005091}.
CC -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000256|ARBA:ARBA00011152}.
CC -!- SIMILARITY: Belongs to the HisA/HisF family.
CC {ECO:0000256|ARBA:ARBA00009667, ECO:0000256|RuleBase:RU003657}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP009889; AIY67045.1; -; Genomic_DNA.
DR RefSeq; WP_040135779.1; NZ_CP009889.1.
DR AlphaFoldDB; A0A0A7EK55; -.
DR STRING; 1348114.OM33_18400; -.
DR KEGG; pseo:OM33_18400; -.
DR eggNOG; COG0107; Bacteria.
DR HOGENOM; CLU_048577_4_0_6; -.
DR OrthoDB; 9781903at2; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000030341; Chromosome 2.
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; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006062; His_biosynth.
DR InterPro; IPR004651; HisF.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR NCBIfam; TIGR00735; hisF; 1.
DR PANTHER; PTHR21235:SF2; IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE HISHF; 1.
DR PANTHER; PTHR21235; IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISF/H IGP SYNTHASE SUBUNIT HISF/H; 1.
DR Pfam; PF00977; His_biosynth; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU003657};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102,
KW ECO:0000256|RuleBase:RU003657};
KW Reference proteome {ECO:0000313|Proteomes:UP000030341}.
SQ SEQUENCE 257 AA; 28268 MW; 6D884DBE27B91333 CRC64;
MLSKRIIPCL DVKNNQVVKG VKFKEHEVVG DILQLADAYS KAGADELVFY EITASVEKRL
LDVSWVEQIA RYINIPFCVA GGIKSVADAA KVLEMGADKI SINSPAIARP ELIKELHDEF
GKQCVVVGID SFYDKESDQY LVYQLTGDPN AASQTRYKTE EWVKQVQDLG AGEIVLNCMN
QDGVRRGYDN TQLSKIRAIC DVPLIASGGA GQIQDFADVF TTSNVDGALA ASVFHKGLID
INDLKTELKR QDIAVRL
//
