ID H6SS10_PARPM Unreviewed; 253 AA.
AC H6SS10;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisF {ECO:0000256|HAMAP-Rule:MF_01013};
DE EC=4.3.2.10 {ECO:0000256|HAMAP-Rule:MF_01013};
DE AltName: Full=IGP synthase cyclase subunit {ECO:0000256|HAMAP-Rule:MF_01013};
DE AltName: Full=IGP synthase subunit HisF {ECO:0000256|HAMAP-Rule:MF_01013};
DE AltName: Full=ImGP synthase subunit HisF {ECO:0000256|HAMAP-Rule:MF_01013};
DE Short=IGPS subunit HisF {ECO:0000256|HAMAP-Rule:MF_01013};
GN Name=hisF {ECO:0000256|HAMAP-Rule:MF_01013,
GN ECO:0000313|EMBL:CCG07689.1};
GN ORFNames=RSPPHO_01063 {ECO:0000313|EMBL:CCG07689.1};
OS Pararhodospirillum photometricum DSM 122.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Pararhodospirillum.
OX NCBI_TaxID=1150469 {ECO:0000313|EMBL:CCG07689.1, ECO:0000313|Proteomes:UP000033220};
RN [1] {ECO:0000313|EMBL:CCG07689.1, ECO:0000313|Proteomes:UP000033220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM122 {ECO:0000313|Proteomes:UP000033220};
RA Duquesne K., Sturgis J.;
RT "Shotgun genome sequence of Phaeospirillum photometricum DSM 122.";
RL Submitted (FEB-2012) 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 ECO:0000256|HAMAP-Rule:MF_01013}.
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, ECO:0000256|HAMAP-
CC Rule:MF_01013};
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, ECO:0000256|HAMAP-Rule:MF_01013}.
CC -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000256|ARBA:ARBA00011152,
CC ECO:0000256|HAMAP-Rule:MF_01013}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01013}.
CC -!- SIMILARITY: Belongs to the HisA/HisF family.
CC {ECO:0000256|ARBA:ARBA00009667, ECO:0000256|HAMAP-Rule:MF_01013,
CC ECO:0000256|RuleBase:RU003657}.
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DR EMBL; HE663493; CCG07689.1; -; Genomic_DNA.
DR RefSeq; WP_014414329.1; NC_017059.1.
DR AlphaFoldDB; H6SS10; -.
DR STRING; 1150469.RSPPHO_01063; -.
DR KEGG; rpm:RSPPHO_01063; -.
DR PATRIC; fig|1150469.3.peg.1211; -.
DR eggNOG; COG0107; Bacteria.
DR HOGENOM; CLU_048577_4_0_5; -.
DR OrthoDB; 9781903at2; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000033220; 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; Aldolase class I; 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 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, ECO:0000256|HAMAP-
KW Rule:MF_01013}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01013};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW Rule:MF_01013};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_01013, ECO:0000313|EMBL:CCG07689.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033220}.
FT ACT_SITE 11
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01013"
FT ACT_SITE 130
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01013"
SQ SEQUENCE 253 AA; 26781 MW; 6D3BCD5D1F64FFCB CRC64;
MLTMRVIPCL DVKDGRVVKG VNFVDLRDAG DPVEQARVYD AAGADELCFL DITASHENRD
TLFDVVARTA EQCFMPLTVG GGVRTLEDIR KLLLAGADKV SINTAAVHHP EFVGEAARKF
GSQCIVVAID AKSVGPNRFE IFTHGGRKPT GIDAVAWARR MTELGAGEIL LTSMDRDGTG
EGFNLPLTRA IADAVSVPVI ASGGVGTLDH LVEGVRDGHA TGVLAASIFH FGTYTIAQAK
AHMAAAGLPM RLC
//
