ID A0A0P0GFD5_9BACT Unreviewed; 259 AA.
AC A0A0P0GFD5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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:ALJ56271.1};
GN ORFNames=AMD24_00076 {ECO:0000313|EMBL:ALJ56271.1};
OS Candidatus Xiphinematobacter sp. Idaho Grape.
OC Bacteria; Verrucomicrobiota; Spartobacteria; Xiphinematobacter.
OX NCBI_TaxID=1704307 {ECO:0000313|EMBL:ALJ56271.1, ECO:0000313|Proteomes:UP000062177};
RN [1] {ECO:0000313|EMBL:ALJ56271.1, ECO:0000313|Proteomes:UP000062177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Idaho Grape {ECO:0000313|EMBL:ALJ56271.1,
RC ECO:0000313|Proteomes:UP000062177};
RX PubMed=26362082; DOI=10.1093/gbe/evv176;
RA Brown A.M., Howe D.K., Wasala S.K., Peetz A.B., Zasada I.A., Denver D.R.;
RT "Comparative Genomics of a Plant-Parasitic Nematode Endosymbiont Suggest a
RT Role in Nutritional Symbiosis.";
RL Genome Biol. Evol. 7:2727-2746(2015).
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; CP012665; ALJ56271.1; -; Genomic_DNA.
DR RefSeq; WP_062100174.1; NZ_CP012665.1.
DR AlphaFoldDB; A0A0P0GFD5; -.
DR STRING; 1704307.AMD24_00076; -.
DR KEGG; xii:AMD24_00076; -.
DR PATRIC; fig|1704307.3.peg.79; -.
DR OrthoDB; 9781903at2; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000062177; 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:ALJ56271.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000062177}.
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 259 AA; 27464 MW; 0FEEB952EF9C33D5 CRC64;
MLAKRIIPCL DVSDGRVVKG TRFSALKDVG HPVECAKAYD TQGADELAFL DVNASLDGRR
ALISLIEEVA EVCFVPLTVG GGIRSIEDVR AVLSAGADKV SINTSAVQTP YLIREGAENF
GSQCMMVAID ARHEPGFGWR VYTHGGSKPT PLEAVAWAHR VEDLGAGEIL LTSMDTDGTC
SGYDCKLTKA VSQSIGIPVI ASGGAGDLVH LAQVLTEGSA DAVLAASIFH FGRYTLQAVK
EFLLLKGIAV RHHVQNHPL
//
