ID X4Z5M3_9BACL Unreviewed; 252 AA.
AC X4Z5M3;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
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 ORFNames=PSAB_00695 {ECO:0000313|EMBL:AHV95081.1};
OS Paenibacillus sabinae T27.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1268072 {ECO:0000313|EMBL:AHV95081.1, ECO:0000313|Proteomes:UP000019772};
RN [1] {ECO:0000313|EMBL:AHV95081.1, ECO:0000313|Proteomes:UP000019772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T27 {ECO:0000313|EMBL:AHV95081.1,
RC ECO:0000313|Proteomes:UP000019772};
RX PubMed=24651173;
RA Xie J.B., Du Z., Bai L., Tian C., Zhang Y., Xie J.Y., Wang T., Liu X.,
RA Chen X., Cheng Q., Chen S., Li J.;
RT "Comparative Genomic Analysis of N2-Fixing and Non-N2-Fixing Paenibacillus
RT spp.: Organization, Evolution and Expression of the Nitrogen Fixation
RT Genes.";
RL PLoS Genet. 10:E1004231-E1004231(2014).
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; CP004078; AHV95081.1; -; Genomic_DNA.
DR RefSeq; WP_025332689.1; NZ_CP004078.1.
DR AlphaFoldDB; X4Z5M3; -.
DR STRING; 1268072.PSAB_00695; -.
DR KEGG; psab:PSAB_00695; -.
DR PATRIC; fig|1268072.3.peg.146; -.
DR eggNOG; COG0107; Bacteria.
DR HOGENOM; CLU_048577_4_0_9; -.
DR OrthoDB; 9781903at2; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000019772; 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}; Lyase {ECO:0000256|HAMAP-Rule:MF_01013}.
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 252 AA; 26870 MW; 671AE218A2BEC337 CRC64;
MLAKRIIPCL DVKDGRVVKG VNFVNLRDAG DPVELAAIYD REGADELVFL DISASVEGRA
TMVEVVRRTA GEISIPFTVG GGISAPEHMK TILRAGADKI GINTAAVNNP QLILEGARRF
GSQCIVVAVD AKYNESWGEW EVYTHGGRKP SGIKALEWVK QAEKLGAGEI LLTSMDADGT
KDGFDIKLTS AVSDLVDIPV IASGGAGKIE HFHDVFTAGK ADAGLAATIF HYKEIAIGDL
KADLKQKGVE IR
//
