ID C7NG18_KYTSD Unreviewed; 266 AA.
AC C7NG18;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
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 OrderedLocusNames=Ksed_09720 {ECO:0000313|EMBL:ACV06018.1};
OS Kytococcus sedentarius (strain ATCC 14392 / DSM 20547 / CCM 314 / 541)
OS (Micrococcus sedentarius).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Kytococcaceae;
OC Kytococcus.
OX NCBI_TaxID=478801 {ECO:0000313|EMBL:ACV06018.1, ECO:0000313|Proteomes:UP000006666};
RN [1] {ECO:0000313|EMBL:ACV06018.1, ECO:0000313|Proteomes:UP000006666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14392 / DSM 20547 / CCM 314 / 541
RC {ECO:0000313|Proteomes:UP000006666};
RX PubMed=21304632; DOI=10.4056/sigs.761;
RA Sims D., Brettin T., Detter J.C., Han C., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F.,
RA Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N.,
RA Mavrommatis K., Chen A., Palaniappan K., D'haeseleer P., Chain P.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Schneider S.,
RA Goker M., Pukall R., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Kytococcus sedentarius type strain (541).";
RL Stand. Genomic Sci. 1:12-20(2009).
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; CP001686; ACV06018.1; -; Genomic_DNA.
DR AlphaFoldDB; C7NG18; -.
DR STRING; 478801.Ksed_09720; -.
DR KEGG; kse:Ksed_09720; -.
DR eggNOG; COG0107; Bacteria.
DR HOGENOM; CLU_048577_4_0_11; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000006666; 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 17
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01013"
FT ACT_SITE 136
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01013"
SQ SEQUENCE 266 AA; 28092 MW; 54DC152AF00C2796 CRC64;
MGAPATRLAR RIVPCLDVRD GRVVKGVRFT DHVDAGGIEE LAARYAAEGA DELVFYDISA
SPQGRAVDID WVRRVARLID IPFSVAGGIR TVEEARAVLH AGADKVSVNT PALERPELVG
ELAGEFGVQC VVVGIDSLRD TDGTWRVRSH TGDPQAMRQA GRSTLEWVAE VVERGAGEVV
LNCMGSDGVR TGYDVEQLAA VRAVCPVPLV ASGGAGSVQD FVDVIEQADV DAALAASVFH
SGAVAIRDVK AALAGRGIEV REQEAR
//
