ID C7MVG8_SACVD Unreviewed; 257 AA.
AC C7MVG8;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
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=Svir_28160 {ECO:0000313|EMBL:ACU97797.1};
OS Saccharomonospora viridis (strain ATCC 15386 / DSM 43017 / JCM 3036 / NBRC
OS 12207 / P101).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=471857 {ECO:0000313|EMBL:ACU97797.1, ECO:0000313|Proteomes:UP000000841};
RN [1] {ECO:0000313|EMBL:ACU97797.1, ECO:0000313|Proteomes:UP000000841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15386 / DSM 43017 / JCM 3036 / NBRC 12207 / P101
RC {ECO:0000313|Proteomes:UP000000841};
RX PubMed=21304650; DOI=10.4056/sigs.20263;
RA Pati A., Sikorski J., Nolan M., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
RA Goodwin L., Chain P., D'haeseleer P., Chen A., Palaniappan K., Ivanova N.,
RA Mavromatis K., Mikhailova N., Rohde M., Tindall B.J., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Saccharomonospora viridis type strain
RT (P101).";
RL Stand. Genomic Sci. 1:141-149(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; CP001683; ACU97797.1; -; Genomic_DNA.
DR RefSeq; WP_015787109.1; NC_013159.1.
DR AlphaFoldDB; C7MVG8; -.
DR STRING; 471857.Svir_28160; -.
DR KEGG; svi:Svir_28160; -.
DR eggNOG; COG0107; Bacteria.
DR HOGENOM; CLU_048577_4_0_11; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000000841; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000841}.
FT ACT_SITE 12
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01013"
FT ACT_SITE 131
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01013"
SQ SEQUENCE 257 AA; 27140 MW; 8CC7D8E770FB54C4 CRC64;
MSVAVRVIPC LDVDAGRVVK GVNFANLRDA GDPVELARLY DAEGADELTF LDVTASSSNR
ETTYDVVRKT AEQVFIPLTV GGGVRSVDDV DRLLRAGADK VSINTAAVAR PELLREASRR
FGAQCVVLSV DARRVPEGEQ PTPSGFEVTT HGGRRGTGID VVEWAARGEE LGVGEILLNS
VDADGTKEGF DLELLELVRA AVRVPLIASG GAGALEHFPP AVRAGADAVL AASVFHFGEL
KIGDVKAALR EEGVEVR
//
