ID A0A0M8K9D4_9CHLR Unreviewed; 252 AA.
AC A0A0M8K9D4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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:GAP64483.1};
GN ORFNames=ARMA_2906 {ECO:0000313|EMBL:GAP64483.1}, SE16_05900
GN {ECO:0000313|EMBL:KPL88350.1};
OS Ardenticatena maritima.
OC Bacteria; Chloroflexota; Ardenticatenia; Ardenticatenales;
OC Ardenticatenaceae; Ardenticatena.
OX NCBI_TaxID=872965 {ECO:0000313|EMBL:GAP64483.1, ECO:0000313|Proteomes:UP000037784};
RN [1] {ECO:0000313|EMBL:GAP64483.1, ECO:0000313|Proteomes:UP000037784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=110S {ECO:0000313|EMBL:GAP64483.1,
RC ECO:0000313|Proteomes:UP000037784};
RA Kawaichi S., Yoshida T., Sako Y., Nakamura R.;
RT "Draft Genome Sequence of a Heterotrophic Facultative Anaerobic
RT Thermophilic Bacterium, Ardenticatena maritima Strain 110ST.";
RL Genome Announc. 3:e01145-15(2015).
RN [2] {ECO:0000313|EMBL:KPL88350.1, ECO:0000313|Proteomes:UP000050502}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=110S {ECO:0000313|EMBL:KPL88350.1,
RC ECO:0000313|Proteomes:UP000050502};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Whole genome sequence of Ardenticatena maritima DSM 23922.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000037784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=110S {ECO:0000313|Proteomes:UP000037784};
RA Kawaichi S., Yoshida T., Sako Y., Nakamura R.;
RT "Draft Genome Sequence of a Heterotrophic Facultative Anaerobic Bacterium
RT Ardenticatena maritima Strain 110S.";
RL Submitted (AUG-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAP64483.1}.
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DR EMBL; BBZA01000265; GAP64483.1; -; Genomic_DNA.
DR EMBL; LGKN01000004; KPL88350.1; -; Genomic_DNA.
DR RefSeq; WP_054494152.1; NZ_LGKN01000004.1.
DR AlphaFoldDB; A0A0M8K9D4; -.
DR STRING; 872965.SE16_05900; -.
DR PATRIC; fig|872965.6.peg.1211; -.
DR InParanoid; A0A0M8K9D4; -.
DR OrthoDB; 9781903at2; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000037784; Unassembled WGS sequence.
DR Proteomes; UP000050502; Unassembled WGS sequence.
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:KPL88350.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037784}.
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; 27100 MW; 46379013B282A768 CRC64;
MLAKRIIPCL DVKDGRVVKG VNFVNLRDAG DPVEQAIVYD RERADELVFL DISATHEGRA
IMRDVVRRVA ENIFIPFTVG GGIRTVEDMR EILAAGAEKI AINSAAVRQP DLIARGAERF
GSQCIVVAID ARKRPEGWWE VVISGGRIPT GLNAVEWAQE VERLGAGEIL LTSMDADGTQ
AGYDIPLTRA VADAVNIPVI ASGGAGAPEH FYEALTVGGA DAALAASLFH YRTLSIGDVK
AYLRERGVVV RP
//
