ID A0A045KJB7_MYCTX Unreviewed; 267 AA.
AC A0A045KJB7;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 80.
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:SGI46060.1};
GN ORFNames=A4S10_01684 {ECO:0000313|EMBL:OMH59516.1}, ERS007661_01268
GN {ECO:0000313|EMBL:CNU85237.1}, ERS007679_00414
GN {ECO:0000313|EMBL:COU80692.1}, ERS007681_01088
GN {ECO:0000313|EMBL:CFE38685.1}, ERS007688_00445
GN {ECO:0000313|EMBL:CFE46850.1}, ERS007720_00908
GN {ECO:0000313|EMBL:COV78049.1}, ERS007741_01374
GN {ECO:0000313|EMBL:COW06811.1}, ERS027646_01597
GN {ECO:0000313|EMBL:CKS29019.1}, ERS027659_03062
GN {ECO:0000313|EMBL:CKS40846.1}, ERS053720_02075
GN {ECO:0000313|EMBL:CFH82194.1}, SAMEA2683035_03642
GN {ECO:0000313|EMBL:SGI46060.1};
OS Mycobacterium tuberculosis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=1773 {ECO:0000313|EMBL:SGI46060.1, ECO:0000313|Proteomes:UP000182946};
RN [1] {ECO:0000313|EMBL:CFH82194.1, ECO:0000313|Proteomes:UP000046674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0351H {ECO:0000313|EMBL:CFH82194.1,
RC ECO:0000313|Proteomes:UP000046674};
RG Pathogen Informatics;
RA Murphy D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OMH59516.1, ECO:0000313|Proteomes:UP000189452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6548 {ECO:0000313|EMBL:OMH59516.1,
RC ECO:0000313|Proteomes:UP000189452};
RA Bigi M., Bigi F., Soria M.A.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SGI46060.1, ECO:0000313|Proteomes:UP000182946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2926STDY5723788 {ECO:0000313|EMBL:SGI46060.1,
RC ECO:0000313|Proteomes:UP000182946}, Bir 172
RC {ECO:0000313|EMBL:CKS29019.1, ECO:0000313|Proteomes:UP000048948}, Bir
RC 185 {ECO:0000313|EMBL:CKS40846.1, ECO:0000313|Proteomes:UP000050164},
RC D00501624 {ECO:0000313|EMBL:CNU85237.1,
RC ECO:0000313|Proteomes:UP000039217}, G09801536
RC {ECO:0000313|EMBL:COU80692.1, ECO:0000313|Proteomes:UP000045842},
RC G09901357 {ECO:0000313|EMBL:CFE38685.1,
RC ECO:0000313|Proteomes:UP000048289}, H09601792
RC {ECO:0000313|EMBL:CFE46850.1, ECO:0000313|Proteomes:UP000046947},
RC M09401471 {ECO:0000313|EMBL:COV78049.1,
RC ECO:0000313|Proteomes:UP000044938}, and P00601463
RC {ECO:0000313|EMBL:COW06811.1, ECO:0000313|Proteomes:UP000048600};
RG Pathogen Informatics;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:OMH59516.1, ECO:0000313|Proteomes:UP000189452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6548 {ECO:0000313|EMBL:OMH59516.1,
RC ECO:0000313|Proteomes:UP000189452};
RA Bigi M.M., Lopez B., Blanco F.C., Sasiain M.C., De La Barrera S.,
RA Ritacco V., Bigi F., Soria M.A.;
RT "Protein polymorphisms may explain contrasting epidemiological fitness of
RT two variants of a multidrug-resistant Mycobacterium tuberculosis strain.";
RL Submitted (FEB-2017) 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}.
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DR EMBL; CFOE01000098; CFE38685.1; -; Genomic_DNA.
DR EMBL; CFOH01000040; CFE46850.1; -; Genomic_DNA.
DR EMBL; CFSW01000011; CFH82194.1; -; Genomic_DNA.
DR EMBL; CNGE01000241; CKS29019.1; -; Genomic_DNA.
DR EMBL; CNFT01000826; CKS40846.1; -; Genomic_DNA.
DR EMBL; CQQC01000335; CNU85237.1; -; Genomic_DNA.
DR EMBL; CSAD01000030; COU80692.1; -; Genomic_DNA.
DR EMBL; CSAJ01000077; COV78049.1; -; Genomic_DNA.
DR EMBL; CHKL01000118; COW06811.1; -; Genomic_DNA.
DR EMBL; LWDQ01000001; OMH59516.1; -; Genomic_DNA.
DR EMBL; FPTZ01000036; SGI46060.1; -; Genomic_DNA.
DR RefSeq; WP_003898942.1; NZ_WUCS01000009.1.
DR GeneID; 45425573; -.
DR PATRIC; fig|1773.2321.peg.1352; -.
DR OMA; WEVYIHG; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000039217; Unassembled WGS sequence.
DR Proteomes; UP000044938; Unassembled WGS sequence.
DR Proteomes; UP000045842; Unassembled WGS sequence.
DR Proteomes; UP000046674; Unassembled WGS sequence.
DR Proteomes; UP000046947; Unassembled WGS sequence.
DR Proteomes; UP000048289; Unassembled WGS sequence.
DR Proteomes; UP000048600; Unassembled WGS sequence.
DR Proteomes; UP000048948; Unassembled WGS sequence.
DR Proteomes; UP000050164; Unassembled WGS sequence.
DR Proteomes; UP000182946; Unassembled WGS sequence.
DR Proteomes; UP000189452; 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:SGI46060.1}.
FT ACT_SITE 22
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01013"
FT ACT_SITE 141
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01013"
SQ SEQUENCE 267 AA; 27221 MW; 2DAF561C3398EBA5 CRC64;
MYADRDLPGA GGLAVRVIPC LDVDDGRVVK GVNFENLRDA GDPVELAAVY DAEGADELTF
LDVTASSSGR ATMLEVVRRT AEQVFIPLTV GGGVRTVADV DSLLRAGADK VAVNTAAIAC
PDLLADMARQ FGSQCIVLSV DARTVPVGSA PTPSGWEVTT HGGRRGTGMD AVQWAARGAD
LGVGEILLNS MDADGTKAGF DLALLRAVRA AVTVPVIASG GAGAVEHFAP AVAAGADAVL
AASVFHFREL TIGQVKAALA AEGITVR
//
