ID A0A1S2HQ44_9MICO Unreviewed; 256 AA.
AC A0A1S2HQ44;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=BIU96_01405 {ECO:0000313|EMBL:OII13603.1};
OS Curtobacterium sp. MCBA15_008.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=1898736 {ECO:0000313|EMBL:OII13603.1, ECO:0000313|Proteomes:UP000180168};
RN [1] {ECO:0000313|EMBL:OII13603.1, ECO:0000313|Proteomes:UP000180168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCBA15_008 {ECO:0000313|EMBL:OII13603.1,
RC ECO:0000313|Proteomes:UP000180168};
RA Chase A.B., Arevalo P., Polz M.F., Berlemont R., Martiny J.B.;
RT "Evidence for ecological flexibility in the cosmopolitan genus
RT Curtobacterium.";
RL Submitted (SEP-2016) 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:OII13603.1}.
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DR EMBL; MJGN01000012; OII13603.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S2HQ44; -.
DR STRING; 1898736.BIU96_01405; -.
DR OrthoDB; 9781903at2; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000180168; 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}; Lyase {ECO:0000256|HAMAP-Rule:MF_01013}.
FT ACT_SITE 15
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01013"
FT ACT_SITE 134
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01013"
SQ SEQUENCE 256 AA; 26582 MW; FAAEACF570695410 CRC64;
MTAGGVAVRV VPCLDVQGGR VVKGVNFLDL QDAGDPVELA ARYYEQGADE LTFLDVGATV
ENRSTMYDTV TRTAEQVFIP LTVGGGVRSV DDVSRLQQCG ADKIGVNSAA IARPELVGEI
ADRFGAQAVV LSLDVKRSDR MPSGFVVTTH GGRTESDLDA VAWAHEAVER GAGELLVNSI
DADGTKNGFD LELVAAVRAV SSVPVIASGG AGRLEHFAPA VEAGADAVLA ASVFHRGEMT
IGDVKDALRA AGHAVR
//
