ID A0A0N0D959_9RHOB Unreviewed; 265 AA.
AC A0A0N0D959;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
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:KPA22034.1};
GN ORFNames=shim_19210 {ECO:0000313|EMBL:KPA22034.1};
OS Shimia sp. SK013.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=1389006 {ECO:0000313|EMBL:KPA22034.1, ECO:0000313|Proteomes:UP000037951};
RN [1] {ECO:0000313|EMBL:KPA22034.1, ECO:0000313|Proteomes:UP000037951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK013 {ECO:0000313|EMBL:KPA22034.1,
RC ECO:0000313|Proteomes:UP000037951};
RA Voget S., Kanukollu S., Daniel R., Engelen B.;
RT "Genome Sequence of Shimia sp. SK013.";
RL Submitted (MAR-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:KPA22034.1}.
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DR EMBL; LAJH01000011; KPA22034.1; -; Genomic_DNA.
DR RefSeq; WP_054002400.1; NZ_LAJH01000011.1.
DR AlphaFoldDB; A0A0N0D959; -.
DR STRING; 1389006.shim_19210; -.
DR PATRIC; fig|1389006.3.peg.1969; -.
DR OrthoDB; 9781903at2; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000037951; 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|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01013};
KW Reference proteome {ECO:0000313|Proteomes:UP000037951}.
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 265 AA; 27603 MW; 6207B92DD797358E CRC64;
MLKTRVIPCL DVADGRVVKG VNFVGLRDAG DPVEAARAYD AAGADEICFL DIHATHDNRG
VMIDMVRRTA EQCFVPLTVG GGVRTVADVR KLLLAGADKV SFNSAAVANP DVIAEAAAQF
GSQCIVCAID AKTIGHDANG VPNKWGIFTH GGRKEALDKD GKPIDAVEFA KLVVAKGAGE
ILLTSMDRDG TKAGFNLPLT RAISDAVSVP VIASGGVGTL DHLVEGVTEG GASAVLAASI
FHFGEFTVQE AKQHMQDAGI PMRLT
//