ID A0A1P8U8X9_9MICO Unreviewed; 254 AA.
AC A0A1P8U8X9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=BOH66_10210 {ECO:0000313|EMBL:APZ34569.1};
OS Microbacterium aurum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=36805 {ECO:0000313|EMBL:APZ34569.1, ECO:0000313|Proteomes:UP000187185};
RN [1] {ECO:0000313|EMBL:APZ34569.1, ECO:0000313|Proteomes:UP000187185}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC 15219 {ECO:0000313|EMBL:APZ34569.1,
RC ECO:0000313|Proteomes:UP000187185};
RA Jung Y., Shin J.-H., Lee Y.-J., Yi H., Bahn Y.-S., Kim J.F., Lee D.-W.;
RT "Complete genome sequence of Microbacterium aurum KACC 15219.";
RL Submitted (DEC-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}.
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DR EMBL; CP018762; APZ34569.1; -; Genomic_DNA.
DR RefSeq; WP_076690880.1; NZ_JAFBCQ010000001.1.
DR AlphaFoldDB; A0A1P8U8X9; -.
DR STRING; 36805.BOH66_10210; -.
DR KEGG; maur:BOH66_10210; -.
DR OrthoDB; 9781903at2; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000187185; 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:UP000187185}.
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 254 AA; 26406 MW; 7899FE49B0F60C59 CRC64;
MTLACRVIPC LDVAAGRVVK GVNFENLRDM GDPVELAALY YAQGADELTL LDVTATVDER
ATTYDVVRRT AEEVFIPLTV GGGVRSTDDV ARLLAVGADK VGVNSAAIAR PALIDEIADR
FGSQVLVLSL DVKRAAGTRS GFVVTTHGGR TATDLDALDW AREAIDRGVG ELLVNSIDAD
GTKDGFDLEL VGLMRELSSV PVIASGGAGA VTDFAPALRA GADAVLAASV FHSGQLSIGD
VKDALVADGI EVRR
//
