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Database: UniProt
Entry: E6WFF4_PANSA
LinkDB: E6WFF4_PANSA
Original site: E6WFF4_PANSA 
ID   E6WFF4_PANSA            Unreviewed;       258 AA.
AC   E6WFF4;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 74.
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   OrderedLocusNames=Pat9b_2568 {ECO:0000313|EMBL:ADU69868.1};
OS   Pantoea sp. (strain At-9b).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=592316 {ECO:0000313|EMBL:ADU69868.1, ECO:0000313|Proteomes:UP000001624};
RN   [1] {ECO:0000313|EMBL:ADU69868.1, ECO:0000313|Proteomes:UP000001624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=At-9b {ECO:0000313|EMBL:ADU69868.1,
RC   ECO:0000313|Proteomes:UP000001624};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pinto A., Currie C., Woyke T.;
RT   "Complete sequence chromosome of Pantoea sp. At-9b.";
RL   Submitted (DEC-2010) 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; CP002433; ADU69868.1; -; Genomic_DNA.
DR   RefSeq; WP_013509723.1; NC_014837.1.
DR   AlphaFoldDB; E6WFF4; -.
DR   STRING; 592316.Pat9b_2568; -.
DR   KEGG; pao:Pat9b_2568; -.
DR   eggNOG; COG0107; Bacteria.
DR   HOGENOM; CLU_048577_4_0_6; -.
DR   OMA; IFHYKET; -.
DR   OrthoDB; 9781903at2; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000001624; 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|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01013}.
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   258 AA;  28268 MW;  4BE1D1E9DB31DCE7 CRC64;
     MLAKRIIPCL DVRDGQVVKG VQFRNHEIIG DIVPLAQRYA QEGADELVFY DITASSDGRV
     VDKSWVSRVA EVIDIPFCVA GGIKSEADAA RILEFGADKI SINSPALADP SLITRLADRF
     GVQCIVVGID TWFDDATGKY HVNQYTGDES RTRVTQWETL DWVQEVQKLG AGEIVLNMMN
     QDGVRNGYDL VQLKKVRDVC KVPLIASGGA GTMAHFLEAF EQANVDGALA ASVFHKQIIN
     IGELKSFLID NGVEIRAC
//
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