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Database: UniProt
Entry: E2ZK78_9FIRM
LinkDB: E2ZK78_9FIRM
Original site: E2ZK78_9FIRM 
ID   E2ZK78_9FIRM            Unreviewed;       202 AA.
AC   E2ZK78;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   RecName: Full=Imidazole glycerol phosphate synthase subunit HisH {ECO:0000256|HAMAP-Rule:MF_00278};
DE            EC=4.3.2.10 {ECO:0000256|HAMAP-Rule:MF_00278};
DE   AltName: Full=IGP synthase glutaminase subunit {ECO:0000256|HAMAP-Rule:MF_00278};
DE            EC=3.5.1.2 {ECO:0000256|HAMAP-Rule:MF_00278};
DE   AltName: Full=IGP synthase subunit HisH {ECO:0000256|HAMAP-Rule:MF_00278};
DE   AltName: Full=ImGP synthase subunit HisH {ECO:0000256|HAMAP-Rule:MF_00278};
DE            Short=IGPS subunit HisH {ECO:0000256|HAMAP-Rule:MF_00278};
GN   Name=hisH {ECO:0000256|HAMAP-Rule:MF_00278,
GN   ECO:0000313|EMBL:EFQ06393.1};
GN   ORFNames=HMPREF9436_02081 {ECO:0000313|EMBL:EFQ06393.1};
OS   Faecalibacterium cf. prausnitzii KLE1255.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Faecalibacterium.
OX   NCBI_TaxID=748224 {ECO:0000313|EMBL:EFQ06393.1, ECO:0000313|Proteomes:UP000006028};
RN   [1] {ECO:0000313|EMBL:EFQ06393.1, ECO:0000313|Proteomes:UP000006028}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KLE1255 {ECO:0000313|EMBL:EFQ06393.1,
RC   ECO:0000313|Proteomes:UP000006028};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to IGP,
CC       AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of
CC       glutamine to glutamate and ammonia as part of the synthesis of IGP and
CC       AICAR. The resulting ammonia molecule is channeled to the active site
CC       of HisF. {ECO:0000256|HAMAP-Rule:MF_00278}.
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_00278};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC         Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001062, ECO:0000256|HAMAP-
CC         Rule:MF_00278};
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_00278}.
CC   -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000256|ARBA:ARBA00011152,
CC       ECO:0000256|HAMAP-Rule:MF_00278}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00278}.
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:EFQ06393.1}.
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DR   EMBL; AECU01000170; EFQ06393.1; -; Genomic_DNA.
DR   RefSeq; WP_005943646.1; NZ_GL538340.1.
DR   AlphaFoldDB; E2ZK78; -.
DR   STRING; 748224.HMPREF9436_02081; -.
DR   eggNOG; COG0118; Bacteria.
DR   HOGENOM; CLU_071837_2_2_9; -.
DR   OrthoDB; 9807137at2; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000006028; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
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:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01748; GATase1_IGP_Synthase; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   HAMAP; MF_00278; HisH; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR010139; Imidazole-glycPsynth_HisH.
DR   NCBIfam; TIGR01855; IMP_synth_hisH; 1.
DR   PANTHER; PTHR42701; IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISH; 1.
DR   PANTHER; PTHR42701:SF1; IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISH; 1.
DR   Pfam; PF00117; GATase; 1.
DR   PIRSF; PIRSF000495; Amidotransf_hisH; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00278}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00278};
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_00278,
KW   ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Glycosyltransferase {ECO:0000313|EMBL:EFQ06393.1};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW   Rule:MF_00278};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00278};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00278};
KW   Transferase {ECO:0000313|EMBL:EFQ06393.1}.
FT   DOMAIN          4..199
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   ACT_SITE        78
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00278,
FT                   ECO:0000256|PIRSR:PIRSR000495-1"
FT   ACT_SITE        184
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00278,
FT                   ECO:0000256|PIRSR:PIRSR000495-1"
FT   ACT_SITE        186
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00278,
FT                   ECO:0000256|PIRSR:PIRSR000495-1"
SQ   SEQUENCE   202 AA;  22136 MW;  64A3DBC1024FA1CD CRC64;
     MIAIIDYGVG NLFSLKSSLK QLGLEAVVTA DADTIRKADR LILPGVGAFA DAMAKLEATG
     LVPVMKEEAE RKPLLGICLG MQLLFEKSYE YGEHEGLGFV KGEVCPLEPD LADKSLKVPQ
     IGWNALHIVK DDPLFKYIRE GEYVYYVHSY YGKNCTESTL AVSDYSIPVT GAVRAGRVYG
     TQFHPEKSGD TGLRILKAFA EL
//
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