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Database: UniProt
Entry: Q1N2Y8_9GAMM
LinkDB: Q1N2Y8_9GAMM
Original site: Q1N2Y8_9GAMM 
ID   Q1N2Y8_9GAMM            Unreviewed;       210 AA.
AC   Q1N2Y8;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   24-JAN-2024, entry version 84.
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   ORFNames=RED65_06538 {ECO:0000313|EMBL:EAT12531.1};
OS   Bermanella marisrubri.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Bermanella.
OX   NCBI_TaxID=207949 {ECO:0000313|EMBL:EAT12531.1, ECO:0000313|Proteomes:UP000004263};
RN   [1] {ECO:0000313|EMBL:EAT12531.1, ECO:0000313|Proteomes:UP000004263}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RED65 {ECO:0000313|EMBL:EAT12531.1,
RC   ECO:0000313|Proteomes:UP000004263};
RA   Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA   Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA   Venter J.C.;
RL   Submitted (MAR-2006) 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:EAT12531.1}.
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DR   EMBL; AAQH01000006; EAT12531.1; -; Genomic_DNA.
DR   RefSeq; WP_007016132.1; NZ_CP051183.1.
DR   AlphaFoldDB; Q1N2Y8; -.
DR   STRING; 207949.RED65_06538; -.
DR   HOGENOM; CLU_071837_2_2_6; -.
DR   OrthoDB; 9807137at2; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000004263; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000004263};
KW   Transferase {ECO:0000313|EMBL:EAT12531.1}.
FT   DOMAIN          27..202
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   ACT_SITE        85
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00278,
FT                   ECO:0000256|PIRSR:PIRSR000495-1"
FT   ACT_SITE        190
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00278,
FT                   ECO:0000256|PIRSR:PIRSR000495-1"
FT   ACT_SITE        192
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00278,
FT                   ECO:0000256|PIRSR:PIRSR000495-1"
SQ   SEQUENCE   210 AA;  23516 MW;  77354FEE55B42D60 CRC64;
     MEINDNSIGV VDYGCGNLFS VENAIKKITK NYFISSDYEK LKSADRIILP GVGSFSKAMS
     NLRALGIDDL IIEHVNSGKP LLGICLGMQI LLSKGYEHGE TKGLDLVSGE VLLFPSLEGY
     RIPHMGWNEV LYKSDVPNEF ENIDNKTCFY FVHSYYCDVT EDIKKVYVNY CDMDVVVGFE
     KGNIKGVQFH PEKSQDAGIY LLRQFINGGT
//
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