ID A0A1N6WLN8_9GAMM Unreviewed; 215 AA.
AC A0A1N6WLN8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=SAMN05421647_11133 {ECO:0000313|EMBL:SIQ91009.1};
OS Marinobacterium stanieri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinobacterium.
OX NCBI_TaxID=49186 {ECO:0000313|EMBL:SIQ91009.1, ECO:0000313|Proteomes:UP000186895};
RN [1] {ECO:0000313|EMBL:SIQ91009.1, ECO:0000313|Proteomes:UP000186895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7027 {ECO:0000313|EMBL:SIQ91009.1,
RC ECO:0000313|Proteomes:UP000186895};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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|HAMAP-
CC Rule:MF_00278}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00278}.
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DR EMBL; FTMN01000011; SIQ91009.1; -; Genomic_DNA.
DR RefSeq; WP_010324413.1; NZ_FTMN01000011.1.
DR AlphaFoldDB; A0A1N6WLN8; -.
DR STRING; 49186.SAMN05421647_11133; -.
DR eggNOG; COG0118; Bacteria.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000186895; 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:SF2; 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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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:UP000186895};
KW Transferase {ECO:0000313|EMBL:SIQ91009.1}.
FT DOMAIN 6..209
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 83
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00278,
FT ECO:0000256|PIRSR:PIRSR000495-1"
FT ACT_SITE 193
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00278,
FT ECO:0000256|PIRSR:PIRSR000495-1"
FT ACT_SITE 195
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00278,
FT ECO:0000256|PIRSR:PIRSR000495-1"
SQ SEQUENCE 215 AA; 23935 MW; 501A33B4EE9C95A9 CRC64;
MSSIAVIDYG MGNLHSVAKA LEHVQPGVEV RVTADPEQVR TADRVLLPGV GAIRDCMAEI
RRLGVDAEVR EAIASGKPFL GICVGYQALM QFSEENNGVD CLGEFEGRVN FFGDDLKDAD
GERLKVPHMG WNQVYQTQDH PLWANIEDGS RFYFVHSYYV KAQQNDLVAA TCNYGVDFDV
AIARDNVFAV QFHPEKSQKV GLQLLQNFLN WNGQP
//
