ID W0P0I2_BUCMP Unreviewed; 196 AA.
AC W0P0I2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
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:0000313|EMBL:AHG60266.1};
GN Synonyms=hisH {ECO:0000256|HAMAP-Rule:MF_00278};
GN ORFNames=BUMPUSDA_CDS00491 {ECO:0000313|EMBL:AHG60266.1};
OS Buchnera aphidicola str. USDA (Myzus persicae).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=1009856 {ECO:0000313|EMBL:AHG60266.1, ECO:0000313|Proteomes:UP000019087};
RN [1] {ECO:0000313|EMBL:AHG60266.1, ECO:0000313|Proteomes:UP000019087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=str. USDA (Myzus persicae) {ECO:0000313|Proteomes:UP000019087};
RX PubMed=24365332; DOI=10.1186/1471-2164-14-917;
RA Jiang Z., Jones D.H., Khuri S., Tsinoremas N.F., Wyss T., Jander G.,
RA Wilson A.C.;
RT "Comparative analysis of genome sequences from four strains of the Buchnera
RT aphidicola Mp endosymbion of the green peach aphid, Myzus persicae.";
RL BMC Genomics 14:917-917(2013).
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|ARBA:ARBA00025299, ECO:0000256|HAMAP-
CC 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}.
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DR EMBL; CP002697; AHG60266.1; -; Genomic_DNA.
DR RefSeq; WP_025368750.1; NZ_CP002697.1.
DR AlphaFoldDB; W0P0I2; -.
DR KEGG; bapu:BUMPUSDA_CDS00491; -.
DR PATRIC; fig|1009856.3.peg.94; -.
DR HOGENOM; CLU_071837_0_0_6; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000019087; Chromosome.
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}.
FT DOMAIN 5..194
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 77
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00278,
FT ECO:0000256|PIRSR:PIRSR000495-1"
FT ACT_SITE 178
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00278,
FT ECO:0000256|PIRSR:PIRSR000495-1"
FT ACT_SITE 180
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00278,
FT ECO:0000256|PIRSR:PIRSR000495-1"
SQ SEQUENCE 196 AA; 21881 MW; 3EB7FACE0FD064D3 CRC64;
MDIVIVDTGC ANLTSIQVAI KRLGYNSIIT SQPSILSKSK KIFLPGVGTA SAVMKVLSEK
KLINIIRDFK KPILGICLGM QLLCNFSEEC QGVKTIGIIP TAVLRLKTNN LPLPHIGWNQ
IAFDTFHPLF EKISNNSRFY FVHSYIVPIN QYTLSTTDYG INFSSVIQKN NFFGVQFHPE
KSGHVGSQLL KNFLEM
//
