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Database: UniProt
Entry: D8IUE0_HERSS
LinkDB: D8IUE0_HERSS
Original site: D8IUE0_HERSS 
ID   D8IUE0_HERSS            Unreviewed;       202 AA.
AC   D8IUE0;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 73.
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:ADJ65672.1};
GN   OrderedLocusNames=Hsero_4203 {ECO:0000313|EMBL:ADJ65672.1};
OS   Herbaspirillum seropedicae (strain SmR1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herbaspirillum.
OX   NCBI_TaxID=757424 {ECO:0000313|EMBL:ADJ65672.1, ECO:0000313|Proteomes:UP000000329};
RN   [1] {ECO:0000313|EMBL:ADJ65672.1, ECO:0000313|Proteomes:UP000000329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SmR1 {ECO:0000313|EMBL:ADJ65672.1,
RC   ECO:0000313|Proteomes:UP000000329};
RA   Pedrosa F.O., Monteiro R.A., Wassem R., Cruz L.M., Ayub R.A., Colauto N.B.,
RA   Fernandez M.A., Fungaro M.H.P., Grisard E.C., Hungria M., Madeira H.M.F.,
RA   Nodari R.O., Osaku C.A., Petzl-Erler M.L., Terenzi H., Vieira L.G.E.,
RA   Almeida M.I.M., Alves L.R., Arantes O.M.N., Balsanelli E., Barcellos F.G.,
RA   Baura V.A., Binde D.R., Campo R.J., Chubatsu L.S., Chueire L.M.O.,
RA   Ciferri R.R., Correa L.C., da Conceicao Silva J.L., Dabul A.N.G.,
RA   Dambros B.P., Faoro H., Favetti A., Friedermann G., Furlaneto M.C.,
RA   Gasques L.S., Gimenes C.C.T., Gioppo N.M.R., Glienke-Blanco C., Godoy L.P.,
RA   Guerra M.P., Karp S., Kava-Cordeiro V., Margarido V.P., Mathioni S.M.,
RA   Menck-Soares M.A., Murace N.K., Nicolas M.F., Oliveira C.E.C.,
RA   Pagnan N.A.B., Pamphile J.A., Patussi E.V., Pereira L.F.P.,
RA   Pereira-Ferrari L., Pinto F.G.S., Precoma C., Prioli A.J., Prioli S.M.A.P.,
RA   Raittz R.T., Ramos H.J.O., Ribeiro E.M.S.F., Rigo L.U., Rocha C.L.M.S.C.,
RA   Rocha S.N., Santos K., Satori D., Silva A.G., Simao R.C.G., Soares M.A.M.,
RA   Souza E.M., Steffens M.B.R., Steindel M., Tadra-Sfeir M.Z., Takahashi E.K.,
RA   Torres R.A., Valle J.S., Vernal J.I., Vilas-Boas L.A., Watanabe M.A.E.,
RA   Weiss V.A., Yates M.A., Souza E.M.;
RT   "The genome of Herbaspirillum seropedicae SmR1, an endophytic, nitrogen-
RT   fixing, plant-growth promoting beta-Proteobacteria.";
RL   Submitted (APR-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}.
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DR   EMBL; CP002039; ADJ65672.1; -; Genomic_DNA.
DR   RefSeq; WP_013236129.1; NC_014323.1.
DR   AlphaFoldDB; D8IUE0; -.
DR   STRING; 757424.Hsero_4203; -.
DR   MEROPS; C26.965; -.
DR   KEGG; hse:Hsero_4203; -.
DR   eggNOG; COG0118; Bacteria.
DR   HOGENOM; CLU_071837_2_0_4; -.
DR   OMA; DKVPHMG; -.
DR   OrthoDB; 9807137at2; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000000329; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000329};
KW   Transferase {ECO:0000313|EMBL:ADJ65672.1}.
FT   DOMAIN          5..199
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   ACT_SITE        81
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;  22423 MW;  4FE37A3A5AFBEA30 CRC64;
     MITIVNYGMG NLGSLLNMFK RIGVKARIES DPEAVRDAEK LVLPGVGAFD AAMHRINETP
     GLRAALDHKA LIERVPVIGV CLGMQLLTRS SEEGKLPGLG WIDGEAIRFP RIDGLKVPHM
     GWNVAHPATP SALTNDIGIE PRYYFVHSYF VKVDNPVHSL MRTQYGVEFD SAIGRDNIYG
     AQFHPEKSHR FGMKILQNFA EL
//
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