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HIS5_CHRVO
ID   HIS5_CHRVO              Reviewed;         212 AA.
AC   Q7P0F1;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Imidazole glycerol phosphate synthase subunit HisH {ECO:0000255|HAMAP-Rule:MF_00278};
DE            EC=4.3.2.10 {ECO:0000255|HAMAP-Rule:MF_00278};
DE   AltName: Full=IGP synthase glutaminase subunit {ECO:0000255|HAMAP-Rule:MF_00278};
DE            EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_00278};
DE   AltName: Full=IGP synthase subunit HisH {ECO:0000255|HAMAP-Rule:MF_00278};
DE   AltName: Full=ImGP synthase subunit HisH {ECO:0000255|HAMAP-Rule:MF_00278};
DE            Short=IGPS subunit HisH {ECO:0000255|HAMAP-Rule:MF_00278};
GN   Name=hisH {ECO:0000255|HAMAP-Rule:MF_00278}; OrderedLocusNames=CV_0616;
OS   Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC
OS   12614 / NCIMB 9131 / NCTC 9757).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Chromobacterium.
OX   NCBI_TaxID=243365;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC
RC   9757;
RX   PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA   Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T.,
RA   Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R.,
RA   Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F.,
RA   Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S.,
RA   Belo A., van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M.,
RA   Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P.,
RA   Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S.,
RA   Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N.,
RA   Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P.,
RA   Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R.,
RA   Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA   Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J.,
RA   Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F.,
RA   Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z.,
RA   de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F.,
RA   Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A.,
RA   Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C.,
RA   Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M.,
RA   Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C.,
RA   Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R.,
RA   Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M.,
RA   Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R.,
RA   Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT   "The complete genome sequence of Chromobacterium violaceum reveals
RT   remarkable and exploitable bacterial adaptability.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003).
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:0000255|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; Evidence={ECO:0000255|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:0000255|HAMAP-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:0000255|HAMAP-Rule:MF_00278}.
CC   -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000255|HAMAP-
CC       Rule:MF_00278}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00278}.
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DR   EMBL; AE016825; AAQ58292.1; -; Genomic_DNA.
DR   RefSeq; WP_011134171.1; NC_005085.1.
DR   AlphaFoldDB; Q7P0F1; -.
DR   SMR; Q7P0F1; -.
DR   STRING; 243365.CV_0616; -.
DR   EnsemblBacteria; AAQ58292; AAQ58292; CV_0616.
DR   KEGG; cvi:CV_0616; -.
DR   eggNOG; COG0118; Bacteria.
DR   HOGENOM; CLU_071837_2_0_4; -.
DR   OMA; WVYFVHS; -.
DR   OrthoDB; 1726024at2; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000001424; 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-KW.
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   PANTHER; PTHR42701; PTHR42701; 1.
DR   Pfam; PF00117; GATase; 1.
DR   PIRSF; PIRSF000495; Amidotransf_hisH; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR01855; IMP_synth_hisH; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Glutamine amidotransferase;
KW   Histidine biosynthesis; Hydrolase; Lyase; Reference proteome.
FT   CHAIN           1..212
FT                   /note="Imidazole glycerol phosphate synthase subunit HisH"
FT                   /id="PRO_0000152366"
FT   DOMAIN          2..212
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00278"
FT   ACT_SITE        82
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00278"
FT   ACT_SITE        190
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00278"
FT   ACT_SITE        192
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00278"
SQ   SEQUENCE   212 AA;  23359 MW;  4E75EF91DD66E600 CRC64;
     MKVAVIDYGM GNLHSVLKSL QAVNENGADI FLTRDPEAVV KADKVVFPGQ GAMPDCMREL
     NRHGLAEAVR ETTQSKPFFG ICVGAQLLFE HSEEGDTAGL GLFPGKVVRF ADDQVAGGER
     LKVPHMGWNQ VYQTRSHPLF AGIADGERFY FVHSYHFAPA DAALTLAESD YPQRFACIVG
     RGNIFATQFH TEKSHRAGLQ MMKNFLAWDG NV
 
 
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