(data stored in ACNUC7421 zone)

SWISSPROT: A0A0F6BII9_GEOS0

ID   A0A0F6BII9_GEOS0        Unreviewed;       211 AA.
AC   A0A0F6BII9;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 27.
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   OrderedLocusNames=GY4MC1_0399 {ECO:0000313|EMBL:ADP73240.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73240.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73240.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73240.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to
CC       IGP, AICAR and glutamate. The HisH subunit catalyzes the
CC       hydrolysis of glutamine to glutamate and ammonia as part of the
CC       synthesis of IGP and AICAR. The resulting ammonia molecule is
CC       channeled to the active site of HisF. {ECO:0000256|HAMAP-
CC       Rule:MF_00278}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-
CC         (5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
CC         = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide +
CC         D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-
CC         glutamate; Xref=Rhea:RHEA:24793, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58278, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:58475, ChEBI:CHEBI:58525; EC=4.3.2.10;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00278,
CC         ECO:0000256|SAAS:SAAS01122713};
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|HAMAP-Rule:MF_00278,
CC         ECO:0000256|SAAS:SAAS01122752};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
CC       {ECO:0000256|HAMAP-Rule:MF_00278, ECO:0000256|SAAS:SAAS00064613}.
CC   -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000256|HAMAP-
CC       Rule:MF_00278, ECO:0000256|SAAS:SAAS00234842}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00278,
CC       ECO:0000256|SAAS:SAAS00234863}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP002293; ADP73240.1; -; Genomic_DNA.
DR   RefSeq; WP_013400004.1; NC_014650.1.
DR   EnsemblBacteria; ADP73240; ADP73240; GY4MC1_0399.
DR   KEGG; gmc:GY4MC1_0399; -.
DR   KO; K02501; -.
DR   OMA; WVYFVHS; -.
DR   OrthoDB; 1726024at2; -.
DR   BioCyc; GSP581103:G1GOQ-444-MONOMER; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000002034; 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   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;
DR   PRODOM; A0A0F6BII9.
DR   SWISS-2DPAGE; A0A0F6BII9.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00278,
KW   ECO:0000256|SAAS:SAAS00448459};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00278,
KW   ECO:0000256|SAAS:SAAS00234860};
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_00278,
KW   ECO:0000256|PROSITE-ProRule:PRU00605, ECO:0000256|SAAS:SAAS00064635,
KW   ECO:0000313|EMBL:ADP73240.1};
KW   Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00278,
KW   ECO:0000256|SAAS:SAAS00448489};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00278,
KW   ECO:0000256|SAAS:SAAS01122743};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00278,
KW   ECO:0000256|SAAS:SAAS01122735};
KW   Transferase {ECO:0000313|EMBL:ADP73240.1}.
FT   DOMAIN        1    211       Glutamine amidotransferase type-1.
FT                                {ECO:0000259|PROSITE:PS51273}.
FT   ACT_SITE     79     79       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00278, ECO:0000256|PIRSR:PIRSR000495-
FT                                1, ECO:0000256|PROSITE-ProRule:PRU00605}.
FT   ACT_SITE    186    186       {ECO:0000256|HAMAP-Rule:MF_00278,
FT                                ECO:0000256|PIRSR:PIRSR000495-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00605}.
FT   ACT_SITE    188    188       {ECO:0000256|HAMAP-Rule:MF_00278,
FT                                ECO:0000256|PIRSR:PIRSR000495-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00605}.
SQ   SEQUENCE   211 AA;  23365 MW;  ED4C599DC0BD7BA7 CRC64;
     MIGIIDYGMG NLYSVSKALE RLRYEYVVSD QPNVLKQTKG LILPGVGSFK DAMHILRKTK
     LDKFIREAVN EGTPLFGICL GMQLLFEESE ENGLTEGLGL LSGRVVRIPG VTAGGERYKV
     PHMGWNRLVF RHPSPLLQNV EEGHVYFVHS YYVVTDDDSV VLASSFYDVE VPAVVGKGNV
     YGTQFHPEKS GEVGMKILQN YAAIVEGKGR V
//

If you have problems or comments...

PBIL Back to PBIL home page