位置:首页 > 蛋白库 > HIS5_PHOPR
HIS5_PHOPR
ID   HIS5_PHOPR              Reviewed;         210 AA.
AC   P62448;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=PBPRA1088;
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
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}.
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; CR378666; CAG19499.1; -; Genomic_DNA.
DR   RefSeq; WP_011217832.1; NC_006370.1.
DR   AlphaFoldDB; P62448; -.
DR   SMR; P62448; -.
DR   STRING; 298386.PBPRA1088; -.
DR   MEROPS; C26.965; -.
DR   EnsemblBacteria; CAG19499; CAG19499; PBPRA1088.
DR   KEGG; ppr:PBPRA1088; -.
DR   eggNOG; COG0118; Bacteria.
DR   HOGENOM; CLU_071837_0_0_6; -.
DR   OMA; WVYFVHS; -.
DR   OrthoDB; 1726024at2; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000000593; Chromosome 1.
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..210
FT                   /note="Imidazole glycerol phosphate synthase subunit HisH"
FT                   /id="PRO_0000152403"
FT   DOMAIN          7..210
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        192
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00278"
FT   ACT_SITE        194
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00278"
SQ   SEQUENCE   210 AA;  22896 MW;  FE525895F7985E15 CRC64;
     MASTNQKVVI IDTGCANVSS VRFAIERLGY TVTISKETSV VLNADKLFLP GVGTASEAMK
     NLQERDLVEL VKQVDKPLLG ICLGMQLLGA LSEEQGQNGK ELVPCLHLCD APIKKLKTGN
     LPLPHMGWNT ITPIDNHPLF QGIPAGSYFY FVHSYAMPVS TGVNDYTIAQ CEYGQPFSAA
     IQSGNYYGVQ FHPERSSKAG SQLIKNFLEM
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024