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HIS51_PSEAE
ID   HIS51_PSEAE             Reviewed;         213 AA.
AC   Q9HU42;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Imidazole glycerol phosphate synthase subunit HisH 1;
DE            EC=4.3.2.10;
DE   AltName: Full=IGP synthase glutaminase subunit 1;
DE            EC=3.5.1.2;
DE   AltName: Full=IGP synthase subunit HisH 1;
DE   AltName: Full=ImGP synthase subunit HisH 1;
DE            Short=IGPS subunit HisH 1;
GN   Name=hisH1; OrderedLocusNames=PA5142;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
CC   -!- FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to IGP,
CC       AICAR and glutamate. The HisH subunit provides the glutamine
CC       amidotransferase activity that produces the ammonia necessary to HisF
CC       for the synthesis of IGP and AICAR (By similarity). {ECO:0000250}.
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   -!- 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   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
CC   -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR   EMBL; AE004091; AAG08527.1; -; Genomic_DNA.
DR   PIR; B83003; B83003.
DR   RefSeq; NP_253829.1; NC_002516.2.
DR   RefSeq; WP_003121251.1; NC_002516.2.
DR   AlphaFoldDB; Q9HU42; -.
DR   SMR; Q9HU42; -.
DR   STRING; 287.DR97_2497; -.
DR   MEROPS; C26.965; -.
DR   PaxDb; Q9HU42; -.
DR   PRIDE; Q9HU42; -.
DR   EnsemblBacteria; AAG08527; AAG08527; PA5142.
DR   GeneID; 878788; -.
DR   KEGG; pae:PA5142; -.
DR   PATRIC; fig|208964.12.peg.5389; -.
DR   PseudoCAP; PA5142; -.
DR   HOGENOM; CLU_071837_2_0_6; -.
DR   InParanoid; Q9HU42; -.
DR   OMA; WVYFVHS; -.
DR   PhylomeDB; Q9HU42; -.
DR   BioCyc; PAER208964:G1FZ6-5257-MON; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000002438; 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; IBA:GO_Central.
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..213
FT                   /note="Imidazole glycerol phosphate synthase subunit HisH
FT                   1"
FT                   /id="PRO_0000152408"
FT   DOMAIN          4..213
FT                   /note="Glutamine amidotransferase type-1"
FT   ACT_SITE        82
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        191
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        193
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   213 AA;  23698 MW;  ECE247CBD0411FE8 CRC64;
     MMQTVAVIDY GMGNLHSVAK ALEHVGAGRV LVSSDAAVIR EADRVVFPGV GAIRDCMAEI
     RRLGFDALVR EVSQDRPFLG ICVGMQALLE RSEENDGVDC IGLFPGQVRF FGKDLHEAGE
     HLKVPHMGWN QVSQAVEHPL WHEIPDQARF YFVHSYYIEA GNPRQVVGHG HYGVDFAAAL
     AEGSRFAVQF HPEKSHTHGL QLLQNFVAWD GRW
 
 
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