HIS52_PSEAE
ID HIS52_PSEAE Reviewed; 202 AA.
AC P72138;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisH 2;
DE EC=4.3.2.10;
DE AltName: Full=IGP synthase glutaminase subunit 2;
DE EC=3.5.1.2;
DE AltName: Full=IGP synthase subunit HisH 2;
DE AltName: Full=ImGP synthase subunit HisH 2;
DE Short=IGPS subunit HisH 2;
GN Name=hisH2; Synonyms=hisH; OrderedLocusNames=PA3152;
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 [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=8939432; DOI=10.1046/j.1365-2958.1996.1351503.x;
RA Burrows L.L., Charter D.F., Lam J.S.;
RT "Molecular characterization of the Pseudomonas aeruginosa serotype O5
RT (PAO1) B-band lipopolysaccharide gene cluster.";
RL Mol. Microbiol. 22:481-495(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Serotype O16, Serotype O18, Serotype O2, Serotype O20, and
RC Serotype O5;
RX PubMed=12057956; DOI=10.1128/jb.184.13.3614-3622.2002;
RA Raymond C.K., Sims E.H., Kas A., Spencer D.H., Kutyavin T.V., Ivey R.G.,
RA Zhou Y., Kaul R., Clendenning J.B., Olson M.V.;
RT "Genetic variation at the O-antigen biosynthetic locus in Pseudomonas
RT aeruginosa.";
RL J. Bacteriol. 184:3614-3622(2002).
RN [3]
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 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 (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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC45859.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U50396; AAC45859.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF498408; AAM27664.1; -; Genomic_DNA.
DR EMBL; AF498410; AAM27695.1; -; Genomic_DNA.
DR EMBL; AF498412; AAM27730.1; -; Genomic_DNA.
DR EMBL; AF498413; AAM27750.1; -; Genomic_DNA.
DR EMBL; AF498416; AAM27803.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06540.1; -; Genomic_DNA.
DR PIR; B83251; B83251.
DR RefSeq; NP_251842.1; NC_002516.2.
DR RefSeq; WP_003113422.1; NZ_QZGE01000023.1.
DR AlphaFoldDB; P72138; -.
DR SMR; P72138; -.
DR STRING; 208964.PA3152; -.
DR MEROPS; C26.965; -.
DR PaxDb; P72138; -.
DR PRIDE; P72138; -.
DR DNASU; 882589; -.
DR EnsemblBacteria; AAG06540; AAG06540; PA3152.
DR GeneID; 882589; -.
DR KEGG; pae:PA3152; -.
DR PseudoCAP; PA3152; -.
DR HOGENOM; CLU_071837_2_0_6; -.
DR InParanoid; P72138; -.
DR OMA; PEKSHRY; -.
DR PhylomeDB; P72138; -.
DR BioCyc; PAER208964:G1FZ6-3212-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 GO; GO:0009243; P:O antigen biosynthetic process; EXP:PseudoCAP.
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..202
FT /note="Imidazole glycerol phosphate synthase subunit HisH
FT 2"
FT /id="PRO_0000152409"
FT DOMAIN 1..202
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 80
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 183
FT /evidence="ECO:0000250"
FT ACT_SITE 185
FT /evidence="ECO:0000250"
SQ SEQUENCE 202 AA; 22695 MW; 41D93A88F97ACE2B CRC64;
MIVVIDYGVG NIASVLNMLK RVGAKAKASD SREDIEQAEK LILPGVGAFD AGMQTLRKSG
LVDVLTEQVM IKRKPVMGVC LGSQMLGLRS EEGAEPGLGW IDMDSVRFER RDDRKVPHMG
WNQVSPQLEH PILSGINEQS RFYFVHSYYM VPKDPDDILL SCNYGQKFTA AVARDNVFGF
QFHPEKSHKF GMQLFKNFVE LV
