HIS5_ECOLI
ID HIS5_ECOLI Reviewed; 196 AA.
AC P60595; P10375;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisH;
DE EC=4.3.2.10 {ECO:0000269|PubMed:8494895};
DE AltName: Full=IGP synthase glutaminase subunit;
DE EC=3.5.1.2 {ECO:0000269|PubMed:8494895};
DE AltName: Full=IGP synthase subunit HisH;
DE AltName: Full=ImGP synthase subunit HisH;
DE Short=IGPS subunit HisH;
GN Name=hisH; OrderedLocusNames=b2023, JW2005;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3062174; DOI=10.1016/0022-2836(88)90194-5;
RA Carlomagno M.S., Chiariotti L., Alifano P., Nappo A.G., Bruni C.B.;
RT "Structure and function of the Salmonella typhimurium and Escherichia coli
RT K-12 histidine operons.";
RL J. Mol. Biol. 203:585-606(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 1-20, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RX PubMed=8494895; DOI=10.1021/bi00070a029;
RA Klem T.J., Davisson V.J.;
RT "Imidazole glycerol phosphate synthase: the glutamine amidotransferase in
RT histidine biosynthesis.";
RL Biochemistry 32:5177-5186(1993).
RN [6]
RP STRUCTURE PREDICTION.
RX PubMed=11551184; DOI=10.1006/jsbi.2001.4390;
RA O'Donoghue P., Amaro R.E., Luthey-Schulten Z.;
RT "On the structure of hisH: protein structure prediction in the context of
RT structural and functional genomics.";
RL J. Struct. Biol. 134:257-268(2001).
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:0000269|PubMed:8494895}.
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 Evidence={ECO:0000269|PubMed:8494895};
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:0000269|PubMed:8494895};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 uM for glutamine {ECO:0000269|PubMed:8494895};
CC pH dependence:
CC Optimum pH is 6-8. {ECO:0000269|PubMed:8494895};
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:0000269|PubMed:8494895}.
CC -!- INTERACTION:
CC P60595; P60664: hisF; NbExp=2; IntAct=EBI-1126953, EBI-9151168;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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DR EMBL; X13462; CAA31815.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75084.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15854.1; -; Genomic_DNA.
DR PIR; JS0132; XQECHH.
DR RefSeq; NP_416527.1; NC_000913.3.
DR RefSeq; WP_001103560.1; NZ_SSUV01000054.1.
DR AlphaFoldDB; P60595; -.
DR SMR; P60595; -.
DR BioGRID; 4260419; 10.
DR ComplexPortal; CPX-5158; Imidazole glycerol phosphate synthase complex.
DR IntAct; P60595; 2.
DR STRING; 511145.b2023; -.
DR MEROPS; C26.965; -.
DR SWISS-2DPAGE; P60595; -.
DR jPOST; P60595; -.
DR PaxDb; P60595; -.
DR PRIDE; P60595; -.
DR EnsemblBacteria; AAC75084; AAC75084; b2023.
DR EnsemblBacteria; BAA15854; BAA15854; BAA15854.
DR GeneID; 60668934; -.
DR GeneID; 946544; -.
DR KEGG; ecj:JW2005; -.
DR KEGG; eco:b2023; -.
DR PATRIC; fig|1411691.4.peg.229; -.
DR EchoBASE; EB0445; -.
DR eggNOG; COG0118; Bacteria.
DR HOGENOM; CLU_071837_0_0_6; -.
DR InParanoid; P60595; -.
DR OMA; WVYFVHS; -.
DR PhylomeDB; P60595; -.
DR BioCyc; EcoCyc:GLUTAMIDOTRANS-MON; -.
DR BioCyc; MetaCyc:GLUTAMIDOTRANS-MON; -.
DR BRENDA; 4.3.1.B2; 2026.
DR UniPathway; UPA00031; UER00010.
DR PRO; PR:P60595; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009382; C:imidazoleglycerol-phosphate synthase complex; IDA:EcoCyc.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IDA:EcoCyc.
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; IDA:ComplexPortal.
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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Cytoplasm; Direct protein sequencing;
KW Glutamine amidotransferase; Histidine biosynthesis; Hydrolase; Lyase;
KW Reference proteome.
FT CHAIN 1..196
FT /note="Imidazole glycerol phosphate synthase subunit HisH"
FT /id="PRO_0000152373"
FT DOMAIN 2..196
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 77
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 178
FT /evidence="ECO:0000250"
FT ACT_SITE 180
FT /evidence="ECO:0000250"
SQ SEQUENCE 196 AA; 21653 MW; B75A500ECD50DDD0 CRC64;
MNVVILDTGC ANLNSVKSAI ARHGYEPKVS RDPDVVLLAD KLFLPGVGTA QAAMDQVRER
ELFDLIKACT QPVLGICLGM QLLGRRSEES NGVDLLGIID EDVPKMTDFG LPLPHMGWNR
VYPQAGNRLF QGIEDGAYFY FVHSYAMPVN PWTIAQCNYG EPFTAAVQKD NFYGVQFHPE
RSGAAGAKLL KNFLEM
