HIS5_CORGL
ID HIS5_CORGL Reviewed; 211 AA.
AC O69043;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisH;
DE EC=4.3.2.10;
DE AltName: Full=IGP synthase glutaminase subunit;
DE EC=3.5.1.2;
DE AltName: Full=IGP synthase subunit HisH;
DE AltName: Full=ImGP synthase subunit HisH;
DE Short=IGPS subunit HisH;
GN Name=hisH; OrderedLocusNames=Cgl2097, cg2300;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RA Jung S.I., Han M.S., Park Y.J., Lee S.K., Lee M.-S.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
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 ---------------------------------------------------------------------------
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; AF060558; AAC15231.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB99490.1; -; Genomic_DNA.
DR EMBL; BX927154; CAF20433.1; -; Genomic_DNA.
DR RefSeq; NP_601296.1; NC_003450.3.
DR RefSeq; WP_011014877.1; NC_006958.1.
DR AlphaFoldDB; O69043; -.
DR SMR; O69043; -.
DR STRING; 196627.cg2300; -.
DR KEGG; cgb:cg2300; -.
DR KEGG; cgl:Cgl2097; -.
DR PATRIC; fig|196627.13.peg.2033; -.
DR eggNOG; COG0118; Bacteria.
DR HOGENOM; CLU_071837_1_0_11; -.
DR OMA; WVYFVHS; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000000582; 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-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..211
FT /note="Imidazole glycerol phosphate synthase subunit HisH"
FT /id="PRO_0000152370"
FT DOMAIN 4..211
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 82
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 192
FT /evidence="ECO:0000250"
FT ACT_SITE 194
FT /evidence="ECO:0000250"
FT CONFLICT 18..24
FT /note="AQRALER -> LRRTRAL (in Ref. 1; AAC15231)"
FT /evidence="ECO:0000305"
FT CONFLICT 28..29
FT /note="EV -> SMF (in Ref. 1; AAC15231)"
FT /evidence="ECO:0000305"
FT CONFLICT 34..41
FT /note="DPEVCTNA -> IQKLHPTH (in Ref. 1; AAC15231)"
FT /evidence="ECO:0000305"
FT CONFLICT 64..69
FT /note="GHRIIG -> DIAYR (in Ref. 1; AAC15231)"
FT /evidence="ECO:0000305"
FT CONFLICT 165..170
FT /note="PEVVWA -> QSCVG (in Ref. 1; AAC15231)"
FT /evidence="ECO:0000305"
FT CONFLICT 174..176
FT /note="NDR -> VS (in Ref. 1; AAC15231)"
FT /evidence="ECO:0000305"
FT CONFLICT 198..211
FT /note="DAGAQLLRNWINYI -> EQGXSYCETGSTTSNR (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 211 AA; 23173 MW; 73FB994AB5200C85 CRC64;
MTKTVALLDY GSGNLRSAQR ALERAGAEVI VSSDPEVCTN ADGLLVPGVG AFDACMKGLK
NVFGHRIIGQ RLAGGRPVMG ICVGMQILFD EGDEHGIKSA GCGEWPGKVE RLQAEILPHM
GWNTLEMPTN SPMFEGISPD ERFYFVHSYG VRKWTLETDD LTTPPEVVWA KHENDRFVAA
VENGTLWATQ FHPEKSGDAG AQLLRNWINY I
