HIS5_CERS4
ID HIS5_CERS4 Reviewed; 212 AA.
AC O33565; Q3J484;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 25-MAY-2022, entry version 125.
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=RHOS4_08320; ORFNames=RSP_2245;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Oriol E., Barbe J., Gibert I.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; X87256; CAA60713.1; -; Genomic_DNA.
DR EMBL; CP000143; ABA78400.1; -; Genomic_DNA.
DR RefSeq; WP_011337344.1; NZ_CP030271.1.
DR RefSeq; YP_352301.1; NC_007493.2.
DR AlphaFoldDB; O33565; -.
DR SMR; O33565; -.
DR STRING; 272943.RSP_2245; -.
DR EnsemblBacteria; ABA78400; ABA78400; RSP_2245.
DR KEGG; rsp:RSP_2245; -.
DR PATRIC; fig|272943.9.peg.1148; -.
DR eggNOG; COG0118; Bacteria.
DR OMA; WVYFVHS; -.
DR PhylomeDB; O33565; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000002703; 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..212
FT /note="Imidazole glycerol phosphate synthase subunit HisH"
FT /id="PRO_0000152417"
FT DOMAIN 2..212
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 87
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 111
FT /note="G -> A (in Ref. 1; CAA60713)"
FT /evidence="ECO:0000305"
FT CONFLICT 131..132
FT /note="ND -> ER (in Ref. 1; CAA60713)"
FT /evidence="ECO:0000305"
FT CONFLICT 200..202
FT /note="GLR -> AA (in Ref. 1; CAA60713)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 212 AA; 23207 MW; 20295625CFC3C4DE CRC64;
MLTVLVDYDS GNLHSAEKAF QRMATETGAG QVLVSDRPED VARADRIVLP GDGAFPACRR
ALGSYGGLSE AIEEAVTRRA RPFLGICIGM QMMATRGLEH EETPGFGWIA GEVVRIAPSD
PHLKVPHMGW NDLTVDHPHP VLTGIETGDH AYFVHSYHFQ VAHDAERLAH ADYGADITAI
VGRDTMVGTQ FHPEKSQKTG LRLIANFLTW KP
