HIS5_NOCFA
ID HIS5_NOCFA Reviewed; 211 AA.
AC Q5YYP7;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisH {ECO:0000255|HAMAP-Rule:MF_00278};
DE EC=4.3.2.10 {ECO:0000255|HAMAP-Rule:MF_00278};
DE AltName: Full=IGP synthase glutaminase subunit {ECO:0000255|HAMAP-Rule:MF_00278};
DE EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_00278};
DE AltName: Full=IGP synthase subunit HisH {ECO:0000255|HAMAP-Rule:MF_00278};
DE AltName: Full=ImGP synthase subunit HisH {ECO:0000255|HAMAP-Rule:MF_00278};
DE Short=IGPS subunit HisH {ECO:0000255|HAMAP-Rule:MF_00278};
GN Name=hisH {ECO:0000255|HAMAP-Rule:MF_00278}; OrderedLocusNames=NFA_18480;
OS Nocardia farcinica (strain IFM 10152).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX NCBI_TaxID=247156;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 10152;
RX PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA Shiba T., Hattori M.;
RT "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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:0000255|HAMAP-Rule:MF_00278}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00278};
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:0000255|HAMAP-Rule:MF_00278};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
CC {ECO:0000255|HAMAP-Rule:MF_00278}.
CC -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000255|HAMAP-
CC Rule:MF_00278}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00278}.
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DR EMBL; AP006618; BAD56694.1; -; Genomic_DNA.
DR RefSeq; WP_011208379.1; NC_006361.1.
DR AlphaFoldDB; Q5YYP7; -.
DR SMR; Q5YYP7; -.
DR STRING; 247156.NFA_18480; -.
DR EnsemblBacteria; BAD56694; BAD56694; NFA_18480.
DR GeneID; 61132632; -.
DR KEGG; nfa:NFA_18480; -.
DR eggNOG; COG0118; Bacteria.
DR HOGENOM; CLU_071837_1_0_11; -.
DR OMA; WVYFVHS; -.
DR BioCyc; NFAR247156:NFA_RS09320-MON; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000006820; 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_0000231741"
FT DOMAIN 5..211
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00278"
FT ACT_SITE 83
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00278"
FT ACT_SITE 192
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00278"
FT ACT_SITE 194
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00278"
SQ SEQUENCE 211 AA; 22476 MW; 297D2A531CC576ED CRC64;
MTRKSVALLD YGSGNLHSAE RALVRAGADV RVTADPDAAL AVDGLVVPGV GAFAACMAGL
RAVRGEKIIG QRLAGGRPVL GICVGMQILF ERGVEFGVET EGCAEWPGVV ERLDAPVLPH
MGWNTVSAPA DSVLFAGMDA DTRFYFVHSY AAQRWELPPN EHFAAPKLTW AEHGVRFLAA
VENGPLSATQ FHPEKSGDAG AQLLRNWVDS L
