HIS5_LACLA
ID HIS5_LACLA Reviewed; 202 AA.
AC Q02132; Q9CG92;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 25-MAY-2022, entry version 133.
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=LL1212; ORFNames=L0069;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCDO 2118;
RX PubMed=1400209; DOI=10.1128/jb.174.20.6571-6579.1992;
RA Delorme C., Ehrlich S.D., Renault P.;
RT "Histidine biosynthesis genes in Lactococcus lactis subsp. lactis.";
RL J. Bacteriol. 174:6571-6579(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(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 (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; U92974; AAB81907.1; -; Genomic_DNA.
DR EMBL; AE005176; AAK05310.1; -; Genomic_DNA.
DR PIR; D86776; D86776.
DR PIR; I45734; I45734.
DR RefSeq; NP_267368.1; NC_002662.1.
DR RefSeq; WP_010905832.1; NC_002662.1.
DR AlphaFoldDB; Q02132; -.
DR SMR; Q02132; -.
DR STRING; 272623.L0069; -.
DR MEROPS; C26.965; -.
DR PaxDb; Q02132; -.
DR EnsemblBacteria; AAK05310; AAK05310; L0069.
DR KEGG; lla:L0069; -.
DR PATRIC; fig|272623.7.peg.1309; -.
DR eggNOG; COG0118; Bacteria.
DR HOGENOM; CLU_071837_2_2_9; -.
DR OMA; WVYFVHS; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000002196; 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..202
FT /note="Imidazole glycerol phosphate synthase subunit HisH"
FT /id="PRO_0000152381"
FT DOMAIN 3..202
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 81
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 183
FT /evidence="ECO:0000250"
FT ACT_SITE 185
FT /evidence="ECO:0000250"
FT CONFLICT 129
FT /note="A -> T (in Ref. 1; AAB81907)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="D -> G (in Ref. 1; AAB81907)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="V -> I (in Ref. 1; AAB81907)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 202 AA; 22454 MW; F248C8B44F7963CB CRC64;
MKKIVIIDYN IGNLQSVQAA FLRLGQETVI SRDLEEIRKA DALILPGVGA FPTAMNNLKK
FNLIELIQER AAAGIPILGI CLGMQVLFEK GYEIEERQGL GLLKGEVIPI KTNEKIPHMG
WNQLNLAKAS PTTHYLSDND EVYFVHSYQA TCPDDELIAY TTYGEVKIPA IVGKNNVIGC
QFHPEKSGEI GRKVLKAFLE EI
