ID A0A087BUW0_9BIFI Unreviewed; 223 AA.
AC A0A087BUW0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisH {ECO:0000256|HAMAP-Rule:MF_00278};
DE EC=4.3.2.10 {ECO:0000256|HAMAP-Rule:MF_00278};
DE AltName: Full=IGP synthase glutaminase subunit {ECO:0000256|HAMAP-Rule:MF_00278};
DE EC=3.5.1.2 {ECO:0000256|HAMAP-Rule:MF_00278};
DE AltName: Full=IGP synthase subunit HisH {ECO:0000256|HAMAP-Rule:MF_00278};
DE AltName: Full=ImGP synthase subunit HisH {ECO:0000256|HAMAP-Rule:MF_00278};
DE Short=IGPS subunit HisH {ECO:0000256|HAMAP-Rule:MF_00278};
GN Name=hisH {ECO:0000256|HAMAP-Rule:MF_00278};
GN ORFNames=BMON_1352 {ECO:0000313|EMBL:KFI74810.1};
OS Bifidobacterium mongoliense DSM 21395.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437603 {ECO:0000313|EMBL:KFI74810.1, ECO:0000313|Proteomes:UP000029082};
RN [1] {ECO:0000313|EMBL:KFI74810.1, ECO:0000313|Proteomes:UP000029082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21395 {ECO:0000313|EMBL:KFI74810.1,
RC ECO:0000313|Proteomes:UP000029082};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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. {ECO:0000256|ARBA:ARBA00025299, ECO:0000256|HAMAP-
CC 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;
CC Evidence={ECO:0000256|ARBA:ARBA00000619, ECO:0000256|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:0000256|ARBA:ARBA00001062, ECO:0000256|HAMAP-
CC 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:0000256|ARBA:ARBA00005091, ECO:0000256|HAMAP-Rule:MF_00278}.
CC -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000256|ARBA:ARBA00011152,
CC ECO:0000256|HAMAP-Rule:MF_00278}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00278}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFI74810.1}.
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DR EMBL; JGZE01000021; KFI74810.1; -; Genomic_DNA.
DR RefSeq; WP_033513151.1; NZ_JGZE01000021.1.
DR AlphaFoldDB; A0A087BUW0; -.
DR STRING; 1437603.GCA_000771525_00284; -.
DR eggNOG; COG0118; Bacteria.
DR OrthoDB; 9807137at2; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000029082; Unassembled WGS sequence.
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-UniRule.
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 NCBIfam; TIGR01855; IMP_synth_hisH; 1.
DR PANTHER; PTHR42701; IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISH; 1.
DR PANTHER; PTHR42701:SF1; IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISH; 1.
DR Pfam; PF00117; GATase; 1.
DR PIRSF; PIRSF000495; Amidotransf_hisH; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00278}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00278};
KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_00278,
KW ECO:0000256|PROSITE-ProRule:PRU00605};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW Rule:MF_00278};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00278};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00278};
KW Reference proteome {ECO:0000313|Proteomes:UP000029082}.
FT DOMAIN 5..210
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 81
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00278,
FT ECO:0000256|PIRSR:PIRSR000495-1"
FT ACT_SITE 196
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00278,
FT ECO:0000256|PIRSR:PIRSR000495-1"
FT ACT_SITE 198
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00278,
FT ECO:0000256|PIRSR:PIRSR000495-1"
SQ SEQUENCE 223 AA; 23462 MW; D617306A13FEF725 CRC64;
MTSVVVFDYG FGNVRSMMRA LINIGVDATL TSDHRQAMAA DGLVVPGVGA FAACMRGLRQ
VGGDEVIVNR LSAGLPVLGV CVGEQIMFER GCEHDESAAG LGLIGGEVTK LEADVVPHMG
WNTVEAPADS SLFAGVERER FYFVHSYAAH NATAPGAGAP AIDYGSSPER VTWCSYGGSR
FVAAYEHGPL SATQFHPEKS AQAGVAVLRN WVAGFGTLKG ERV
//
