ID D3PZV8_STANL Unreviewed; 202 AA.
AC D3PZV8;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 24-JAN-2024, entry version 78.
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 OrderedLocusNames=Snas_3993 {ECO:0000313|EMBL:ADD43645.1};
OS Stackebrandtia nassauensis (strain DSM 44728 / CIP 108903 / NRRL B-16338 /
OS NBRC 102104 / LLR-40K-21).
OC Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC Stackebrandtia.
OX NCBI_TaxID=446470 {ECO:0000313|EMBL:ADD43645.1, ECO:0000313|Proteomes:UP000000844};
RN [1] {ECO:0000313|EMBL:ADD43645.1, ECO:0000313|Proteomes:UP000000844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44728 / CIP 108903 / NRRL B-16338 / NBRC 102104 /
RC LLR-40K-21 {ECO:0000313|Proteomes:UP000000844};
RX PubMed=21304662; DOI=10.4056/sigs.47643;
RA Munk C., Lapidus A., Copeland A., Jando M., Mayilraj S.,
RA Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F.,
RA Han C., Detter J.C., Bruce D., Goodwin L., Chain P., Pitluck S., Goker M.,
RA Ovchinikova G., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Stackebrandtia nassauensis type strain (LLR-
RT 40K-21).";
RL Stand. Genomic Sci. 1:292-299(2009).
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}.
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DR EMBL; CP001778; ADD43645.1; -; Genomic_DNA.
DR AlphaFoldDB; D3PZV8; -.
DR STRING; 446470.Snas_3993; -.
DR KEGG; sna:Snas_3993; -.
DR eggNOG; COG0118; Bacteria.
DR HOGENOM; CLU_071837_1_0_11; -.
DR OMA; WVYFVHS; -.
DR OrthoDB; 9807137at2; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000000844; 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-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:UP000000844};
KW Transferase {ECO:0000313|EMBL:ADD43645.1}.
FT DOMAIN 6..198
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 82
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00278,
FT ECO:0000256|PIRSR:PIRSR000495-1"
FT ACT_SITE 183
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00278,
FT ECO:0000256|PIRSR:PIRSR000495-1"
FT ACT_SITE 185
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00278,
FT ECO:0000256|PIRSR:PIRSR000495-1"
SQ SEQUENCE 202 AA; 20962 MW; 02A3297C925D00F2 CRC64;
MKPSVVVFDY GSGNLRSAAR ALEHAGADVT VTADTAAAVR AHGLVVPGVG AFASCMDGIR
SCGGDKVIAE RRAAATPVLG ICVGAQILFD AGTEHGTRTT GLGVFDGEVT ALRAERVPHM
GWNTVDQTGM PLFEGLAPDA RFYFVHSYAV HGTIPGAQVA TCDYGDPFVA AISRDTVSAT
QFHPEKSGSA GLTLLSNWVR SL
//