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Database: UniProt
Entry: D3PZV8_STANL
LinkDB: D3PZV8_STANL
Original site: D3PZV8_STANL 
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
//
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