ID A0A395NUW1_TRIAR Unreviewed; 547 AA.
AC A0A395NUW1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 13-SEP-2023, entry version 15.
DE RecName: Full=Imidazole glycerol phosphate synthase hisHF {ECO:0000256|PIRNR:PIRNR036936};
DE Includes:
DE RecName: Full=Glutaminase {ECO:0000256|PIRNR:PIRNR036936};
DE EC=3.5.1.2 {ECO:0000256|PIRNR:PIRNR036936};
DE Includes:
DE RecName: Full=Cyclase {ECO:0000256|PIRNR:PIRNR036936};
GN ORFNames=TARUN_2454 {ECO:0000313|EMBL:RFU79773.1};
OS Trichoderma arundinaceum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=490622 {ECO:0000313|EMBL:RFU79773.1, ECO:0000313|Proteomes:UP000266272};
RN [1] {ECO:0000313|EMBL:RFU79773.1, ECO:0000313|Proteomes:UP000266272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40837 {ECO:0000313|EMBL:RFU79773.1,
RC ECO:0000313|Proteomes:UP000266272};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
CC -!- FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to IGP,
CC AICAR and glutamate. The glutaminase domain produces the ammonia
CC necessary for the cyclase domain to produce IGP and AICAR from PRFAR.
CC The ammonia is channeled to the active site of the cyclase domain.
CC {ECO:0000256|PIRNR:PIRNR036936}.
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,
CC ECO:0000256|PIRNR:PIRNR036936};
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,
CC ECO:0000256|PIRNR:PIRNR036936};
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|PIRNR:PIRNR036936}.
CC -!- SIMILARITY: Belongs to the HisA/HisF family.
CC {ECO:0000256|RuleBase:RU003657}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the HisA/HisF family.
CC {ECO:0000256|PIRNR:PIRNR036936}.
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:RFU79773.1}.
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DR EMBL; PXOA01000139; RFU79773.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395NUW1; -.
DR STRING; 490622.A0A395NUW1; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000266272; Unassembled WGS sequence.
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:0016833; F:oxo-acid-lyase activity; IEA:UniProtKB-UniRule.
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 CDD; cd04731; HisF; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_00278; HisH; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR006062; His_biosynth.
DR InterPro; IPR004651; HisF.
DR InterPro; IPR014640; IGPS_HisHF.
DR InterPro; IPR010139; Imidazole-glycPsynth_HisH.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR NCBIfam; TIGR00735; hisF; 1.
DR NCBIfam; TIGR01855; IMP_synth_hisH; 1.
DR PANTHER; PTHR21235:SF2; IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE HISHF; 1.
DR PANTHER; PTHR21235; IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISF/H IGP SYNTHASE SUBUNIT HISF/H; 1.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF00977; His_biosynth; 1.
DR PIRSF; PIRSF036936; IGPS_HisHF; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR PROSITE; PS51274; GATASE_COBBQ; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|PIRNR:PIRNR036936};
KW Glutamine amidotransferase {ECO:0000256|PIRNR:PIRNR036936,
KW ECO:0000256|PROSITE-ProRule:PRU00605};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102,
KW ECO:0000256|PIRNR:PIRNR036936};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR036936};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR036936};
KW Multifunctional enzyme {ECO:0000256|PIRNR:PIRNR036936};
KW Reference proteome {ECO:0000313|Proteomes:UP000266272}.
FT DOMAIN 6..193
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT REGION 357..358
FT /note="PRFAR binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT REGION 395..397
FT /note="PRFAR binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT REGION 467..468
FT /note="PRFAR binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT REGION 493..494
FT /note="PRFAR binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT REGION 516..517
FT /note="PRFAR binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT ACT_SITE 81
FT /note="For GATase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT ACT_SITE 81
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 188
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 188
FT /note="For GATase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT ACT_SITE 190
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 190
FT /note="For GATase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT ACT_SITE 238
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT ACT_SITE 397
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT BINDING 81
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT BINDING 325
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT BINDING 462
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
SQ SEQUENCE 547 AA; 59486 MW; 71C5D09A3A68392D CRC64;
MPTVHLLDYV AGNIRSLVNA IEKLGYEVDW IKSPEDVPKA EKLILPGVGH FGHCMTQLAQ
ANYLPAIKKH IEEGKPFMGI CVGLQALFQG SEEDHEVPGI GLIPASLTRF DDSDKSVPHI
GWNNANTGGK AMYDLRSDSK YYYVHTYKSP YNKSELEAQG WTVATGTYGN ETFVGAIAKG
NIYATQFHPE KSGVAGLRTI RAFLTGSGAQ NLGADLPSSV APADLKDGLT RRLIACLDVR
TNDQGDLVVT KGDQYDVREK GADRNVRNLG KPVEMAKKYY ESGADEVTFL NITSFRDCPL
ADLPMLEVLR QTSLTVFVPL TIGGGIRDTV DTDGTKVSAL DIATMYFKSG ADKVSIGSDA
VLAAEEYYSL GKKLFGNTAI EQISRAYGRQ AVVVSVDPKR VYVPKLDATR HAIIETKYPG
PKGEAFCWYA CTIKGGRETR DMDVVELAQA VEAMGAGEIL LNCIDKDGTN SGFDLELIQQ
VKNAIKIPVI ASSGAGNPGH FQEVFEKTTT DAALGAGMFH RGEYTVKQVK DYLQDKGLLV
RQFDGDL
//
