ID A0A178AB40_9PLEO Unreviewed; 550 AA.
AC A0A178AB40;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=IQ06DRAFT_329968 {ECO:0000313|EMBL:OAK94801.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK94801.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAK94801.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK94801.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KV441724; OAK94801.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178AB40; -.
DR STRING; 765868.A0A178AB40; -.
DR InParanoid; A0A178AB40; -.
DR OrthoDB; 2782495at2759; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000077206; 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; 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:UP000077206}.
FT DOMAIN 6..209
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT REGION 360..361
FT /note="PRFAR binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT REGION 398..400
FT /note="PRFAR binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT REGION 470..471
FT /note="PRFAR binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT REGION 496..497
FT /note="PRFAR binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT REGION 519..520
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 194
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 194
FT /note="For GATase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT ACT_SITE 196
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 196
FT /note="For GATase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT ACT_SITE 240
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT ACT_SITE 400
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 328
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT BINDING 465
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
SQ SEQUENCE 550 AA; 60042 MW; 5F1E8AB78476EEF8 CRC64;
MSTVHLLDYV AGNVRSLVNA IEKVGYTVEW VKSPADVPKA HKLIIPGVGH FGHCLSQLEK
AGYSEPIREH IRAGKPFMGI CVGIQALFES SEEDPNVKGL GVIPARLKKF DDKDKSVPHI
GWNSANTSRT GHVTDESLYG LRPDSKYYYV HTYAVPYEEG KLEKEGWTVA TARYGNEEFV
GAVARDNVFA TQFHPEKSGA AGLRVLKAFL DGKRSQKLLD KPSEAATKEG LTRRVIACLD
VRTNDQGDLV VTKGDQYDVR EKDGTGNAVR NLGKPVDMAK KYYEQGADEV TFLNITSFRN
CPVADTPMLE ILRRTSETVF VPLTIGGGIR DTVDTDGSKI SALDIATMYF KSGADKVSIG
SDAVTAAEEY WARGGKLAGD TAIESISSAY GNQAVVISVD PKRIYVESPD ATFHHTIRTS
TPGPNSEQYC WYQCTIKGGR EGRDFDVRQL VTAVEAMGAG EILLNCIDKD GSNSGFDLEL
INDVKAAIKI PVIASSGAGH PGHFEEVFAQ TRTDAALGAG MFHRGEYTVK QVKDHLQENG
LVVRPFERDI
//
