ID W7HUS4_9PEZI Unreviewed; 1370 AA.
AC W7HUS4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=phosphoribosylformylglycinamidine synthase {ECO:0000256|ARBA:ARBA00012747};
DE EC=6.3.5.3 {ECO:0000256|ARBA:ARBA00012747};
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase {ECO:0000256|ARBA:ARBA00032632};
DE AltName: Full=Formylglycinamide ribotide amidotransferase {ECO:0000256|ARBA:ARBA00029823};
GN ORFNames=DRE_07301 {ECO:0000313|EMBL:EWC43792.1};
OS Drechslerella stenobrocha 248.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Drechslerella.
OX NCBI_TaxID=1043628 {ECO:0000313|EMBL:EWC43792.1, ECO:0000313|Proteomes:UP000024837};
RN [1] {ECO:0000313|EMBL:EWC43792.1, ECO:0000313|Proteomes:UP000024837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=248 {ECO:0000313|EMBL:EWC43792.1,
RC ECO:0000313|Proteomes:UP000024837};
RA Liu X., Zhang W., Liu K.;
RT "Drechslerella stenobrocha genome reveals carnivorous origination and
RT mechanical trapping mechanism of predatory fungi.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC phospho-D-ribosyl)glycinamide: step 1/2.
CC {ECO:0000256|ARBA:ARBA00004920}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS family.
CC {ECO:0000256|ARBA:ARBA00008608}.
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DR EMBL; KI966451; EWC43792.1; -; Genomic_DNA.
DR HOGENOM; CLU_001031_0_2_1; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000024837; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01740; GATase1_FGAR_AT; 1.
DR CDD; cd02203; PurL_repeat1; 1.
DR CDD; cd02204; PurL_repeat2; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 1.10.8.750; Phosphoribosylformylglycinamidine synthase, linker domain; 1.
DR Gene3D; 3.90.650.10; PurM-like C-terminal domain; 2.
DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 2.
DR HAMAP; MF_00419; PurL_1; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR040707; FGAR-AT_N.
DR InterPro; IPR010073; PurL_large.
DR InterPro; IPR041609; PurL_linker.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR036921; PurM-like_N_sf.
DR InterPro; IPR036604; PurS-like_sf.
DR NCBIfam; TIGR01735; FGAM_synt; 1.
DR PANTHER; PTHR10099; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR PANTHER; PTHR10099:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR Pfam; PF02769; AIRS_C; 2.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR Pfam; PF18076; FGAR-AT_N; 1.
DR Pfam; PF13507; GATase_5; 1.
DR SMART; SM01211; GATase_5; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF109736; FGAM synthase PurL, linker domain; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 2.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
DR SUPFAM; SSF82697; PurS-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000024837}.
FT DOMAIN 60..181
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 210..262
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 477..630
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 897..1015
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT REGION 639..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1370 AA; 147383 MW; EDA4F57A7DBBACE0 CRC64;
MSAWLPLPGS PALSSFRIVE LTKAINSKLG SSSPVQLETI SSLHVHYIQT TSLQSLAALE
KPRSKERQAL DQLLQYGDEA NLSEPITQLL QDSIENTEFN INGLPDVLVL FASPRPGTIS
PWSSKATSIA HVCDMGGLVG RIERGVAFAL KFSGDASSLD ISLFGDLLHD RMTQSLSKSM
PVESLSHDDA TPASATQIKL LSSPDPRQTL EDANKTYGLA LDASEKEYLL SAFSSTGPCP
RDPYDVELFM FAQVNSEHCR HKQFNASWTI DGTNKPNSLF GMIRNTHRVS PEYTISAYSD
NAAVLEGSDA TFWAPDAKTK QWTLTNEKVH FVAKVETHNH PTAVSPYPGA ATGSGGEIRD
EGAVGRGSKP KAGLSGFNVS NLLIPNFKRP WELDVGKPYH IASPLDIMLD APIGSAAFNN
EFGRPCITGY FRTLTTSVPV SDKEAEVRGY HKPIMIAGGL GTIRPGHALK EKGAISPGAY
LIVLGGPAML IGLGGGAASS VTSGEGSVEL DFASVQRGNP EMQRRAQMVI DTCTALGDQN
PIRSIHDVGA GGLSNALPEL VHDAGLGAKF ELRDVESADH GMSPLQIWCC EAQERYVLAV
AEDGLEVFKQ MAERERCGFR VVGRAVGGSE DEQSLVLTDR ESKEHPTPID LPMSTLFGKP
PKMHKDVQTR KLPVPSFDAS LKQYVPDSSA SILPEAIERV LTLPSVGSKQ FLITIGDRSV
TGLVVRDQMV GPWQTPVADV GVTATSLSTN VTTGEAMAMG ERPTLALVSP ASSARMAVAE
SLTNLAAANL LGGLKRVRLS ANWMAAGSHP GEGAALYEAV EAVGLDLCPK LGISIPVGKD
SMSMKMKWDK TKEVTAPISL VVTAFCAVAD IGTTWTPTLS RDESTILLLV DLAAGFRTLG
GSALAQVFGQ VGNEVPDVRD AEVLKKFFDL VNDLHHEKSV LAYHDRSDGG LITTLLEMAF
AGRTGLEITL DELAASDSDS DVIPTLFNEE LGAVFQVRGD DLPRFYEICN QYGLPKESIY
KVARPITNSS QPINISYKGR RLFSSSRAAL QQSWSRTSYE LQKIRDNPSC AEQEYTAITD
DENPGLSFQP SFNPAAPFIP PSPQNPRVAI LREQGVNGHA EMAFAFLAAG FTPIDVHMTD
LISGTTSLSD FTGLAACGGF SYGDVLGAGA GWAKSVLLHP RTRGDFAAFF ERADTFALGV
CNGCQFLSHL KELIPGAGNT WPSFERNESE QYEARVCMVE VIEEAGAKPS VFLSGMAGTK
MPIVTAHGEG RAVFRTPGSS AEGLQEKGLV SLRYVDNRGK VTERYPENPN GSPLGITGVR
SADGRVLAMM PHPERTVLLQ AHSWVSEEAQ QWGHLGPWVQ MFRNARKWVG
//
