ID A0A1G4JSX7_9SACH Unreviewed; 1348 AA.
AC A0A1G4JSX7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=LADA_0G05402G {ECO:0000313|EMBL:SCU93892.1};
OS Lachancea dasiensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1072105 {ECO:0000313|EMBL:SCU93892.1, ECO:0000313|Proteomes:UP000190274};
RN [1] {ECO:0000313|Proteomes:UP000190274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Devillers H.;
RL Submitted (MAR-2016) 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; LT598457; SCU93892.1; -; Genomic_DNA.
DR STRING; 1266660.A0A1G4JSX7; -.
DR OrthoDB; 2891567at2759; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000190274; Chromosome G.
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-UniRule.
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.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|PROSITE-ProRule:PRU00605};
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:UP000190274}.
FT DOMAIN 41..170
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 205..255
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 470..627
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 860..997
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT REGION 337..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1179
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1309
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1311
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1348 AA; 147078 MW; 51B2085D60126A93 CRC64;
MSVLILPGPQ ALSAFRVENL ARGIEAYCNS SSVISEVRSC YVHYVDVEGQ EALSERERQL
LEVLLTYDQA LDDSDGYVQQ LKTGIVSSSS GQLGPDTYLV RILPRPGTIS PWSSKATNIA
RVCGLETKIG RIERGLALLI KTVPGFPLVE NLNEESLKSC FDRMTQELFL MEAPVPATIF
SHESPKPLGH VKLFSDKSAP PKEILEDANQ KLGLALDKGE IDYLIGAFVD TLHRDPSDVE
LFMFAQVNSE HCRHKIFNAD WTIDGLQKQL TLFKMIRNTH AHTSDYTISA YSDNSAVLDT
GNDSYYYAPD FKTKTWKAVK ENVPMLVKVE THNHPTAVSP FPGAATGSGG EIRDEGATGR
GSKSKCGLSG FAVSDLLIPG FKQPWELDVG KPNHIASALD IMVEAPLGSA AFNNEFGRPC
INGYFRTLTT KVTNSDDKEE VRGFHKPVMM AGGFGAVRPQ FALKNKPITP GSSLIVLGGE
SMLIGLGGGA ASSINSGEGS AELDFASVQR GNPEMERRCQ QVIDACISLD SGNPIQSIHD
VGAGGLSNAL PELVHDNDLG AKFDIRKVLS LEPGMSPVEI WCNESQERYV LGVSQQNLPL
FEDICKRERA PYAVVGNATA EQRLIVEDPL LKTTPIDLEM SILFGKPPKM TREAITQPLS
LPPADLSVIS SLGDAIDRVL TLPTVGSKSF LITIGDRTVT GLIDRDQFVG PWQVPVADVG
VTGTALGDEI CRTGEALAMG ERPTNALISA AASAKLCVAE SLLNLFAADI KSLKHVKLSA
NWMSPASHQG EGSKLYEAVQ AIGMDLCPDL DIAIPVGKDS MSMKMKWGDK EVTAPLTLNI
TAFGPVNNTS NTWTPLLKKQ EGTVLVLVDL AAKQQEHSLG GSALLQVYNQ VGNTSPTVHD
NKLFKGVLES LLELHQTDLV FSYHDRSDGG VIVTLLEMAF ASRCGMDIVV DNASSVYTPL
FNEELGCVFQ IAEQNLSTFE EIFSKHGVSR DHISVIGLPK FDSQSIIIRN KAGLVKYENT
RASLQQTWSA TSYQLQKMRD NPISADQEFA NIADDKDPGL HYSLTYDLTD DMKVGQLAAI
SKPRVAILRE QGVNGQMEMA WSFQQAGFTA VDVTMTDLLE GRAHLDDFVG LAACGGFSYG
DVLGAGAGWA KSVLYHEGVR KQFVNFFNER EDTFAFGACN GCQFLSRLKD IIPGCENWPS
FERNASEQYE ARVCMLEITQ DDGCKTESVF LNGMVGSKIP IAVAHGEGRA SFKDQKEMER
FEEGALCGVR YVDNYGNVTS KYPFNPNGST NSIAGVRSPN GRVLAMMPHP ERVTRLEANS
WYPAGKYEEW EGYGPWIRMF RSARRWVG
//
