ID A0A059AKJ9_EUCGR Unreviewed; 1417 AA.
AC A0A059AKJ9;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=EUGRSUZ_I00206 {ECO:0000313|EMBL:KCW54226.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW54226.1};
RN [1] {ECO:0000313|EMBL:KCW54226.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW54226.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-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; KK198761; KCW54226.1; -; Genomic_DNA.
DR RefSeq; XP_010027660.1; XM_010029358.2.
DR STRING; 71139.A0A059AKJ9; -.
DR EnsemblPlants; KCW54226; KCW54226; EUGRSUZ_I00206.
DR GeneID; 104418123; -.
DR Gramene; KCW54226; KCW54226; EUGRSUZ_I00206.
DR KEGG; egr:104418123; -.
DR eggNOG; KOG1907; Eukaryota.
DR InParanoid; A0A059AKJ9; -.
DR OMA; LSANWMW; -.
DR OrthoDB; 2891567at2759; -.
DR UniPathway; UPA00074; UER00128.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
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 GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
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}.
FT DOMAIN 127..244
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 271..320
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 534..688
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 943..1072
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1237
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1372
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1374
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1417 AA; 155351 MW; 70EC3EB910C8DB84 CRC64;
MACAREITAA EFLKGTSRQT LFLQRNVQRR RTHLLWGTRQ RQNLVGSAKD GRQIALRCRA
QAKPKAVVSE GVSSALEEES ALSEKPAKEV IHFFRIPLIQ ENATSELLKS VQAKVSNQIV
GLKTEQCFNI GLESRLSSEK LSVLKWLLQE TYEPENLGTE SFLEKKRQEG LNTVVVEVGP
RLSFTTAWSA NAVSICRACG LSEVTRLERS RGYLLYSKGP LQDHQIYEFA QMVHDRMTEC
VYAQRLTSFE TSVVPEEVRY IPVMEKGRKA LEEINEQMGL AFDEQDLQYY TRLFREDIKR
DPTTVELFDI AQSNSEHSRH WFFTGKMVID GQPMNRTLMQ IVKSTLQANP NNSVIGFKDN
SSAIKGFLVN QLRPVQPGST CPLNETGREL DILFTAETHN FPCAVAPYPG AETGAGGRIR
DTHATGRGSF VVAATAGYCV GNLNLEGSYA PWEDLSFSYP SNLASPLQIL IDASNGASDY
GNKFGEPLIQ GYTRTFGMRL PNGERREWLK PIMFSAGIGQ IDHTHIVKGE PDIGMLVVKI
GGPAYRIGMG GGAASSMVSG QNDAELDFNA VQRGDAEMAQ KLYRVVRACI EMGEKNPIIS
IHDQGAGGNC NVVKEIIYPK GAEIDIRAIV VGDHTMSVLE IWGAEYQEQD AILVEPGSRE
LLQSICERER VSMAVIGSIN GQGRVVLVDS HLTKKSKASG LPTPPPAVDL ELEKVLGDMP
QKCFEFQRVV HPLEPLDIAP GITVMDSLKR VMRLPSVCSK RFLTTKVDRC VTGLVAQQQT
VGPLQITLAD VAVIAQTYDN LTGGACAIGE QPIKGLLDPK AMARLAVGEA LTNLVWAKVT
SLSDVKASGN WMYAAKLDGE GAAMYDAATA LSEAMIELGI AIDGGKDSLS MAAHAAGEVV
KAPGNLVISV YVTCPDVTKT VTPDLKLGDD GFLLHIDLAK GKRRLGGSAL AHVFDQIGDE
CPDLEDVSYL KRVFDGVQNL IDDEMISAGH DISDGGLLVS VLEMAFAGNC GFAISLDSHG
NSPFQTLFAE ELGVILEVSK KNLDSVLEKL SEVGVSSQII GRVTSAPMID LKVDGVTHLN
EHTALLRDLW EETSFNLEKL QRLASCVDQE KEGLKSRREP SWNLSFIPSF TDQKYINTSL
KPKVAVIREE GSNGDREMSA AFYAAGFEPW DVTISDLLNG SVSLNEFRGM VFVGGFSYAD
VLDSAKGWSA SIRFNKPLLA QFQEFYRRPD TFSLGVCNGC QLMALLGWVP GPQVGGVLGA
GGDPSQPRFI HNESGRFECR FTSVTIKDSP AIMFKGMEGS TLGVWAAHGE GRAYFPDDGV
LDRVLHSQLV PLRYCDDDGN PTEAYPFNVN GSPLGVAAIC SPDGRHLAMM PHPERCFLMW
QFPWYPKHWD VEKKGPSPWL RMFQNARAWC LETTDKA
//
