ID Q8VYU2_VIGUN Unreviewed; 1289 AA.
AC Q8VYU2;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 24-JAN-2024, entry version 73.
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};
DE Flags: Fragment;
GN Name=pur4 {ECO:0000313|EMBL:AAL55431.1};
OS Vigna unguiculata (Cowpea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3917 {ECO:0000313|EMBL:AAL55431.1};
RN [1] {ECO:0000313|EMBL:AAL55431.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Nodule {ECO:0000313|EMBL:AAL55431.1};
RA Mann A.J., Smith P.M.;
RT "Vupur4 mRNA from cowpea nodules encoding formylglycinamide ribonucleotide
RT amidotransferase.";
RL Submitted (DEC-2001) 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; AY069939; AAL55431.1; -; mRNA.
DR UniPathway; UPA00074; UER00128.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
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, ECO:0000313|EMBL:AAL55431.1};
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 Transferase {ECO:0000313|EMBL:AAL55431.1}.
FT DOMAIN 4..122
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 149..198
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 412..566
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 821..951
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1115
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1250
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1252
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAL55431.1"
SQ SEQUENCE 1289 AA; 141630 MW; 9A67804ABD485459 CRC64;
QTEQCYNVGL SSQLSSENFS VLKWLLQETF EPENLGNESF LEKKRKEGLS PVIVEVGPRL
SFTTAWSTNA VAICHACGLT EVTRLERSRR YLLFTTSELQ DHQINEFAYM VHDRMTECVY
SQKLTSFETS IVPEEIRYIP VMERGRKALE EINLEMGFAF DDHDLEYYTK LFREDIKRNP
TNVELFDIAQ SNSEHSRHWF FTGKIFIDGQ LMNKTLMQIV KSTLQANPNN SVIGFKDNSS
AIRGFPVKQL RPVQPGSSCP LEIAIHELDI LFTAETHNFP CAVAPYPGAE TGAGGRIRDT
HATGRGSFVQ AATAGYCVGN LNTSNFYAPW EDPSFTYPSN LAPPLQILID SSNGASDYGN
KFGEPLIQGF CRTFGMRLPS GERREWLKPI MFSAGIGQID HLHITKGEPD IGMLVVKIGG
PAYRIGMGGG AASSMVSGQN DAELDFNAVQ RGDAEMAQKL YRLVRACIEM GDKNPIISIH
DQGAGGNCNV VKEIIYPKGA EIDVRAIVVG DHTMSVLEIW GAEYQEQDAI LVKPESRDLL
ESICRREKVS MAVIGTISGD GRVVLVDSLA TQQCISNGLP PPPPAVDLEL EKVLGDMPKK
SFHFSRVVYE REPLDIAPAI TVIDSLKRVL SLPSVCSKRF LTTKVDRCVT GLVAQQQTVG
PLQIPLADVA VTAQTFTDLT GGACAIGEQP IKGLLDPKAM ARLAVGEALT NLVWAKVTSL
SDVKASGNWM YAAKLDGEGA DMYDAAISLS EAMIELGIAI DGGKDSLSMA ARSDGEVVKA
PGNLVISVYV TCPDITKTVT PDLKLRDEGV LLHIDLSKGK RRLGGSALAQ AFDQVGDECP
DLDDVPYLKK VFEGVQDLLT DELISAGHDI SDGGLLVCAL EMAFAGNCGF NLNLASQGNS
LFQTLYAEEL GLVLEVSKKN LTLVMEKLGN VGVSAEVIGQ VTANPSIEVK VDGEIFLTEK
TTILRDMWEE TSFQLEKFQR LASCVDMEKE GLKHRYEPSW DLTYSPVFTE EKFLSATVKP
KLAVIREEGS NGDREMAAAF YAAGFEPWDV TMSDLLNRKI SLQEFRGIVF VGGFSYADVL
DSAKGWSACI RFNEHVLQQF QEFYKRPDTF SLGVCNGCQL MALLGWIPGP VIGGVHGAGG
DLSQPRFIHN ASGRFECRFT SVTILPSPAL MFKGMAGSTM GIWAAHGEGK AYFPDEGVFD
RIVHSELAPV RYCDDAGNPT ESYPFNVNGS PLGVAAICSP DGRHLAMMPH PERCFLMWQF
PWYPKHWDVE KNGPSPWLRM FQNAREWCS
//