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Database: UniProt
Entry: Q8VYU2_VIGUN
LinkDB: Q8VYU2_VIGUN
Original site: Q8VYU2_VIGUN 
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
//
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