ID H3G9D6_PHYRM Unreviewed; 1366 AA.
AC H3G9D6;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
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};
OS Phytophthora ramorum (Sudden oak death agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=164328 {ECO:0000313|EnsemblProtists:Phyra71606, ECO:0000313|Proteomes:UP000005238};
RN [1] {ECO:0000313|Proteomes:UP000005238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pr102 {ECO:0000313|Proteomes:UP000005238};
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
RN [2] {ECO:0000313|EnsemblProtists:Phyra71606}
RP IDENTIFICATION.
RC STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra71606};
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
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; DS566028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 164328.H3G9D6; -.
DR EnsemblProtists; Phyra71606; Phyra71606; Phyra71606.
DR VEuPathDB; FungiDB:PSURA_71606; -.
DR eggNOG; KOG1907; Eukaryota.
DR HOGENOM; CLU_001031_0_0_1; -.
DR InParanoid; H3G9D6; -.
DR OMA; LSANWMW; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000005238; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000005238}.
FT DOMAIN 58..182
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 209..258
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 476..637
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 875..1025
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1190
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1325
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1327
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1366 AA; 149233 MW; F055B59582F416E5 CRC64;
MASSPEKKQK TASIATASSL LRFYRTPAFT AHANRTLLAS LRAQVADTGI SVDELATEYC
FYVETHAAAG PLSTADQETL HWLLSETFEP QQTRAAEPFL AAAEQSKEWL VEVGPRMNFS
TAWSSNAVAI CQACGISSIK RIERATRYLV RYTATKPEGL EKLKHALLRH QCDRMTQQVY
EKPLASFWHG KTVQPVRKIP IMERGIDALK EINEEIGLGF DDWDLQYYLN LFKDKLRRNP
TDVECFDMGQ SNSEHSRHWF FGGKIVVDGK EMPQTLFQMV KDTLTENAKK NSVIAFHDNS
SVIKGANIVT LGPVNPGEPS AVQERTLDSH LLLTAETHNF PSGVAPFPGA ETGTGGRIRD
VQATGRGANV VAGVSAYSVG NLNLEGYKLP WEDEKLEYPS NLAHPRDILI QASNGASDYG
NKFGEPVVTG FARSFGMVLP NGERREYIKP IMFSAGLGQL DGRHCTKGEP EIQMWVVKIG
GPCYRIGMGG GAASSRIQDA KTADLDFNAV QRGDAEMECK LNKVIRACCD LGEKNPIVSI
HDQGAGGNGN VLKEIVEVSN SKPGDANRGG ARYEVRDILV GDDTLSVLEI WGAEYQENDA
LLLRPEHVEL FDKICKRENC PYALLGQVTG DGHVVLHDAQ DDSTPFDLDL DLVLGKMPQK
TFTDTKATEP VTELSLPADI TLRDALDRVL RLLSVGSKRF LTSKVDRSVS GLVAQQQTVG
PLQLTLADCA VVAQSNVPNK DGKFTGVVSA CGEQPVKGLV NPGAMARLSV AESLTNMVWA
ALGGRGLDDC KCSANWMWAA KLPNEAARMY ECCEAMTTFM KQVGVSVDGG KDSLSMAAKV
NQKDVKTPGT LVITMYAPTE DVELKVTPDL KTHAGDSLVY YVDVGKGANR LGGSALAQVY
GQVGDVTPDV EDALLFKNAF NAVQEGIKKG HLLAGHDRSD GGLIVTLLEM AFAGNCGLDV
DIPFAGGKAT TKDVIEVLFA EELGFVFQVA AGQHATEVES IFSKLNVPLV KLGKVTTDGA
IKVSVNGESV LEDQMVDLRD VWEATSFELE KRQCNPECVA QEQRSLRTRT APSWKLAYEP
TPTPERQLST RAQHRVAVIR EEGSNGEREM LAAFHHAGFE VWDITMSDLV NKRAVLDERF
RGVAFVGGFT FADVLGSAKG WSGVVKFHGD VLKQFAAFKA REDTFSFGAC NGCQFMTLLG
WLDHPEAKAL EEETKSSAQP RFVHNESGRH ESRFVSVQIQ ESNSVMLRGM AGSSLGVWLS
HGEGRAHFTH PTILDKYVSS GAAPIRYVDD SNVPTEEYPF NPNGSPQGIA GLVSSDGRHM
CLMPHPERCF LKYQWPYMPA EFEAHPVSPW MQIFQNAKTF CEGGAQ
//
