ID W9ISC4_FUSOX Unreviewed; 1355 AA.
AC W9ISC4;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=FOYG_04625 {ECO:0000313|EMBL:EWY95644.1};
OS Fusarium oxysporum NRRL 32931.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660029 {ECO:0000313|EMBL:EWY95644.1, ECO:0000313|Proteomes:UP000030753};
RN [1] {ECO:0000313|EMBL:EWY95644.1, ECO:0000313|Proteomes:UP000030753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL Submitted (JUN-2011) 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; JH717841; EWY95644.1; -; Genomic_DNA.
DR OrthoDB; 2891567at2759; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000030753; Unassembled WGS sequence.
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:UP000030753}.
FT DOMAIN 38..154
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 178..226
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 441..596
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 882..1013
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1189
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1316
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1318
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1355 AA; 147717 MW; 8AFD75653A96E28B CRC64;
MHHVLIGESC YTASEVQKLV QRINDQSPVK VAKLTGSWQY YLDLETEDAA VLGSIKKILE
AIEQPTDAPS TGDNKNAIDI YVSPRNVSPW SSKATSIALV CDLKTVNRIE RGRVIHIELE
DGFKGEEDLS FRDILHDRMT EFFSLSPPAL DTMFAHGARN PLVVVDIFSD ERGPLAALQD
HNKQAGLGLD QPNMEYLVKQ YTALGRSPND VELFMFAQVN SEHCRHHVFN ASWTIDGVSQ
ENSLFGMIKN THKSNPEYVI SAYSDNAAVL SGDEGNYWAP DYSTGSWKLT REVVQPLIKV
ETHNHPTAIS PFPGAATGSG GEIRDEGAVG RGSSPKAGLA GFWVSDLLIP GNKRPWELDI
GRPSHYASSL DIMLEAPIGS ARFNNEFGRP ALTGTFRTLL TNEAGSDVPE YRGYHKPIMI
AGGIGSVRPQ HALKEESYVE EGAHVIVLGG PAMLIGLGGG AASSNTGSDA TADLDFDSVQ
RGNPEMERRA QMVINTCVAL GPESPIAFIH DVGAGGLSNA LPELVKDAGF GGKFELRQVE
SADNSMSPLQ IWCNEAQERY VLLVNRDGLN RFTSICRRER CGFSVVGTAV TKDESGVSKL
VLTDREPTIQ PPVDPINLPM DVLFPPGRRI SKDVQRVEKN LRPFDAVKSL TEHCGSSDIG
DLVTKATELV FNLPSVGSKN FLITIGDRTV GGLSVRDQLV GPWQTPVADV AVTLTSFSLD
DKKRRGEAMA MGEKPNLALI SAAASARMAV VESLMNLGAA DIKPGPVNGD LKRVKLSANW
MAAVGHPGEG AALYDAVQAI GMELCPQLGV SIPVGKDSLS MKASWKDKET SESQTVTAPV
SLVISAFSLV EDVRSTWTPQ LRRVEEVGES VLVFVDLAQG FRAMGGSALA QTLGQIGNES
PDVRDVQIIR DFFDALWQLH QEDIVLAYHD RSDGGLLTTV AEMMFAGRCG ADISLDSLAE
SEDKVLDALF NEELGAVFQI RRGDEIKFKR CFATCGPPHG LIKTIGYVRP TSKQSLLVKY
RSKTIVDLER AKIQQWWTST SYEMQKLRDN PECAQSEFEA IQDNRDPGLH YKLKFDPADV
SLPALTSIKS LVYKPRVAIL REQGVNGHAE MAFAFRAAGF DAVDVHMSDI LDGFSLDGFR
GLAACGGFSY GDVLGAGNGW AQSILMHDGA RKTFEAFFKR PDTFSLGVCN GCQMLTRLKE
LIPGAEHWPT FVENASTQFE GRYSMVTIED KSENSVFFSG MSGSSFPIVV SHGEGRAAFS
SANDLQSVND SGLIPFRYVD NYGSVTERYP FNPNGSPQGV AGVQSRDGRV VAMMPHPERT
IMADVGSWKP ERQLAEWGQY GPWFQLFLNA RKWAA
//
