ID L7N3J6_XENTR Unreviewed; 1348 AA.
AC L7N3J6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 4.
DT 24-JAN-2024, entry version 59.
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 Name=pfas {ECO:0000313|Ensembl:ENSXETP00000035008};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000035008};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000035008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000035008};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000035008}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JAN-2013) 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 STRING; 8364.ENSXETP00000035008; -.
DR Ensembl; ENSXETT00000035008; ENSXETP00000035008; ENSXETG00000030220.
DR eggNOG; KOG1907; Eukaryota.
DR InParanoid; L7N3J6; -.
DR Reactome; R-XTR-73817; Purine ribonucleoside monophosphate biosynthesis.
DR UniPathway; UPA00074; UER00128.
DR Bgee; ENSXETG00000030220; Expressed in gastrula and 13 other cell types or tissues.
DR ExpressionAtlas; L7N3J6; differential.
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}.
FT DOMAIN 95..172
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 199..247
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 459..615
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 871..995
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1169
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1303
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1305
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1348 AA; 146542 MW; 5830BB255FEC3FF9 CRC64;
MYARPLLLTY NSLSSPEVPP RAGKMVVLHF YRSLQNSSET LRLPGAENIQ SLQRELCYNV
NWTGPAAPSS QETDALRWLF SCPFDPQSIS DTSSLHSEPS DLLVEIGPRL NFSTATSTNA
VSICRSVGLT NVDRIECSKR YLIKFQTRPQ GSEEQELLAS LYDRMTECVY PEPVRSFEVS
VRPEKVYEVD ILGQGRAALE KANTELGLAF DSWDLDYYSS LFQRVGRNPS SVECFDLAQS
NSEHSRHWFF KGKLKVDGQE KEMSLFDMIM KTQDTSNPNN VIKFCDNSSA IQGREVASLI
PTDPSCAGPY HLCRSTRHLI FTAETHNFPT GVAPFSGATT GTGGRIRDVQ STGRGAHVIA
GTAGYCFGNL HIPGYSLPWE DPAYQYPVQF ARPLEVAIEA SNGASDYGNK FGEPVLAGFA
RSFGVRLPSG ERREWVKPIM FSGGIGSMED VHRTKEAPEP GMHVVKVGGP VYRIGVGGGA
ASSIQVQGDN ASELDFGAVQ RGDAEMEQKM NRAVRACVER GGKNPICSIH DQGAGGNGNV
LKELSEPQGA VIYTKSFQLG DPTLSVLEIW GAEYQESNAL LLRPDDAEFL RSVCRRERSP
VDFVGKITGD GRIVLINGSD TDPAPDSTDR NAVPVDLQLE WVLGKMPRKE FVLNRVAPNL
QPLVLPSGLT VGQALDRVLR LPSVASKRYL TNKVDRSVTG LVAQQQCVGP LHTPLADVAV
VSLSYSDIVG GATAIGEQPI KSLLNPAAGA RLAVAEALTN LLFAQVTDLK DVKCSGNWMW
AAKLPGEGAL LYDACAAMCD VMAQLGVAID GGKDSLSMAA RVGTETVKAP GSLVISVYAV
CPDITTTVTP DLKNPGQKGV LLYLPLCPGQ HRLGGSALAQ CYSQLGETPP DLDDPQTLIS
CFNVTQQLLR DRVLSAGHDV SDGGLVTCIL EMAFAGNCGL DIEISSSCTN VLELLFAEEP
GLVLEVAEQS VELVMERYRA AGVECVRIGC TKERGPASMV RIRANGQEVV NEKLGSLRAV
WEETSFQLER LQANPSCVSQ EEAGLRVREG PSYHLTFNPS EIPLVPPSVG GNQPRVAVVR
EEGSNGDREM AASLLMAGFQ VWDVTMEDLL AGGTTLDSFR GLVFVGGFSY ADVLGSAKGW
AASVKFNASV REQFENFRRR ADTFSLGVCN GCQLMALLGW VGPDNPTDTV GDLPTQGVLL
SHNLSGRFES RFVTLKIQQS PSILLRGMAG STLGVWVAHG EGYMRFRSPK VQDYVTSNHL
APLCYVDDGG KPTEEYPMNP NGSPLGIAGL CSADGRHLAM MPHPERCVMK WQWPWMPESW
RHSLDVSPWM RLFQNGYRWC QENPSRDN
//