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Database: UniProt
Entry: L7N3J6_XENTR
LinkDB: L7N3J6_XENTR
Original site: L7N3J6_XENTR 
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
//
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