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Database: UniProt
Entry: G5B5F7_HETGA
LinkDB: G5B5F7_HETGA
Original site: G5B5F7_HETGA 
ID   G5B5F7_HETGA            Unreviewed;      1337 AA.
AC   G5B5F7;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 41.
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=GW7_13859 {ECO:0000313|EMBL:EHB04518.1};
OS   Heterocephalus glaber (Naked mole rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Heterocephalus.
OX   NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB04518.1, ECO:0000313|Proteomes:UP000006813};
RN   [1] {ECO:0000313|EMBL:EHB04518.1, ECO:0000313|Proteomes:UP000006813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993625; DOI=10.1038/nature10533;
RA   Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA   Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA   Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA   Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA   Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA   Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT   "Genome sequencing reveals insights into physiology and longevity of the
RT   naked mole rat.";
RL   Nature 479:223-227(2011).
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; JH168588; EHB04518.1; -; Genomic_DNA.
DR   STRING; 10181.G5B5F7; -.
DR   eggNOG; KOG1907; Eukaryota.
DR   InParanoid; G5B5F7; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000006813; 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:UP000006813}.
FT   DOMAIN          83..155
FT                   /note="Phosphoribosylformylglycinamidine synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18076"
FT   DOMAIN          184..232
FT                   /note="Phosphoribosylformylglycinamidine synthase linker"
FT                   /evidence="ECO:0000259|Pfam:PF18072"
FT   DOMAIN          444..602
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   DOMAIN          876..975
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   REGION          604..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1158
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1297
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1299
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   1337 AA;  144206 MW;  9EE401464B660B23 CRC64;
     MAPVLRFYVR PSGHEGAASG QSVRKLQEKL PELERVETEL CYNVNWTAEA VPSTLEMKKL
     KWLFGCPLFL DDVAQESWLR PGSNDLLLEV GPRLNFSTPT STNIVSVCQA AGLVAVNRVE
     PTRRYQLSFA RRPSAEMKAM ALAALHDRMT EQHFPHPIQS FLPESTPAPL SGPINILQEG
     RSALEKANQK LGLALDSWDL DFYTKRFQEL QRNPSTVEAF DLAQSNSEHS RHWFFKGQLH
     VDGKKLLHSL FESIMSTQAS SNPNNVLKFC DNSSAIQGKE VRFLQPEDPI KPSCFRQQQR
     LRHVVFTAET HNFPTGVSPF SGATTGTGGR IRDVQCTGRG AHVVAGTAGY CFGNLCIPGY
     SLPWEDPSFQ YPGNFARPLE IAIEASNGAS DYGNKFGEPV LAGFARSLGL QLPDGQRREW
     IKPIMFSGGI GSMEAEHVGK QPPEPGMEVV KVGGPVYRIG VGGGAASSVQ VQGDNSSDLD
     FGAVQRGDPE MEQKMNRVIR ACVEAPRGNP ICSLHDQGAG GNGNVLKELS DPAGAIIYTS
     RFQLGDPTLN ALEIWGAEYQ ESNALLLRPP HRDFLSCVSA RERCPASFVG TITGDKRIVL
     VDDRESPVGV NDQGDAPTAP PPTPVDLELD WVLGKMPRKE FFLQREPPVL QPLALPPGLT
     VRQALERVLR LPAVASKRYL TNKVDRSVGG LVAQQQCVGP LQTPLADVAV MALSHQELIG
     AATALGEQPV KSLLDPKVAA RLAVAEALTN LVFALVTDLR DVKCSGNWMW AAKLPGEGAA
     LVDACEAMVA VMAALGVAVD GGKDSLSMAA RVGSETVRAP GALVISAYAV CPDITATVTP
     DLKHPEGRGH LLYVPLSPGQ YRLGGTALAQ CFSQLGEQPP DLDLPENLVR AFSITQGLLK
     DRLLCSGHDV SDGGLVTCLL EMAFAGNCGI EVDVPAPGVD ALPVLFAEEP GLVLEVQEPN
     LAGVLQRYRG AGLCCLDLGC TGEAGPHAMV RVSVNGVVAM EEAVGQLRAL WEETSFQLDR
     LQAEPHCVAE EEQGLKERMG PNYCLPPTFP KASVPREPGS PSLRVAILRE EGSNGDREMA
     DAFHLAGFEV WDVTMQDLCS GAIGLDTFRG VAFVGGFSYA DVLGSAKGWA AAVTFNPKAR
     AELSRFRKRP DTFSLGVCNG CQLLALLGWV GSDTNEEAGD LGHDSWPAQP SLLLCHNLSG
     RYESRWASVR VGPGPALMLR GMEGAVLPVW SAHGEGYMAF SSPELQAQME ASGFVSLHWA
     DDDGNPTERY PLNPNGSPGG MAGICSCDGR HLALMPHPER AVRPWQWAWR PSPFDTLTTS
     PWLQLFINAQ DWAQGGC
//
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