ID A0A226E6D9_FOLCA Unreviewed; 1352 AA.
AC A0A226E6D9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=Fcan01_12038 {ECO:0000313|EMBL:OXA53192.1};
OS Folsomia candida (Springtail).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA53192.1, ECO:0000313|Proteomes:UP000198287};
RN [1] {ECO:0000313|EMBL:OXA53192.1, ECO:0000313|Proteomes:UP000198287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VU population {ECO:0000313|EMBL:OXA53192.1,
RC ECO:0000313|Proteomes:UP000198287};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXA53192.1};
RA Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N., Roelofs D.;
RT "The genome of Folsomia candida.";
RL Submitted (DEC-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OXA53192.1}.
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DR EMBL; LNIX01000006; OXA53192.1; -; Genomic_DNA.
DR STRING; 158441.A0A226E6D9; -.
DR OMA; LSANWMW; -.
DR OrthoDB; 2891567at2759; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000198287; 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:UP000198287}.
FT DOMAIN 41..159
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 188..237
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 451..607
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 870..993
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1172
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1310
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1312
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1352 AA; 148433 MW; 0554A099C8368C47 CRC64;
MATVVKFYRT PGLSPHIEND KLKAIEKHSP LRIEGMETES TFYVETQSRL TDKEILQIRW
VLAPVLNPDV LTDVSRFPLK GDKNHLIIEI GPRLNFSTAF STNAVSIFNA VGLKKITRLE
ISTRYVIRFE DTPTTPETLA KIEGKVVGAL HDRMTQCRYL EPLQSFALDK KPEPWFEVDI
MGKGRAALEK VNDQLGLAFD NWDLDYYTEL FKNKLKRNPT SVECFDLAQS NSEHSRHWFF
KGEMIVDGVP HQKSLIDMIM DTQKTTNQNN VIQFSDNSSA IIGYNVKNML PNEVVEPSAF
HIKPGTRHII FTAETHNFPT GVAPFSGATT GTGGRLRDVQ AVGRGGYVIA GTAGYSFGSL
LIPDYELPWE EKNLDYPSNF APPVEIAIEA SNGASDYGNK FGEPVISGFA RSFGMVIDQS
SKERREYIKP IMFSGGIGSM DDNMIDKLKP EPGMQVVKLG GPIYRIGVGG GSASSVQVQG
DNKAELDFDA VQRGDAEMEQ KLNRVIRSCL ELGEKNPICS IHDQGAGGNG NVLKELVEPN
GAVIFTKKFQ LGDPTINTLE LWGAEYQESD AILCRTEDAS LLQQIADRER CPVNFVGTVT
GDGKVVLTEI PVQPSGSVQV SAEELAAIQK RPNPVNLDLE FVLGKMPRKV FKMEKYKVNL
RPLVLPKGLT VADALKRVLR LPSVASKRYL TNKVDRSVSG LVAQQQCVGP LHTPLADVAV
IALSHFEKTG SATSIGEQPI KGLLCPAAGA RMTVAEALSN LVFAPISDLK DVKCSGNWMW
AAKLPGEGAA LLEACEAMCN VMQQLGIAVD GGKDSLSMAA RVGTDTVKAP GTLVISTYAP
CPNITKVVTP DLKAPSAGKE SLLLFVDLSG GKSRLGGTSL AQCYKQLGDT VPDLEDPAIL
VNAFNTTQAL ITDGYVLSGH DVSDGGLVTC LLEMAFGGHC GLRADITHRE SDCPLEVLFS
EEVGWVLEVD GTHVEKVLSP FKKAKVPVYP IGVSSGYGPA SRIEISVNGK MEVESLMVDL
YQLWEETSWQ LEKRQANPVC VTQEYQSLRT RHVPNYKFTF DPNVIKISTA LTQVNAPNVA
VIREEGSNGD REMIASLYMA GFQVWDVTMQ DIVTRKITLD KFRGIVFPGG FSYADVLGSA
KGWAASFLFD QSTKDQLAHF RARKDTFSLG VCNGCQLLAL LQWIGLNSKT DVVGDDHGVP
SVPDVFLDHN QSDRYESRFS TVKIEKSNSI MLKGMEGSVL GAWIAHAEGR FNYKNLSVYT
ELDKSNCIAL RYVDDSMKPT EEYPMNPNGS KYGVAGVCST DGRHLAMMPH PERCVLPWQW
PWISQNLKGQ MKQATPWLQM FVNAKNWCTS SN
//
