ID W4VRR3_9DIPT Unreviewed; 1348 AA.
AC W4VRR3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
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};
OS Corethrella appendiculata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Chaoboridae;
OC Corethrella.
OX NCBI_TaxID=1370023 {ECO:0000313|EMBL:JAB59109.1};
RN [1] {ECO:0000313|EMBL:JAB59109.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary glands {ECO:0000313|EMBL:JAB59109.1};
RA Ribeiro J.M.C., Chagas A.C., Pham V.M., Lounibos L.P., Calvo E.;
RT "An insight into the sialome of the frog biting fly, Corethrella
RT appendiculata.";
RL Insect Biochem. Mol. Biol. 44:23-32(2014).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GANO01000762; JAB59109.1; -; mRNA.
DR UniPathway; UPA00074; UER00128.
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; IPR016188; PurM-like_N.
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; PF00586; AIRS; 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 2: Evidence at transcript level;
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 51..166
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 191..240
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 309..414
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 453..610
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 870..1005
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1168
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1306
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1308
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1348 AA; 150460 MW; 313E0B90ADC0CDCC CRC64;
MPIVRFYLLD AFDEAKTTTL LNSLRRINPD IIELKTEKCI HVENEKYEQF PDKEEKILRW
ILKNPQDSFD QITHQSAFAQ VADDKSITIE IGPRFNFSTA DSTNSVSICH NIGLTFINRI
EVSVKYLIKF SYDKITDAEE SQLIGVLSDR MTQCRYTSEN LPQRSFYERL PKVENSQWYY
VPLLEQGQRA LEEVNVRLGL AFDNWDLDYY TNLFTNNLRR NPTNVELFDL AQSNSEHSRH
WFFKGRMVID GIEQGRTLLQ MIMDTQRFSN QNNRIKFSDN SSAVKGYLHR TLRPMFFTGP
GLIEVKNVAT DLIFTAETHN MPTAVAPFSG ATTGTGGRLR DIQAVGRGGL PIAGTAGYCV
GNLNIPNYRL SYEEQRPYPP SFETPLKIII EASNGASDYG NKFGEPVISG FAISYGCINA
SGKRDEYVKP VMFSGGMGTM DTNHNFKQYP ARGMLLAKIG GPVYRIGVGG GAASSVEVQG
DNNSELDFNA VQRGDAEMGN KLNRVVRACV ELAFRNPIVA IHDQGAGGNG NVLKELVEPG
NSGAIIFSKE FQLGDPTITA LELWGAEYQE SNAILCKPED RKLLEEICLR EKCPLNFVGV
VSKNGHVTLV EDNADFEKYL NRSVSQSWGN VPFNMKLRDV LCEMPMKTFH LQNIEQVLKP
LDLSEVKINE ALSRVLSTLT VGSKRFLTNK VDRCVTGLVA QQQCVGPLHT PLADCAVVAV
SHFGLEGIVS SIGTQPIKGL IDPGAAARMS VAEAISNIVF AGVSELPDIK CSGNWMWAAK
LPGEGAKMYK ACQEMCKLMN DLNIAIDGGK DSLSMAARVQ EETIKSPGTL VISAYAPCPD
IRVKITPDLK SPSFGRGGDL ILIKIEDKFR LGGSVLAQCY QQQGNESPNI ERSTLLKRAF
IVTQQLLVNR KLLSGHDISD GGLVTCILEM AFAGFCGVNI DLTELLDFSY DNLEEAALKI
LFTEECGWVL EVKSIDLESV LHEFRIKKVP VFHLGKSTVE KSAVFRIKGQ TIINESILHL
FKKWERTSFE LEKLQMNPEC AMEEFATLDY RKGPTYHCTF DLTIYVNPIL SVVRVAVIRE
EGTNSDREMA AALIKANFEV HDVTMSDLLM RKATLDPYRG VIFPGGFSYA DTLGSAKGWA
ASIIYSNLLA PQFENFKNRK DTFSLGVCNG CQLMSLIGWV GGDFEDGQNR SAEEKLNIPN
VALLHNKSQR FECRWSTVKI APTKAILLNR LSGSVLGCWT AHGEGRFSFK NDSIFQNIKS
EYCVALNYVD DYSNVTETYP MNPNGSRDGI AGICSKDGRH LAMMPHPERC HEMWQWPYVS
PTFLDTDKCP WQCMFDEAYI WCNRPLNN
//
