ID A0A0V1LAP7_9BILA Unreviewed; 1572 AA.
AC A0A0V1LAP7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=T02_7541 {ECO:0000313|EMBL:KRZ56605.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ56605.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ56605.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ56605.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-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:KRZ56605.1}.
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DR EMBL; JYDW01000091; KRZ56605.1; -; Genomic_DNA.
DR STRING; 6335.A0A0V1LAP7; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000054721; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP 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; 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 InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR040707; FGAR-AT_N.
DR InterPro; IPR010073; PurL_large.
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; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000054721}.
FT DOMAIN 175..288
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 581..731
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 995..1095
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1276
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1406
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1408
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1572 AA; 177013 MW; 6BE3AEF04F6A38F9 CRC64;
MIVVRLQELF VQCSSSKAGW HEKPKEENPF KLPIEWKNVV NAVSKNISNR KQSKNHPIKH
PLLAHSKKHA APVRRLPSQE IVILISATAQ KCSFDDCEKS SFSVIFLVST AYPTVVINIT
SITVIKMPNE TVFRFYYWQI NEQLGNEILK KLLNDMLEGE NLSVESVRCE FTFCVVSTRS
SITNEEIAKL KWLIERPFNM ETLAAESAFA YTRPENRVII EIGTRPYLVT PFNINAVVAC
KLAGLNFVSR LEKTRRYCIH YNRGKLSLPI RRKILTALHD RMTECEYTSD VVDFGTRRER
QKVQEVEIMI DDKVGLEFFN KKKDLTIEDE DIKYMLDLFK YKLKRNPTDV EIYDLTQICR
HWFFKGKLMV ENELQPISML QMVKDTQLFS RENNILKFSY NGSVIRGLNV LQMRPVDPTE
ASEFQIFPVL SHIVLAAETN NFQAEFDANL GICPSTGAAS GTGGRIRNIH ATGRGAYVVA
GIFGLAFGNL NVPGHRLPWE RCNHAESCTF ASPLQICVQA SDGSSEYGNK FGEPVICGFT
RSFDQYVNEL ACRYAYLKPV MFSGGVGRID EINIQKLKPA PGMLIVKLGG PAYRVSLGGG
TSSTIEIHGN GCLQYEAVHR GDPGMGQKLN RTIRTCSELG RNNPIISIYD QAAGGNGNVI
RKLIEPYGAS IESDNFSLGD SSLSIQELWS SEYQESDAIL MNPKNVPLIE KICQRERCLY
NVVGSVTENE KLLVKNFHDA ADSFQLPVNL DLALVKPYHN HQAINPCVQQ HRYLENFLWM
PPLRRRSKEY YFCRLWEVDR SVTGLVAQQQ CVGPFHTPVA DVAVTALSYF ETVGAAVAVG
EQPIKMLIHP EVGARLTVGE SLTNLVFAKI TNLEDVKCNA NWMWPATSPE ERYRMLEACD
AMCKIMNKLG IAVDGGNESL FLEAEINEEV VKAPGTLVIT SYALCTDITK TVTPDLKCTT
EDGCLILVRF ASLFDSWRLG GCAIAQGYGR TGCDSPDLDN VEQFKSAFRI TQSLISDRMI
TAGHDISDGG LIVCLLEMAF SGGRSIVIDL PFTEKPINLL FSEELGIVIE VSQSNFDKVL
NDFHAANVPV AYIGKSKSLT DEEPMIEIKI NGDVVLAGSV QSYRCTWQQT SCRLEKLQCN
PICVEEEVFR LKLKLPKYEM QSLMEIPAVS QHATVKDAST PCVAILREEG TTGDREMAAA
FMCAGFRVWD LSMQDLFDNN ISLNNFQGIV FPGGFSYSDV LGASKAWACS ILYHPKVKYQ
IEQFLQRRDT FSLGVCNGCQ LMATLGWIGS NEAIGRSVQS VSLEQNISGR FESRFATVRI
ERSRSIMLRG MENSVLGIWI AHGEGRFQFR DDLAYAAVEF NHLIALRYVD WENEIALAYP
YNPNGSPGGI AAICSANGRH LAMMPHPERS FMTWQWPYWP YEHAPVSPWY HMFRNAYEWS
FLLRGFNGQW IEPVKCLDYI SSSICSGILK VYGEDRCRID FLFGRYQCCW TCAATLGIPI
DSLGRFNDQQ GFYFYHPGCP NNVRDAIDAL GSSSTQWCMH WKEKNNGMNC YEPLFQYKCY
KTCRVKCGAF SD
//
