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Database: UniProt
Entry: A0A0V1N8Q8_9BILA
LinkDB: A0A0V1N8Q8_9BILA
Original site: A0A0V1N8Q8_9BILA 
ID   A0A0V1N8Q8_9BILA        Unreviewed;      1547 AA.
AC   A0A0V1N8Q8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
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};
DE   Flags: Fragment;
GN   Name=PFAS {ECO:0000313|EMBL:KRZ80303.1};
GN   ORFNames=T10_6476 {ECO:0000313|EMBL:KRZ80303.1};
OS   Trichinella papuae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ80303.1, ECO:0000313|Proteomes:UP000054843};
RN   [1] {ECO:0000313|EMBL:KRZ80303.1, ECO:0000313|Proteomes:UP000054843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ80303.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-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:KRZ80303.1}.
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DR   EMBL; JYDO01000003; KRZ80303.1; -; Genomic_DNA.
DR   STRING; 268474.A0A0V1N8Q8; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000054843; 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; 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; 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:UP000054843}.
FT   DOMAIN          143..256
FT                   /note="Phosphoribosylformylglycinamidine synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18076"
FT   DOMAIN          287..333
FT                   /note="Phosphoribosylformylglycinamidine synthase linker"
FT                   /evidence="ECO:0000259|Pfam:PF18072"
FT   DOMAIN          561..711
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   DOMAIN          967..1070
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   ACT_SITE        1251
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1381
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1383
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRZ80303.1"
FT   NON_TER         1547
FT                   /evidence="ECO:0000313|EMBL:KRZ80303.1"
SQ   SEQUENCE   1547 AA;  173321 MW;  560B37EC9DFF6A37 CRC64;
     SKTARHEKPK KENPFKQPIE WENAINAVSK KISNPISMQL RCDVCHEEIV ILISTTAQKC
     SFDEGETFSF SVIFLVSIGY STTVINITSF TVIKMPNQTV FRFYHWQINE PLGNEILKKL
     LNDMLEGENL SVESVRCEFA FCVVSTRSSI TNEEIAKLKW LIERPFNMET LAAESAFAYT
     RQENRLIIEI GTRPYFVTPF NINAVVACKL AGLNFVSRLE KTRRYCIHYN SGELSLSLRR
     KILTALHDRM TECEYTSDVV DFGTRRERQK VQEVEIMFDD KVGLEFFNKK NDLTIEDEDI
     EYMLDLFKYK LKRNPTDVEI YDLTQSNSEV CCHWFFKGKL IVENELRPIS MLQMVKDTQS
     FSTENNILKF SYGGSVMRGL NVLQMRPIDP TEASEFQILP VLSHIVLTAE TNNFQADFFV
     NFSQKFDADL GICPSTGAAT GTGSRIRNVH ATGRGAYVVA AIFGLSFGNL NVPGHRLPWE
     RCNHSDSCTF ASPLQICVQA SDGSSEYGNK FGEPIICGFT RSFDQYVNEL SCRYAYLKPV
     MFSGGVGRID EINIQKLKAA PGMLIVKLGG PAYRVSLGGG TSSTIEIHGN GSLHYEAIQR
     GDPVMGQKLN RTIRACSELG RNNPIISIYD QAAGGNGNVI RKLIEPYGAS IEPDNFSLGD
     SSLSIRELWS SEYQESDAIL MSPKNVPLIE KICQRERCLY NVVGTVTESE KLLVKNFYDA
     TDSFELPVNL DLPLKSFILS KTVRSATQIL RKFSLDAAIE TALKRVLLLP SVGSKNFITN
     KVDRSVTGLV AQQQCVGPFH TPVADVAVTA LSYFETVGAA VAVGEQPMKM LIYPEVGARL
     TVGESLTNLD VKCNANWMWP ATSPEERYRM LEACEAMCKV MNKLGIAVDG GNESLLMAAE
     INEEVVKAPG TLVITSYAVC TDITKTVTPD LKCTTEDGCL ILVRFASLFD SWRLGGCAIA
     QCYGRTGSDS PDLDNVEQFK SAFRITQNLI SDRVITAGHD ISDGGLIVCL LEMAFSGGRS
     IAIDLPFTRE PINLLFSEEL GIVIEVSQSN LDKVLNDFHT ANVPVVYIGK SKSLTDEEPM
     IEIKINGDVV LAGSAQSYRC KWQETSCRLE KLQCNPICVE EEVFRLKLKP PMYEMQFLME
     IPAVSQHATV KDASTPCVAI LREEGTTGDR EMAAAFMCAG FRVWDLSMQD LFDNNISLNN
     FRGIVFPGGF SYSDVLGASK AWACSVIYHP KVKHQIEQFL QRRDTFSLGV CNGCQLMASL
     GWIGSNEAIG RSRQTISLEQ NISGRFESRF CTVRIERSRS IMLKGMENSV LGIWIAHGEG
     RFQFKDELAY AAVEINHLIA LRYVDSENEI ALAYPYNPNG SPGGIAAICS ANGRHLAMMP
     HPERSFMTWQ WAYWPYEHAP VSPWFHMFRN AYEWSFLLRG FNGQWIEPVK CLDYISSSLC
     SGILKVYGED RCRIDFLFGR YQCCWTCAAT LGIPIDSLGR FNDQQGFYFY HPGCPNNVRD
     AIDALGSSST QWCMHWKEKN NGMNCYEPLF QYKCYKTCRV KCGTLSD
//
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