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
//