ID A0A0V1PDZ3_9BILA Unreviewed; 1331 AA.
AC A0A0V1PDZ3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, 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};
DE Flags: Fragment;
GN Name=PFAS {ECO:0000313|EMBL:KRZ94187.1};
GN ORFNames=T08_16284 {ECO:0000313|EMBL:KRZ94187.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ94187.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ94187.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ94187.1};
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:KRZ94187.1}.
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DR EMBL; JYDM01000020; KRZ94187.1; -; Genomic_DNA.
DR STRING; 92180.A0A0V1PDZ3; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000054924; 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:UP000054924}.
FT DOMAIN 63..176
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 207..253
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 467..617
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 881..981
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1162
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1292
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1294
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ94187.1"
SQ SEQUENCE 1331 AA; 149678 MW; C8ACB1AA1907B2CF CRC64;
LYWIGKIAFH TVIKMPNETV FRFYYWQINE QLGNEILKKL LNDMLEGENL SVESVRCEFT
FCVVSTRSSI TNEEIAKLKW LIERPFNMET LAAESAFAYT RPENRVIIEI GTRPYLVTPF
NINAVVACKL AGLNFVSRLE KTRRYCIHYN RGKLSLPIRR KILTALHDRM TECEYTSDVV
DFGTRRERQK VQEVEIMIDD KVGLEFFNKK KDLTIEDEDI KYMLDLFKYK LKRNPTDVEI
YDLTQSNSEV CRHWFFKGKL MVENELQPIS MLQMVKDTQL FSRENNILKF SYNGSVIRGL
NVLQMRPVDP TEASEFQIFP VLSHIVLAAE TNNFQAGICP STGAASGTGG RIRNIHATGR
GAYVVAGIFG LAFGNLNVPG HRLPWERCNH AESCTFASPL QICVQASDGS SEYGNRFGEP
VICGFTRSFD QYVNELACRY AYLKPVMFSG GVGRIDEINI QKLKPAPGML IVKLGGPAYR
VSLGGGTSST IEIHGNGCLQ YEAVHRGDPG MGQKLNRTIR TCSELGRNNP IISIYDQAAG
GNGNVIRKLI EPYGASIESD NFSLGDSSLS IQELWSSEYQ ESDAILMNPK NVPLIEKICQ
RERCLYNVVG SVTENEKLLV KNFHDAADSF ELPVNLDLAL VKPYHNHQAI NPCVQQHRYL
ENFLWMPPLR RRSKEYYFCR LWEVDRSVTG LVAQQQCVGP FHTPVADVAV TALSYFETVG
AAVAVGEQPI KMLIHPEVGA RLTVGESLTN LVFAKITNLE DVKCNANWMW PATSPEERYR
MLEACDAMCK IMNKLGIAVD GGNESLFLEA EINEEVVKAP GTLVITSYAL CTDITKTVTP
DLKCTTEDGC LILVRFASLF DSWRLGGCAI AQGYGRTGCD SPDLDNVEQF KSAFRITQSL
ISDRMISAGH DISDGGLIVC LLEMAFSGGR SIVIDLPFTE KPINLLFSEE LGIVIEVSQS
NFDKVLNDFH AANVPVAYIG KSKSLTDEEP MIEIKINGDV VLAGSVQSYR CTWQQTSCRL
EKLQCNPICV EEEVFRLKLK LPKYEMQSLM EIPAVSQHAT VKDASTPCVA ILREEGTTGD
REMAAAFMCA GFRVWDLSMQ DLFDNNISLN NFQGIVFPGG FSYSDVLGAS KAWACSILYH
PKVKYQIEQF LQRRDTFSLG VCNGCQLMAT LGWIGSNEAI GRSVQSVSLE QNISGRFESR
FATVRIERSR SIMLRGMENS VLGIWIAHGE GRFQFRDDLA YAAVEFNHLI ALRYVDWENE
IALAYPYNPN GSPGGIAAIC SANGRHLAMM PHPERSFMTW QWPYWPYEHA PVSPWYHMFR
NAYEWCLEVR S
//
