ID A0A0V0W5T7_9BILA Unreviewed; 1098 AA.
AC A0A0V0W5T7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 08-NOV-2023, entry version 29.
DE RecName: Full=phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000256|ARBA:ARBA00013047};
DE EC=6.3.3.1 {ECO:0000256|ARBA:ARBA00013047};
GN Name=GART {ECO:0000313|EMBL:KRX70990.1};
GN ORFNames=T06_177 {ECO:0000313|EMBL:KRX70990.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX70990.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX70990.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX70990.1};
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 2/2.
CC {ECO:0000256|ARBA:ARBA00004686}.
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:KRX70990.1}.
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DR EMBL; JYDK01000258; KRX70990.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0W5T7; -.
DR STRING; 92179.A0A0V0W5T7; -.
DR UniPathway; UPA00074; UER00129.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:InterPro.
DR GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:InterPro.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR CDD; cd08645; FMT_core_GART; 1.
DR CDD; cd02196; PurM; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.40.50.170; Formyl transferase, N-terminal domain; 1.
DR Gene3D; 3.90.600.10; Phosphoribosylglycinamide synthetase, C-terminal domain; 1.
DR Gene3D; 3.90.650.10; PurM-like C-terminal domain; 1.
DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 1.
DR HAMAP; MF_00741; AIRS; 1.
DR HAMAP; MF_01930; PurN; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR004607; GART.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp.
DR InterPro; IPR020560; PRibGlycinamide_synth_C-dom.
DR InterPro; IPR037123; PRibGlycinamide_synth_C_sf.
DR InterPro; IPR020562; PRibGlycinamide_synth_N.
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; IPR004733; PurM_cligase.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR NCBIfam; TIGR00878; purM; 1.
DR NCBIfam; TIGR00639; PurN; 1.
DR PANTHER; PTHR10520:SF12; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3; 1.
DR PANTHER; PTHR10520; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3-RELATED; 1.
DR Pfam; PF00586; AIRS; 1.
DR Pfam; PF02769; AIRS_C; 1.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR Pfam; PF01071; GARS_A; 2.
DR Pfam; PF02843; GARS_C; 1.
DR Pfam; PF02844; GARS_N; 1.
DR SMART; SM01209; GARS_A; 1.
DR SMART; SM01210; GARS_C; 1.
DR SUPFAM; SSF53328; Formyltransferase; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 1.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673}.
FT DOMAIN 113..360
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 1098 AA; 120559 MW; 648B6CBE1D6C3A74 CRC64;
MLNKPAVVVV IGSGGREHAL IWKLSQSEHV DRIFALPGNY GIASLPKTRC IVEDDSCVEY
FCVKNKVDLV VVGPEASLAD GVVDTLTALG IRCFGPTKAA AQIEVNSSKA YAKLFMRRFD
IPTAEFEIFT DSEKAKSHIK RCEYDAWVVK ASSPTASGSG VYVGTSDDEA CSAVDDLINV
SQWELSVRLL VWLLISERSA LSRWKGDCSR KFPCRQRIVR KSTKLAVHYM QLFVNNIFQF
LALCFTDGYC VKVMPLVQNY KRLLDNNCGP NTDGMGACCP YLDITVQHIR FIEECILQKV
VNILREEGKL FKGVLHADVM ITEFGIRVLE FNSTFGDLEA QVLLPLLETD LLEILLSCTD
QTLSQCSIRW KPGQFSCGIL LAASGYPVLS NVQTGYPIEG ISNGNSNFQK FETKKLFCDY
PGLEQRCSDV LVFHSGTKAD SSGLPVTSDG RVLCMVGVGN TFRFARKKAY DAVQCINFKG
VQYRSDIGNG FLPPNFGLLS DPESETSFVD SECDMEFSFA DDLVKSLVHV CQPIVRPGSG
VLDYSQQGEY GAAFDLRLSG YRDPILISGT DGVGTKLMIA AKAKQYDTIG VDLVAVCVND
ILTRNAEPLF FLDCIAQTDL REEVLLALLQ GIAKGCLEAG CSLIGGKTAC MPGLYARGEF
ELAGFAVGAV ERSQIALPAK QRMENGDVII GIASNGFHSN GYSLIKSVLE SQNIELNDPC
PWNPQQTVAI NLLLPTKIYV NTLLELLRSG RVKGAAHITG GGLVDNIPRI LPSDLIAKID
MSTWPIPDEF LWLASAGSIS ASEMVNVFNC GIGMVLIVGR KDVPYVEAHL QSRSERFFKI
GIVEKPKIDS TEKSESEQVD HNKVELENLE VAFQQENKVV PTLSNANHVN RKRVAILISG
SGSNMLSLIH SSKKAASVYE IVLVISNVET ASGLLKAEEE DIETSIVSHE DKSREDFEEQ
IQNLLTSKQV EFVCLAGFNR TLSEPLVNNW LGKMIDIHPS LLPMFRGPRP HKCALQAGVR
ISGCTVHFVE AGNDPGGIIL QDSVAVHPDD SEQSLRDRVK AVENVLYPKA LDHVVRGDVV
RQNDGKAHWT KLPITDHK
//
