ID A0A2V3J1J9_9FLOR Unreviewed; 1378 AA.
AC A0A2V3J1J9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=BWQ96_02883 {ECO:0000313|EMBL:PXF47270.1};
OS Gracilariopsis chorda.
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gracilariales;
OC Gracilariaceae; Gracilariopsis.
OX NCBI_TaxID=448386 {ECO:0000313|EMBL:PXF47270.1, ECO:0000313|Proteomes:UP000247409};
RN [1] {ECO:0000313|EMBL:PXF47270.1, ECO:0000313|Proteomes:UP000247409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKKU-2015 {ECO:0000313|EMBL:PXF47270.1,
RC ECO:0000313|Proteomes:UP000247409};
RC TISSUE=Whole body {ECO:0000313|EMBL:PXF47270.1};
RX PubMed=29688518; DOI=10.1093/molbev/msy081;
RA Lee J., Yang E.C., Graf L., Yang J.H., Qiu H., Zel Zion U., Chan C.X.,
RA Stephens T.G., Weber A.P.M., Boo G.H., Boo S.M., Kim K.M., Shin Y.,
RA Jung M., Lee S.J., Yim H.S., Lee J.H., Bhattacharya D., Yoon H.S.;
RT "Analysis of the draft genome of the red seaweed Gracilariopsis chorda
RT provides insights into genome size evolution in Rhodophyta.";
RL Mol. Biol. Evol. 0:0-0(2018).
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:PXF47270.1}.
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DR EMBL; NBIV01000026; PXF47270.1; -; Genomic_DNA.
DR STRING; 448386.A0A2V3J1J9; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000247409; 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; cd02203; PurL_repeat1; 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 HAMAP; MF_00419; PurL_1; 1.
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:UP000247409}.
FT DOMAIN 107..219
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 246..294
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 507..661
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 912..1039
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1207
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1338
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1340
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1378 AA; 151527 MW; 521F7EAAE3FE0537 CRC64;
MTNPAFTTPA TLPNTKPSTS STLSINTGFV PELHPRVPLS HPRCRPPRSC PTAPIASNPL
PTSVSATVIP SSTVLHFYRY HEQVPPATLR IATQIFQDQP LIINQETVFN IRLTKSLDPH
QLQILRWLLS ETFAPQLLKS SSSLNEPAIH VGPRLNFQTA WSSNAVSICH ACGIQAIDRL
ERSRRYTLQY PDGSFPAQHL VEQFQAAVFD RMTETVYPKV LASFDTPIQP QKAFTIDILG
HGENALRDFN NTDGLAFDED DIAYYSKLFR QLHRNPTNVE LYDLAQSNSE HSRHWFFKGQ
LIVDGQQIDD HLLNIVREPL RVNPSNSVIA FADNSSTMRS GPVPLLMPRT PGLSSPLIAK
EIDTDILFTA ETHNFPSGVA PFPGAETGTG GRIRDTAATG VGSLVGVATA GYSVGNLHIP
DFPLPWEDPT FEYPNNLASP LDILIQASNG ASDYGNKFGE PVINGFARTY GIKLQNGQRR
EYVKPIMFSG GMGQMHHQHA RKGQPETGLL VVKVGGPAYR IGMGGGAASS MMQGDNKADL
DFNAVQRGDA EMAQRVYRVL RACVEMGGDN PIVSIHDQGA GGNCNVVKEL IYPSGAKIHI
RNVLVGDNTL SALEIWVAEY QEQFGLLLRP THEPMFRKMC ARENVEPAVL GSIDGSGRIV
LWDDQEKQAV VDMDLEAVLG DLPQKSFTDY RVAFHGVPLY IPTDTSVAEM LRRVLSLMSV
GSKRFLTTKV DRSVTGLIAQ QQCVGPLQLP LSDYAVSTQS YFALRGSATA IGERPTITAL
SPQAMARMSV GEMMTNLCGA KVTSRDHIKC EGNWMWAAKL PGDCASLYDA AASTRDVMIE
LGIAIDGGKD SLSMAARCPT KDGSMETVRA PGTLVISGYC TMENVQEKLT PDLKAPGESS
LLLIDIAKGK RRTGGSALAQ VFSQVGERPP DLDEPSLLAK AFDTVQQLIG HNGVLSCHDV
SDGGLITTLL EMGFAGNCGI DVSMNSKDME YDIVQALFAE ELGIVIEVSS QSEQDVCEVL
RRDGLPYQRV GQTRRDHEVR ILNGSNELLV DDIRDLRDIW ESTSFALDRQ QANTQCVDVE
QKNLRSKQGP QYRVTFKARE TPRMVIEQLA KPKVAIIREE GSNGDREMSA AFHMSGFETW
DVSVRDIASK SISLSDFKGI AFVGGFSYAD VLDSAKGWAG VIRFSDLVRS EFDRFYARTD
TFSLGVCNGC QLMALLGRIP FSSDVLDEKS QPRFIHNESG RYESRFSTVK ISEDSPAIML
RGMGSSQLGV WVAHGEGRAY FADEEILKKV EQMNLAPLRY VGEDGEVTMM YPDNPNGSMN
GIAGICSKDG RHLAMMPHPE RTVLKWQWGY LPREIEALDA SPWLKMFQNA YEWVVNGD
//
