ID A0A316W8H4_9BASI Unreviewed; 1413 AA.
AC A0A316W8H4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=IE81DRAFT_319693 {ECO:0000313|EMBL:PWN45854.1};
OS Ceraceosorus guamensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX NCBI_TaxID=1522189 {ECO:0000313|EMBL:PWN45854.1, ECO:0000313|Proteomes:UP000245783};
RN [1] {ECO:0000313|EMBL:PWN45854.1, ECO:0000313|Proteomes:UP000245783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4658 {ECO:0000313|EMBL:PWN45854.1,
RC ECO:0000313|Proteomes:UP000245783};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
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}.
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DR EMBL; KZ819353; PWN45854.1; -; Genomic_DNA.
DR STRING; 1522189.A0A316W8H4; -.
DR InParanoid; A0A316W8H4; -.
DR OrthoDB; 2891567at2759; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000245783; 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-KW.
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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
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:UP000245783}.
FT DOMAIN 64..186
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 211..270
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 497..655
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 919..1058
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
SQ SEQUENCE 1413 AA; 150155 MW; 396A5D965B3CD6EA CRC64;
MVHNSSAAES KAMLALAGSS PMPVAKREQT LKAVQAHIPH LVSLDSLYLH FVSPTSSSAL
QLLSTASSSE RLLLDNLLGY GDHHALPHTR SAIQAALAAQ SSGASTTTVL FVTPRPGNIS
PWSSKATDIA RLCTLGDHVE RIERGQAYVL TGMELNEAQI ASFADLLHDR MTQSISTAPP
NATALFGKDD PAPLRTVSLG EKDFDAAVAK LSSANEQLGL ALAPDEINYL VKAFVSGGQD
VGAAEALGRD PTDVELFMFA QVNSEHCRHK IFNADWTIDG QRMPNTLFGM IRNTHKLHPE
HTISAYSDNA AVLEGSDANH FAARASDAPL TRYEAHYEAM PILIKVETHN HPTAISPYPG
AATGSGGEIR DEGAVGQGSK PKAGLVGFMT SNLLLPEPCA PESGSKARQP WEQDVGKPSH
IASALDIMLD APLGSANFNN EFGRPGLGGF WRTWCQRVPT EGPEGSTEIR GYHKPIMLAG
GMGNVRPSHA IKQTITPGSA IIVLGGPGML IGLGGGAASS MASSASRAAL DFASVQRENP
EMQRRCQSVI DACTASLDAP NPIISIHDVG AGGLSNALPE LVHDSGCGGR FEIRKVLIDD
PGMSPMEIWC NESQERYVLA VSQSELSRFE SVAKRERCPY SVVGVATEEL RLVVTDSLLN
STPIDLPMAT LFGKPPKIAR QSKHSSPPRY PFDTTLKTYL GSATDISAAV TEAFDRVLRL
PTVGSKSFLI TIGDRSITGL VARDQMVGPW QVPVADVAVT RTAYGFDDAL AGEAMASGER
TPLALLDAAA SARMAVGEAL TNLAAASVPD LKRVKLSANW MCAASHGDEG ARLYDAVQAV
GLDLCPKLGL SIPVGKDSMS MKMGWQEQGA QREVTAPLSL VITAFAPVDR IDRTWTPQLR
ADVDEETVLL FVDLASGKAR MGGSALAQTF EQLGKEAPDV ESADVLKGFF EACATLKALE
VQGRTDHSLI MAYHDRSDGG LAATILEMAF AGHVGVNVNL DTIPGGAKDP VAALFNEELG
AVMQVRARDV KAVSAVLSSA GVPAEALHII GQIVPSTDEQ QIHFAADSRP VFSGARHDLQ
RAWSETSWRM QSLRDNPETA SSEWALIGPQ SHGPNTISFQ LAYQPGAEFA LGTLPIPEAP
LDSRPKVAIL REQGVNGQLE MAYAFTAAGF CAIDVHMSDL ITGRVTLGDF VGLAACGGFS
FGDVLGAGSG WAKSCLLNPK ARTELSAFFT RKNTFALGVC NGCQLFSQLG QAGLIPGAEQ
WPTFKVNESA RFEGRLCMVE VDDGPVTSKS VFLRDMVGSR LPAVIAHGEG RASFRDRADQ
DAVESSGLVG LRYVEHDAPK GQGTTRYPIN PNGSPHGITA VSTPDGRILA LMPHPERGIS
AESMSWKPAG ASKAWRGRGP WLQMFQSART WVG
//
