ID A0A0F7S1S0_9BASI Unreviewed; 1403 AA.
AC A0A0F7S1S0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
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 Name=SSCI17670.1 {ECO:0000313|EMBL:CDW96822.1};
GN ORFNames=SPSC_05859 {ECO:0000313|EMBL:CDU25688.1};
OS Sporisorium scitamineum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=49012 {ECO:0000313|EMBL:CDW96822.1, ECO:0000313|Proteomes:UP000242770};
RN [1] {ECO:0000313|EMBL:CDW96822.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Berkman J.Paul.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDU25688.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SscI8 {ECO:0000313|EMBL:CDU25688.1};
RA Ju J., Zhang J.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000242770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Berkman P.J.;
RL Submitted (JUN-2014) 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}.
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DR EMBL; LK056691; CDU25688.1; -; Genomic_DNA.
DR EMBL; CCFA01000918; CDW96822.1; -; Genomic_DNA.
DR STRING; 49012.A0A0F7S1S0; -.
DR OrthoDB; 2891567at2759; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000242770; 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}.
FT DOMAIN 39..179
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 208..265
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 481..650
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 915..1054
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1233
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1357
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1359
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1403 AA; 150159 MW; B234FF23DC49213A CRC64;
MLSLIGSSLL HPSKRTQLLE RANAKLGGGA NLASIDAVYI HFVNAASEQA NAVLADTASP
QRNVLDSLLV YGDNVDLPHT RPAIQSILAG QAGPPQQTVL FVLPRPGSIS PWSSKATDIA
RTCTLKDHVD RIERGVAFVL EPVPNSTLEA ADLAKVHDLL HDRMTQFISA VPPTADALFH
KAQPAPLTHV DLLGADGTSD RQVAKQRLVD ANEKLGLALA NDEIDYLVDA FIAGKGDGSD
ALRRNPTDVE LFMFAQVNSE HCRHKIFNAD WTIDGKTMPN TLFGMIRNTH KLHPQHTISA
YSDNAAVIEG YEATRFAPSP AAGSTVYQGV KEPMPFLAKV ETHNHPTAVS PYPGAATGSG
GEIRDEGAVG RGSKPKAGLV GFMTSNLLLE GDGRQPWEED FGKPSHISSA YDIMIGGPLG
SSAFNNEFGR PGLSGFWRTW SERVPIDDAS SEVRGYHKPI MLAGGLGNVR PKNALKSKIT
PDAAIIVLGG PGMLIGLGGG AASSMASGSS SRAALDFASV QRDNPEMQRR CQQVIDACTA
LSDAPGVIEG RVGEGNPIQS IHDVGAGGIS NALPELVHDA GLGARFEIRD VLVDDPSMSP
MEIWCNESQE RYVLAVGQED LPRFEAIAKR ERCPYSVVGR ATVEQELVVT DRLLGGTPIH
LPMPILFGKP PKIARQAQSK QLLRVPFDST LTSYLPHIKD DPVKMFAEAV DRILHLPTVA
SKNFLITIGD RSITGLVVRD QMVGPYQVPV ADVAVTRTSY GFDESLTGEA VASGERTPLA
LISAAASARM AVAESLTNIA AASIESLERI KLSANWMCAA SHSDEGARLY EAVQAIGLDL
CPKLGLAIPV GKDSMSMKMA WESAEGDKRE VTAPLSLTVT AFGPVDDITR TWTPQLRTDV
DDTVLLFVDL AGGKQRLGGS CLAQVFRQLG HEAPDVEDAS VLKAFFEACY TLKQLRVQKR
DEGSLVLAYH DRSDGGLITA ILEMCFAGHC GAELFVDALD AELRDPVAAL FNEELGAVMQ
VQAGDVKAVS AVLTAAGVPS HNLHVVGRVT PDSQEIKVVA RSQPLLSSTR ATLQKAWAEM
SFRMQSLRDN PETAAAEYSL ITDEPTSAAA LRYELTYSPR EDVLGASVVQ AALETRPKVV
ILREQGVNGQ IEMAWAFTRA GFCAVDVHMS DLVEGRVTLD QFVGLAACGG FSFGDVLGAG
SGWAKSILLN PNVKAQFVDF FQKRTDTFAL GVCNGCQLLS QLGVAGLIPE AENWPLFKPN
ESGRFEGRLS NVEITKTGGA SSIFLADMAG SVLPAIIAHG EGRASFHNEG DLEACKAKNQ
VAMQYVDQRY PINPNGSPEG ITAITANGGR VLALMPHPER GVALSSMSWA PAEAYGSGAK
GWQGKGPWFR MFENARKWVD SRK
//
