ID A0A3E2HJF0_SCYLI Unreviewed; 1358 AA.
AC A0A3E2HJF0;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, 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 ORFNames=B7463_g2793 {ECO:0000313|EMBL:RFU33519.1};
OS Scytalidium lignicola (Hyphomycete).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Scytalidium.
OX NCBI_TaxID=5539 {ECO:0000313|EMBL:RFU33519.1, ECO:0000313|Proteomes:UP000258309};
RN [1] {ECO:0000313|EMBL:RFU33519.1, ECO:0000313|Proteomes:UP000258309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105466 {ECO:0000313|EMBL:RFU33519.1,
RC ECO:0000313|Proteomes:UP000258309};
RA Buettner E., Gebauer A.M., Hofrichter M., Liers C., Kellner H.;
RT "Draft genome sequence of Scytalidium lignicola DSM 105466, a ubiquitous
RT saprotrophic fungus.";
RL Submitted (MAY-2018) 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:RFU33519.1}.
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DR EMBL; NCSJ02000034; RFU33519.1; -; Genomic_DNA.
DR STRING; 5539.A0A3E2HJF0; -.
DR OMA; LSANWMW; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000258309; 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 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:UP000258309}.
FT DOMAIN 42..159
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 183..232
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 447..602
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 880..989
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT REGION 313..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1191
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1319
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1321
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFU33519.1"
FT NON_TER 1358
FT /evidence="ECO:0000313|EMBL:RFU33519.1"
SQ SEQUENCE 1358 AA; 148411 MW; B4ABD7A27554CDA3 CRC64;
MEYLVSHGGE AFTPAEANKL TARINKLGSV KVTAVEGVWE YYTHFKTSNA DINKKTEEKV
LELLSDVRDS KGSSVLAQNP LSRVYYITPR NISPWSSKAT SIAHVCGLKA QVDRIERGRA
VVVRFAEVFE SDEITFKDVL YDRMTENIST TEPDVKQMFA EEKPYPLEVI DLSAPGTTPI
DVLKDYNKKR GLALDQLEME YLVQAYTQLG RSPYDIELFM FAQVNSEHCR HKQFNANWTI
DGLSMGASLF DMIRNTHMKS PEYTVSAYSD NAAVLQGEMA SFWAPDYSTG SWRQTKEKVH
FLAKVETHNH PTAISPFSGA ATGSGGEIRD EGSVGRGSIP KAGLCGFWVS DLLIPDQPQP
WEIDIGKPAH YASSLDIMLE APIGSARFNN EFGRPCLTGC FRTLLIQDDL DSEGCEYRGY
HKPIMIAGGV GTVRPQHALK DGRDVQQGAH IIVLGGPAML IGLGGGAASS NTSGESSVEL
DFDSVQRGNP EMQRRAQMVI NACIALDPNP IALIHDVGAG GISNALPELV KDAGYGGRFE
LRQIESADSS MSPLQIWCCE AQERYVLIVN KDSLNRFVSI ANRERCGFSD VGSVVERDRD
GVTRLVLTDR DSVEYPRPID LPMSTLFPKG KKLDRVVQSK KPKLPAFDPM SSLRLHYPQI
PDHDLIRSAV KRVLSMPAVG SKSFLITIGD RTVGGLTVRD QMVGPWQTPV ADVAVTATAL
NIGDKIKTGE AMAMGEKPTL ALISPSASAR MAVAESLLNL GAADLLGGLP RVRLSANWMA
AVNHPGEGAA LYEAVHAIGM ELCPQLGVSI PVGKDSTSMK ASWKDQKTGD TKSVTAPVSV
VISAFAPVAR VRETWTPALR RLEDVGETIL VYVDLAQGHK AMGGSTLAQA FGQLGNEAPD
VRDADLIVDY FDALSQLHDS GIVLAYHDIS DGGIFTTVAE MMFAGRCGAE IVIEGFTKSS
SPNDVIEALF NEELGAIFQV RKSDEINFMR CFATCGPPPG MIRKIGRIPS SSKQKLSIRY
GQQSILHIDR SELQEQWAWT SYQMQRLRDN PSCADSEFNT IRDDHDPGLS YKLTFEPKES
ILPLTSTISS VFTKAPRVAI LREQGVNGHA EMAFAFKAAG FDAVDVHMTD IIGGLSLADF
VGIAACGGFS YGDVLGAGQG WAKSILLHEE NARPEFERFF KRPDTFALGV CNGCQMLTRI
SELIPGTQHW PLFLQNASQQ FEGRVSMVKI QDNAKAPSVF LHGMHDSSLP IVGSHGEGRA
SFKHPSDLEG MNADGLIPIR YVDNRGKLAT QYPFNPNGST EGIAAVRSLD GRVLAMMPHP
ERTIMADVGS YVPKDLVEEW GEFGPWVRMF KSARRWVG
//
