ID X0M1G2_FUSOX Unreviewed; 1141 AA.
AC X0M1G2;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=FOTG_03685 {ECO:0000313|EMBL:EXM32089.1};
OS Fusarium oxysporum f. sp. vasinfectum 25433.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089449 {ECO:0000313|EMBL:EXM32089.1};
RN [1] {ECO:0000313|EMBL:EXM32089.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=25433 {ECO:0000313|EMBL:EXM32089.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum Cotton.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EXM32089.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=25433 {ECO:0000313|EMBL:EXM32089.1};
RG The Broad Institute Genomics Platform;
RA Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Annotation of Fusarium oxysporum Cotton.";
RL Submitted (MAY-2012) 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; JH657922; EXM32089.1; -; Genomic_DNA.
DR AlphaFoldDB; X0M1G2; -.
DR HOGENOM; CLU_001031_0_2_1; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000030701; Unassembled WGS sequence.
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; 3.90.650.10; PurM-like C-terminal domain; 2.
DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 2.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR010073; PurL_large.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR036921; PurM-like_N_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; PF13507; GATase_5; 1.
DR SMART; SM01211; GATase_5; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 2.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605}.
FT DOMAIN 227..382
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 668..799
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 975
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1102
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1104
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1141 AA; 123883 MW; 2A0AB657B5687D3D CRC64;
MFAQVNSEHC RHHVFNASWT IDGVSQENSL FGMIKNTHKS NPEYVISAYS DNAAVLSGDE
GNYWAPDYST GSWKLTREVV QPLIKVETHN HPTAISPFPG AATGSGGEIR DEGAVGRGSS
PKAGLAGFWV SDLLIPGNKR PWELDIGRPS HYASSLDIML EAPIGSARFN NEFGRPALTG
TFRTLLTNEA GSDVPEYRGY HKPIMIAGGI GSVRPQHALK EESHVEEGAH VIVLGGPAML
IGLGGGAASS NTGSDATADL DFDSVQRGNP EMERRAQMVI NTCVALGPES PIAFIHDVGA
GGLSNALPEL VKDAGFGGKF ELRQVESADN SMSPLQIWCN EAQERYVLLV NRDGLNRFTS
ICRRERCGFS VVGTAVTKDE SGVSKLVLTD REPTIQPPVD PINLPMDVLF PPGRRISKDV
QRVEKNLRPF DAVKSLTEHC GSSDIGDLVT KATELVFNLP SVGSKNFLIT IGDRTVGGLS
VRDQLVGPWQ TPVADVAVTL TSFSLDDKKR RGEAMAMGEK PNLALISAAA SARMAVVESL
MNLGAADIKP GPVNGDLKRV KLSANWMAAV GHPGEGAALY DAVQAIGMEL CPQLGVSIPV
GKDSLSMKAS WKDKETSESQ TVTAPVSLVI SAFSLVEDVR STWTPQLRRV EEVGESVLVF
VDLAQGFRAM GGSALAQTLG QIGNESPDVR DVQIIRDFFD ALWQLHQEDI VLAYHDRSDG
GLLTTVAEMM FAGRCGADIS LDSLAESEDK VLDALFNEEL GAVFQIRRGD EIKFKRCFAT
CGPPHGLIKT IGYVRPTSKQ SLLVKYRSKT IVDLERAKIQ QWWTSTSYEM QKLRDNPECA
QSEFEAIQDN RDPGLHYKLK FDPADVSLPA LTSIKSLVYK PRVAILREQG VNGHAEMAFA
FRAAGFDAVD VHMSDILDGF SLDGFRGLAA CGGFSYGDVL GAGNGWAQSI LMHDGARKTF
EAFFKRPDTF SLGVCNGCQM LTRLKELIPG AEHWPTFVEN ASTQFEGRYS MVTIEDKSEN
SVFFSGMSGS SFPIVVSHGE GRAAFSSAND LQSVNDSGLI PFRYVDNYGS VTERYPFNPN
GSPQGIAGVQ SRDGRVVAMM PHPERTIMAD VGSWKPERQL AEWGQYGPWF QLFLNARKWA
A
//
