ID N4UDZ4_FUSC1 Unreviewed; 1340 AA.
AC N4UDZ4;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, 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 ORFNames=FOC1_g10011334 {ECO:0000313|EMBL:ENH74008.1};
OS Fusarium oxysporum f. sp. cubense (strain race 1) (Panama disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1229664 {ECO:0000313|EMBL:ENH74008.1, ECO:0000313|Proteomes:UP000016928};
RN [1] {ECO:0000313|Proteomes:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RA Fang X., Huang J.;
RT "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RX PubMed=24743270;
RA Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA Fang X., Peng M., Huang J.;
RT "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL PLoS ONE 9:E95543-E95543(2014).
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; KB730051; ENH74008.1; -; Genomic_DNA.
DR STRING; 1229664.N4UDZ4; -.
DR VEuPathDB; FungiDB:FOC1_g10011334; -.
DR HOGENOM; CLU_001031_0_2_1; -.
DR OMA; LSANWMW; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000016928; 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; 3.
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:UP000016928}.
FT DOMAIN 38..154
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 178..226
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 513..581
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 867..998
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1174
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1301
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1303
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1340 AA; 146301 MW; C4EBB0CA065FD61C CRC64;
MHHVLIGESC YTASEVQKLV QRINDQSPVK VAKLTGSWQY YLDLETEDAA VLGSIKKILE
AIEQPTDAPS TGDNKNAIDI YVSPRNVSPW SSKATSIALV CDLKTVNRIE RGRVIHIELE
DGFKGEEDLS FRDILHDRMT EFFSLSPPAL DTMFAHGARN PLVVVDIFSD ERGPLAALQD
HNKQAGLGLD QPNMEYLVKQ YTALGRSPND VELFMFAQVN SEHCRHHVFN ASWTIDGVSQ
ENSLFGMIKN THKSNPEYVI SAYSDNAAVL SGDEGNYWAP DYSTGSWKLT REVVQPLIKV
ETHNHPTAIS PFPGAATGSG GEIRDEGAVG RGSSPKAGLA GFWVSDLLIP GNKRPWELDI
GRPSHYASSL DIMLEAPIGS ARFNNEFGRP ALTGTFRTLL TNEAGSDAPE YRGYHKPIMI
AGGIGSVRPQ HALKEESHVE EGAHVIVLGG PAMLIGLGGG AASSNTGSDA TADLDFDSVQ
RGNPEMERRA QMVINTCVAL GPESPIAFIH VDAGFGGKFE LRQVESADNS MSPLQIWCNE
AQERYVLLVN RDGLNRFTSI CRRERCGFSV VGTAVTKDES GVSKLVLTDR EPTIQPPVDP
INLPMDVLFP PGRRISKDVQ RVEKNLRPFD AVESLTEHCC SSDIGDLVTK ATELVFNLPS
VGSKNFLITI GDRTVGGLSV RDQLVGPWQT PVADVAVTLT SFSLDDKKRR GEAMAMGEKP
NLALISAAAS ARMAVVESLM NLGAADIKPG PVNGDLKRVK LSANWMAAVG HPGEGAALYD
AVQAIGMELC PQLGVSIPVG KDSLSMKASW KDKETSESQT VTAPVSLVIS AFSLVEDVRS
TWTPQLRRVE EVGESVLVFV DLAQGFRAMG GSALAQTLGQ IGNESPDVRD VQIIRDFFDA
LWQLHQEDIV LAYHDRSDGG LLTTVAEMMF AGRCGADISL DSLAESEDKV LDALFNEELG
AVFQIRRGDE IKFKRCFATC GPPHGLIKTI GYVRPTSKQS LLVKYRSKTI VDLERAKIQQ
WWTSTSYEMQ KLRDNPECAQ SEFEAIQDNR DPGLHYKLKF DPADVSLPAL TSIKSLVYKP
RVAILREQGV NGHAEMAFAF RAAGFDAVDV HMSDILDGFS LDGFRGLAAC GGFSYGDVLG
AGNGWAQSIL MHDGARKTFE AFFKRPDTFS LGVCNGCQML TRLKELIPGA EHWPTFVENA
STQFEGRYSM VTIEDKSENS VFFSGMSGSS FPIVVSHGEG RAAFSSANDL QSVNDSGLIP
FRYVDNYGSV TERYPFNPNG SPQGIAGVQS RDGRVVAMMP HPERTIMADV GSWKPERQLA
EWGQYGPWFQ LFLNARKWAA
//