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Database: UniProt
Entry: N4UDZ4_FUSC1
LinkDB: N4UDZ4_FUSC1
Original site: N4UDZ4_FUSC1 
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
//
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