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Database: UniProt
Entry: M2UF10_COCH5
LinkDB: M2UF10_COCH5
Original site: M2UF10_COCH5 
ID   M2UF10_COCH5            Unreviewed;      1721 AA.
AC   M2UF10;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 40.
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=COCHEDRAFT_1193785 {ECO:0000313|EMBL:EMD92276.1};
OS   Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) (Southern
OS   corn leaf blight fungus) (Bipolaris maydis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=701091 {ECO:0000313|EMBL:EMD92276.1, ECO:0000313|Proteomes:UP000016936};
RN   [1] {ECO:0000313|EMBL:EMD92276.1, ECO:0000313|Proteomes:UP000016936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
RN   [2] {ECO:0000313|Proteomes:UP000016936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
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; KB445575; EMD92276.1; -; Genomic_DNA.
DR   STRING; 701091.M2UF10; -.
DR   eggNOG; KOG1907; Eukaryota.
DR   eggNOG; KOG3007; Eukaryota.
DR   HOGENOM; CLU_001031_0_1_1; -.
DR   OMA; LSANWMW; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000016936; 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.30.1780.10; ornithine cyclodeaminase, domain 1; 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; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR003462; ODC_Mu_crystall.
DR   InterPro; IPR023401; ODC_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   Pfam; PF02423; OCD_Mu_crystall; 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; SSF51735; NAD(P)-binding Rossmann-fold domains; 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:UP000016936}.
FT   DOMAIN          393..525
FT                   /note="Phosphoribosylformylglycinamidine synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18076"
FT   DOMAIN          548..598
FT                   /note="Phosphoribosylformylglycinamidine synthase linker"
FT                   /evidence="ECO:0000259|Pfam:PF18072"
FT   DOMAIN          814..971
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   DOMAIN          1237..1365
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   ACT_SITE        1548
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1683
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1685
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   1721 AA;  187449 MW;  B013E05E5EE94E96 CRC64;
     MAFTVLSDND IRSLLCSLSP ADAEKLTSRL NQALSQYSCN DEAPYQPHRA QVTRPDGQVS
     LFMPATTPSS IGVKIVGVAP SQAPPPGEKP RPALKSVLTI CDELGQAVGV LNAAELTAFR
     TALGTMLLYR YRKFTQNIVV FGAGKQAEWH IRLAVLLKSN DISKITIVNR SRARADQLVE
     TLTRAGLSSH VQIKVFEGGE DSLESLVKES QVMFCTTPST TPLFPASYLA SEADKPRFIS
     AIGSYRLDMQ EIDPHLLSQI TTPRSLFASQ VHDACIAVDS IKGCMDEAGE LVKAGIATER
     MIEVGKMDGL RQDNGAKRWL EQGFVVYKSV GVGVMDIAIG KALLELSGEK GVAHTMASTE
     DPYLILPGSA AHSDFRLQRL AQAIGAKQVR SLWLHFVNPL KELADDELKT LQQILHYGEY
     PDSNDRLAQT LLDAVHRGGE PRDGETVLFY VSPRAGTISP WSSLASMIAR TCTLDQAVKR
     IERGMVIAAT FDRTLDADEI PNRDHLYDRM TQTISRTAPN LEAIFGEGEP AQATTISFDE
     YNSAHAALDH ANRELGLAMD KSEIDYLVEA YTQELKRGPV DVELFMFAQV NSEHCRHKQF
     NADFTVDGMR KSMSLFGMIR NTHQKNPQHV VSAYSDNAAV LQGEEASFWA PNDLTGEWNG
     AKETVHILCK VETHNHPTAV SPFPGAATGS GGEIRDEGAV GRGSKPKAGL AGFTVSDLNL
     EGFERPWELK DVGKPAHIAS SRDIMLEAPI GSAQFNNEFG RPCTVGYFRT MLMRVFTNEK
     ESEIRGYHKP IMLAGGVGTV RPQHALKDPD VVPAGSHLLV IGGPAMLIGL GGGAASSIQS
     GEGKVDLDFA SVQRGNPEVQ RRAQEVIDTC RSMGDKNPIL FIHDVGAGGL SNALPELVHD
     SGLGAIFELR EVDSADKSMS PLQIWCCEAQ ERYVLAVAPD QLDLFKRICN RERCGYSVVG
     TATKEQRLVL KDRDSKENPT PIDLPMATLF GKPPKMSRIV ESRKLRLPAF DSSLSMYIPD
     TPKDGLISEA VDRVLTLPAV GSKSFLITIG DRTVGGLTVR DQMVGKWQTP VADVSVTATS
     LLAGVKTGEA MTMGEKPTLA LISPVASARM AVAESLMNIA AASLFDRLSR VRLSANWMSA
     SSHPGEGAAL YEAVEAIGMD LCPKLGISIP VGKDSMSMKM KWSEGGEAKE VTAPMSLVIT
     AFAPVDRIDR TWTPALERVE SVGETILMYV DLAAGRKHLG GSALAQTFGQ VGDEAPDVYD
     ADVIKDYFDA IDQLHESGIV LAYHDRSDGG LFTTLVEMAF AGRCGLEIML DRVAASSEPK
     DVLEALFNEE LGAVFQVRKK DETAFNRCFA TCGPPPGMIK KIGRVPEASK QDISFYVGTK
     NVYRNSRQKL QQRWAETSYR MQKLRDNPVC ADAEFNSILD DKDPGLSYNL TFKPSENIMP
     LMSNLKSPFT AKPRVAILRE EGVNGQAEMA FAFHQAGFSA IDVHMTDIIS GRVSLAGFVG
     LAACGGFSYG DVLGAGQGWA KSVLLHPETR KEFQDFFTRP NTFALGVCNG CQFMSKLKEL
     IPGAELWPSF ERNASEQYEA RVCMVEVLDP KGTNTPPSVF LHGMAGSKLP IVTAHGEGRA
     QFSSSASSAS TPQTLYNENL VSLRYVDNYG KQTETYPYNP NGSPMGITGV RSADGRVLAL
     MPHPERTILK EVASYLPKNT EEWGELGPWS RMFKSARRWV G
//
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