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Database: UniProt
Entry: E9DVV6_METAQ
LinkDB: E9DVV6_METAQ
Original site: E9DVV6_METAQ 
ID   E9DVV6_METAQ            Unreviewed;      1357 AA.
AC   E9DVV6;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 49.
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=MAC_01754 {ECO:0000313|EMBL:EFY92153.1};
OS   Metarhizium acridum (strain CQMa 102).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499};
RN   [1] {ECO:0000313|EMBL:EFY92153.1, ECO:0000313|Proteomes:UP000002499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY92153.1,
RC   ECO:0000313|Proteomes:UP000002499};
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA   Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA   Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA   Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(2011).
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; GL698477; EFY92153.1; -; Genomic_DNA.
DR   RefSeq; XP_007808094.1; XM_007809903.1.
DR   STRING; 655827.E9DVV6; -.
DR   GeneID; 19246065; -.
DR   KEGG; maw:MAC_01754; -.
DR   eggNOG; KOG1907; Eukaryota.
DR   HOGENOM; CLU_001031_0_2_1; -.
DR   InParanoid; E9DVV6; -.
DR   OMA; LSANWMW; -.
DR   OrthoDB; 2891567at2759; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000002499; 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:UP000002499}.
FT   DOMAIN          38..155
FT                   /note="Phosphoribosylformylglycinamidine synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18076"
FT   DOMAIN          179..228
FT                   /note="Phosphoribosylformylglycinamidine synthase linker"
FT                   /evidence="ECO:0000259|Pfam:PF18072"
FT   DOMAIN          446..598
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   DOMAIN          881..984
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   ACT_SITE        1190
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1318
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1320
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   1357 AA;  147854 MW;  6D190DC1EF0EED68 CRC64;
     MPHDILVGSS CYTATSAQEI KARANKTSQP KIQQIRGQWV YFVDLKSSSK AVLEKVKTLL
     QDVDSEPLLA SESTSNTITV YVTPRYLSPW SSQATNIAHV CGLKEQVNRI EKGRLIVIDF
     EEPYQTGQDA TFRDVLYDRM TEIFSFEKPE LDVMFAAGVP APLVVVDIFA DGKDPLIVLR
     DYNKEKGLSL DESEMAYLVD VFKKLGRSPH DVELFMFAQV NSEHCRHKVF NASWTIDSVK
     KNNSLFEMIR NTHKKTPDYT VSAYSDNAAV LQGESANFWA PDYSTGTWTM TPEVAHILAK
     VETHNHPTAI SPFPGAATGS GGEIRDEAAV GRGSVTKGGL AGYWVSDLLI PDHRAPWEVD
     IGRPSHYASS LDIMLEAPIG SARFNNEFGR PCLTGCFRTL LTPETPTEDA KAEASAWRGY
     HKPIMLAGGV GTVRPSNALK EERFVREGAH VIVLGGPAML IGLGGGAASS NASGESNADL
     DFDSVQRGNP EMERRAQMVI NTCTALGEQN PIAMIHDVGA GGLSNALPEL VKDAGFGGNF
     ELRQVESADR SMSPLQIWCN EAQERYVLLI NPENMNRFTS ICRRERCGFS DVGAVATKDA
     NGDARLILTD RESKEYPRPI DLPMDALFPP KHQQERNVSS KKPNLTPFDA LASLRKAFGA
     DLDNATLLKN AVERVFLMPA VGSKSFLITI GDRTVGGLTA RDQFVGPWQT PVADVAVTAT
     SFSLGGKQRT GEAMAMGEKP TLALINPAAS ARMAVAESLM NIGAADVMGD LRRVKLSANW
     MAAVSHPGEG AALYEAVEAI GMKMCPEISV SIPVGKDSTS MKAVWKEQNE VKSVTAPVSV
     AISAFAVVED ILSTWTPQLR RVEEVGESIL MFVDLAEGRR AMGGSALAQS LGAIGNEAPD
     MKNFNLITDY FDALSQLHKS GVVLAYHDRS DGGLITTIAE MMFAGRCGVD MMMDGISKSG
     SASDMVEALF NEELGAVFQV KASDEINFKR CFATCGPPPG LIRKFGVVKA SPNQSLTIRH
     GATTFANLDR AEMQQWWSKT SHQMQRLRDN PACADSEYAT ISDVSDPGLS YHLTYSPSEN
     ILPLTSSITG FFNKTPRVAV LREQGVNGHA ELAFAFRAAG FEPVDVHMTD VLGGRSLADF
     TGIAAPGGFS YGDVLGAGQG WARSVLMHES TRREFEHFFR RPDTFALGVC NGCQFLTRIQ
     ELIPGTEHWP TFVHNESAQF EGRYSMVTIK EDESKPSVFF HGMNGSSLPV VVSHGEGRAK
     FSSPNSLQEL TNSGMIPMRY VDNRLKVTEK YPYNPNGSPG GVAGVSSKDG RFVAMMPHPE
     RTIVAGVNSY IPPKATEEWG DFGPWVRIFK SVRRWVG
//
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