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Database: UniProt
Entry: A0A094IAT1_9PEZI
LinkDB: A0A094IAT1_9PEZI
Original site: A0A094IAT1_9PEZI 
ID   A0A094IAT1_9PEZI        Unreviewed;      1360 AA.
AC   A0A094IAT1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=V500_03624 {ECO:0000313|EMBL:KFY93662.1};
OS   Pseudogymnoascus sp. VKM F-4518 (FW-2643).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420913 {ECO:0000313|EMBL:KFY93662.1, ECO:0000313|Proteomes:UP000029284};
RN   [1] {ECO:0000313|EMBL:KFY93662.1, ECO:0000313|Proteomes:UP000029284}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4518 (FW-2643) {ECO:0000313|Proteomes:UP000029284};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFY93662.1}.
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DR   EMBL; JPKC01001129; KFY93662.1; -; Genomic_DNA.
DR   STRING; 1420913.A0A094IAT1; -.
DR   HOGENOM; CLU_001031_0_2_1; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000029284; 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; 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:UP000029284}.
FT   DOMAIN          39..159
FT                   /note="Phosphoribosylformylglycinamidine synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18076"
FT   DOMAIN          183..232
FT                   /note="Phosphoribosylformylglycinamidine synthase linker"
FT                   /evidence="ECO:0000259|Pfam:PF18072"
FT   DOMAIN          445..597
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   DOMAIN          882..995
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   ACT_SITE        1193
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1321
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1323
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   1360 AA;  147901 MW;  C5E8E50F75F9A9A5 CRC64;
     MEYLTLLGED AYTSSSARKI QDLIAKTSSA KVDEVSAVYI HYARLKQGTN DVAKETDAKL
     RQLLPNPRPD FFREVSGGSS GNFRVYYVTP RNISPWSSKA TSIAAVCGVK GLERIERGRA
     ILVKFAEPFE GSDDSFKHVL FDRMTENISS SEPDVKGMFA EGQRIPLEVV DIFAEGAKPI
     EILKGYNKER GLALDEPEME YLIQAYSKIG RSPYDVELFM FAQVNSEHCR HKQFNANWTI
     DDVAMGKSLF EMIKNTHKNN PKYTVSAYSD NAAVLEGNFA SFWAPDYNTG SWKATKEMVH
     YIIKVETHNH PTAISPFAGA ATGSGGEIRD EGAVGRGSQP KAGLCGFWVS DLLIPDFEQP
     WEIDFGKPAH YASSLDIMLE APIGSARFNN EFGRPCLTGC FRTLLTDTGS NEAEDYRGYH
     KPIMIAGGVG TVRPQFAIKR QGDVKPGAHV IVLGGPAMLI GLGGGAASSN ASGEGSAELD
     FDSVQRGNPE MERRAQMVIN ACCALHDANP IAMIHDVGAG GLSNALPELV KDAGYGGRFE
     LRQIESADSS MSPLQIWCCE AQERYVLCVN EEGLNKFVNI CNRERCGFSD VGTVTGTIGD
     SESTLVVTDR EGTEYPKPID LPMTTLFPRD RKLERNVKTK KNNMKAFDSF QSLCSLKTTK
     SCRGSAEFLH RAMEIVLKVP AVGSKAFLIT IGDRTVGGMT TRDQMVGPWQ TPVADVAVTV
     TSLATGGMLT GEAMAVGEKP ALALISPAAS SRMAVAESLL NLAAADIQGG LDRVRLSANW
     MAAVNHEGEG SALYEAVQAI GMEMCPKLGI SIPVGKDSTS MKASWKDSSN GESKSVTAPV
     TVVISAFAPV QRVSHTWTPA LRRLEDVGET VLMFVDLAQG KQAMGGSAFA QACGQLGNES
     PDVHDIDLIA DYFDAITQLH ESGIVLAYHD RSDGGLFTTI VEMMFAGRCG AEIMLDGVAK
     SDETGDVLDA IFNEELGAVF QVKKSDEINF IRCFATCGPP PGLVKKIGRI PAATKQELSI
     RYKTETVTHL DRSTMQEWWS STSYQMQRLR DNPASADSEF SLIKDNKDPG LSFNLTFDPK
     ESILPMTTLL SSPFIKAPRV AILREQGVNG YAEMAFAFKA AGFDAIDVHM TDIIAGRSLA
     DFVGIAACGG FSYGDVLGAG QGWAKSILMH EENARPEFKK FFERKDTFAL GVCNGCQMLS
     RLAELIPGAE NWPIFVDNES QQFEGRVSMV QIKDNSDSPS VFFHGMDGSS LPIVISHGEG
     RAQFKNDTDL QALTQAGLVP VRYTDNYGKV TEKYPYNPNG SAQGIAGVTS KDGRVLALMP
     HPERSIMASV GSYIPDGMTE EWGEYGPWVR MFKSARRWVG
//
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