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Database: UniProt
Entry: A0A165D519_EXIGL
LinkDB: A0A165D519_EXIGL
Original site: A0A165D519_EXIGL 
ID   A0A165D519_EXIGL        Unreviewed;       210 AA.
AC   A0A165D519;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=phosphoribosylglycinamide formyltransferase 1 {ECO:0000256|ARBA:ARBA00012254};
DE            EC=2.1.2.2 {ECO:0000256|ARBA:ARBA00012254};
GN   ORFNames=EXIGLDRAFT_683441 {ECO:0000313|EMBL:KZV83800.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV83800.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV83800.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV83800.1,
RC   ECO:0000313|Proteomes:UP000077266};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-
CC       formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-
CC       ribosyl)glycinamide (10-formyl THF route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005054}.
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DR   EMBL; KV426254; KZV83800.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165D519; -.
DR   STRING; 1314781.A0A165D519; -.
DR   InParanoid; A0A165D519; -.
DR   OrthoDB; 5621at2759; -.
DR   Proteomes; UP000077266; Unassembled WGS sequence.
DR   GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:InterPro.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:InterPro.
DR   CDD; cd08645; FMT_core_GART; 1.
DR   Gene3D; 3.40.50.170; Formyl transferase, N-terminal domain; 1.
DR   HAMAP; MF_01930; PurN; 1.
DR   InterPro; IPR002376; Formyl_transf_N.
DR   InterPro; IPR036477; Formyl_transf_N_sf.
DR   InterPro; IPR004607; GART.
DR   NCBIfam; TIGR00639; PurN; 1.
DR   PANTHER; PTHR43369; PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE; 1.
DR   PANTHER; PTHR43369:SF2; PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE; 1.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   SUPFAM; SSF53328; Formyltransferase; 1.
PE   3: Inferred from homology;
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KZV83800.1}.
FT   DOMAIN          5..203
FT                   /note="Formyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00551"
SQ   SEQUENCE   210 AA;  23396 MW;  1E85209D419098EA CRC64;
     MSRRRIAVLI SGSGSNLQAL IDATKSGVIP NAEICVVLSN RKAAYGLERA RNEGIPTEYL
     ALQPFLKKNP EKTRDDYDAE IARMVLKHSP DLVVLAGWMH ILGDGFLEIV YADQESRRPL
     PVINLHPALP GAFDGANALD RAYEAFQKGE ITYTGAMVHR VVKDVDRGEP VVVRQIDFVP
     GEPQDAFETR LHKVEWEIIV EATNKILQQL
//
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