ID   PUR2_DROME              Reviewed;        1353 AA.
AC   P00967; Q9VM53;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 2.
DT   24-JAN-2024, entry version 203.
DE   RecName: Full=Trifunctional purine biosynthetic protein adenosine-3;
DE   Includes:
DE     RecName: Full=Phosphoribosylamine--glycine ligase;
DE              EC=6.3.4.13 {ECO:0000269|PubMed:3086869};
DE     AltName: Full=Glycinamide ribonucleotide synthetase;
DE              Short=GARS;
DE     AltName: Full=Phosphoribosylglycinamide synthetase;
DE   Includes:
DE     RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase;
DE              EC=6.3.3.1 {ECO:0000269|PubMed:3086869};
DE     AltName: Full=AIR synthase;
DE              Short=AIRS;
DE     AltName: Full=Phosphoribosyl-aminoimidazole synthetase;
DE   Includes:
DE     RecName: Full=Phosphoribosylglycinamide formyltransferase;
DE              EC=2.1.2.2 {ECO:0000269|PubMed:3086869};
DE     AltName: Full=5'-phosphoribosylglycinamide transformylase;
DE     AltName: Full=GAR transformylase;
DE              Short=GART;
GN   Name=Gart {ECO:0000312|FlyBase:FBgn0000053};
GN   Synonyms=ade3 {ECO:0000312|FlyBase:FBgn0000053};
GN   ORFNames=CG31628 {ECO:0000312|FlyBase:FBgn0000053};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS LONG AND SHORT).
RC   STRAIN=Canton-S; TISSUE=Embryo;
RX   PubMed=3123310; DOI=10.1093/genetics/117.4.711;
RA   Henikoff S., Eghtedarzadeh M.K.;
RT   "Conserved arrangement of nested genes at the Drosophila Gart locus.";
RL   Genetics 117:711-725(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 60-1353, AND ALTERNATIVE SPLICING.
RC   STRAIN=Canton-S, and Oregon-R; TISSUE=Embryo;
RX   PubMed=6413075; DOI=10.1016/0092-8674(83)90374-4;
RA   Henikoff S., Sloan J.S., Kelly J.D.;
RT   "A Drosophila metabolic gene transcript is alternatively processed.";
RL   Cell 34:405-414(1983).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1147-1353 (ISOFORM LONG).
RC   STRAIN=Oregon-R; TISSUE=Embryo;
RX   PubMed=6300768; DOI=10.1093/nar/11.3.789;
RA   Henikoff S., Furlong C.E.;
RT   "Sequence of a Drosophila DNA segment that functions in Saccharomyces
RT   cerevisiae and its regulation by a yeast promoter.";
RL   Nucleic Acids Res. 11:789-800(1983).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND MUTAGENESIS OF GLY-1164.
RX   PubMed=3086869; DOI=10.1073/pnas.83.11.3919;
RA   Henikoff S., Nash D., Hards R., Bleskan J., Woolford J.F., Naguib F.,
RA   Patterson D.;
RT   "Two Drosophila melanogaster mutations block successive steps of de novo
RT   purine synthesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:3919-3923(1986).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-814 AND SER-816, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
CC   -!- FUNCTION: Trifunctional enzyme that catalyzes three distinct reactions
CC       as part of the 'de novo' inosine monophosphate biosynthetic pathway.
CC       {ECO:0000269|PubMed:3086869}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) +
CC         N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate;
CC         Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58681,
CC         ChEBI:CHEBI:143788, ChEBI:CHEBI:456216; EC=6.3.4.13;
CC         Evidence={ECO:0000269|PubMed:3086869};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17454;
CC         Evidence={ECO:0000305|PubMed:3086869};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP
CC         = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) +
CC         phosphate; Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:137981,
CC         ChEBI:CHEBI:147287, ChEBI:CHEBI:456216; EC=6.3.3.1;
CC         Evidence={ECO:0000269|PubMed:3086869};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23033;
CC         Evidence={ECO:0000305|PubMed:3086869};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-10-formyltetrahydrofolate + N(1)-(5-phospho-beta-D-
CC         ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N(2)-
CC         formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide;
CC         Xref=Rhea:RHEA:15053, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453,
CC         ChEBI:CHEBI:143788, ChEBI:CHEBI:147286, ChEBI:CHEBI:195366;
CC         EC=2.1.2.2; Evidence={ECO:0000269|PubMed:3086869};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15054;
CC         Evidence={ECO:0000305|PubMed:3086869};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P15640, ECO:0000255|PROSITE-
CC         ProRule:PRU00409};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00409};
CC       Note=Binds 1 magnesium or manganese ion per subunit.
CC       {ECO:0000255|PROSITE-ProRule:PRU00409};
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 2/2. {ECO:0000269|PubMed:3086869}.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-
CC       (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-
CC       diphosphate: step 2/2. {ECO:0000269|PubMed:3086869}.
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:0000269|PubMed:3086869}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P22102}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long; Synonyms=A, 4.7 kb;
CC         IsoId=P00967-1; Sequence=Displayed;
CC       Name=Short; Synonyms=1.7 kb;
CC         IsoId=P00967-2; Sequence=VSP_005512, VSP_005513;
CC   -!- DOMAIN: The N-terminal ATP-grasp domain carries the
CC       phosphoribosylamine--glycine ligase activity.
CC       {ECO:0000305|PubMed:3086869}.
CC   -!- DOMAIN: The central AIRS domain carries the
CC       phosphoribosylformylglycinamidine cyclo-ligase activity.
CC       {ECO:0000305|PubMed:3086869}.
CC   -!- DOMAIN: The C-terminal GART domain carries the
CC       phosphoribosylglycinamide formyltransferase activity.
CC       {ECO:0000305|PubMed:3086869}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the GARS family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the central section; belongs to the AIR synthase family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the GART family.
CC       {ECO:0000305}.
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DR   EMBL; J02527; AAA28562.1; -; Genomic_DNA.
DR   EMBL; J02527; AAA28563.1; -; Genomic_DNA.
DR   EMBL; AE014134; AAF52474.2; -; Genomic_DNA.
DR   EMBL; X00041; CAA24923.1; -; Genomic_DNA.
DR   PIR; S01206; AJFFPM.
DR   RefSeq; NP_001014477.1; NM_001014477.2. [P00967-2]
DR   RefSeq; NP_001285698.1; NM_001298769.1.
DR   RefSeq; NP_523497.2; NM_078773.3.
DR   AlphaFoldDB; P00967; -.
DR   SMR; P00967; -.
DR   BioGRID; 60135; 2.
DR   IntAct; P00967; 19.
DR   STRING; 7227.FBpp0308722; -.
DR   iPTMnet; P00967; -.
DR   PaxDb; 7227-FBpp0079059; -.
DR   DNASU; 33986; -.
DR   EnsemblMetazoa; FBtr0100353; FBpp0099760; FBgn0000053. [P00967-2]
DR   GeneID; 33986; -.
DR   KEGG; dme:Dmel_CG31628; -.
DR   AGR; FB:FBgn0000053; -.
DR   CTD; 2618; -.
DR   FlyBase; FBgn0000053; Gart.
DR   VEuPathDB; VectorBase:FBgn0000053; -.
DR   eggNOG; KOG0237; Eukaryota.
DR   eggNOG; KOG3076; Eukaryota.
DR   HOGENOM; CLU_005361_0_1_1; -.
DR   InParanoid; P00967; -.
DR   OrthoDB; 729at2759; -.
DR   PhylomeDB; P00967; -.
DR   Reactome; R-DME-73817; Purine ribonucleoside monophosphate biosynthesis.
DR   UniPathway; UPA00074; UER00125.
DR   UniPathway; UPA00074; UER00126.
DR   UniPathway; UPA00074; UER00129.
DR   BioGRID-ORCS; 33986; 1 hit in 3 CRISPR screens.
DR   GenomeRNAi; 33986; -.
DR   PRO; PR:P00967; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0000053; Expressed in capitellum (Drosophila) and 38 other cell types or tissues.
DR   ExpressionAtlas; P00967; baseline and differential.
DR   GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IDA:FlyBase.
DR   GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IDA:FlyBase.
DR   GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IDA:FlyBase.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046084; P:adenine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009113; P:purine nucleobase biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
DR   CDD; cd08645; FMT_core_GART; 1.
DR   CDD; cd02196; PurM; 2.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.40.50.170; Formyl transferase, N-terminal domain; 1.
DR   Gene3D; 3.90.600.10; Phosphoribosylglycinamide synthetase, C-terminal 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_00741; AIRS; 1.
DR   HAMAP; MF_00138; GARS; 1.
DR   HAMAP; MF_01930; PurN; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR002376; Formyl_transf_N.
DR   InterPro; IPR036477; Formyl_transf_N_sf.
DR   InterPro; IPR004607; GART.
DR   InterPro; IPR001555; GART_AS.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp.
DR   InterPro; IPR000115; PRibGlycinamide_synth.
DR   InterPro; IPR020560; PRibGlycinamide_synth_C-dom.
DR   InterPro; IPR037123; PRibGlycinamide_synth_C_sf.
DR   InterPro; IPR020559; PRibGlycinamide_synth_CS.
DR   InterPro; IPR020562; PRibGlycinamide_synth_N.
DR   InterPro; IPR010918; PurM-like_C_dom.
DR   InterPro; IPR036676; PurM-like_C_sf.
DR   InterPro; IPR016188; PurM-like_N.
DR   InterPro; IPR036921; PurM-like_N_sf.
DR   InterPro; IPR004733; PurM_cligase.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   NCBIfam; TIGR00877; purD; 1.
DR   NCBIfam; TIGR00878; purM; 2.
DR   NCBIfam; TIGR00639; PurN; 1.
DR   PANTHER; PTHR10520:SF12; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3; 1.
DR   PANTHER; PTHR10520; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3-RELATED; 1.
DR   Pfam; PF00586; AIRS; 2.
DR   Pfam; PF02769; AIRS_C; 2.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   Pfam; PF01071; GARS_A; 1.
DR   Pfam; PF02843; GARS_C; 1.
DR   Pfam; PF02844; GARS_N; 1.
DR   SMART; SM01209; GARS_A; 1.
DR   SMART; SM01210; GARS_C; 1.
DR   SUPFAM; SSF53328; Formyltransferase; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF56042; PurM C-terminal domain-like; 2.
DR   SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS00184; GARS; 1.
DR   PROSITE; PS00373; GART; 1.
DR   Genevisible; P00967; DM.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Ligase; Magnesium; Manganese;
KW   Metal-binding; Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
KW   Purine biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..1353
FT                   /note="Trifunctional purine biosynthetic protein adenosine-
FT                   3"
FT                   /id="PRO_0000074934"
FT   DOMAIN          114..321
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   REGION          441..1155
FT                   /note="AIRS domain"
FT                   /evidence="ECO:0000250|UniProtKB:P21872"
FT   REGION          1153..1353
FT                   /note="GART domain"
FT                   /evidence="ECO:0000250|UniProtKB:P21872"
FT   ACT_SITE        1263
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P08179"
FT   BINDING         193..196
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P22102"
FT   BINDING         200
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P22102"
FT   BINDING         223
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P22102"
FT   BINDING         232
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P22102"
FT   BINDING         291
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         293
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         1164..1166
FT                   /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT                   /ligand_id="ChEBI:CHEBI:143788"
FT                   /evidence="ECO:0000250|UniProtKB:P22102"
FT   BINDING         1219
FT                   /ligand="(6R)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:195366"
FT                   /evidence="ECO:0000250|UniProtKB:P22102"
FT   BINDING         1244..1247
FT                   /ligand="(6R)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:195366"
FT                   /evidence="ECO:0000250|UniProtKB:P22102"
FT   BINDING         1261
FT                   /ligand="(6R)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:195366"
FT                   /evidence="ECO:0000250|UniProtKB:P22102"
FT   BINDING         1295..1299
FT                   /ligand="(6R)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:195366"
FT                   /evidence="ECO:0000250|UniProtKB:P22102"
FT   BINDING         1325..1328
FT                   /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT                   /ligand_id="ChEBI:CHEBI:143788"
FT                   /evidence="ECO:0000250|UniProtKB:P22102"
FT   SITE            1299
FT                   /note="Raises pKa of active site His"
FT                   /evidence="ECO:0000250|UniProtKB:P08179"
FT   MOD_RES         814
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         816
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   VAR_SEQ         434
FT                   /note="I -> M (in isoform Short)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_005512"
FT   VAR_SEQ         435..1353
FT                   /note="Missing (in isoform Short)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_005513"
FT   MUTAGEN         1164
FT                   /note="G->S: Loss of phosphoribosylglycinamide
FT                   formyltransferase enzymatic activity."
FT                   /evidence="ECO:0000269|PubMed:3086869"
FT   CONFLICT        515
FT                   /note="F -> L (in Ref. 2; AAF52474)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        602
FT                   /note="H -> Q (in Ref. 2; AAF52474)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        907
FT                   /note="G -> E (in Ref. 2; AAF52474)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        960
FT                   /note="A -> D (in Ref. 2; AAF52474)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1193
FT                   /note="P -> T (in Ref. 2; AAF52474)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1353 AA;  144448 MW;  A68DAB61A02DFD4F CRC64;
     MSHRVLVIGS GGREHAICWK LSQSPKVAQI YALPGSHGIQ LVEKCRNLDA KTLDPKDFEA
     IAKWSKENQI ALVVVGPEDP LALGLGDVLQ SAGIPCFGPG KQGAQIEADK KWAKDFMLRH
     GIPTARYESF TDTEKAKAFI RSAPYPALVV KAAGLAAGKG VVVAANAKEA CQAVDEILGD
     LKYGQAGATL VVEELLEGEE VSVLAFTDGK SVRAMLPAQD HKRLGNGDTG PNTGGMGAYC
     PCPLISQPAL ELVQKAVLER AVQGLIKERI NYQGVLYAGL MLTRDGPRVL EFNCRFGDPE
     TQVILPLLES DLFDVMEACC SGKLDKIPLQ WRNGVSAVGV ILASAGYPET STKGCIISGL
     PAANTPTQLV FHSGLAVNAQ KEALTNGGRV LIAIALDGSL KEAAAKATKL AGSISFSGSG
     AQYRTDIAQK AFKIASASTP GLSYKDSGVD IDAGDALVQR IKPLSRGTQR PGVIGGLGGF
     GGLFRLKELT YKEPVIAEAT QGVGAKIHLA LTHEFYENVG YDLFALAAND VLEVGAEPVA
     FLDYIACGKL QVPLAAQLVK GMADGCRDAR CALVGGETAE MPSLYAPGQH DMAGYCVGIV
     EHSRILPRFD LYQPGDLLIG LPSSGLHCAG FNEILTQLAA SKVNLRERSP VDGGDDGLTL
     AHVLATPTQL YVQQLLPHLQ KGDEIKSVAH VTHGLLNDIL RLLPDGFETT LDFGAVPVPK
     IFGWLAGKLK LSAQTILERH NCGIGMVLIL PQSSQLWRTS LPGAKVLGVL QRRSKVSGSP
     VQVRNFVEQL EKVASPFGGL GDRELPEELK KLPSNSDLSA PREECFENAA GRRLTRIPTH
     YKDPILILGT DGVGTKLKIA QQTNRNTSVG IDLVAMCVND ILCNGAEPIS FSSYYACGHW
     QEQLAKGVHS GVQEGARQAN SSFIDSHSAA LPLLYEPQVY DLAGFALGIA EHTGILPLLA
     EIQPGDVLIG LPSSGVHSNG FSLVHAVLKR VGLGLHDKAP FSDKTLGEEL LVPTKIYVKA
     LSTLLSRGKH GIKALAHITG GGLSENIPRV LRKDLAVRLD ANKFQLPPVF AWLAAAGNIS
     STELQRTYNC GLGMVLVVAP TEVEDVLKEL RYPQRAAVVG EVVARKDPKK SQVVVQNFEA
     SLARTQKMLS QRRKRVAVLI SGTGSNLQAL IDATRDSAQG IHADVVLVIS NKPGVLGLQR
     ATQAGIPSLV ISHKDFASRE VYDAELTRNL KAARVDLICL AGFMRVLSAP FVREWRGRLV
     NIHPSLLPKY PGLHVQKQAL EAGEKESGCT VHFVDEGVDT GAIIVQAAVP ILPDDDEDSL
     TQRIHKAEHW AFPRALAMLV NGTALISPEV SSQ
//