PUR2_DROME
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 03-AUG-2022, entry version 197.
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=(6S)-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:57454, ChEBI:CHEBI:143788, ChEBI:CHEBI:147286;
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,
CC ECO:0000255|PROSITE-ProRule:PRU00409};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-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.FBpp0079059; -.
DR iPTMnet; P00967; -.
DR PaxDb; P00967; -.
DR PRIDE; P00967; -.
DR DNASU; 33986; -.
DR EnsemblMetazoa; FBtr0100353; FBpp0099760; FBgn0000053. [P00967-2]
DR GeneID; 33986; -.
DR KEGG; dme:Dmel_CG31628; -.
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 OMA; KATVCKY; -.
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 tissues.
DR ExpressionAtlas; P00967; baseline and differential.
DR Genevisible; P00967; DM.
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; 3.30.1330.10; -; 2.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.90.600.10; -; 1.
DR Gene3D; 3.90.650.10; -; 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 PANTHER; PTHR10520; PTHR10520; 2.
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; SM01210; GARS_C; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR SUPFAM; SSF53328; SSF53328; 1.
DR SUPFAM; SSF55326; SSF55326; 2.
DR SUPFAM; SSF56042; SSF56042; 2.
DR TIGRFAMs; TIGR00877; purD; 1.
DR TIGRFAMs; TIGR00878; purM; 2.
DR TIGRFAMs; TIGR00639; PurN; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00184; GARS; 1.
DR PROSITE; PS00373; GART; 1.
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="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000250|UniProtKB:P22102"
FT BINDING 1244..1247
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000250|UniProtKB:P22102"
FT BINDING 1261
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000250|UniProtKB:P22102"
FT BINDING 1295..1299
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
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
