PURA_ARATH
ID PURA_ARATH Reviewed; 490 AA.
AC Q96529;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Adenylosuccinate synthetase, chloroplastic {ECO:0000255|HAMAP-Rule:MF_03125};
DE Short=AMPSase {ECO:0000255|HAMAP-Rule:MF_03125};
DE Short=AdSS {ECO:0000255|HAMAP-Rule:MF_03125};
DE EC=6.3.4.4 {ECO:0000255|HAMAP-Rule:MF_03125};
DE AltName: Full=IMP--aspartate ligase {ECO:0000255|HAMAP-Rule:MF_03125};
DE Flags: Precursor;
GN Name=PURA {ECO:0000255|HAMAP-Rule:MF_03125}; OrderedLocusNames=At3g57610;
GN ORFNames=F15B8.200;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8790347; DOI=10.1073/pnas.93.18.9431;
RA Fonne-Pfister R., Chemla P., Ward E., Girardet M., Kreuz K.E.,
RA Honzatko R.B., Fromm H.J., Schaer H.-P., Gruetter M.G., Cowan-Jacob S.W.;
RT "The mode of action and the structure of a herbicide in complex with its
RT target: binding of activated hydantocidin to the feedback regulation site
RT of adenylosuccinate synthetase.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:9431-9436(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-46, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER ALA-45, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 48-490 IN COMPLEX WITH GDP.
RX PubMed=10669609; DOI=10.1006/jmbi.1999.3473;
RA Prade L., Cowan-Jacob S.W., Chemla P., Potter S., Ward E.,
RA Fonne-Pfister R.;
RT "Structures of adenylosuccinate synthetase from Triticum aestivum and
RT Arabidopsis thaliana.";
RL J. Mol. Biol. 296:569-577(2000).
CC -!- FUNCTION: Plays an important role in the de novo pathway and in the
CC salvage pathway of purine nucleotide biosynthesis. Catalyzes the first
CC committed step in the biosynthesis of AMP from IMP.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-
CC dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053,
CC ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03125};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03125};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03125};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC from IMP: step 1/2. {ECO:0000255|HAMAP-Rule:MF_03125}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03125,
CC ECO:0000269|PubMed:10669609}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_03125}.
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DR EMBL; U49389; AAB16828.1; -; mRNA.
DR EMBL; AL049660; CAB41194.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79678.1; -; Genomic_DNA.
DR EMBL; AY054606; AAK96797.1; -; mRNA.
DR EMBL; AY081461; AAM10023.1; -; mRNA.
DR PIR; T06759; T06759.
DR RefSeq; NP_191320.1; NM_115621.5.
DR PDB; 1DJ2; X-ray; 2.90 A; A/B=48-490.
DR PDBsum; 1DJ2; -.
DR AlphaFoldDB; Q96529; -.
DR SMR; Q96529; -.
DR BioGRID; 10245; 31.
DR STRING; 3702.AT3G57610.1; -.
DR iPTMnet; Q96529; -.
DR PaxDb; Q96529; -.
DR PRIDE; Q96529; -.
DR ProteomicsDB; 226003; -.
DR EnsemblPlants; AT3G57610.1; AT3G57610.1; AT3G57610.
DR GeneID; 824930; -.
DR Gramene; AT3G57610.1; AT3G57610.1; AT3G57610.
DR KEGG; ath:AT3G57610; -.
DR Araport; AT3G57610; -.
DR TAIR; locus:2076606; AT3G57610.
DR eggNOG; KOG1355; Eukaryota.
DR HOGENOM; CLU_029848_0_0_1; -.
DR InParanoid; Q96529; -.
DR OMA; FHHAKPI; -.
DR OrthoDB; 1276527at2759; -.
DR PhylomeDB; Q96529; -.
DR BioCyc; ARA:AT3G57610-MON; -.
DR BioCyc; MetaCyc:AT3G57610-MON; -.
DR BRENDA; 6.3.4.4; 399.
DR UniPathway; UPA00075; UER00335.
DR EvolutionaryTrace; Q96529; -.
DR PRO; PR:Q96529; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q96529; baseline and differential.
DR Genevisible; Q96529; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0004019; F:adenylosuccinate synthase activity; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0046040; P:IMP metabolic process; IBA:GO_Central.
DR CDD; cd03108; AdSS; 1.
DR Gene3D; 1.10.300.10; -; 1.
DR Gene3D; 3.40.440.10; -; 1.
DR Gene3D; 3.90.170.10; -; 1.
DR HAMAP; MF_00011; Adenylosucc_synth; 1.
DR InterPro; IPR018220; Adenylosuccin_syn_GTP-bd.
DR InterPro; IPR033128; Adenylosuccin_syn_Lys_AS.
DR InterPro; IPR042109; Adenylosuccinate_synth_dom1.
DR InterPro; IPR042110; Adenylosuccinate_synth_dom2.
DR InterPro; IPR042111; Adenylosuccinate_synth_dom3.
DR InterPro; IPR001114; Adenylosuccinate_synthetase.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11846; PTHR11846; 1.
DR Pfam; PF00709; Adenylsucc_synt; 1.
DR SMART; SM00788; Adenylsucc_synt; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00184; purA; 1.
DR PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1.
DR PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chloroplast; GTP-binding; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Plastid; Purine biosynthesis;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..45
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 46..490
FT /note="Adenylosuccinate synthetase, chloroplastic"
FT /id="PRO_0000029870"
FT ACT_SITE 78
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT ACT_SITE 106
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 77..83
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 78..81
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 78
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 103..106
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 105..107
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 195
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 209
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 289
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 304
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 364..370
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 368
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 370
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 396..398
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 479..481
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT MOD_RES 46
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT STRAND 67..77
FT /evidence="ECO:0007829|PDB:1DJ2"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:1DJ2"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:1DJ2"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:1DJ2"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:1DJ2"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:1DJ2"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:1DJ2"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:1DJ2"
FT HELIX 142..153
FT /evidence="ECO:0007829|PDB:1DJ2"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:1DJ2"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:1DJ2"
FT STRAND 163..171
FT /evidence="ECO:0007829|PDB:1DJ2"
FT HELIX 174..186
FT /evidence="ECO:0007829|PDB:1DJ2"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:1DJ2"
FT HELIX 214..218
FT /evidence="ECO:0007829|PDB:1DJ2"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:1DJ2"
FT HELIX 223..237
FT /evidence="ECO:0007829|PDB:1DJ2"
FT HELIX 245..262
FT /evidence="ECO:0007829|PDB:1DJ2"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:1DJ2"
FT HELIX 269..278
FT /evidence="ECO:0007829|PDB:1DJ2"
FT STRAND 283..290
FT /evidence="ECO:0007829|PDB:1DJ2"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:1DJ2"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:1DJ2"
FT HELIX 311..315
FT /evidence="ECO:0007829|PDB:1DJ2"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:1DJ2"
FT STRAND 327..341
FT /evidence="ECO:0007829|PDB:1DJ2"
FT HELIX 350..359
FT /evidence="ECO:0007829|PDB:1DJ2"
FT TURN 364..366
FT /evidence="ECO:0007829|PDB:1DJ2"
FT STRAND 371..376
FT /evidence="ECO:0007829|PDB:1DJ2"
FT HELIX 377..387
FT /evidence="ECO:0007829|PDB:1DJ2"
FT STRAND 390..395
FT /evidence="ECO:0007829|PDB:1DJ2"
FT HELIX 397..402
FT /evidence="ECO:0007829|PDB:1DJ2"
FT STRAND 404..413
FT /evidence="ECO:0007829|PDB:1DJ2"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:1DJ2"
FT HELIX 427..432
FT /evidence="ECO:0007829|PDB:1DJ2"
FT STRAND 434..441
FT /evidence="ECO:0007829|PDB:1DJ2"
FT HELIX 458..471
FT /evidence="ECO:0007829|PDB:1DJ2"
FT STRAND 475..479
FT /evidence="ECO:0007829|PDB:1DJ2"
FT STRAND 481..485
FT /evidence="ECO:0007829|PDB:1DJ2"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:1DJ2"
SQ SEQUENCE 490 AA; 52964 MW; B1E82BA386DF93CB CRC64;
MSLSSLTLDS NPRFAVGGPY HRRYPPLHHP RSFVSCSAKR PAVSASLSVA ADSAATESLG
RIGSLSQVSG VLGCQWGDEG KGKLVDILAQ HFDIVARCQG GANAGHTIYN SEGKKFALHL
VPSGILNEDT TCVIGNGVVV HLPGLFKEID GLESNGVSCK GRILVSDRAH LLFDFHQEVD
GLRESELAKS FIGTTKRGIG PAYSSKVIRN GIRVGDLRHM DTLPQKLDLL LSDAAARFQG
FKYTPEMLRE EVEAYKRYAD RLEPYITDTV HFINDSISQK KKVLVEGGQA TMLDIDFGTY
PFVTSSSPSA GGICTGLGIA PSVVGDLIGV VKAYTTRVGS GPFPTENLGT GGDLLRLAGQ
EFGTTTGRPR RCGWLDIVAL KFSCQINGFA SLNLTKLDVL SDLNEIQLGV AYKRSDGTPV
KSFPGDLRLL EELHVEYEVL PGWKSDISSV RNYSDLPKAA QQYVERIEEL VGVPIHYIGI
GPGRDALIYK
