PURA_WHEAT
ID PURA_WHEAT Reviewed; 476 AA.
AC O24396;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
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: Fragment;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Kanzler;
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 X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 35-476 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 (By similarity).
CC {ECO:0000250}.
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 -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC Rule:MF_03125}.
CC -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_03125}.
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DR EMBL; U49387; AAB16829.1; -; mRNA.
DR PIR; T06792; T06792.
DR PDB; 1DJ3; X-ray; 3.00 A; A/B=35-476.
DR PDBsum; 1DJ3; -.
DR AlphaFoldDB; O24396; -.
DR SMR; O24396; -.
DR STRING; 4565.Traes_4DL_CDDD5E13E.1; -.
DR PRIDE; O24396; -.
DR eggNOG; KOG1355; Eukaryota.
DR BRENDA; 6.3.4.4; 6500.
DR UniPathway; UPA00075; UER00335.
DR EvolutionaryTrace; O24396; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; O24396; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004019; F:adenylosuccinate synthase activity; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; Chloroplast; GTP-binding; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Plastid; Purine biosynthesis; Reference proteome.
FT CHAIN <1..476
FT /note="Adenylosuccinate synthetase, chloroplastic"
FT /id="PRO_0000029872"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 64
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT ACT_SITE 92
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 63..69
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 64..67
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 64
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 89..92
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 91..93
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 91
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 181
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 195
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 275
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 290
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 350..356
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 354
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 356
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 382..384
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 465..467
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT NON_TER 1
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1DJ3"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:1DJ3"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1DJ3"
FT HELIX 67..74
FT /evidence="ECO:0007829|PDB:1DJ3"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:1DJ3"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:1DJ3"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:1DJ3"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:1DJ3"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:1DJ3"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:1DJ3"
FT HELIX 128..139
FT /evidence="ECO:0007829|PDB:1DJ3"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:1DJ3"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:1DJ3"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:1DJ3"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1DJ3"
FT HELIX 160..172
FT /evidence="ECO:0007829|PDB:1DJ3"
FT HELIX 185..193
FT /evidence="ECO:0007829|PDB:1DJ3"
FT HELIX 200..204
FT /evidence="ECO:0007829|PDB:1DJ3"
FT HELIX 206..223
FT /evidence="ECO:0007829|PDB:1DJ3"
FT HELIX 231..248
FT /evidence="ECO:0007829|PDB:1DJ3"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:1DJ3"
FT HELIX 255..264
FT /evidence="ECO:0007829|PDB:1DJ3"
FT STRAND 269..276
FT /evidence="ECO:0007829|PDB:1DJ3"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:1DJ3"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:1DJ3"
FT HELIX 297..303
FT /evidence="ECO:0007829|PDB:1DJ3"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:1DJ3"
FT STRAND 313..323
FT /evidence="ECO:0007829|PDB:1DJ3"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:1DJ3"
FT HELIX 336..345
FT /evidence="ECO:0007829|PDB:1DJ3"
FT TURN 350..352
FT /evidence="ECO:0007829|PDB:1DJ3"
FT STRAND 357..362
FT /evidence="ECO:0007829|PDB:1DJ3"
FT HELIX 363..373
FT /evidence="ECO:0007829|PDB:1DJ3"
FT STRAND 376..381
FT /evidence="ECO:0007829|PDB:1DJ3"
FT HELIX 383..386
FT /evidence="ECO:0007829|PDB:1DJ3"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:1DJ3"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:1DJ3"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:1DJ3"
FT HELIX 413..416
FT /evidence="ECO:0007829|PDB:1DJ3"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:1DJ3"
FT HELIX 444..457
FT /evidence="ECO:0007829|PDB:1DJ3"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:1DJ3"
FT STRAND 467..471
FT /evidence="ECO:0007829|PDB:1DJ3"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:1DJ3"
SQ SEQUENCE 476 AA; 50918 MW; 7E2D9E7F616783DF CRC64;
AAAAAGRGRS FSPAAPAPSS VRLPGRQAPA PAAASALAVE ADPAADRVSS LSQVSGVLGS
QWGDEGKGKL VDVLAPRFDI VARCQGGANA GHTIYNSEGK KFALHLVPSG ILHEGTLCVV
GNGAVIHVPG FFGEIDGLQS NGVSCDGRIL VSDRAHLLFD LHQTVDGLRE AELANSFIGT
TKRGIGPCYS SKVTRNGLRV CDLRHMDTFG DKLDVLFEDA AARFEGFKYS KGMLKEEVER
YKRFAERLEP FIADTVHVLN ESIRQKKKIL VEGGQATMLD IDFGTYPFVT SSSPSAGGIC
TGLGIAPRVI GDLIGVVKAY TTRVGSGPFP TELLGEEGDV LRKAGMEFGT TTGRPRRCGW
LDIVALKYCC DINGFSSLNL TKLDVLSGLP EIKLGVSYNQ MDGEKLQSFP GDLDTLEQVQ
VNYEVLPGWD SDISSVRSYS ELPQAARRYV ERIEELAGVP VHYIGVGPGR DALIYK
