ID   PUR7_VIGAC              Reviewed;         341 AA.
AC   Q07463;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase, chloroplastic;
DE            EC=6.3.2.6;
DE   AltName: Full=SAICAR synthetase;
DE   Flags: Precursor; Fragment;
GN   Name=PUR7; Synonyms=PURC;
OS   Vigna aconitifolia (Moth bean) (Phaseolus aconitifolius).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Root nodule;
RX   PubMed=8111040; DOI=10.1007/bf00020176;
RA   Chapman K.A., Delauney A.J., Kim J.H., Verma D.P.S.;
RT   "Structural organization of de novo purine biosynthesis enzymes in plants:
RT   5-aminoimidazole ribonucleotide carboxylase and 5-aminoimidazole-4-N-
RT   succinocarboxamide ribonucleotide synthetase cDNAs from Vigna
RT   aconitifolia.";
RL   Plant Mol. Biol. 24:389-395(1994).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP +
CC         L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-
CC         4-carboxamido]succinate + ADP + 2 H(+) + phosphate;
CC         Xref=Rhea:RHEA:22628, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58443,
CC         ChEBI:CHEBI:77657, ChEBI:CHEBI:456216; EC=6.3.2.6;
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-
CC       phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: First expressed in 19-day old nodules.
CC   -!- SIMILARITY: Belongs to the SAICAR synthetase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC37399.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M92931; AAC37399.1; ALT_INIT; mRNA.
DR   PIR; S43323; S43323.
DR   PIR; S45524; S45524.
DR   AlphaFoldDB; Q07463; -.
DR   SMR; Q07463; -.
DR   UniPathway; UPA00074; UER00131.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00137; SAICAR_synth; 1.
DR   InterPro; IPR028923; SAICAR_synt/ADE2_N.
DR   InterPro; IPR018236; SAICAR_synthetase_CS.
DR   Pfam; PF01259; SAICAR_synt; 1.
DR   PROSITE; PS01057; SAICAR_SYNTHETASE_1; 1.
DR   PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chloroplast; Ligase; Nucleotide-binding; Plastid;
KW   Purine biosynthesis; Transit peptide.
FT   TRANSIT         <1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..341
FT                   /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT                   synthase, chloroplastic"
FT                   /id="PRO_0000029874"
FT   NON_TER         1
SQ   SEQUENCE   341 AA;  38100 MW;  46145613F1A2C4A4 CRC64;
     RDSTTHQSHF RGGVGVTKIS FKPHGFRAIR ASVMPSEGQQ QSSLGDSLVN SPHRNDVVDV
     IRKSAISNCL SETNLHNTVP GLVSKTRGKV RDIYDAGDYL VLVTTDRQSA FDRILASIPF
     KGQVLNETSL WWFERTKQIV PNAVVSAPDK NVTIAKKCSV FPVEFVARGF VTGSTDTSLW
     TVYNKGARNY CGNVLPDGMV KNQKLSENIL TPTTKAADHD VPVTPDEIIE RGLMTRSDYE
     EVSEKALSLF EYGQQVASEH GLILVDTKYE FGKANDGSIM LIDEVHTPDS SRYWIASSYP
     ERFQNGLEPE NIDKEFLRLW FKSHCNPYED EVLPDAPEDL L