ID   PUR6_VIGAC              Reviewed;         557 AA.
AC   P55195;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Phosphoribosylaminoimidazole carboxylase, chloroplastic;
DE            EC=4.1.1.21;
DE   AltName: Full=AIR carboxylase;
DE            Short=AIRC;
DE   Flags: Precursor; Fragment;
GN   Name=PURKE;
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 + H(+)
CC         = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + CO2;
CC         Xref=Rhea:RHEA:10792, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:77657, ChEBI:CHEBI:137981; EC=4.1.1.21;
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-
CC       phospho-D-ribosyl)imidazole (carboxylase route): step 1/1.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the AIR carboxylase
CC       family. Class I subfamily. {ECO:0000305}.
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DR   EMBL; L22584; AAC37400.1; -; mRNA.
DR   PIR; S43322; S43322.
DR   AlphaFoldDB; P55195; -.
DR   SMR; P55195; -.
DR   UniPathway; UPA00074; UER00130.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0043727; F:5-amino-4-imidazole carboxylate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   HAMAP; MF_01929; PurE_classI; 1.
DR   HAMAP; MF_01928; PurK; 1.
DR   InterPro; IPR016301; Ade2_fungi/plant.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR003135; ATP-grasp_carboxylate-amine.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR033747; PurE_ClassI.
DR   InterPro; IPR000031; PurE_dom.
DR   InterPro; IPR005875; PurK.
DR   InterPro; IPR040686; PurK_C.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   Pfam; PF00731; AIRC; 1.
DR   Pfam; PF02222; ATP-grasp; 1.
DR   Pfam; PF17769; PurK_C; 1.
DR   PIRSF; PIRSF001340; AIR_carboxylase; 1.
DR   SMART; SM01001; AIRC; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR01162; purE; 1.
DR   TIGRFAMs; TIGR01161; purK; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chloroplast; Decarboxylase; Lyase; Nucleotide-binding;
KW   Plastid; Purine biosynthesis; Transit peptide.
FT   TRANSIT         <1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..557
FT                   /note="Phosphoribosylaminoimidazole carboxylase,
FT                   chloroplastic"
FT                   /id="PRO_0000029879"
FT   DOMAIN          108..293
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   REGION          ?..386
FT                   /note="AIR carboxylase ATPase subunit"
FT   REGION          387..557
FT                   /note="AIR carboxylase catalytic subunit"
FT   BINDING         132..189
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   NON_TER         1
SQ   SEQUENCE   557 AA;  60942 MW;  E88FEAB6415B4EC2 CRC64;
     GLYEVVVGVL GGGQLGRMMC QAASQMAIKV MVLDPQENCP ASSLSYHHMV GSFDESTKVE
     EFAKRCGVLT VEIEHVDVDT LEKLEKQGVD CQPKASTVRI IQDKYQQKVA LLPAWIPLPE
     FMKIDDLKAK KWDSLDIHFM IKSRRLAYDG RGNFVAKSEE ELSSAVDALG GFDRGLYAEK
     WAPFVKELAV IVARGRDNSI SCYPVVELFT GHICHIVKSP ANVNWKTREL AIEVAFNAVK
     SLEVPGVFAV ELFLTKEGEI LLNEVAPRPH NSGHHTIESC HTSQFEQHLP AVVGLPLGDP
     SMKTPAAIMY NILGEEEGEH GFQLAHQLMK RAMTIPGASV HWYDKPEMRK QRKMCHITIV
     GSSLSSIESN LAILLEGKGL HDKTAVCSTL LGFIMGSDSD LPVMKSAAEM MEMFGVPHEV
     RIVSAHRTPE LMFCYASSAH ERGYQVIIAG AGGAAHLPGM VASLTPLPVV GVPVRASTLD
     GLDSLLSIVQ MPRGVPVATV AVNNATNAGL LAVRMLGVAN DNLLSRMSQY QEDQKEAVLR
     EGDKLEKHGW ESYLKNS