ID   PUR5_VIGUN              Reviewed;         388 AA.
AC   P52424;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   13-SEP-2023, entry version 98.
DE   RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase, chloroplastic/mitochondrial;
DE            EC=6.3.3.1;
DE   AltName: Full=AIR synthase;
DE            Short=AIRS;
DE   AltName: Full=Phosphoribosyl-aminoimidazole synthetase;
DE   AltName: Full=VUpur5;
DE   Flags: Precursor;
GN   Name=PUR5;
OS   Vigna unguiculata (Cowpea).
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=3917;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Vita 3; TISSUE=Root nodule;
RX   PubMed=9520274; DOI=10.1023/a:1005969830314;
RA   Smith P.M.C., Mann A.J., Goggin D.E., Atkins C.A.;
RT   "AIR synthetase in cowpea nodules: a single gene product targeted to two
RT   organelles?";
RL   Plant Mol. Biol. 36:811-820(1998).
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   -!- 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.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Mitochondrion.
CC   -!- SIMILARITY: Belongs to the AIR synthase family. {ECO:0000305}.
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DR   EMBL; U30895; AAC14578.1; -; mRNA.
DR   PIR; T10963; T10963.
DR   AlphaFoldDB; P52424; -.
DR   SMR; P52424; -.
DR   BRENDA; 6.3.3.1; 6657.
DR   UniPathway; UPA00074; UER00129.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd02196; PurM; 1.
DR   Gene3D; 3.90.650.10; PurM-like C-terminal domain; 1.
DR   Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 1.
DR   HAMAP; MF_00741; AIRS; 1.
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   NCBIfam; TIGR00878; purM; 1.
DR   PANTHER; PTHR10520:SF12; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3; 1.
DR   PANTHER; PTHR10520; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3-RELATED; 1.
DR   Pfam; PF00586; AIRS; 1.
DR   Pfam; PF02769; AIRS_C; 1.
DR   SUPFAM; SSF56042; PurM C-terminal domain-like; 1.
DR   SUPFAM; SSF55326; PurM N-terminal domain-like; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chloroplast; Ligase; Mitochondrion; Nucleotide-binding;
KW   Plastid; Purine biosynthesis; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast and mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..388
FT                   /note="Phosphoribosylformylglycinamidine cyclo-ligase,
FT                   chloroplastic/mitochondrial"
FT                   /id="PRO_0000029882"
SQ   SEQUENCE   388 AA;  40427 MW;  15D0EF11127C9EE6 CRC64;
     MSLSACAELS RCFAAAASAK PNSGKSNSTA ATSLVISSPI GHDGAVSSVS RSRKTSRIVA
     EASQGLTYRD AGVDIDAGAE LVRRIAKMAP GIGGFGGLYP LGDSYLVAGT DGVGTKLMLA
     FETGIHDTIG IDLVAMSVND IVTSGAKPLF FLDYFATGRL DVDVAEKVVK GIVDGCKQSD
     CVLLGGETAE MPGLYKEGEY DLSGCAVGIV KKDSVINGKN IVAGDVIIGL PSSGVHSNGF
     SLVRRVLAQS GLSLKDQLPG SNITLAEALM APTVIYVKQV LDLISKGGVK GIAHITGGGF
     TDNIPRVFPE GLGALIYDGS WEVPAVFRWL QEAGKIEDSE MRRTFNMGIG MILVVSPEAA
     NRILENKGQA DKFYRIGEII SGNGVTFS
//