PUR5_VIGUN
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 25-MAY-2022, entry version 95.
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; 3.30.1330.10; -; 1.
DR Gene3D; 3.90.650.10; -; 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 PANTHER; PTHR10520; PTHR10520; 1.
DR Pfam; PF00586; AIRS; 1.
DR Pfam; PF02769; AIRS_C; 1.
DR SUPFAM; SSF55326; SSF55326; 1.
DR SUPFAM; SSF56042; SSF56042; 1.
DR TIGRFAMs; TIGR00878; purM; 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