PUR5_RHILE
ID PUR5_RHILE Reviewed; 357 AA.
AC Q9XAT2;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000255|HAMAP-Rule:MF_00741};
DE EC=6.3.3.1 {ECO:0000255|HAMAP-Rule:MF_00741};
DE AltName: Full=AIR synthase {ECO:0000255|HAMAP-Rule:MF_00741};
DE AltName: Full=AIRS {ECO:0000255|HAMAP-Rule:MF_00741};
DE AltName: Full=Phosphoribosyl-aminoimidazole synthetase {ECO:0000255|HAMAP-Rule:MF_00741};
GN Name=purM {ECO:0000255|HAMAP-Rule:MF_00741};
OS Rhizobium leguminosarum.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=384;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10659713; DOI=10.1094/mpmi.2000.13.2.228;
RA Stevens J.B., De Luca N.G., Beringer J.E., Ringer J.P., Yeoman K.H.,
RA Johnston A.W.B.;
RT "The purMN genes of Rhizobium leguminosarum and a superficial link with
RT siderophore production.";
RL Mol. Plant Microbe Interact. 13:228-231(2000).
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00741};
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. {ECO:0000255|HAMAP-
CC Rule:MF_00741}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00741}.
CC -!- SIMILARITY: Belongs to the AIR synthase family. {ECO:0000255|HAMAP-
CC Rule:MF_00741}.
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DR EMBL; AJ243305; CAB46525.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9XAT2; -.
DR SMR; Q9XAT2; -.
DR STRING; 936136.ARRT01000006_gene2625; -.
DR eggNOG; COG0150; Bacteria.
DR UniPathway; UPA00074; UER00129.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Purine biosynthesis.
FT CHAIN 1..357
FT /note="Phosphoribosylformylglycinamidine cyclo-ligase"
FT /id="PRO_0000148237"
SQ SEQUENCE 357 AA; 36910 MW; 6B5A0EF10334BE0E CRC64;
MSQSGKNGLT YSDAGVDIDA GNLLVEKIKP AVRSTRRPGG DGEIGGFGGL FDLKAAAFTD
PVLVAANDGV GTKLKIAIDA DYHDTVGIDL VAMCVNDLVV QGAEPLFFLD YFATGKLDPD
QGAAIVGGIA ARCREAGCAL IGGETAEMPG MYSSGDYDLA GFAVGAAERG KLLPSGDIAE
GDVILGLASS GVHSNGFSLV RKIVELSGLD WSAAAPFAER RLLGEALLEP TRIYVKPLLK
AIRETGAIKA LAHITGGGFP ENIPRVLPKH LAAEIDLDAV KVPPVFSWLA KTGGVESREM
LRTFNCGVGM IAVVAAENVA AVSEALEAEG ETVITLGRMI VRDEGAAGTV YKGTLAI
