ID PUR5_AGRFC Reviewed; 357 AA. AC Q8UG98; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2003, sequence version 2. DT 27-MAR-2024, entry version 107. 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}; GN OrderedLocusNames=Atu1141; ORFNames=AGR_C_2111; OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens OS (strain C58)). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium; OC Agrobacterium tumefaciens complex. OX NCBI_TaxID=176299; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C58 / ATCC 33970; RX PubMed=11743193; DOI=10.1126/science.1066804; RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K., RA Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y., RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P., RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R., RA Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G., RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y., RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S., RA Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F., RA Gordon M.P., Olson M.V., Nester E.W.; RT "The genome of the natural genetic engineer Agrobacterium tumefaciens RT C58."; RL Science 294:2317-2323(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C58 / ATCC 33970; RX PubMed=11743194; DOI=10.1126/science.1066803; RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B., RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K., RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M., RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C., RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.; RT "Genome sequence of the plant pathogen and biotechnology agent RT Agrobacterium tumefaciens C58."; RL Science 294:2323-2328(2001). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE007869; AAK86944.2; -; Genomic_DNA. DR PIR; AD2717; AD2717. DR PIR; G97498; G97498. DR RefSeq; NP_354159.2; NC_003062.2. DR RefSeq; WP_006312859.1; NC_003062.2. DR AlphaFoldDB; Q8UG98; -. DR SMR; Q8UG98; -. DR STRING; 176299.Atu1141; -. DR EnsemblBacteria; AAK86944; AAK86944; Atu1141. DR KEGG; atu:Atu1141; -. DR PATRIC; fig|176299.10.peg.1158; -. DR eggNOG; COG0150; Bacteria. DR HOGENOM; CLU_047116_0_0_5; -. DR OrthoDB; 9777881at2; -. DR PhylomeDB; Q8UG98; -. DR BioCyc; AGRO:ATU1141-MONOMER; -. DR UniPathway; UPA00074; UER00129. DR Proteomes; UP000000813; Chromosome circular. 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; 3.90.650.10; 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 3: Inferred from homology; KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Purine biosynthesis; KW Reference proteome. FT CHAIN 1..357 FT /note="Phosphoribosylformylglycinamidine cyclo-ligase" FT /id="PRO_0000148193" SQ SEQUENCE 357 AA; 36799 MW; C57C009287B9B9CF CRC64; MSQSGKNGLT YSDAGVDIDA GNLMVEKIKP AVRSTRRPGA DGEIGGFGGL FDLKAAGFTD PVLVAANDGV GTKLKIAIDA DYHDTVGIDL VAMCVNDLVV QGAEPLFFLD YFATGKLDPD QGAAIVSGIA AGCRESGCAL IGGETAEMPG MYSDGDYDLA GFAVGAAERG QLLPAGDIAE GDVILGLSSS GVHSNGFSLV RKIVSLSGLE WSAPAPFADG KKLGEALLTP TRIYVKPLLK AIRETGALKA LAHITGGGFP ENIPRVLPKH LAAEIDLAAI KVPAVFSWLA KTGGVEAHEM LRTFNCGVGM IVVVSAENAT KVTEALTAEG ETVFPLGRMV AREDGAHGTI YKGTLGL //