PUR5_SYNJA
ID PUR5_SYNJA Reviewed; 351 AA.
AC Q2JQY9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 93.
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}; OrderedLocusNames=CYA_2883;
OS Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone
OS A-Prime).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=321327;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-3-3Ab;
RX PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT "Population level functional diversity in a microbial community revealed by
RT comparative genomic and metagenomic analyses.";
RL ISME J. 1:703-713(2007).
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; CP000239; ABD00983.1; -; Genomic_DNA.
DR RefSeq; WP_011431653.1; NC_007775.1.
DR AlphaFoldDB; Q2JQY9; -.
DR SMR; Q2JQY9; -.
DR STRING; 321327.CYA_2883; -.
DR EnsemblBacteria; ABD00983; ABD00983; CYA_2883.
DR KEGG; cya:CYA_2883; -.
DR eggNOG; COG0150; Bacteria.
DR HOGENOM; CLU_047116_0_0_3; -.
DR OMA; EPLFMTD; -.
DR OrthoDB; 923547at2; -.
DR UniPathway; UPA00074; UER00129.
DR Proteomes; UP000008818; Chromosome.
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..351
FT /note="Phosphoribosylformylglycinamidine cyclo-ligase"
FT /id="PRO_1000148305"
SQ SEQUENCE 351 AA; 37868 MW; 9B982EBDAA0E7101 CRC64;
MDYRSAGVDI ELGRAFVKGI RERVEGSQAQ SSGSSGTLGG IGGFAGLLEL PAGYRAPVLV
AGTDGVGTKL EIAQQWGQHR GVGIDLVAMC VNDVLTVGAR PLFFLDYIAT GKLEPEALWQ
VIDGILEGCQ EAGCQLLGGE TAEMPGFYPP GKYDLAGFCV GIVERADVLD SSRVQLGDRL
WALPSSGLHS NGFSLVRRIV AERGWPWDHQ PPGWDRPLAE VFLTPTRIYV QAVQRLQAAG
IPLHGMAHIT GGGIPENLPR CLAPEQAARL EPHSWPIPPE FLWLQEQGQV ETLEMFNTFN
LGVGYVLVIP PEAENRLRSL LPEAFPIGEV VPARPGESRV LGLEEWGSLV P