PUR5_STAES
ID PUR5_STAES Reviewed; 343 AA.
AC Q8CT29;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase;
DE EC=6.3.3.1;
DE AltName: Full=AIR synthase;
DE AltName: Full=AIRS;
DE AltName: Full=Phosphoribosyl-aminoimidazole synthetase;
GN Name=purM; OrderedLocusNames=SE_0769;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AIR synthase family. {ECO:0000305}.
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DR EMBL; AE015929; AAO04366.1; -; Genomic_DNA.
DR RefSeq; NP_764324.1; NC_004461.1.
DR RefSeq; WP_001831685.1; NZ_WBME01000028.1.
DR AlphaFoldDB; Q8CT29; -.
DR SMR; Q8CT29; -.
DR STRING; 176280.SE_0769; -.
DR EnsemblBacteria; AAO04366; AAO04366; SE_0769.
DR GeneID; 50019091; -.
DR KEGG; sep:SE_0769; -.
DR PATRIC; fig|176280.10.peg.741; -.
DR eggNOG; COG0150; Bacteria.
DR HOGENOM; CLU_047116_0_0_9; -.
DR OMA; EPLFMTD; -.
DR UniPathway; UPA00074; UER00129.
DR Proteomes; UP000001411; 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.
FT CHAIN 1..343
FT /note="Phosphoribosylformylglycinamidine cyclo-ligase"
FT /id="PRO_0000148251"
SQ SEQUENCE 343 AA; 37391 MW; EDA595E1C7ADDBD1 CRC64;
MSKAYEESGV NIQAGYEAVE RITSHVERTL RKEVLGGLGG FGATFDLSQL KMKAPVLVSG
TDGVGTKLKL AIDYGKHDTI GIDAVAMCVN DILTTGAEPL YFLDYIATNK VVPSTIEQIV
KGISDGCEQT NTALIGGETA EMGEMYHEGE YDIAGFAVGA VEKEDYIDGS NVEEGQAIIG
LASSGIHSNG YSLVRKMIKE SGVQLHDQFN GQTFLETFLA PTKLYVKPIL ELKKHIDIKA
MSHITGGGFY ENIPRALPKG LSAKIDTQSF PTLEVFNWLQ KQGNISTNEM YNIFNMGIGY
TIIVDKKDVQ TTLTTLRAMD TTAYEIGEII KDDDTPIHLL EVE
