PUR5_SHIFL
ID PUR5_SHIFL Reviewed; 345 AA.
AC Q83QL4;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 119.
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=SF2543, S2692;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(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 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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAN44044.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAP17854.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005674; AAN44044.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE014073; AAP17854.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_708337.1; NC_004337.2.
DR RefSeq; WP_001295474.1; NZ_UIQL01000001.1.
DR AlphaFoldDB; Q83QL4; -.
DR SMR; Q83QL4; -.
DR STRING; 198214.SF2543; -.
DR EnsemblBacteria; AAN44044; AAN44044; SF2543.
DR EnsemblBacteria; AAP17854; AAP17854; S2692.
DR GeneID; 1024382; -.
DR GeneID; 66673636; -.
DR KEGG; sfl:SF2543; -.
DR KEGG; sfx:S2692; -.
DR PATRIC; fig|198214.7.peg.3039; -.
DR HOGENOM; CLU_047116_0_0_6; -.
DR OrthoDB; 923547at2; -.
DR UniPathway; UPA00074; UER00129.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..345
FT /note="Phosphoribosylformylglycinamidine cyclo-ligase"
FT /id="PRO_0000148244"
SQ SEQUENCE 345 AA; 36873 MW; 2DBC0975E81815D7 CRC64;
MTDKTSLSYK DAGVDIDAGN ALVGRIKGVV KKTRRPEVMG GLGGFGALCA LPQKYREPVL
VSGTDGVGTK LRLAMDLKRH DTIGIDLVAM CVNDLVVQGA EPLFFLDYYA TGKLDVDTAS
AVISGIAEGC LQSGCSLVGG ETAEMPGMYH GEDYDVAGFC VGVVEKSEII DGSKVSDGDV
LIALGSSGPH SNGYSLVRKI LEVSGCDPQT TELDGKPLAD HLLAPTRIYV KSVLELIEKV
DVHAIAHLTG GGFWENIPRV LPDNTQAVID ESSWQWPEVF NWLQTAGNVE RHEMYRTFNC
GVGMIIALPA PEVDKALALL NANGENAWKI GIIKASDSEQ RVVIE
