PUR5_BACAN
ID PUR5_BACAN Reviewed; 346 AA.
AC Q81ZH0; Q6I4B7; Q6KY19;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 131.
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=BA_0296, GBAA_0296, BAS0283;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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; AE016879; AAP24332.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT29383.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT52614.1; -; Genomic_DNA.
DR RefSeq; NP_842846.1; NC_003997.3.
DR RefSeq; WP_001262436.1; NZ_WXXJ01000007.1.
DR RefSeq; YP_026563.1; NC_005945.1.
DR PDB; 2BTU; X-ray; 2.31 A; A/B=1-346.
DR PDBsum; 2BTU; -.
DR AlphaFoldDB; Q81ZH0; -.
DR SMR; Q81ZH0; -.
DR STRING; 261594.GBAA_0296; -.
DR DNASU; 1085673; -.
DR EnsemblBacteria; AAP24332; AAP24332; BA_0296.
DR EnsemblBacteria; AAT29383; AAT29383; GBAA_0296.
DR GeneID; 45020355; -.
DR KEGG; ban:BA_0296; -.
DR KEGG; bar:GBAA_0296; -.
DR KEGG; bat:BAS0283; -.
DR PATRIC; fig|198094.11.peg.287; -.
DR eggNOG; COG0150; Bacteria.
DR HOGENOM; CLU_047116_0_0_9; -.
DR OMA; EPLFMTD; -.
DR UniPathway; UPA00074; UER00129.
DR EvolutionaryTrace; Q81ZH0; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW Purine biosynthesis; Reference proteome.
FT CHAIN 1..346
FT /note="Phosphoribosylformylglycinamidine cyclo-ligase"
FT /id="PRO_0000148194"
FT TURN 19..26
FT /evidence="ECO:0007829|PDB:2BTU"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:2BTU"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:2BTU"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:2BTU"
FT STRAND 53..63
FT /evidence="ECO:0007829|PDB:2BTU"
FT HELIX 68..74
FT /evidence="ECO:0007829|PDB:2BTU"
FT HELIX 80..93
FT /evidence="ECO:0007829|PDB:2BTU"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:2BTU"
FT STRAND 98..110
FT /evidence="ECO:0007829|PDB:2BTU"
FT HELIX 113..130
FT /evidence="ECO:0007829|PDB:2BTU"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:2BTU"
FT STRAND 152..162
FT /evidence="ECO:0007829|PDB:2BTU"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:2BTU"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:2BTU"
FT HELIX 191..199
FT /evidence="ECO:0007829|PDB:2BTU"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:2BTU"
FT HELIX 217..221
FT /evidence="ECO:0007829|PDB:2BTU"
FT HELIX 229..238
FT /evidence="ECO:0007829|PDB:2BTU"
FT HELIX 251..255
FT /evidence="ECO:0007829|PDB:2BTU"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:2BTU"
FT STRAND 264..269
FT /evidence="ECO:0007829|PDB:2BTU"
FT HELIX 277..286
FT /evidence="ECO:0007829|PDB:2BTU"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:2BTU"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:2BTU"
FT STRAND 301..307
FT /evidence="ECO:0007829|PDB:2BTU"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:2BTU"
FT HELIX 312..322
FT /evidence="ECO:0007829|PDB:2BTU"
FT STRAND 326..341
FT /evidence="ECO:0007829|PDB:2BTU"
SQ SEQUENCE 346 AA; 37256 MW; 6A4825D9FF515A43 CRC64;
MANAYKQAGV DIEAGYEAVS RMKKHVQTTM RKEVLGGLGG FGGMFDLSKF ALEEPVLVSG
TDGVGTKLML AFMADKHDTI GIDAVAMCVN DIVVQGAEPL FFLDYIACGK AEPSKIENIV
KGISEGCRQA GCALIGGETA EMPGMYSTEE YDLAGFTVGI VDKKKIVTGE KIEAGHVLIG
LASSGIHSNG YSLVRKVLLE DGELSLDRIY GRLELPLGEE LLKPTKIYVK PILELLKNHE
VYGMAHITGG GFIENIPRML PEGIGAEIEL GSWKIQPIFS LLQEVGKLEE KEMFNIFNMG
IGMVVAVKEE DAKDIVRLLE EQGETARIIG RTVQGAGVTF NGGKAL
