PUR5_ECOLI
ID PUR5_ECOLI Reviewed; 345 AA.
AC P08178;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase;
DE EC=6.3.3.1 {ECO:0000269|PubMed:3530323};
DE AltName: Full=AIR synthase;
DE AltName: Full=AIRS;
DE AltName: Full=Phosphoribosyl-aminoimidazole synthetase;
GN Name=purM; Synonyms=purG; OrderedLocusNames=b2499, JW2484;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3015935; DOI=10.1016/s0021-9258(18)67432-0;
RA Smith J.M., Daum H.A. III;
RT "Nucleotide sequence of the purM gene encoding 5'-phosphoribosyl-5-
RT aminoimidazole synthetase of Escherichia coli K12.";
RL J. Biol. Chem. 261:10632-10636(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION, AND CATALYTIC ACTIVITY.
RX PubMed=3530323; DOI=10.1021/bi00363a028;
RA Schrimsher J.L., Schendel F.J., Stubbe J., Smith J.M.;
RT "Purification and characterization of aminoimidazole ribonucleotide
RT synthetase from Escherichia coli.";
RL Biochemistry 25:4366-4371(1986).
RN [6]
RP PROTEIN SEQUENCE OF 2-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=10508786; DOI=10.1016/s0969-2126(99)80182-8;
RA Li C., Kappock T.J., Stubbe J., Weaver T.M., Ealick S.E.;
RT "X-ray crystal structure of aminoimidazole ribonucleotide synthetase
RT (PurM), from the Escherichia coli purine biosynthetic pathway at 2.5-A
RT resolution.";
RL Structure 7:1155-1166(1999).
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:0000269|PubMed:3530323};
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:0000305|PubMed:3530323}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:3530323}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the AIR synthase family. {ECO:0000305}.
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DR EMBL; M13747; AAA83898.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75552.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16387.1; -; Genomic_DNA.
DR PIR; A25955; AJECPC.
DR RefSeq; NP_416994.1; NC_000913.3.
DR RefSeq; WP_001336050.1; NZ_LN832404.1.
DR PDB; 1CLI; X-ray; 2.50 A; A/B/C/D=2-345.
DR PDBsum; 1CLI; -.
DR AlphaFoldDB; P08178; -.
DR SMR; P08178; -.
DR BioGRID; 4261439; 54.
DR BioGRID; 851314; 1.
DR IntAct; P08178; 4.
DR STRING; 511145.b2499; -.
DR jPOST; P08178; -.
DR PaxDb; P08178; -.
DR PRIDE; P08178; -.
DR EnsemblBacteria; AAC75552; AAC75552; b2499.
DR EnsemblBacteria; BAA16387; BAA16387; BAA16387.
DR GeneID; 946975; -.
DR KEGG; ecj:JW2484; -.
DR KEGG; eco:b2499; -.
DR PATRIC; fig|1411691.4.peg.4239; -.
DR EchoBASE; EB0791; -.
DR eggNOG; COG0150; Bacteria.
DR HOGENOM; CLU_047116_0_0_6; -.
DR InParanoid; P08178; -.
DR OMA; EPLFMTD; -.
DR PhylomeDB; P08178; -.
DR BioCyc; EcoCyc:AIRS-MON; -.
DR BioCyc; MetaCyc:AIRS-MON; -.
DR BRENDA; 6.3.3.1; 2026.
DR UniPathway; UPA00074; UER00129.
DR EvolutionaryTrace; P08178; -.
DR PRO; PR:P08178; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IBA:GO_Central.
DR GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IDA:EcoCyc.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046084; P:adenine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
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; Direct protein sequencing; Ligase;
KW Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 2..345
FT /note="Phosphoribosylformylglycinamidine cyclo-ligase"
FT /id="PRO_0000148211"
FT CONFLICT 12
FT /note="A -> D (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:1CLI"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:1CLI"
FT HELIX 18..25
FT /evidence="ECO:0007829|PDB:1CLI"
FT HELIX 27..31
FT /evidence="ECO:0007829|PDB:1CLI"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:1CLI"
FT STRAND 42..50
FT /evidence="ECO:0007829|PDB:1CLI"
FT STRAND 56..66
FT /evidence="ECO:0007829|PDB:1CLI"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:1CLI"
FT HELIX 83..95
FT /evidence="ECO:0007829|PDB:1CLI"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1CLI"
FT STRAND 101..113
FT /evidence="ECO:0007829|PDB:1CLI"
FT HELIX 116..133
FT /evidence="ECO:0007829|PDB:1CLI"
FT STRAND 136..144
FT /evidence="ECO:0007829|PDB:1CLI"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:1CLI"
FT STRAND 154..165
FT /evidence="ECO:0007829|PDB:1CLI"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:1CLI"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:1CLI"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:1CLI"
FT HELIX 194..203
FT /evidence="ECO:0007829|PDB:1CLI"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:1CLI"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:1CLI"
FT HELIX 218..223
FT /evidence="ECO:0007829|PDB:1CLI"
FT HELIX 230..239
FT /evidence="ECO:0007829|PDB:1CLI"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:1CLI"
FT HELIX 252..256
FT /evidence="ECO:0007829|PDB:1CLI"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:1CLI"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:1CLI"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:1CLI"
FT HELIX 278..287
FT /evidence="ECO:0007829|PDB:1CLI"
FT HELIX 291..297
FT /evidence="ECO:0007829|PDB:1CLI"
FT STRAND 302..308
FT /evidence="ECO:0007829|PDB:1CLI"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:1CLI"
FT HELIX 313..321
FT /evidence="ECO:0007829|PDB:1CLI"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:1CLI"
FT STRAND 327..335
FT /evidence="ECO:0007829|PDB:1CLI"
FT STRAND 340..343
FT /evidence="ECO:0007829|PDB:1CLI"
SQ SEQUENCE 345 AA; 36854 MW; 8DA61375E8180401 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 HHEMYRTFNC
GVGMIIALPA PEVDKALALL NANGENAWKI GIIKASDSEQ RVVIE
