PURK_ECOLI
ID PURK_ECOLI Reviewed; 355 AA.
AC P09029; Q2MBQ7;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=N5-carboxyaminoimidazole ribonucleotide synthase {ECO:0000255|HAMAP-Rule:MF_01928, ECO:0000305};
DE Short=N5-CAIR synthase {ECO:0000255|HAMAP-Rule:MF_01928, ECO:0000305};
DE EC=6.3.4.18 {ECO:0000255|HAMAP-Rule:MF_01928, ECO:0000269|PubMed:8117684};
DE AltName: Full=5-(carboxyamino)imidazole ribonucleotide synthetase {ECO:0000255|HAMAP-Rule:MF_01928, ECO:0000305};
GN Name=purK {ECO:0000255|HAMAP-Rule:MF_01928};
GN OrderedLocusNames=b0522 {ECO:0000312|EMBL:AAC73624.1},
GN JW0511 {ECO:0000312|EMBL:BAE76299.1};
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=2464576; DOI=10.1128/jb.171.1.205-212.1989;
RA Tiedeman A.A., Keyhani J., Kamholz J., Daum H.A. III, Gots J.S.,
RA Smith J.M.;
RT "Nucleotide sequence analysis of the purEK operon encoding 5'-
RT phosphoribosyl-5-aminoimidazole carboxylase of Escherichia coli K-12.";
RL J. Bacteriol. 171:205-212(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2644189; DOI=10.1128/jb.171.1.198-204.1989;
RA Watanabe W., Sampei G., Aiba A., Mizobuchi K.;
RT "Identification and sequence analysis of Escherichia coli purE and purK
RT genes encoding 5'-phosphoribosyl-5-amino-4-imidazole carboxylase for de
RT novo purine biosynthesis.";
RL J. Bacteriol. 171:198-204(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP PROTEIN SEQUENCE OF 1-20.
RX PubMed=1534690; DOI=10.1021/bi00136a016;
RA Meyer E., Leonard N.J., Bhat B., Stubbe J., Smith J.M.;
RT "Purification and characterization of the purE, purK, and purC gene
RT products: identification of a previously unrecognized energy requirement in
RT the purine biosynthetic pathway.";
RL Biochemistry 31:5022-5032(1992).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND PATHWAY.
RX PubMed=8117684; DOI=10.1021/bi00174a038;
RA Mueller E.J., Meyer E., Rudolph J., Davisson V.J., Stubbe J.;
RT "N5-carboxyaminoimidazole ribonucleotide: evidence for a new intermediate
RT and two new enzymatic activities in the de novo purine biosynthetic pathway
RT of Escherichia coli.";
RL Biochemistry 33:2269-2278(1994).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ATP ANALOG, AND
RP SUBUNIT.
RX PubMed=10569930; DOI=10.1021/bi991618s;
RA Thoden J.B., Kappock T.J., Stubbe J., Holden H.M.;
RT "Three-dimensional structure of N5-carboxyaminoimidazole ribonucleotide
RT synthetase: a member of the ATP grasp protein superfamily.";
RL Biochemistry 38:15480-15492(1999).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH ATP, AND SUBUNIT.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=19053251; DOI=10.1021/bi801734z;
RA Thoden J.B., Holden H.M., Firestine S.M.;
RT "Structural analysis of the active site geometry of N5-
RT carboxyaminoimidazole ribonucleotide synthetase from Escherichia coli.";
RL Biochemistry 47:13346-13353(2008).
CC -!- FUNCTION: Catalyzes the ATP-dependent conversion of 5-aminoimidazole
CC ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole
CC ribonucleotide (N5-CAIR). {ECO:0000255|HAMAP-Rule:MF_01928,
CC ECO:0000269|PubMed:8117684}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ATP +
CC hydrogencarbonate = 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole +
CC ADP + 2 H(+) + phosphate; Xref=Rhea:RHEA:19317, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58730, ChEBI:CHEBI:137981, ChEBI:CHEBI:456216;
CC EC=6.3.4.18; Evidence={ECO:0000255|HAMAP-Rule:MF_01928,
CC ECO:0000269|PubMed:8117684};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-
CC phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2.
CC {ECO:0000255|HAMAP-Rule:MF_01928, ECO:0000269|PubMed:8117684}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01928,
CC ECO:0000269|PubMed:10569930, ECO:0000269|PubMed:19053251}.
CC -!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000255|HAMAP-
CC Rule:MF_01928, ECO:0000305}.
CC -!- CAUTION: Was originally thought to be the ATPase subunit of
CC phosphoribosylaminoimidazole carboxylase, with catalytic subunit PurE.
CC {ECO:0000305|PubMed:2464576}.
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DR EMBL; X12982; CAA31421.1; -; Genomic_DNA.
DR EMBL; M19657; AAA24450.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40275.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73624.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76299.1; -; Genomic_DNA.
DR PIR; JU0001; DCECPK.
DR RefSeq; NP_415055.1; NC_000913.3.
DR RefSeq; WP_000815571.1; NZ_LN832404.1.
DR PDB; 1B6R; X-ray; 2.10 A; A=1-355.
DR PDB; 1B6S; X-ray; 2.50 A; A/B/C/D=1-355.
DR PDB; 3ETH; X-ray; 1.60 A; A/B=1-355.
DR PDB; 3ETJ; X-ray; 1.60 A; A/B=1-355.
DR PDBsum; 1B6R; -.
DR PDBsum; 1B6S; -.
DR PDBsum; 3ETH; -.
DR PDBsum; 3ETJ; -.
DR AlphaFoldDB; P09029; -.
DR SMR; P09029; -.
DR BioGRID; 4259875; 17.
DR IntAct; P09029; 5.
DR STRING; 511145.b0522; -.
DR SWISS-2DPAGE; P09029; -.
DR jPOST; P09029; -.
DR PaxDb; P09029; -.
DR PRIDE; P09029; -.
DR EnsemblBacteria; AAC73624; AAC73624; b0522.
DR EnsemblBacteria; BAE76299; BAE76299; BAE76299.
DR GeneID; 945153; -.
DR KEGG; ecj:JW0511; -.
DR KEGG; eco:b0522; -.
DR PATRIC; fig|1411691.4.peg.1756; -.
DR EchoBASE; EB0789; -.
DR eggNOG; COG0026; Bacteria.
DR HOGENOM; CLU_011534_0_0_6; -.
DR InParanoid; P09029; -.
DR OMA; ITFDHEH; -.
DR PhylomeDB; P09029; -.
DR BioCyc; EcoCyc:PURK-MON; -.
DR BioCyc; MetaCyc:PURK-MON; -.
DR BRENDA; 6.3.4.18; 2026.
DR SABIO-RK; P09029; -.
DR UniPathway; UPA00074; UER00942.
DR EvolutionaryTrace; P09029; -.
DR PRO; PR:P09029; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0034028; F:5-(carboxyamino)imidazole ribonucleotide synthase activity; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; IDA:EcoliWiki.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1490.20; -; 1.
DR HAMAP; MF_01928; PurK; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR003135; ATP-grasp_carboxylate-amine.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR005875; PurK.
DR InterPro; IPR040686; PurK_C.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR Pfam; PF02222; ATP-grasp; 1.
DR Pfam; PF17769; PurK_C; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR TIGRFAMs; TIGR01161; purK; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; Ligase;
KW Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..355
FT /note="N5-carboxyaminoimidazole ribonucleotide synthase"
FT /id="PRO_0000074997"
FT DOMAIN 84..267
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928,
FT ECO:0000269|PubMed:10569930, ECO:0000269|PubMed:19053251"
FT BINDING 120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928,
FT ECO:0000269|PubMed:10569930, ECO:0000269|PubMed:19053251"
FT BINDING 125..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928,
FT ECO:0000269|PubMed:10569930, ECO:0000269|PubMed:19053251"
FT BINDING 153..156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928,
FT ECO:0000269|PubMed:10569930, ECO:0000269|PubMed:19053251"
FT BINDING 161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928,
FT ECO:0000269|PubMed:10569930, ECO:0000269|PubMed:19053251"
FT BINDING 184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928,
FT ECO:0000269|PubMed:10569930, ECO:0000269|PubMed:19053251"
FT BINDING 237..238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928,
FT ECO:0000269|PubMed:10569930, ECO:0000269|PubMed:19053251"
FT CONFLICT 64..65
FT /note="RH -> PD (in Ref. 1; CAA31421)"
FT /evidence="ECO:0000305"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:3ETH"
FT HELIX 11..20
FT /evidence="ECO:0007829|PDB:3ETH"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:3ETH"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:3ETH"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:3ETH"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:3ETJ"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:3ETH"
FT HELIX 57..63
FT /evidence="ECO:0007829|PDB:3ETH"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:3ETH"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:3ETH"
FT HELIX 80..89
FT /evidence="ECO:0007829|PDB:3ETH"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:3ETH"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:3ETH"
FT HELIX 106..113
FT /evidence="ECO:0007829|PDB:3ETH"
FT STRAND 115..124
FT /evidence="ECO:0007829|PDB:3ETH"
FT TURN 127..130
FT /evidence="ECO:0007829|PDB:3ETH"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:3ETH"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:1B6S"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:3ETH"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:3ETH"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:3ETH"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:3ETH"
FT STRAND 159..168
FT /evidence="ECO:0007829|PDB:3ETH"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3ETH"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:3ETH"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:3ETH"
FT HELIX 200..217
FT /evidence="ECO:0007829|PDB:3ETH"
FT STRAND 221..230
FT /evidence="ECO:0007829|PDB:3ETH"
FT STRAND 233..242
FT /evidence="ECO:0007829|PDB:3ETH"
FT HELIX 245..249
FT /evidence="ECO:0007829|PDB:3ETH"
FT HELIX 250..253
FT /evidence="ECO:0007829|PDB:3ETH"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:3ETH"
FT HELIX 258..266
FT /evidence="ECO:0007829|PDB:3ETH"
FT STRAND 280..287
FT /evidence="ECO:0007829|PDB:3ETH"
FT HELIX 292..296
FT /evidence="ECO:0007829|PDB:3ETH"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:3ETH"
FT STRAND 314..321
FT /evidence="ECO:0007829|PDB:3ETH"
FT HELIX 325..335
FT /evidence="ECO:0007829|PDB:3ETH"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:3ETH"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:3ETH"
FT HELIX 344..353
FT /evidence="ECO:0007829|PDB:3ETH"
SQ SEQUENCE 355 AA; 39461 MW; 93464E111E29AD9C CRC64;
MKQVCVLGNG QLGRMLRQAG EPLGIAVWPV GLDAEPAAVP FQQSVITAEI ERWPETALTR
ELARHPAFVN RDVFPIIADR LTQKQLFDKL HLPTAPWQLL AERSEWPAVF DRLGELAIVK
RRTGGYDGRG QWRLRANETE QLPAECYGEC IVEQGINFSG EVSLVGARGF DGSTVFYPLT
HNLHQDGILR TSVAFPQANA QQQAQAEEML SAIMQELGYV GVMAMECFVT PQGLLINELA
PRVHNSGHWT QNGASISQFE LHLRAITDLP LPQPVVNNPS VMINLIGSDV NYDWLKLPLV
HLHWYDKEVR PGRKVGHLNL TDSDTSRLTA TLEALIPLLP PEYASGVIWA QSKFG
