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Database: UniProt
Entry: P09029
LinkDB: P09029
Original site: P09029 
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   13-FEB-2019, entry version 162.
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-
RT   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
RT   purK genes encoding 5'-phosphoribosyl-5-amino-4-imidazole carboxylase
RT   for de 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.,
RA   Mau B., 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
RT   MG1655 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
RT   requirement in 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
RT   intermediate and two new enzymatic activities in the de novo purine
RT   biosynthetic pathway 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
RT   ribonucleotide synthetase: a member of the ATP grasp protein
RT   superfamily.";
RL   Biochemistry 38:15480-15492(1999).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH ATP, AND
RP   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
RT   coli.";
RL   Biochemistry 47:13346-13353(2008).
CC   -!- FUNCTION: Catalyzes the ATP-dependent conversion of 5-
CC       aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-
CC       carboxyaminoimidazole ribonucleotide (N5-CAIR).
CC       {ECO:0000255|HAMAP-Rule:MF_01928, 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-
CC         ribosyl)imidazole + ADP + 2 H(+) + phosphate;
CC         Xref=Rhea:RHEA:19317, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58730,
CC         ChEBI:CHEBI:137981, ChEBI:CHEBI:456216; EC=6.3.4.18;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01928,
CC         ECO:0000269|PubMed:8117684};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-
CC       amino-1-(5-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
CC       PurE. {ECO:0000305|PubMed:2464576}.
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   ProteinModelPortal; P09029; -.
DR   SMR; P09029; -.
DR   BioGrid; 4259875; 17.
DR   IntAct; P09029; 5.
DR   STRING; 316385.ECDH10B_0478; -.
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   EcoGene; EG10796; purK.
DR   eggNOG; ENOG4105CY8; Bacteria.
DR   eggNOG; COG0026; LUCA.
DR   HOGENOM; HOG000034026; -.
DR   InParanoid; P09029; -.
DR   KO; K01589; -.
DR   PhylomeDB; P09029; -.
DR   BioCyc; EcoCyc:PURK-MONOMER; -.
DR   BioCyc; ECOL316407:JW0511-MONOMER; -.
DR   BioCyc; MetaCyc:PURK-MONOMER; -.
DR   BRENDA; 6.3.4.18; 2026.
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; Complete proteome;
KW   Direct protein sequencing; Ligase; Nucleotide-binding;
KW   Purine biosynthesis; Reference proteome.
FT   CHAIN         1    355       N5-carboxyaminoimidazole ribonucleotide
FT                                synthase.
FT                                /FTId=PRO_0000074997.
FT   DOMAIN       84    267       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_01928}.
FT   NP_BIND     125    131       ATP. {ECO:0000255|HAMAP-Rule:MF_01928,
FT                                ECO:0000269|PubMed:10569930,
FT                                ECO:0000269|PubMed:19053251}.
FT   NP_BIND     153    156       ATP. {ECO:0000255|HAMAP-Rule:MF_01928,
FT                                ECO:0000269|PubMed:10569930,
FT                                ECO:0000269|PubMed:19053251}.
FT   NP_BIND     237    238       ATP. {ECO:0000255|HAMAP-Rule:MF_01928,
FT                                ECO:0000269|PubMed:10569930,
FT                                ECO:0000269|PubMed:19053251}.
FT   BINDING      80     80       ATP. {ECO:0000255|HAMAP-Rule:MF_01928,
FT                                ECO:0000269|PubMed:10569930,
FT                                ECO:0000269|PubMed:19053251}.
FT   BINDING     120    120       ATP. {ECO:0000255|HAMAP-Rule:MF_01928,
FT                                ECO:0000269|PubMed:10569930,
FT                                ECO:0000269|PubMed:19053251}.
FT   BINDING     161    161       ATP. {ECO:0000255|HAMAP-Rule:MF_01928,
FT                                ECO:0000269|PubMed:10569930,
FT                                ECO:0000269|PubMed:19053251}.
FT   BINDING     184    184       ATP. {ECO:0000255|HAMAP-Rule:MF_01928,
FT                                ECO:0000269|PubMed:10569930,
FT                                ECO:0000269|PubMed:19053251}.
FT   CONFLICT     64     65       RH -> PD (in Ref. 1; CAA31421).
FT                                {ECO:0000305}.
FT   STRAND        3      8       {ECO:0000244|PDB:3ETH}.
FT   HELIX        11     20       {ECO:0000244|PDB:3ETH}.
FT   HELIX        21     23       {ECO:0000244|PDB:3ETH}.
FT   STRAND       26     30       {ECO:0000244|PDB:3ETH}.
FT   HELIX        36     38       {ECO:0000244|PDB:3ETH}.
FT   HELIX        41     43       {ECO:0000244|PDB:3ETJ}.
FT   STRAND       44     49       {ECO:0000244|PDB:3ETH}.
FT   HELIX        57     63       {ECO:0000244|PDB:3ETH}.
FT   TURN         69     72       {ECO:0000244|PDB:3ETH}.
FT   HELIX        73     78       {ECO:0000244|PDB:3ETH}.
FT   HELIX        80     89       {ECO:0000244|PDB:3ETH}.
FT   STRAND       97    100       {ECO:0000244|PDB:3ETH}.
FT   HELIX       103    105       {ECO:0000244|PDB:3ETH}.
FT   HELIX       106    113       {ECO:0000244|PDB:3ETH}.
FT   STRAND      115    124       {ECO:0000244|PDB:3ETH}.
FT   TURN        127    130       {ECO:0000244|PDB:3ETH}.
FT   STRAND      131    135       {ECO:0000244|PDB:3ETH}.
FT   TURN        136    138       {ECO:0000244|PDB:1B6S}.
FT   HELIX       139    141       {ECO:0000244|PDB:3ETH}.
FT   HELIX       144    146       {ECO:0000244|PDB:3ETH}.
FT   TURN        147    149       {ECO:0000244|PDB:3ETH}.
FT   STRAND      150    154       {ECO:0000244|PDB:3ETH}.
FT   STRAND      159    168       {ECO:0000244|PDB:3ETH}.
FT   STRAND      174    176       {ECO:0000244|PDB:3ETH}.
FT   STRAND      180    185       {ECO:0000244|PDB:3ETH}.
FT   STRAND      188    194       {ECO:0000244|PDB:3ETH}.
FT   HELIX       200    217       {ECO:0000244|PDB:3ETH}.
FT   STRAND      221    230       {ECO:0000244|PDB:3ETH}.
FT   STRAND      233    242       {ECO:0000244|PDB:3ETH}.
FT   HELIX       245    249       {ECO:0000244|PDB:3ETH}.
FT   HELIX       250    253       {ECO:0000244|PDB:3ETH}.
FT   STRAND      254    256       {ECO:0000244|PDB:3ETH}.
FT   HELIX       258    266       {ECO:0000244|PDB:3ETH}.
FT   STRAND      280    287       {ECO:0000244|PDB:3ETH}.
FT   HELIX       292    296       {ECO:0000244|PDB:3ETH}.
FT   STRAND      301    304       {ECO:0000244|PDB:3ETH}.
FT   STRAND      314    321       {ECO:0000244|PDB:3ETH}.
FT   HELIX       325    335       {ECO:0000244|PDB:3ETH}.
FT   HELIX       336    338       {ECO:0000244|PDB:3ETH}.
FT   HELIX       341    343       {ECO:0000244|PDB:3ETH}.
FT   HELIX       344    353       {ECO:0000244|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
//
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