Документ взят из кэша поисковой машины. Адрес оригинального документа : http://kodomo.cmm.msu.ru/~vasilisa/kad_ecoli.entret Дата изменения: Sat Oct 6 16:56:48 2007 Дата индексирования: Tue Oct 2 03:48:29 2012 Кодировка: Поисковые слова: m 13

ID KAD_ECOLI Reviewed; 214 AA.
AC P69441; P05082; P77123; Q2MBV3;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 24-JUL-2007, entry version 35.
DE Adenylate kinase (EC 2.7.4.3) (ATP-AMP transphosphorylase) (AK).
GN Name=adk; Synonyms=dnaW, plsA; OrderedLocusNames=b0474, JW0463;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX MEDLINE=86041903; PubMed=2997739; DOI=10.1093/nar/13.19.7139;
RA Brune M., Schumann R., Wittinghofer F.;
RT "Cloning and sequencing of the adenylate kinase gene (adk) of
RT Escherichia coli.";
RL Nucleic Acids Res. 13:7139-7151(1985).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX MEDLINE=97426617; 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 277:1453-1474(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
RT MG1655 and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.
RX MEDLINE=87260952; PubMed=3299380;
RA Bardwell J.C.A., Craig E.A.;
RT "Eukaryotic Mr 83,000 heat shock protein has a homologue in
RT Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5177-5181(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 108-214.
RX MEDLINE=91269316; PubMed=2051480; DOI=10.1016/0022-2836(91)90180-E;
RA Miyamoto K., Nakahigashi K., Nishimura K., Inokuchi H.;
RT "Isolation and characterization of visible light-sensitive mutants of
RT Escherichia coli K12.";
RL J. Mol. Biol. 219:393-398(1991).
RN [7]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX MEDLINE=97443975; PubMed=9298646;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded
RT in the genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [8]
RP PROTEIN SEQUENCE OF 1-11.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.;
RL Submitted (FEB-1996) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 1-4.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX MEDLINE=98263247; PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M.,
RA Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D.,
RA Williams K.L., Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in
RT proteome projects.";
RL J. Mol. Biol. 278:599-608(1998).
RN [10]
RP MUTAGENESIS.
RX MEDLINE=89000670; PubMed=2844237; DOI=10.1021/bi00413a020;
RA Reinstein J., Brune M., Wittinghofer A.;
RT "Mutations in the nucleotide binding loop of adenylate kinase of
RT Escherichia coli.";
RL Biochemistry 27:4712-4720(1988).
RN [11]
RP MUTAGENESIS.
RX MEDLINE=91027759; PubMed=2223776; DOI=10.1021/bi00484a014;
RA Reinstein J., Schlichting I., Wittinghofer A.;
RT "Structurally and catalytically important residues in the phosphate
RT binding loop of adenylate kinase of Escherichia coli.";
RL Biochemistry 29:7451-7459(1990).
RN [12]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10398370;
RX DOI=10.1002/(SICI)1097-0134(19990801)36:2<238::AID-PROT9>3.3.CO;2-B;
RA Munier-Lehmann H., Burlacu-Miron S., Craescu C.T., Mantsch H.H.,
RA Schultz C.P.;
RT "A new subfamily of short bacterial adenylate kinases with the
RT Mycobacterium tuberculosis enzyme as a model: a predictive and
RT experimental study.";
RL Proteins 36:238-248(1999).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF COMPLEX WITH THE INHIBITOR
RP AP5A.
RX MEDLINE=92194314; PubMed=1548697; DOI=10.1016/0022-2836(92)90582-5;
RA Mueller C.W., Schulz G.E.;
RT "Structure of the complex between adenylate kinase from Escherichia
RT coli and the inhibitor Ap5A refined at 1.9-A resolution. A model for a
RT catalytic transition state.";
RL J. Mol. Biol. 224:159-177(1992).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANTS PRO-9 AND GLY-10 IN
RP COMPLEX WITH THE INHIBITOR AP5A.
RX MEDLINE=93197288; PubMed=8451239; DOI=10.1002/prot.340150106;
RA Mueller C.W., Schulz G.E.;
RT "Crystal structures of two mutants of adenylate kinase from
RT Escherichia coli that modify the Gly-loop.";
RL Proteins 15:42-49(1993).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF COMPLEX WITH AMP AND AMPPNP.
RX MEDLINE=95023870; PubMed=7937733; DOI=10.1002/prot.340190304;
RA Berry M.B., Meador B., Bilderback T., Liang P., Glaser M.,
RA Phillips G.N. Jr.;
RT "The closed conformation of a highly flexible protein: the structure
RT of E. coli adenylate kinase with bound AMP and AMPPNP.";
RL Proteins 19:183-198(1994).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RC STRAIN=K12;
RX PubMed=8805521; DOI=10.1016/S0969-2126(96)00018-4;
RA Mueller C.W., Schlauderer G.J., Reinstein J., Schulz G.E.;
RT "Adenylate kinase motions during catalysis: an energetic counterweight
RT balancing substrate binding.";
RL Structure 4:147-156(1996).
CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal
CC phosphate group between ATP and AMP. This small ubiquitous enzyme
CC involved in the energy metabolism and nucleotide synthesis, is
CC essential for maintenance and cell growth.
CC -!- CATALYTIC ACTIVITY: ATP + AMP = 2 ADP.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=51 uM for ATP (at pH 7.4 and 30 degrees Celsius);
CC KM=38 uM for AMP (at pH 7.4 and 30 degrees Celsius);
CC KM=92 uM for ADP (at pH 7.4 and 30 degrees Celsius);
CC Vmax=1020 umol/min/mg enzyme for the forward reaction (at pH 7.4
CC and 30 degrees Celsius);
CC Vmax=605 umol/min/mg enzyme for the reverse reaction (at pH 7.4
CC and 30 degrees Celsius);
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius. Thermostable. Is
CC half-inactivated at 52 degrees Celsius;
CC -!- PATHWAY: Nucleotide metabolism; purine metabolism.
CC -!- SUBUNIT: Monomer.
CC -!- INTERACTION:
CC P0A8T7:rpoC; NbExp=1; IntAct=EBI-543592, EBI-543604;
CC P77806:ybdL; NbExp=1; IntAct=EBI-543592, EBI-543661;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: Consists of three domains, a large central CORE domain and
CC two small peripheral domains, AMP binding and LID. The LID domain
CC closes over the site of phosphoryl transfer upon ATP binding.
CC -!- SIMILARITY: Belongs to the adenylate kinase family.
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DR EMBL; X03038; CAA26840.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40228.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73576.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76253.1; -; Genomic_DNA.
DR EMBL; M38777; AAA23461.1; -; Genomic_DNA.
DR EMBL; D90259; BAA14303.1; -; Genomic_DNA.
DR PIR; A24275; KIECA.
DR PDB; 1AKE; X-ray; A/B=1-214.
DR PDB; 1ANK; X-ray; A/B=-.
DR PDB; 1E4V; X-ray; A/B=1-214.
DR PDB; 1E4Y; X-ray; A/B=1-214.
DR PDB; 2ECK; X-ray; A/B=1-214.
DR PDB; 4AKE; X-ray; A/B=1-214.
DR IntAct; P69441; -.
DR SWISS-2DPAGE; P69441; COLI.
DR ECO2DBASE; F026.0; 6TH EDITION.
DR GenomeReviews; U00096_GR; b0474.
DR GenomeReviews; AP009048_GR; JW0463.
DR KEGG; ecj:JW0463; -.
DR KEGG; eco:b0474; -.
DR EchoBASE; EB0031; -.
DR EcoGene; EG10032; adk.
DR BioCyc; EcoCyc:ADENYL-KIN-MONOMER; -.
DR LinkHub; P69441; -.
DR GO; GO:0005515; F:protein binding; IPI:IntAct.
DR HAMAP; MF_00235; -; 1.
DR InterPro; IPR011769; Ad_Ct_kin_N.
DR InterPro; IPR006259; Adenyl_kin_sub.
DR InterPro; IPR000850; Adenylate_kin.
DR InterPro; IPR007862; ADK_lid.
DR PANTHER; PTHR23359; Adenylate_kin; 1.
DR Pfam; PF00406; ADK; 1.
DR Pfam; PF05191; ADK_lid; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR ProDom; PD000657; Adenylate_kin; 1.
DR TIGRFAMs; TIGR01351; adk; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Kinase; Nucleotide biosynthesis;
KW Nucleotide-binding; Transferase.
FT CHAIN 1 214 Adenylate kinase.
FT /FTId=PRO_0000158767.
FT NP_BIND 7 15 ATP.
FT NP_BIND 31 59 AMP.
FT REGION 122 159 LID.
FT MUTAGEN 9 9 P->G: No loss of enzyme activity.
FT MUTAGEN 10 10 G->V: No loss of enzyme activity.
FT MUTAGEN 13 13 K->Q: Drastic reduction in enzyme
FT activity.
FT STRAND 2 8
FT HELIX 13 24
FT STRAND 28 30
FT HELIX 31 41
FT TURN 44 46
FT HELIX 47 49
FT HELIX 50 55
FT HELIX 61 73
FT HELIX 75 79
FT STRAND 81 85
FT HELIX 90 98
FT STRAND 104 110
FT HELIX 113 115
FT HELIX 116 121
FT STRAND 123 125
FT TURN 127 129
FT STRAND 132 134
FT TURN 135 137
FT TURN 147 149
FT HELIX 161 174
FT TURN 175 177
FT HELIX 178 187
FT STRAND 190 197
FT HELIX 202 213
SQ SEQUENCE 214 AA; 23586 MW; BB917C84000A80EE CRC64;
MRIILLGAPG AGKGTQAQFI MEKYGIPQIS TGDMLRAAVK SGSELGKQAK DIMDAGKLVT
DELVIALVKE RIAQEDCRNG FLLDGFPRTI PQADAMKEAG INVDYVLEFD VPDELIVDRI
VGRRVHAPSG RVYHVKFNPP KVEGKDDVTG EELTTRKDDQ EETVRKRLVE YHQMTAPLIG
YYSKEAEAGN TKYAKVDGTK PVAEVRADLE KILG
//