(data stored in ACNUC7421 zone)

SWISSPROT: KAD_ECO27

ID   KAD_ECO27               Reviewed;         214 AA.
AC   B7UKF4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 63.
DE   RecName: Full=Adenylate kinase {ECO:0000255|HAMAP-Rule:MF_00235};
DE            Short=AK {ECO:0000255|HAMAP-Rule:MF_00235};
DE            EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_00235};
DE   AltName: Full=ATP-AMP transphosphorylase {ECO:0000255|HAMAP-Rule:MF_00235};
DE   AltName: Full=ATP:AMP phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00235};
DE   AltName: Full=Adenylate monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_00235};
GN   Name=adk {ECO:0000255|HAMAP-Rule:MF_00235};
GN   OrderedLocusNames=E2348C_0409;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Catalyzes the reversible transfer of the terminal
CC       phosphate group between ATP and AMP. Plays an important role in
CC       cellular energy homeostasis and in adenine nucleotide metabolism.
CC       {ECO:0000255|HAMAP-Rule:MF_00235}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC         EC=2.7.4.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00235};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway;
CC       AMP from ADP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00235}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00235}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00235}.
CC   -!- DOMAIN: Consists of three domains, a large central CORE domain and
CC       two small peripheral domains, NMPbind and LID, which undergo
CC       movements during catalysis. The LID domain closes over the site of
CC       phosphoryl transfer upon ATP binding. Assembling and dissambling
CC       the active center during each catalytic cycle provides an
CC       effective means to prevent ATP hydrolysis. {ECO:0000255|HAMAP-
CC       Rule:MF_00235}.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00235}.
DR   EMBL; FM180568; CAS07957.1; -; Genomic_DNA.
DR   RefSeq; WP_001313630.1; NC_011601.1.
DR   SMR; B7UKF4; -.
DR   PRIDE; B7UKF4; -.
DR   EnsemblBacteria; CAS07957; CAS07957; E2348C_0409.
DR   KEGG; ecg:E2348C_0409; -.
DR   KO; K00939; -.
DR   OMA; EKFTSQG; -.
DR   BioCyc; ECOL574521:E2348C_RS02145-MONOMER; -.
DR   UniPathway; UPA00588; UER00649.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway.
DR   CDD; cd01428; ADK; 1.
DR   HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR   InterPro; IPR006259; Adenyl_kin_sub.
DR   InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR   InterPro; IPR033690; Adenylat_kinase_CS.
DR   InterPro; IPR007862; Adenylate_kinase_lid-dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23359; PTHR23359; 1.
DR   Pfam; PF05191; ADK_lid; 1.
DR   PRINTS; PR00094; ADENYLTKNASE.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01351; adk; 1.
DR   PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7UKF4.
DR   SWISS-2DPAGE; B7UKF4.
KW   Acetylation; ATP-binding; Complete proteome; Cytoplasm; Kinase;
KW   Nucleotide biosynthesis; Nucleotide-binding; Transferase.
FT   CHAIN         1    214       Adenylate kinase.
FT                                /FTId=PRO_1000191143.
FT   NP_BIND      10     15       ATP. {ECO:0000255|HAMAP-Rule:MF_00235}.
FT   NP_BIND      57     59       AMP. {ECO:0000255|HAMAP-Rule:MF_00235}.
FT   NP_BIND      85     88       AMP. {ECO:0000255|HAMAP-Rule:MF_00235}.
FT   NP_BIND     132    133       ATP. {ECO:0000255|HAMAP-Rule:MF_00235}.
FT   REGION       30     59       NMPbind. {ECO:0000255|HAMAP-
FT                                Rule:MF_00235}.
FT   REGION      122    159       LID.
FT   BINDING      31     31       AMP. {ECO:0000255|HAMAP-Rule:MF_00235}.
FT   BINDING      36     36       AMP. {ECO:0000255|HAMAP-Rule:MF_00235}.
FT   BINDING      92     92       AMP. {ECO:0000255|HAMAP-Rule:MF_00235}.
FT   BINDING     123    123       ATP. {ECO:0000255|HAMAP-Rule:MF_00235}.
FT   BINDING     156    156       AMP. {ECO:0000255|HAMAP-Rule:MF_00235}.
FT   BINDING     167    167       AMP. {ECO:0000255|HAMAP-Rule:MF_00235}.
FT   BINDING     200    200       ATP; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00235}.
FT   MOD_RES     192    192       N6-acetyllysine. {ECO:0000250}.
SQ   SEQUENCE   214 AA;  23542 MW;  BB917C84000A879E CRC64;
     MRIILLGAPG AGKGTQAQFI MEKYGIPQIS TGDMLRAAVK SGSELGKQAK DIMDAGKLVT
     DELVIALVKE RIAQEDCRNG FLLDGFPRTI PQADAMKEAG INVDYVLEFD VPDELIVDRI
     VGRRVHAPSG RVYHVKFNPP KVEGKDDVTG EELTTRKDDQ EETVRKRLVE YHQMTAPLIG
     YYSKEAEAGN TKYAKVDGTK PVAEVRAALE KILG
//

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