(data stored in ACNUC10821 zone)

SWISSPROT: C8U2G0_ECO10

ID   C8U2G0_ECO10            Unreviewed;       214 AA.
AC   C8U2G0;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 72.
DE   RecName: Full=Adenylate kinase {ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS00914410};
DE            Short=AK {ECO:0000256|HAMAP-Rule:MF_00235};
DE            EC=2.7.4.3 {ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS00763757};
DE   AltName: Full=ATP-AMP transphosphorylase {ECO:0000256|HAMAP-Rule:MF_00235};
DE   AltName: Full=ATP:AMP phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00235};
DE   AltName: Full=Adenylate monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_00235};
GN   Name=adk {ECO:0000256|HAMAP-Rule:MF_00235,
GN   ECO:0000313|EMBL:BAI29318.1};
GN   OrderedLocusNames=ECO103_0450 {ECO:0000313|EMBL:BAI29318.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29318.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29318.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(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:0000256|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:0000256|HAMAP-Rule:MF_00235,
CC         ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS01123758};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway;
CC       AMP from ADP: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00235,
CC       ECO:0000256|SAAS:SAAS00914379}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00235,
CC       ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS00914390}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00235,
CC       ECO:0000256|RuleBase:RU003331}.
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:0000256|HAMAP-
CC       Rule:MF_00235}.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|RuleBase:RU003330}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00235}.
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DR   EMBL; AP010958; BAI29318.1; -; Genomic_DNA.
DR   RefSeq; WP_001220233.1; NC_013353.1.
DR   SMR; C8U2G0; -.
DR   EnsemblBacteria; BAI29318; BAI29318; ECO103_0450.
DR   KEGG; eoh:ECO103_0450; -.
DR   HOGENOM; HOG000238772; -.
DR   KO; K00939; -.
DR   OMA; EKFTSQG; -.
DR   BioCyc; ECOL585395:ECO103_RS02355-MONOMER; -.
DR   UniPathway; UPA00588; UER00649.
DR   Proteomes; UP000000959; 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; C8U2G0.
DR   SWISS-2DPAGE; C8U2G0.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00235,
KW   ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS00763703};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00235};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00235,
KW   ECO:0000256|RuleBase:RU003330, ECO:0000313|EMBL:BAI29318.1};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00235,
KW   ECO:0000256|SAAS:SAAS00914406};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00235,
KW   ECO:0000256|RuleBase:RU003331};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00235,
KW   ECO:0000256|RuleBase:RU003330}.
FT   DOMAIN      123    158       ADK_lid. {ECO:0000259|Pfam:PF05191}.
FT   NP_BIND      10     15       ATP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   NP_BIND      57     59       AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   NP_BIND      85     88       AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   NP_BIND     132    133       ATP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   REGION       30     59       NMPbind. {ECO:0000256|HAMAP-Rule:
FT                                MF_00235}.
FT   REGION      122    159       LID. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   BINDING      31     31       AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   BINDING      36     36       AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   BINDING      92     92       AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   BINDING     123    123       ATP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   BINDING     156    156       AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   BINDING     167    167       AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   BINDING     200    200       ATP; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00235}.
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
//

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