(data stored in SCRATCH3701 zone)

SWISSPROT: KAD_SYNS3

ID   KAD_SYNS3               Reviewed;         183 AA.
AC   Q0ID24;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   11-DEC-2019, entry version 83.
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}; OrderedLocusNames=sync_0418;
OS   Synechococcus sp. (strain CC9311).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=64471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9311;
RX   PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA   Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA   Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA   Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA   Paulsen I.T.;
RT   "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT   coastal environment.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
CC   -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate
CC       group between ATP and AMP. Plays an important role in cellular energy
CC       homeostasis and in adenine nucleotide metabolism. {ECO:0000255|HAMAP-
CC       Rule:MF_00235}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00235};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC       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 two
CC       small peripheral domains, NMPbind and LID, which undergo movements
CC       during catalysis. The LID domain closes over the site of phosphoryl
CC       transfer upon ATP binding. Assembling and dissambling the active center
CC       during each catalytic cycle provides an effective means to prevent ATP
CC       hydrolysis. {ECO:0000255|HAMAP-Rule:MF_00235}.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00235}.
DR   EMBL; CP000435; ABI47824.1; -; Genomic_DNA.
DR   RefSeq; WP_011618383.1; NC_008319.1.
DR   SMR; Q0ID24; -.
DR   STRING; 64471.sync_0418; -.
DR   EnsemblBacteria; ABI47824; ABI47824; sync_0418.
DR   KEGG; syg:sync_0418; -.
DR   eggNOG; ENOG4105CC8; Bacteria.
DR   eggNOG; COG0563; LUCA.
DR   HOGENOM; HOG000238772; -.
DR   KO; K00939; -.
DR   OMA; FHNRMRV; -.
DR   OrthoDB; 1491686at2; -.
DR   BioCyc; SSP64471:G1G72-406-MONOMER; -.
DR   UniPathway; UPA00588; UER00649.
DR   Proteomes; UP000001961; 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; IPR000850; Adenylat/UMP-CMP_kin.
DR   InterPro; IPR033690; Adenylat_kinase_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23359; PTHR23359; 1.
DR   PRINTS; PR00094; ADENYLTKNASE.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q0ID24.
DR   SWISS-2DPAGE; Q0ID24.
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide biosynthesis;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..183
FT                   /note="Adenylate kinase"
FT                   /id="PRO_1000058926"
FT   NP_BIND         12..17
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   NP_BIND         59..61
FT                   /note="AMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   NP_BIND         86..89
FT                   /note="AMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   REGION          32..61
FT                   /note="NMPbind"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   REGION          127..133
FT                   /note="LID"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   BINDING         33
FT                   /note="AMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   BINDING         38
FT                   /note="AMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   BINDING         93
FT                   /note="AMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   BINDING         128
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   BINDING         130
FT                   /note="AMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   BINDING         141
FT                   /note="AMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   BINDING         169
FT                   /note="ATP; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
SQ   SEQUENCE   183 AA;  19813 MW;  FE727636E702DCBF CRC64;
     MKQRLLFLGP PGAGKGTQAA LLCDRHGLRH LSTGDLLRAE VSAGSALGQE AESVMNRGEL
     VSDSLVLAIV KAQLGALNGQ GWLLDGFPRN VAQAEALDPL LQELNQPIEA VVLLELDDAV
     LIERLLSRGR DDDNEAVIRN RLVVYADKTE PLIEHYRQRG LLQSVEAHGS IEAITERIEG
     VLA
//

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