(data stored in ACNUC7421 zone)

SWISSPROT: KAD_DESOH

ID   KAD_DESOH               Reviewed;         224 AA.
AC   A8ZTL5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   11-DEC-2019, entry version 67.
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=Dole_0469;
OS   Desulfococcus oleovorans (strain DSM 6200 / Hxd3).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulfococcus.
OX   NCBI_TaxID=96561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6200 / Hxd3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Wawrik B.,
RA   Richardson P.;
RT   "Complete sequence of Desulfococcus oleovorans Hxd3.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000859; ABW66279.1; -; Genomic_DNA.
DR   RefSeq; WP_012173898.1; NC_009943.1.
DR   SMR; A8ZTL5; -.
DR   STRING; 96561.Dole_0469; -.
DR   PRIDE; A8ZTL5; -.
DR   EnsemblBacteria; ABW66279; ABW66279; Dole_0469.
DR   KEGG; dol:Dole_0469; -.
DR   eggNOG; ENOG4105CC8; Bacteria.
DR   eggNOG; COG0563; LUCA.
DR   HOGENOM; HOG000238772; -.
DR   KO; K00939; -.
DR   OMA; VKNRWIH; -.
DR   OrthoDB; 1491686at2; -.
DR   BioCyc; DOLE96561:G1GAC-483-MONOMER; -.
DR   UniPathway; UPA00588; UER00649.
DR   Proteomes; UP000008561; 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; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23359; PTHR23359; 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; A8ZTL5.
DR   SWISS-2DPAGE; A8ZTL5.
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide biosynthesis;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..224
FT                   /note="Adenylate kinase"
FT                   /id="PRO_1000100558"
FT   NP_BIND         10..15
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   NP_BIND         57..59
FT                   /note="AMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   NP_BIND         85..88
FT                   /note="AMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   REGION          30..59
FT                   /note="NMPbind"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   REGION          126..165
FT                   /note="LID"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   BINDING         31
FT                   /note="AMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   BINDING         36
FT                   /note="AMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   BINDING         92
FT                   /note="AMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   BINDING         127
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   BINDING         162
FT                   /note="AMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   BINDING         174
FT                   /note="AMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   BINDING         211
FT                   /note="ATP; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
SQ   SEQUENCE   224 AA;  24744 MW;  050527C875E4930B CRC64;
     MNILFFGPNG SGKGTQGAIL KEKYSLPHIE SGAIFRENIS KGTELGAKAK EYIDRGDLVP
     DDITIPMILD RLQQDDCKKG WLLDGFPRNK VQAETLDATL KKANMALDIV VEIELDREIA
     KNRIMGRRLC VNDNNHPNNI FIDAIKPDGD KCRVCGGELK TRSDDQDEAA IDKRHNIYYD
     TETGTLAAAY YFRDLAAKGG SLKYITLDGA PGVKEVAAEL VSKL
//

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