(data stored in ACNUC7421 zone)

SWISSPROT: KAD_EXIS2

ID   KAD_EXIS2               Reviewed;         215 AA.
AC   B1YGX1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   11-DEC-2019, entry version 82.
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=Exig_0117;
OS   Exiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15).
OC   Bacteria; Firmicutes; Bacilli; Bacillales;
OC   Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX   NCBI_TaxID=262543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17290 / JCM 13490 / 255-15;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C.,
RA   Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T.,
RA   Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15.";
RL   Submitted (APR-2008) 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. Some bacteria have evolved a zinc-coordinating structure
CC       that stabilizes the LID domain. {ECO:0000255|HAMAP-Rule:MF_00235}.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00235}.
DR   EMBL; CP001022; ACB59604.1; -; Genomic_DNA.
DR   RefSeq; WP_012369030.1; NC_010556.1.
DR   SMR; B1YGX1; -.
DR   STRING; 262543.Exig_0117; -.
DR   EnsemblBacteria; ACB59604; ACB59604; Exig_0117.
DR   KEGG; esi:Exig_0117; -.
DR   eggNOG; ENOG4105CC8; Bacteria.
DR   eggNOG; COG0563; LUCA.
DR   HOGENOM; HOG000238772; -.
DR   KO; K00939; -.
DR   OMA; FHNRMRV; -.
DR   OrthoDB; 1491686at2; -.
DR   UniPathway; UPA00588; UER00649.
DR   Proteomes; UP000001681; 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:0008270; F:zinc ion 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; B1YGX1.
DR   SWISS-2DPAGE; B1YGX1.
KW   ATP-binding; Cytoplasm; Kinase; Metal-binding; Nucleotide biosynthesis;
KW   Nucleotide-binding; Transferase; Zinc.
FT   CHAIN           1..215
FT                   /note="Adenylate kinase"
FT                   /id="PRO_1000100563"
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   NP_BIND         136..137
FT                   /note="ATP"
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..163
FT                   /note="LID"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   METAL           130
FT                   /note="Zinc; structural"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   METAL           133
FT                   /note="Zinc; structural"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   METAL           150
FT                   /note="Zinc; structural"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   METAL           153
FT                   /note="Zinc; structural"
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         160
FT                   /note="AMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   BINDING         171
FT                   /note="AMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   BINDING         199
FT                   /note="ATP; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
SQ   SEQUENCE   215 AA;  23637 MW;  83F737EAA6FFE0E7 CRC64;
     MNLVLMGLPG AGKGTQAAKI IEDYAIPHIS TGDMFRAAIK DQTPLGQEAK SYMDKGELVP
     DEVTIGIVRE RLAKEDCANG FLLDGFPRTV KQADALEVLL ADLNKQIDHV VHIGVNPEKL
     VPRLTGRRIC PTCGATYHVI YNPPKVEGVC DIDGSALVQR EDDQEETVRR RLEVNVAQAQ
     PLIDFYAEKG YLRNLDGDRP INEVYSDVQA LLGGQ
//

If you have problems or comments...

PBIL Back to PBIL home page