(data stored in ACNUC7421 zone)

SWISSPROT: KAD_SALTY

ID   KAD_SALTY               Reviewed;         214 AA.
AC   P0A1V4; P37407;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   11-DEC-2019, entry version 89.
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=STM0488;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RX   PubMed=7814329; DOI=10.1128/jb.177.2.390-400.1995;
RA   Gutierrez J.A., Csonka L.N.;
RT   "Isolation and characterization of adenylate kinase (adk) mutations in
RT   Salmonella typhimurium which block the ability of glycine betaine to
RT   function as an osmoprotectant.";
RL   J. Bacteriol. 177:390-400(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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; L26246; AAA65969.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL19442.1; -; Genomic_DNA.
DR   RefSeq; NP_459483.1; NC_003197.2.
DR   RefSeq; WP_001220237.1; NC_003197.2.
DR   SMR; P0A1V4; -.
DR   PaxDb; P0A1V4; -.
DR   PRIDE; P0A1V4; -.
DR   EnsemblBacteria; AAL19442; AAL19442; STM0488.
DR   GeneID; 1252008; -.
DR   KEGG; stm:STM0488; -.
DR   PATRIC; fig|99287.12.peg.521; -.
DR   eggNOG; ENOG4105CC8; Bacteria.
DR   eggNOG; COG0563; LUCA.
DR   HOGENOM; HOG000238772; -.
DR   KO; K00939; -.
DR   OMA; FHNRMRV; -.
DR   PhylomeDB; P0A1V4; -.
DR   BioCyc; SENT99287:STM0488-MONOMER; -.
DR   UniPathway; UPA00588; UER00649.
DR   Proteomes; UP000001014; 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; P0A1V4.
DR   SWISS-2DPAGE; P0A1V4.
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide biosynthesis;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..214
FT                   /note="Adenylate kinase"
FT                   /id="PRO_0000158842"
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         132..133
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          122..159
FT                   /note="LID"
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         123
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   BINDING         156
FT                   /note="AMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   BINDING         167
FT                   /note="AMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT   BINDING         200
FT                   /note="ATP; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
SQ   SEQUENCE   214 AA;  23488 MW;  57FD9BBA6CA95A3B CRC64;
     MRIILLGAPG AGKGTQAQFI MEKYGIPQIS TGDMLRAAVK SGSELGKQAK DIMDAGKLVT
     DELVIALVKE RIAQEDCRNG FLLDGFPRTI PQADAMKEAG IVVDYVLEFD VPDELIVDRI
     VGRRVHAASG RVYHVKFNPP KVEGKDDVTG EDLTTRKDDQ EETVRKRLVE YHQMTAPLIG
     YYQKEAEAGN TKYAKVDGTQ AVADVRAALE KILG
//

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