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Database: UniProt
Entry: O51378
LinkDB: O51378
Original site: O51378 
ID   KAD_BORBU               Reviewed;         211 AA.
AC   O51378;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   08-MAY-2019, entry version 124.
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=BB_0417;
OS   Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM
OS   4680).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / B31 / CIP 102532 / DSM 4680;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K.,
RA   Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D.,
RA   Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A.,
RA   Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K.,
RA   Roberts K.M., Hatch B., Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia
RT   burgdorferi.";
RL   Nature 390:580-586(1997).
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:0000255|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:0000255|HAMAP-Rule:MF_00235};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway;
CC       AMP from ADP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00235}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00235}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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. Some bacteria have
CC       evolved a zinc-coordinating structure that stabilizes the LID
CC       domain. {ECO:0000255|HAMAP-Rule:MF_00235}.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00235}.
DR   EMBL; AE000783; AAC66782.1; -; Genomic_DNA.
DR   PIR; H70151; H70151.
DR   RefSeq; NP_212551.1; NC_001318.1.
DR   RefSeq; WP_002655966.1; NC_001318.1.
DR   SMR; O51378; -.
DR   PRIDE; O51378; -.
DR   EnsemblBacteria; AAC66782; AAC66782; BB_0417.
DR   GeneID; 1195255; -.
DR   KEGG; bbu:BB_0417; -.
DR   PATRIC; fig|224326.49.peg.811; -.
DR   eggNOG; ENOG4105CC8; Bacteria.
DR   eggNOG; COG0563; LUCA.
DR   KO; K00939; -.
DR   OMA; EKFTSQG; -.
DR   UniPathway; UPA00588; UER00649.
DR   Proteomes; UP000001807; 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; IPR036193; ADK_active_lid_dom_sf.
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   SUPFAM; SSF57774; SSF57774; 1.
DR   TIGRFAMs; TIGR01351; adk; 1.
DR   PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Kinase; Metal-binding;
KW   Nucleotide biosynthesis; Nucleotide-binding; Reference proteome;
KW   Transferase; Zinc.
FT   CHAIN         1    211       Adenylate kinase.
FT                                /FTId=PRO_0000158737.
FT   NP_BIND      10     15       ATP. {ECO:0000255|HAMAP-Rule:MF_00235}.
FT   NP_BIND      57     59       AMP. {ECO:0000255|HAMAP-Rule:MF_00235}.
FT   NP_BIND      85     88       AMP. {ECO:0000255|HAMAP-Rule:MF_00235}.
FT   NP_BIND     131    132       ATP. {ECO:0000255|HAMAP-Rule:MF_00235}.
FT   REGION       30     59       NMPbind. {ECO:0000255|HAMAP-
FT                                Rule:MF_00235}.
FT   REGION      121    158       LID. {ECO:0000255|HAMAP-Rule:MF_00235}.
FT   METAL       125    125       Zinc; structural. {ECO:0000255|HAMAP-
FT                                Rule:MF_00235}.
FT   METAL       128    128       Zinc; structural. {ECO:0000255|HAMAP-
FT                                Rule:MF_00235}.
FT   METAL       145    145       Zinc; structural. {ECO:0000255|HAMAP-
FT                                Rule:MF_00235}.
FT   METAL       148    148       Zinc; structural. {ECO:0000255|HAMAP-
FT                                Rule:MF_00235}.
FT   BINDING      31     31       AMP. {ECO:0000255|HAMAP-Rule:MF_00235}.
FT   BINDING      36     36       AMP. {ECO:0000255|HAMAP-Rule:MF_00235}.
FT   BINDING      92     92       AMP. {ECO:0000255|HAMAP-Rule:MF_00235}.
FT   BINDING     122    122       ATP. {ECO:0000255|HAMAP-Rule:MF_00235}.
FT   BINDING     155    155       AMP. {ECO:0000255|HAMAP-Rule:MF_00235}.
FT   BINDING     166    166       AMP. {ECO:0000255|HAMAP-Rule:MF_00235}.
FT   BINDING     194    194       ATP; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00235}.
SQ   SEQUENCE   211 AA;  24099 MW;  1F4EF1AEDF116911 CRC64;
     MGLVFLGPPG SGKGTISKII SNEFKYQHIS TGDLFRENIL NSTALGQEIK KIVERGELVP
     DLITIKIVED KIKAIKKNKD FILDGFPRNI CQAEALDKFL PNVKIINFLI DEELVIKRLS
     GRRICKSCNN IFNIYTLTTK KNGICDVCGG DLYQREDDKE ECLKTRLKEY KLQTKPLIEF
     YSKCSRLNNV DASVKIDEIK KKIIKIMLKK N
//
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