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Adenylate kinase (AK) (EC 2.7.4.3) (ATP-AMP transphosphorylase) (ATP:AMP phosphotransferase) (Adenylate monophosphate kinase)

 KAD_ORITB               Reviewed;         210 AA.
A5CCJ2;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
12-JUN-2007, sequence version 1.
25-OCT-2017, entry version 70.
RecName: Full=Adenylate kinase {ECO:0000255|HAMAP-Rule:MF_00235};
Short=AK {ECO:0000255|HAMAP-Rule:MF_00235};
EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_00235};
AltName: Full=ATP-AMP transphosphorylase {ECO:0000255|HAMAP-Rule:MF_00235};
AltName: Full=ATP:AMP phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00235};
AltName: Full=Adenylate monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_00235};
Name=adk {ECO:0000255|HAMAP-Rule:MF_00235};
OrderedLocusNames=OTBS_0356;
Orientia tsutsugamushi (strain Boryong) (Rickettsia tsutsugamushi).
Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
Rickettsiaceae; Rickettsieae; Orientia.
NCBI_TaxID=357244;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Boryong;
PubMed=17483455; DOI=10.1073/pnas.0611553104;
Cho N.-H., Kim H.-R., Lee J.-H., Kim S.-Y., Kim J., Cha S., Kim S.-Y.,
Darby A.C., Fuxelius H.-H., Yin J., Kim J.H., Kim J., Lee S.J.,
Koh Y.-S., Jang W.-J., Park K.-H., Andersson S.G.E., Choi M.-S.,
Kim I.-S.;
"The Orientia tsutsugamushi genome reveals massive proliferation of
conjugative type IV secretion system and host-cell interaction
genes.";
Proc. Natl. Acad. Sci. U.S.A. 104:7981-7986(2007).
-!- FUNCTION: Catalyzes the reversible transfer of the terminal
phosphate group between ATP and AMP. Plays an important role in
cellular energy homeostasis and in adenine nucleotide metabolism.
{ECO:0000255|HAMAP-Rule:MF_00235}.
-!- CATALYTIC ACTIVITY: ATP + AMP = 2 ADP. {ECO:0000255|HAMAP-
Rule:MF_00235}.
-!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway;
AMP from ADP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00235}.
-!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00235}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00235}.
-!- DOMAIN: Consists of three domains, a large central CORE domain and
two small peripheral domains, NMPbind and LID, which undergo
movements during catalysis. The LID domain closes over the site of
phosphoryl transfer upon ATP binding. Assembling and dissambling
the active center during each catalytic cycle provides an
effective means to prevent ATP hydrolysis. Some bacteria have
evolved a zinc-coordinating structure that stabilizes the LID
domain. {ECO:0000255|HAMAP-Rule:MF_00235}.
-!- SIMILARITY: Belongs to the adenylate kinase family.
{ECO:0000255|HAMAP-Rule:MF_00235}.
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EMBL; AM494475; CAM79422.1; -; Genomic_DNA.
ProteinModelPortal; A5CCJ2; -.
SMR; A5CCJ2; -.
STRING; 357244.OTBS_0356; -.
EnsemblBacteria; CAM79422; CAM79422; OTBS_0356.
KEGG; ots:OTBS_0356; -.
eggNOG; ENOG4105CC8; Bacteria.
eggNOG; COG0563; LUCA.
HOGENOM; HOG000238772; -.
KO; K00939; -.
OMA; EKFTSQG; -.
OrthoDB; POG091H01SU; -.
UniPathway; UPA00588; UER00649.
Proteomes; UP000001565; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-EC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway.
CDD; cd01428; ADK; 1.
HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
InterPro; IPR006259; Adenyl_kin_sub.
InterPro; IPR000850; Adenylat/UMP-CMP_kin.
InterPro; IPR033690; Adenylat_kinase_CS.
InterPro; IPR007862; Adenylate_kinase_lid-dom.
InterPro; IPR036193; ADK_active_lid_dom_sf.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR23359; PTHR23359; 1.
Pfam; PF05191; ADK_lid; 1.
PRINTS; PR00094; ADENYLTKNASE.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF57774; SSF57774; 1.
TIGRFAMs; TIGR01351; adk; 1.
PROSITE; PS00113; ADENYLATE_KINASE; 1.
3: Inferred from homology;
ATP-binding; Complete proteome; Cytoplasm; Kinase; Metal-binding;
Nucleotide biosynthesis; Nucleotide-binding; Reference proteome;
Transferase; Zinc.
CHAIN 1 210 Adenylate kinase.
/FTId=PRO_1000021752.
NP_BIND 10 15 ATP. {ECO:0000255|HAMAP-Rule:MF_00235}.
NP_BIND 55 57 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}.
NP_BIND 83 86 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}.
NP_BIND 130 131 ATP. {ECO:0000255|HAMAP-Rule:MF_00235}.
REGION 28 57 NMPbind. {ECO:0000255|HAMAP-
Rule:MF_00235}.
REGION 120 158 LID. {ECO:0000255|HAMAP-Rule:MF_00235}.
METAL 124 124 Zinc; structural. {ECO:0000255|HAMAP-
Rule:MF_00235}.
METAL 127 127 Zinc; structural. {ECO:0000255|HAMAP-
Rule:MF_00235}.
METAL 144 144 Zinc; structural. {ECO:0000255|HAMAP-
Rule:MF_00235}.
METAL 147 147 Zinc; structural. {ECO:0000255|HAMAP-
Rule:MF_00235}.
BINDING 34 34 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}.
BINDING 90 90 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}.
BINDING 121 121 ATP. {ECO:0000255|HAMAP-Rule:MF_00235}.
BINDING 155 155 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}.
BINDING 166 166 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}.
BINDING 194 194 ATP; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_00235}.
SEQUENCE 210 AA; 23647 MW; 868AC2B76875B225 CRC64;
MILVFIGPPG SGKGTQASLL SEKFSIISVG KVLRTVMESN TAEADVVKKF IKSGKLVPSN
ITNKIVVNAL KNIEQCKSII LDGYPRDIFQ ADFLQENLQM DFKVLFFDID DAVVLRRLRG
RISCTDCGTI YNKLYCMPKI NGVCDICNSS SFQNRVDDDE SIIKLRLESY KKETLPLLEF
YKAQNKLTLI DANQSTENIL KKIKKMSGIY


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