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

 F7XUM1_MIDMI            Unreviewed;       217 AA.
F7XUM1;
21-SEP-2011, integrated into UniProtKB/TrEMBL.
21-SEP-2011, sequence version 1.
07-JUN-2017, entry version 47.
RecName: Full=Adenylate kinase {ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS00763757};
Short=AK {ECO:0000256|HAMAP-Rule:MF_00235};
EC=2.7.4.3 {ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS00763757};
AltName: Full=ATP-AMP transphosphorylase {ECO:0000256|HAMAP-Rule:MF_00235};
AltName: Full=ATP:AMP phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00235};
AltName: Full=Adenylate monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_00235};
Name=adk {ECO:0000256|HAMAP-Rule:MF_00235,
ECO:0000313|EMBL:AEI88370.1};
OrderedLocusNames=midi_00044 {ECO:0000313|EMBL:AEI88370.1};
Midichloria mitochondrii (strain IricVA).
Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
Candidatus Midichloriaceae; Candidatus Midichloria.
NCBI_TaxID=696127 {ECO:0000313|EMBL:AEI88370.1, ECO:0000313|Proteomes:UP000006639};
[1] {ECO:0000313|EMBL:AEI88370.1, ECO:0000313|Proteomes:UP000006639}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IricVA {ECO:0000313|EMBL:AEI88370.1,
ECO:0000313|Proteomes:UP000006639};
PubMed=21690562; DOI=10.1093/molbev/msr159;
Sassera D., Lo N., Epis S., D'Auria G., Montagna M., Comandatore F.,
Horner D., Pereto J., Luciano A.M., Franciosi F., Ferri E., Crotti E.,
Bazzocchi C., Daffonchio D., Sacchi L., Moya A., Latorre A., Bandi C.;
"Phylogenomic evidence for the presence of a flagellum and cbb3
oxidase in the free-living mitochondrial ancestor.";
Mol. Biol. Evol. 28:3285-3296(2011).
-!- 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:0000256|HAMAP-Rule:MF_00235}.
-!- CATALYTIC ACTIVITY: ATP + AMP = 2 ADP. {ECO:0000256|HAMAP-
Rule:MF_00235, ECO:0000256|RuleBase:RU003331,
ECO:0000256|SAAS:SAAS00763738}.
-!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway;
AMP from ADP: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00235}.
-!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00235,
ECO:0000256|RuleBase:RU003331}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00235,
ECO:0000256|RuleBase:RU003331}.
-!- 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. {ECO:0000256|HAMAP-
Rule:MF_00235}.
-!- SIMILARITY: Belongs to the adenylate kinase family.
{ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|RuleBase:RU003330}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00235}.
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EMBL; CP002130; AEI88370.1; -; Genomic_DNA.
RefSeq; WP_013950588.1; NC_015722.1.
STRING; 696127.midi_00044; -.
EnsemblBacteria; AEI88370; AEI88370; midi_00044.
KEGG; mmn:midi_00044; -.
eggNOG; ENOG4105CC8; Bacteria.
eggNOG; COG0563; LUCA.
KO; K00939; -.
OMA; RVKNRWI; -.
OrthoDB; POG091H01SU; -.
UniPathway; UPA00588; UER00649.
Proteomes; UP000006639; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-HAMAP.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
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; IPR027417; P-loop_NTPase.
PANTHER; PTHR23359; PTHR23359; 1.
PRINTS; PR00094; ADENYLTKNASE.
SUPFAM; SSF52540; SSF52540; 2.
TIGRFAMs; TIGR01351; adk; 1.
PROSITE; PS00113; ADENYLATE_KINASE; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00235,
ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS00763703};
Complete proteome {ECO:0000313|Proteomes:UP000006639};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00235};
Kinase {ECO:0000256|HAMAP-Rule:MF_00235,
ECO:0000256|RuleBase:RU003330, ECO:0000313|EMBL:AEI88370.1};
Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00235};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00235,
ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS00763703};
Reference proteome {ECO:0000313|Proteomes:UP000006639};
Transferase {ECO:0000256|HAMAP-Rule:MF_00235,
ECO:0000256|RuleBase:RU003330, ECO:0000313|EMBL:AEI88370.1}.
NP_BIND 10 15 ATP. {ECO:0000256|HAMAP-Rule:MF_00235}.
NP_BIND 84 87 AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
REGION 30 59 NMPbind. {ECO:0000256|HAMAP-
Rule:MF_00235}.
REGION 125 162 LID. {ECO:0000256|HAMAP-Rule:MF_00235}.
BINDING 31 31 AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
BINDING 36 36 AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
BINDING 91 91 AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
BINDING 126 126 ATP. {ECO:0000256|HAMAP-Rule:MF_00235}.
BINDING 159 159 AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
BINDING 170 170 AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
BINDING 198 198 ATP; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_00235}.
SEQUENCE 217 AA; 24407 MW; 1D38DCAAF768B276 CRC64;
MRLILLGAPG VGKGTQGMKL AEFYSIPKLS TGEILRNEVN SKTELGLHIA EILKKGMLVS
DGIVEKIVAE KLSNSYGNGF ILDGFPRTLH QAVYLSEILQ ELPVDGTFVI NIEMNFEKLI
PRLSNRVTCA DCVYTFNGDI TDVKLMTCPK CGSKNCYQRD DDKKESIIKR LAVYDELTKP
MIDYYRNQRC WIEVDGDNTI DFVFNSIIAS IKQKIVV


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