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Database: UniProt
Entry: K0BB29_9ARCH
LinkDB: K0BB29_9ARCH
Original site: K0BB29_9ARCH 
ID   K0BB29_9ARCH            Unreviewed;       192 AA.
AC   K0BB29;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Adenylate kinase {ECO:0000256|ARBA:ARBA00019926, ECO:0000256|HAMAP-Rule:MF_00234};
DE            Short=AK {ECO:0000256|HAMAP-Rule:MF_00234};
DE            EC=2.7.4.3 {ECO:0000256|ARBA:ARBA00012955, ECO:0000256|HAMAP-Rule:MF_00234};
DE   AltName: Full=ATP-AMP transphosphorylase {ECO:0000256|ARBA:ARBA00033336, ECO:0000256|HAMAP-Rule:MF_00234};
GN   Name=adkA {ECO:0000256|HAMAP-Rule:MF_00234};
GN   ORFNames=NSED_01950 {ECO:0000313|EMBL:AFS82200.1};
OS   Candidatus Nitrosopumilus sediminis.
OC   Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC   Nitrosopumilaceae; Nitrosopumilus.
OX   NCBI_TaxID=1229909 {ECO:0000313|EMBL:AFS82200.1, ECO:0000313|Proteomes:UP000006100};
RN   [1] {ECO:0000313|EMBL:AFS82200.1, ECO:0000313|Proteomes:UP000006100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AR2 {ECO:0000313|EMBL:AFS82200.1,
RC   ECO:0000313|Proteomes:UP000006100};
RX   PubMed=23209211; DOI=10.1128/JB.01869-12;
RA   Park S.J., Kim J.G., Jung M.Y., Kim S.J., Cha I.T., Ghai R.,
RA   Martin-Cuadrado A.B., Rodriguez-Valera F., Rhee S.K.;
RT   "Draft Genome Sequence of an Ammonia-Oxidizing Archaeon, "Candidatus
RT   Nitrosopumilus sediminis" AR2, from Svalbard in the Arctic Circle.";
RL   J. Bacteriol. 194:6948-6949(2012).
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:0000256|ARBA:ARBA00000582, ECO:0000256|HAMAP-
CC         Rule:MF_00234};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00234}.
CC   -!- SIMILARITY: Belongs to the archaeal adenylate kinase family.
CC       {ECO:0000256|ARBA:ARBA00007088, ECO:0000256|HAMAP-Rule:MF_00234}.
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DR   EMBL; CP003843; AFS82200.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0BB29; -.
DR   STRING; 1229909.NSED_01950; -.
DR   KEGG; nir:NSED_01950; -.
DR   PATRIC; fig|1229909.8.peg.407; -.
DR   eggNOG; arCOG01039; Archaea.
DR   HOGENOM; CLU_119371_0_0_2; -.
DR   OrthoDB; 26198at2157; -.
DR   Proteomes; UP000006100; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00234; Adenylate_kinase_AdkA; 1.
DR   InterPro; IPR023477; Adenylate_kinase_AdkA.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF13207; AAA_17; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00234};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00234};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00234, ECO:0000313|EMBL:AFS82200.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00234};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00234}.
FT   BINDING         11..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00234"
SQ   SEQUENCE   192 AA;  21375 MW;  8B5A91E16EF12DB9 CRC64;
     MAESKKIVMV GIPGVGKTTL LSKIVEHIKD HQKSIQVISF GTLMFEVAKE NGIKDRDELR
     RLSIPRQQEL QKIAAEKIAS QTEEVVIIDT HAFISSPEGY YPGLPEHVLK IIKPSNFISV
     SAKPEEIYSR RMTDETRNRD KNTIENVKKE LDVQSGMISA CAVITGSPVK HVLNREGKVD
     EAADKIIQSL GL
//
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