KADY_CAEEL
ID KADY_CAEEL Reviewed; 222 AA.
AC Q09629;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Probable adenylate kinase isoenzyme ZK673.2;
DE Short=AK;
DE EC=2.7.4.3;
DE AltName: Full=ATP-AMP transphosphorylase;
DE AltName: Full=ATP:AMP phosphotransferase;
DE AltName: Full=Adenylate monophosphate kinase;
GN ORFNames=ZK673.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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.
CC {ECO:0000250|UniProtKB:P69441}.
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:0000250|UniProtKB:P69441};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P69441}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P69441}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000305}.
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DR EMBL; Z48585; CAA88479.1; -; Genomic_DNA.
DR PIR; T27960; T27960.
DR RefSeq; NP_496245.1; NM_063844.4.
DR AlphaFoldDB; Q09629; -.
DR SMR; Q09629; -.
DR STRING; 6239.ZK673.2; -.
DR EPD; Q09629; -.
DR PaxDb; Q09629; -.
DR PeptideAtlas; Q09629; -.
DR EnsemblMetazoa; ZK673.2.1; ZK673.2.1; WBGene00014058.
DR GeneID; 174608; -.
DR KEGG; cel:CELE_ZK673.2; -.
DR UCSC; ZK673.2.1; c. elegans.
DR CTD; 174608; -.
DR WormBase; ZK673.2; CE01714; WBGene00014058; -.
DR eggNOG; KOG3078; Eukaryota.
DR GeneTree; ENSGT00940000175921; -.
DR HOGENOM; CLU_032354_1_1_1; -.
DR InParanoid; Q09629; -.
DR OMA; HIARGTE; -.
DR OrthoDB; 1004067at2759; -.
DR PhylomeDB; Q09629; -.
DR Reactome; R-CEL-499943; Interconversion of nucleotide di- and triphosphates.
DR Reactome; R-CEL-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:Q09629; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00014058; Expressed in larva and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0004017; F:adenylate kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046899; F:nucleoside triphosphate adenylate kinase activity; IBA:GO_Central.
DR GO; GO:0046033; P:AMP metabolic process; IBA:GO_Central.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01428; ADK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
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 PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..222
FT /note="Probable adenylate kinase isoenzyme ZK673.2"
FT /id="PRO_0000158934"
FT REGION 34..63
FT /note="NMP"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 123..160
FT /note="LID"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 11..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 40
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 61..63
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 87..90
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 94
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 157
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 168
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
SQ SEQUENCE 222 AA; 24904 MW; B1F2AB913854334A CRC64;
MYRVLLSGAA GSGKGTIARM LVREFEPLGF NYFAAGDFIR DHIARGTEFG VRAQSFLNKG
EHVPDSILNG AILAEMLKAG PRVVLDGYPR NMSQLKMVEE QAPLNLIVEL KVPRKVLIDR
LSKQLVHPAS GRAYNLEVNP PKEEGKDDIT GEPLFKRSTD QLEVARRRLE VYDKTENKVL
DYYKKQNKCI TMSGESSKAV FESVAEVMRR DLLTTTPRTA YA
