KAD1_CAEEL
ID KAD1_CAEEL Reviewed; 210 AA.
AC Q20140;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Adenylate kinase isoenzyme 1 {ECO:0000255|HAMAP-Rule:MF_03171};
DE Short=AK 1 {ECO:0000255|HAMAP-Rule:MF_03171};
DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_03171};
DE AltName: Full=ATP-AMP transphosphorylase 1 {ECO:0000255|HAMAP-Rule:MF_03171};
DE AltName: Full=ATP:AMP phosphotransferase {ECO:0000255|HAMAP-Rule:MF_03171};
DE AltName: Full=Adenylate monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_03171};
GN ORFNames=F38B2.4;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Bristol N2;
RA Kohara Y., Shin-i T., Suzuki Y., Sugano S., Potdevin M., Thierry-Mieg Y.,
RA Thierry-Mieg D., Thierry-Mieg J.;
RT "The Caenorhabditis elegans transcriptome project, a complementary view of
RT the genome.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-
CC Rule:MF_03171}.
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:0000255|HAMAP-Rule:MF_03171};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03171}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03171}.
CC -!- DOMAIN: Consists of three domains, a large central CORE domain and two
CC small peripheral domains, NMPbind and LID, which undergo movements
CC during catalysis. The LID domain closes over the site of phosphoryl
CC transfer upon ATP binding. Assembling and dissambling the active center
CC during each catalytic cycle provides an effective means to prevent ATP
CC hydrolysis. {ECO:0000255|HAMAP-Rule:MF_03171}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03171}.
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DR EMBL; Z50045; CAA90364.1; -; Genomic_DNA.
DR EMBL; AF304123; AAG50236.1; -; mRNA.
DR PIR; T21947; T21947.
DR RefSeq; NP_001257141.1; NM_001270212.1.
DR AlphaFoldDB; Q20140; -.
DR SMR; Q20140; -.
DR BioGRID; 46227; 18.
DR IntAct; Q20140; 1.
DR STRING; 6239.F38B2.4a; -.
DR EPD; Q20140; -.
DR PaxDb; Q20140; -.
DR PeptideAtlas; Q20140; -.
DR EnsemblMetazoa; F38B2.4a.1; F38B2.4a.1; WBGene00009531.
DR GeneID; 181317; -.
DR KEGG; cel:CELE_F38B2.4; -.
DR UCSC; F38B2.4; c. elegans.
DR CTD; 181317; -.
DR WormBase; F38B2.4a; CE02218; WBGene00009531; -.
DR eggNOG; KOG3079; Eukaryota.
DR GeneTree; ENSGT00940000158325; -.
DR HOGENOM; CLU_032354_0_3_1; -.
DR InParanoid; Q20140; -.
DR OMA; TQCDRMI; -.
DR OrthoDB; 1378291at2759; -.
DR PhylomeDB; Q20140; -.
DR BRENDA; 2.7.4.3; 1045.
DR Reactome; R-CEL-499943; Interconversion of nucleotide di- and triphosphates.
DR PRO; PR:Q20140; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00009531; Expressed in larva and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; 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:0004550; F:nucleoside diphosphate kinase activity; IEA:InterPro.
DR GO; GO:0006172; P:ADP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046033; P:AMP metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046034; P:ATP metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; IBA:GO_Central.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; IBA:GO_Central.
DR CDD; cd01428; ADK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR HAMAP; MF_03171; Adenylate_kinase_AK1; 1.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR033690; Adenylat_kinase_CS.
DR InterPro; IPR028582; AK1.
DR InterPro; IPR006267; AK1/5.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359; PTHR23359; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01360; aden_kin_iso1; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..210
FT /note="Adenylate kinase isoenzyme 1"
FT /id="PRO_0000158932"
FT REGION 50..79
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT REGION 144..154
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 30..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 51
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 56
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 77..79
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 107..110
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 114
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 145
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 151
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 162
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 190
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
SQ SEQUENCE 210 AA; 22597 MW; 786CB879D83DDFFC CRC64;
MAPTVERKNI NLAPLKAAGV PIFFIVGGPG SGKGTQCDKI VAKYGLTHLS SGDLLRDEVK
SGSPRGAQLT AIMESGALVP LEVVLDLVKE AMLKAIEKGS KGFLIDGYPR EVAQGQQFES
EIQEAKLVLF FDVAEETLVK RLLHRAQTSG RADDNADTIK KRLHTFVTST APVVDYYESK
GKLVRINAEG SVDDIFAVVV ANLDKATSKL
