KAD1_CHICK
ID KAD1_CHICK Reviewed; 194 AA.
AC P05081;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 130.
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 EC=2.7.4.6 {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};
DE AltName: Full=Myokinase {ECO:0000255|HAMAP-Rule:MF_03171};
GN Name=AK1 {ECO:0000255|HAMAP-Rule:MF_03171};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Muscle;
RX PubMed=2419325; DOI=10.1016/s0021-9258(17)35877-5;
RA Kishi F., Maruyama M., Tanizawa Y., Nakazawa A.;
RT "Isolation and characterization of cDNA for chicken muscle adenylate
RT kinase.";
RL J. Biol. Chem. 261:2942-2945(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Muscle;
RX PubMed=2844738; DOI=10.1093/oxfordjournals.jbchem.a122315;
RA Suminami Y., Kishi F., Torigoe T., Nakazawa A.;
RT "Structure and complete nucleotide sequence of the gene encoding chicken
RT cytosolic adenylate kinase.";
RL J. Biochem. 103:611-617(1988).
RN [3]
RP MUTAGENESIS OF LYS-22 AND LYS-28.
RX PubMed=2161682; DOI=10.1021/bi00470a006;
RA Tian G.C., Yan H.G., Jiang R.T., Kishi F., Nakazawa A., Tsai M.D.;
RT "Mechanism of adenylate kinase. Are the essential lysines essential?";
RL Biochemistry 29:4296-4304(1990).
CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate
CC group between ATP and AMP. Also displays broad nucleoside diphosphate
CC kinase activity. Plays an important role in cellular energy homeostasis
CC and in adenine nucleotide metabolism.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-
CC deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316,
CC ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03171};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-
CC triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03171};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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; M12153; AAB59961.1; -; mRNA.
DR EMBL; D00251; BAA00182.1; -; Genomic_DNA.
DR PIR; A25327; A25327.
DR RefSeq; NP_990440.1; NM_205109.2.
DR AlphaFoldDB; P05081; -.
DR SMR; P05081; -.
DR STRING; 9031.ENSGALP00000042094; -.
DR Ensembl; ENSGALT00000043760; ENSGALP00000042094; ENSGALG00000029150.
DR Ensembl; ENSGALT00000097345; ENSGALP00000068126; ENSGALG00000029150.
DR Ensembl; ENSGALT00000102583; ENSGALP00000067246; ENSGALG00000029150.
DR Ensembl; ENSGALT00000103661; ENSGALP00000071483; ENSGALG00000029150.
DR GeneID; 396002; -.
DR KEGG; gga:396002; -.
DR CTD; 203; -.
DR VEuPathDB; HostDB:geneid_396002; -.
DR eggNOG; KOG3079; Eukaryota.
DR GeneTree; ENSGT00940000158325; -.
DR HOGENOM; CLU_032354_0_3_1; -.
DR InParanoid; P05081; -.
DR OMA; TQCDRMI; -.
DR OrthoDB; 1378291at2759; -.
DR PhylomeDB; P05081; -.
DR BRENDA; 2.7.4.3; 1306.
DR Reactome; R-GGA-499943; Interconversion of nucleotide di- and triphosphates.
DR SABIO-RK; P05081; -.
DR PRO; PR:P05081; -.
DR Proteomes; UP000000539; Chromosome 17.
DR Bgee; ENSGALG00000029150; Expressed in muscle tissue and 14 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; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; ISS:UniProtKB.
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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..194
FT /note="Adenylate kinase isoenzyme 1"
FT /id="PRO_0000158915"
FT REGION 39..68
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT REGION 132..142
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 19..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 40
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 45
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 66..68
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 95..98
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 102
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 139
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 150
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT MUTAGEN 22
FT /note="K->M: Reduced activity."
FT /evidence="ECO:0000269|PubMed:2161682"
FT MUTAGEN 28
FT /note="K->M: No loss in activity."
FT /evidence="ECO:0000269|PubMed:2161682"
SQ SEQUENCE 194 AA; 21683 MW; 7DCAEF3E1DD474EC CRC64;
MSTEKLKHHK IIFVVGGPGS GKGTQCEKIV HKYGYTHLST GDLLRAEVSS GSERGKKLQA
IMEKGELVPL DTVLDMLRDA MLAKADTSKG FLIDGYPREV KQGEEFEKKI APPTLLLYVD
AGKETMVKRL LKRGETSGRV DDNEETIKKR LETYYKATEP VIAFYKGRGI VRQLNAEGTV
DEVFQQVCSY LDKL
