KAD1_RABIT
ID KAD1_RABIT Reviewed; 194 AA.
AC P00569;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 110.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RX PubMed=6089869; DOI=10.1021/bi00306a012;
RA Kuby S.A., Palmieri R.H., Frischat A., Fischer A.H., Wu L.H., Maland L.,
RA Manship M.;
RT "Studies on adenosine triphosphate transphosphorylases. Amino acid sequence
RT of rabbit muscle ATP-AMP transphosphorylase.";
RL Biochemistry 23:2393-2399(1984).
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 PIR; A00680; KIRBA.
DR AlphaFoldDB; P00569; -.
DR BMRB; P00569; -.
DR SMR; P00569; -.
DR STRING; 9986.ENSOCUP00000004478; -.
DR BindingDB; P00569; -.
DR ChEMBL; CHEMBL5709; -.
DR iPTMnet; P00569; -.
DR eggNOG; KOG3079; Eukaryota.
DR InParanoid; P00569; -.
DR SABIO-RK; P00569; -.
DR Proteomes; UP000001811; Unplaced.
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-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 Acetylation; ATP-binding; Cytoplasm; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..194
FT /note="Adenylate kinase isoenzyme 1"
FT /id="PRO_0000158913"
FT REGION 38..67
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT REGION 131..141
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 18..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 39
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 44
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 65..67
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 94..97
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 101
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 138
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 149
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171,
FT ECO:0000269|PubMed:6089869"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00568"
SQ SEQUENCE 194 AA; 21638 MW; B579871616963214 CRC64;
MEEKLKKAKI IFVVGGPGSG KGTQCEKIVH KYGYTHLSTG DLLRAEVSSG SARGKKLSEI
MEKGQLVPLE TVLDMLRDAM VAKADTSKGF LIDGYPRQVQ QGEEFERRIA QPTLLLYVDA
GPETMQKRLL KRGETSGRVD DNEETIKKRL ETYYKATEPV IAFYEKRGIV RKVNAEGSVD
NVFSQVCTHL DALK
