KAD1_PIG
ID KAD1_PIG Reviewed; 194 AA.
AC P00571;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 145.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RC TISSUE=Skeletal muscle;
RX PubMed=4366177; DOI=10.1111/j.1432-1033.1974.tb03393.x;
RA Heil A., Mueller G., Noda L., Pinder T., Schirmer R.H., Schirmer I.,
RA von Zabern I.;
RT "The amino-acid sequence of sarcine adenylate kinase from skeletal
RT muscle.";
RL Eur. J. Biochem. 43:131-144(1974).
RN [2]
RP ATP-BINDING SITE.
RX PubMed=2869483; DOI=10.1073/pnas.83.4.907;
RA Fry D.C., Kuby S.A., Mildvan A.S.;
RT "ATP-binding site of adenylate kinase: mechanistic implications of its
RT homology with ras-encoded p21, F1-ATPase, and other nucleotide-binding
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:907-911(1986).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=4367210; DOI=10.1038/250120a0;
RA Schulz G.E., Elzinga M., Marx F., Schirmer R.H.;
RT "Three dimensional structure of adenyl kinase.";
RL Nature 250:120-123(1974).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=2832612; DOI=10.1016/0022-2836(88)90319-1;
RA Dreusicke D., Karplus P.A., Schulz G.E.;
RT "Refined structure of porcine cytosolic adenylate kinase at 2.1 A
RT resolution.";
RL J. Mol. Biol. 199:359-371(1988).
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. {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 -!- 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. {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 ECO:0000305|PubMed:2832612, ECO:0000305|PubMed:4367210}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03171}.
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DR PIR; A00682; KIPGA.
DR RefSeq; XP_003122225.3; XM_003122177.5.
DR RefSeq; XP_005660509.1; XM_005660452.2.
DR PDB; 3ADK; X-ray; 2.10 A; A=1-194.
DR PDBsum; 3ADK; -.
DR AlphaFoldDB; P00571; -.
DR SMR; P00571; -.
DR STRING; 9823.ENSSSCP00000006028; -.
DR iPTMnet; P00571; -.
DR PaxDb; P00571; -.
DR PeptideAtlas; P00571; -.
DR PRIDE; P00571; -.
DR Ensembl; ENSSSCT00015081508; ENSSSCP00015032986; ENSSSCG00015060480.
DR Ensembl; ENSSSCT00025061292; ENSSSCP00025026029; ENSSSCG00025045130.
DR Ensembl; ENSSSCT00030102473; ENSSSCP00030047275; ENSSSCG00030073169.
DR Ensembl; ENSSSCT00035030554; ENSSSCP00035011914; ENSSSCG00035023319.
DR Ensembl; ENSSSCT00045014609; ENSSSCP00045010135; ENSSSCG00045008653.
DR Ensembl; ENSSSCT00050017947; ENSSSCP00050007413; ENSSSCG00050013292.
DR Ensembl; ENSSSCT00055035865; ENSSSCP00055028487; ENSSSCG00055017917.
DR Ensembl; ENSSSCT00055035936; ENSSSCP00055028537; ENSSSCG00055017917.
DR Ensembl; ENSSSCT00055035994; ENSSSCP00055028584; ENSSSCG00055017917.
DR Ensembl; ENSSSCT00065104781; ENSSSCP00065046509; ENSSSCG00065075808.
DR GeneID; 100521423; -.
DR KEGG; ssc:100521423; -.
DR CTD; 203; -.
DR eggNOG; KOG3079; Eukaryota.
DR HOGENOM; CLU_032354_0_3_1; -.
DR InParanoid; P00571; -.
DR OrthoDB; 1378291at2759; -.
DR TreeFam; TF354283; -.
DR Reactome; R-SSC-499943; Interconversion of nucleotide di- and triphosphates.
DR EvolutionaryTrace; P00571; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P00571; SS.
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 3D-structure; Acetylation; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..194
FT /note="Adenylate kinase isoenzyme 1"
FT /id="PRO_0000158912"
FT REGION 38..67
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171,
FT ECO:0000269|PubMed:2832612, ECO:0000269|PubMed:4367210"
FT REGION 131..141
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171,
FT ECO:0000269|PubMed:2832612, ECO:0000269|PubMed:4367210"
FT BINDING 18..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171,
FT ECO:0000269|PubMed:2869483"
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:4366177"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT HELIX 2..6
FT /evidence="ECO:0007829|PDB:3ADK"
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:3ADK"
FT HELIX 21..31
FT /evidence="ECO:0007829|PDB:3ADK"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:3ADK"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:3ADK"
FT HELIX 52..61
FT /evidence="ECO:0007829|PDB:3ADK"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:3ADK"
FT HELIX 69..81
FT /evidence="ECO:0007829|PDB:3ADK"
FT TURN 82..86
FT /evidence="ECO:0007829|PDB:3ADK"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:3ADK"
FT HELIX 99..108
FT /evidence="ECO:0007829|PDB:3ADK"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:3ADK"
FT HELIX 122..136
FT /evidence="ECO:0007829|PDB:3ADK"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:3ADK"
FT HELIX 158..164
FT /evidence="ECO:0007829|PDB:3ADK"
FT TURN 165..168
FT /evidence="ECO:0007829|PDB:3ADK"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:3ADK"
FT HELIX 179..191
FT /evidence="ECO:0007829|PDB:3ADK"
SQ SEQUENCE 194 AA; 21639 MW; 554202B49B1E74B4 CRC64;
MEEKLKKSKI IFVVGGPGSG KGTQCEKIVQ KYGYTHLSTG DLLRAEVSSG SARGKMLSEI
MEKGQLVPLE TVLDMLRDAM VAKVDTSKGF LIDGYPREVK QGEEFERKIG QPTLLLYVDA
GPETMTKRLL KRGETSGRVD DNEETIKKRL ETYYKATEPV IAFYEKRGIV RKVNAEGSVD
DVFSQVCTHL DTLK
