KAD2_BOVIN
ID KAD2_BOVIN Reviewed; 241 AA.
AC P08166; P08167; Q2KIJ7;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Adenylate kinase 2, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03168};
DE Short=AK 2 {ECO:0000255|HAMAP-Rule:MF_03168};
DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_03168};
DE AltName: Full=ATP-AMP transphosphorylase 2 {ECO:0000255|HAMAP-Rule:MF_03168};
DE AltName: Full=ATP:AMP phosphotransferase {ECO:0000255|HAMAP-Rule:MF_03168};
DE AltName: Full=Adenylate monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_03168};
DE Contains:
DE RecName: Full=Adenylate kinase 2, mitochondrial, N-terminally processed {ECO:0000255|HAMAP-Rule:MF_03168};
GN Name=AK2 {ECO:0000255|HAMAP-Rule:MF_03168};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS AK2A AND AK2B).
RX PubMed=3040716; DOI=10.1016/s0021-9258(18)60880-4;
RA Kishi F., Tanizawa Y., Nakazawa A.;
RT "Isolation and characterization of two types of cDNA for mitochondrial
RT adenylate kinase and their expression in Escherichia coli.";
RL J. Biol. Chem. 262:11785-11789(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2227435; DOI=10.1016/0378-1119(90)90228-j;
RA Tanaka H., Yamada M., Kishi F., Nakazawa A.;
RT "Isolation and characterization of the gene encoding bovine adenylate
RT kinase isozyme 2.";
RL Gene 93:221-227(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM AK2B).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM AK2B).
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 2-239.
RX PubMed=3002789; DOI=10.1111/j.1432-1033.1986.tb09380.x;
RA Frank R., Trosin M., Tomasselli A.G., Noda L., Krauth-Siegel R.L.,
RA Schirmer R.H.;
RT "Mitochondrial adenylate kinase (AK2) from bovine heart. The complete
RT primary structure.";
RL Eur. J. Biochem. 154:205-211(1986).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS), AND DISULFIDE BOND.
RX PubMed=8868479; DOI=10.1002/pro.5560050304;
RA Schlauderer G.J., Schulz G.E.;
RT "The structure of bovine mitochondrial adenylate kinase: comparison with
RT isoenzymes in other compartments.";
RL Protein Sci. 5:434-441(1996).
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. Adenylate kinase
CC activity is critical for regulation of the phosphate utilization and
CC the AMP de novo biosynthesis pathways. Plays a key role in
CC hematopoiesis. {ECO:0000255|HAMAP-Rule:MF_03168}.
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_03168};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=AK2A;
CC IsoId=P08166-1; Sequence=Displayed;
CC Name=AK2B;
CC IsoId=P08166-2; Sequence=VSP_002789;
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.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03168}.
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DR EMBL; M16224; AAA30364.1; -; mRNA.
DR EMBL; M16225; AAA30365.1; -; mRNA.
DR EMBL; D90069; BAA14110.1; -; Genomic_DNA.
DR EMBL; D90069; BAA14109.1; -; Genomic_DNA.
DR EMBL; BT025476; ABF57432.1; -; mRNA.
DR EMBL; BC112613; AAI12614.1; -; mRNA.
DR PIR; B29792; B29792.
DR PIR; JS0422; JS0422.
DR RefSeq; NP_776314.1; NM_173889.1. [P08166-2]
DR RefSeq; XP_005202939.1; XM_005202882.1. [P08166-1]
DR PDB; 1AK2; X-ray; 1.92 A; A=2-233.
DR PDB; 2AK2; X-ray; 2.10 A; A=2-233.
DR PDBsum; 1AK2; -.
DR PDBsum; 2AK2; -.
DR AlphaFoldDB; P08166; -.
DR SMR; P08166; -.
DR IntAct; P08166; 1.
DR STRING; 9913.ENSBTAP00000023406; -.
DR PaxDb; P08166; -.
DR PeptideAtlas; P08166; -.
DR PRIDE; P08166; -.
DR Ensembl; ENSBTAT00000023406; ENSBTAP00000023406; ENSBTAG00000017605. [P08166-2]
DR GeneID; 280716; -.
DR KEGG; bta:280716; -.
DR CTD; 204; -.
DR VEuPathDB; HostDB:ENSBTAG00000017605; -.
DR eggNOG; KOG3078; Eukaryota.
DR GeneTree; ENSGT00940000154576; -.
DR HOGENOM; CLU_032354_1_0_1; -.
DR InParanoid; P08166; -.
DR OMA; FHNRMRV; -.
DR OrthoDB; 1004067at2759; -.
DR TreeFam; TF300896; -.
DR Reactome; R-BTA-499943; Interconversion of nucleotide di- and triphosphates.
DR SABIO-RK; P08166; -.
DR EvolutionaryTrace; P08166; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000017605; Expressed in rumen papilla and 105 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:AgBase.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:AgBase.
DR GO; GO:0004017; F:adenylate kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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: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 HAMAP; MF_03168; Adenylate_kinase_AK2; 1.
DR InterPro; IPR006259; Adenyl_kin_sub.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR033690; Adenylat_kinase_CS.
DR InterPro; IPR007862; Adenylate_kinase_lid-dom.
DR InterPro; IPR028587; AK2.
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 TIGRFAMs; TIGR01351; adk; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Direct protein sequencing; Disulfide bond; Kinase; Mitochondrion;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..241
FT /note="Adenylate kinase 2, mitochondrial"
FT /id="PRO_0000423211"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168,
FT ECO:0000269|PubMed:3002789"
FT CHAIN 2..241
FT /note="Adenylate kinase 2, mitochondrial, N-terminally
FT processed"
FT /id="PRO_0000158916"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..76
FT /note="NMP"
FT REGION 143..180
FT /note="LID"
FT BINDING 27..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 48
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 53
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 74..76
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 102..105
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 109
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 153..154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 177
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 188
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P54819"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54819"
FT MOD_RES 64
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP6"
FT MOD_RES 95
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP6"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54819"
FT MOD_RES 183
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP6"
FT MOD_RES 197
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P54819"
FT DISULFID 44..94
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168,
FT ECO:0000269|PubMed:8868479"
FT VAR_SEQ 234..241
FT /note="CKDLVMFI -> S (in isoform AK2B)"
FT /evidence="ECO:0000303|PubMed:16305752,
FT ECO:0000303|PubMed:3040716, ECO:0000303|Ref.4"
FT /id="VSP_002789"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:1AK2"
FT HELIX 30..41
FT /evidence="ECO:0007829|PDB:1AK2"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:1AK2"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:1AK2"
FT HELIX 61..71
FT /evidence="ECO:0007829|PDB:1AK2"
FT HELIX 78..89
FT /evidence="ECO:0007829|PDB:1AK2"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:1AK2"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:1AK2"
FT HELIX 107..120
FT /evidence="ECO:0007829|PDB:1AK2"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:1AK2"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:1AK2"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:1AK2"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:1AK2"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:1AK2"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:1AK2"
FT HELIX 182..205
FT /evidence="ECO:0007829|PDB:1AK2"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:1AK2"
FT HELIX 218..232
FT /evidence="ECO:0007829|PDB:1AK2"
SQ SEQUENCE 241 AA; 26497 MW; D9232C61C431F9F4 CRC64;
MAPNVPAAEP VPESPKGVRA VLLGPPGAGK GTQAPKLAKN FCVCHLATGD MLRAMVASGS
ELGKKLKATM DAGKLVSDEM VLELIEKNLE TPPCKNGFLL DGFPRTVRQA EMLDDLMEKR
KEKLDSVIEF SIPDSLLIRR ITGRLIHPQS GRSYHEEFNP PKEPMKDDIT GEPLIRRSDD
NKKALKIRLE AYHTQTTPLV EYYSKRGIHS AIDASQTPDV VFASILAAFS KATCKDLVMF
I
