ID KAD5_BOVIN Reviewed; 562 AA.
AC A4IFD0;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 24-JAN-2024, entry version 108.
DE RecName: Full=Adenylate kinase isoenzyme 5;
DE Short=AK 5;
DE EC=2.7.4.3;
DE EC=2.7.4.6;
DE AltName: Full=ATP-AMP transphosphorylase 5;
GN Name=Ak5;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
CC -!- FUNCTION: Nucleoside monophosphate (NMP) kinase that catalyzes the
CC reversible transfer of the terminal phosphate group between nucleoside
CC triphosphates and monophosphates. Active on AMP and dAMP with ATP as a
CC donor. When GTP is used as phosphate donor, the enzyme phosphorylates
CC AMP, CMP, and to a small extent dCMP. Also displays broad nucleoside
CC diphosphate kinase activity. {ECO:0000250|UniProtKB:Q9Y6K8}.
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:0000250|UniProtKB:Q9Y6K8};
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;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6K8};
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:0000250|UniProtKB:Q9Y6K8};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P00568}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y6K8}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000305}.
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DR EMBL; BC134521; AAI34522.1; -; mRNA.
DR RefSeq; NP_001077226.1; NM_001083757.1.
DR AlphaFoldDB; A4IFD0; -.
DR SMR; A4IFD0; -.
DR STRING; 9913.ENSBTAP00000069785; -.
DR PaxDb; 9913-ENSBTAP00000023151; -.
DR GeneID; 613448; -.
DR KEGG; bta:613448; -.
DR CTD; 26289; -.
DR eggNOG; KOG3079; Eukaryota.
DR HOGENOM; CLU_034712_1_0_1; -.
DR InParanoid; A4IFD0; -.
DR OrthoDB; 1330004at2759; -.
DR TreeFam; TF313747; -.
DR Proteomes; UP000009136; Unplaced.
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; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; ISS:UniProtKB.
DR GO; GO:0046034; P:ATP metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01428; ADK; 2.
DR CDD; cd22978; DD_AK5; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 2.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR033690; Adenylat_kinase_CS.
DR InterPro; IPR006267; AK1/5.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR01360; aden_kin_iso1; 1.
DR PANTHER; PTHR23359:SF79; ADENYLATE KINASE ISOENZYME 5; 1.
DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR Pfam; PF00406; ADK; 2.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF47391; Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00113; ADENYLATE_KINASE; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..562
FT /note="Adenylate kinase isoenzyme 5"
FT /id="PRO_0000382203"
FT REGION 133..316
FT /note="Adenylate kinase 1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6K8"
FT REGION 162..193
FT /note="NMP 1"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT REGION 256..266
FT /note="LID 1"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT REGION 377..559
FT /note="Adenylate kinase 2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6K8"
FT REGION 406..435
FT /note="NMP 2"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT REGION 499..509
FT /note="LID 2"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 142..147
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 168
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 191..193
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 219..222
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 226
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 263
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 274
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 386..391
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 407
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 433..435
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 462..465
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 469
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 500
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 517
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 545
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00568"
SQ SEQUENCE 562 AA; 63273 MW; DF2A96FB6B2324B8 CRC64;
MNTNEAKEYL ARREIPQLFE SLLNGLMCSK PEDPVEYLES CLQKVKELGG CDKVKWDTFV
SQEKKTLPPL NGGQSRRSFL RNVMPENSNF PYRRYDRLPP IHQFSIESDT DLSETAELIE
EYEVFDPTRP RPKIILVIGG PGSGKGTQSL KIAERYGFQY ISVGELLRKK IHSTSSNRKW
SLIAKIITTG ELAPQETTIT EIKQKLMQMP DEVGIVIDGF PRDVAQALSF EDQICTPDLV
VFLACTNQRL KERLLKRAEQ QGRPDDNLKA TQRRLMNFKQ NAAPLVKYFQ EKGLIMTFDA
DRDEDEVFYD ISMAVDSKLF PNKEAAAGSS DLDPSMMLDT GEVIDTGSDY EDQGDDQLNV
FGEDTMGGFM EDLKKCKIIF MIGGPGSGKG TQCGKLAEKY GFTHLSTDEL LQNELSSESG
RSKLIRDIME RGELVPSGII LELLKEAMVA SLSNTKGFLI DGYPREVKQG EEFGRRIGDP
HLVICMDCSA DTMTNRLLQR SRNSPQADDN TTTIAKRLET YYRASIPVVA YYETKTQLHK
INAEGTPEEV FLQLCTAIDS IF
//
