ID KAD8_XENLA Reviewed; 485 AA.
AC Q5M7G4;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Adenylate kinase 8;
DE Short=AK 8;
DE EC=2.7.4.3;
DE EC=2.7.4.6;
DE AltName: Full=ATP-AMP transphosphorylase 8;
GN Name=ak8;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Nucleoside monophosphate (NMP) kinase that catalyzes the
CC reversible transfer of the terminal phosphate group between nucleoside
CC triphosphates and monophosphates. Has highest activity toward AMP, and
CC weaker activity toward dAMP, CMP and dCMP. Also displays broad
CC nucleoside diphosphate kinase activity. {ECO:0000250|UniProtKB:Q96MA6}.
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:Q96MA6};
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:Q96MA6};
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:Q96MA6};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q96MA6}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000305}.
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DR EMBL; BC088665; AAH88665.1; -; mRNA.
DR RefSeq; NP_001088862.1; NM_001095393.1.
DR AlphaFoldDB; Q5M7G4; -.
DR SMR; Q5M7G4; -.
DR MaxQB; Q5M7G4; -.
DR DNASU; 496205; -.
DR GeneID; 496205; -.
DR KEGG; xla:496205; -.
DR AGR; Xenbase:XB-GENE-5831351; -.
DR CTD; 496205; -.
DR Xenbase; XB-GENE-5831351; ak8.L.
DR OrthoDB; 314591at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 496205; Expressed in testis and 16 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0004017; F:adenylate kinase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004127; F:cytidylate kinase activity; ISS:UniProtKB.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; ISS:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01428; ADK; 2.
DR CDD; cd22979; DD_AK8; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359:SF81; ADENYLATE KINASE 8; 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.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..485
FT /note="Adenylate kinase 8"
FT /id="PRO_0000279388"
FT REGION 58..258
FT /note="Adenylate kinase 1"
FT /evidence="ECO:0000250|UniProtKB:Q96MA6"
FT REGION 87..113
FT /note="NMP 1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 177..206
FT /note="LID 1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 269..471
FT /note="Adenylate kinase 2"
FT /evidence="ECO:0000250|UniProtKB:Q96MA6"
FT REGION 298..327
FT /note="NMP 2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 391..424
FT /note="LID 2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 67..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 140..143
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 147
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 218
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 278..283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 325..327
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 354..357
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 361
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 432
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
SQ SEQUENCE 485 AA; 54885 MW; CE8768D37BB05070 CRC64;
MDATRKPLRI PPAMAVYAEE HGVFDIIQKM VEKVLVDRPE DPIQYMIDHL SNDNDDVPRV
FILGPPASGK HTMAKLLCKR LNATHLTPEN VLSSDVSLLV KEAQSYRDKG QEVPDELWAK
LMRERLSQVD CIKRGWVLEG FPKTRDQALM LQMAGVCPGH LVVLDAPDIV LIERNMGKRI
DITDGEVYHT TFDWPSDPAV QRNLVEPEGI SEEETGQRLL EFHRNIPGLL RTYSKVSKKI
NVDQPYMDVF SQVLTFVLSK QRSLAPHTPR ILLYGPPGSG RSLQASLLAQ KYGIINICCG
QVLKEAVADQ TKLGELIQPY IENDQQVPDN FVLKILTDHL SSLESAKHGW VLHGFPQDTD
QAALLKDAGF MPNRVFSLDL SDDVVIERLS LCMTDPVSGE RYHSIYKPAP RSEVQERLQQ
NPKYSEEKVQ ARLDVYHANA DELEEFYQDV IHINADQDPY TVFEFIESYI VSPLPKSLPE
EPTSP
//
