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KAD8_XENLA
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   03-AUG-2022, entry version 84.
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   CTD; 496205; -.
DR   Xenbase; XB-GENE-5831351; ak8.L.
DR   OrthoDB; 961384at2759; -.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 496205; Expressed in testis and 16 other 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:0006165; P:nucleoside diphosphate phosphorylation; ISS:UniProtKB.
DR   GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; ISS:UniProtKB.
DR   CDD; cd01428; ADK; 2.
DR   Gene3D; 3.40.50.300; -; 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; PTHR23359; 2.
DR   PRINTS; PR00094; ADENYLTKNASE.
DR   SUPFAM; SSF52540; SSF52540; 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
 
 
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