ID A0A1S3PRJ2_SALSA Unreviewed; 474 AA.
AC A0A1S3PRJ2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Adenylate kinase 8 {ECO:0000256|ARBA:ARBA00029501};
DE EC=2.7.4.3 {ECO:0000256|ARBA:ARBA00012955};
DE EC=2.7.4.6 {ECO:0000256|ARBA:ARBA00012966};
DE AltName: Full=ATP-AMP transphosphorylase 8 {ECO:0000256|ARBA:ARBA00042874};
GN Name=ak8 {ECO:0000313|RefSeq:XP_014030302.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014030302.1};
RN [1] {ECO:0000313|RefSeq:XP_014030302.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014030302.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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.
CC {ECO:0000256|ARBA:ARBA00037483}.
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:0000256|ARBA:ARBA00000582};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family.
CC {ECO:0000256|RuleBase:RU003330}.
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DR RefSeq; XP_014030302.1; XM_014174827.1.
DR AlphaFoldDB; A0A1S3PRJ2; -.
DR GeneID; 106587015; -.
DR CTD; 158067; -.
DR OrthoDB; 314591at2759; -.
DR Proteomes; UP000087266; Chromosome ssa26.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0043227; C:membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0004017; F:adenylate kinase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01428; ADK; 2.
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; IPR036193; ADK_active_lid_dom_sf.
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; SSF57774; Microbial and mitochondrial ADK, insert 'zinc finger' domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003330};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003330}.
SQ SEQUENCE 474 AA; 53736 MW; E4BFFE28FE44C682 CRC64;
MTPITFSLAT CECVLASDLD SCYKLTLVTN LMVDKPEDPI QYLIVLLKRG SVEVPRVMLL
GPPASGKRTV ARKLCEHTQV IHITDSNILQ EDTDLTKKAL QYKAKQQEIP CDLWIKLIQQ
RLSKIDCVRR GWVLEGIPQT REEALSLQEA GVAPNHVVLL EAPDAVLIER SQGKRIDPVT
GDVYHVTFIW PEDKEVVQRL ERQKTVSEEQ LVAQLMQHHR EVHALRKTYR NCLKGIDADQ
PHVDVFDQVL TYILSRHCSV APHTPRVLLF GPPGSGKSLQ AKLISQKYNI VNLCCGELLE
AVSADVTNMG ELIKPYLESG QQVPDSMVLQ ILTERLSRLD CTTRGWVLHG FPRDLEQAEK
LQESNFIPSR VFFLEMTDDV AIERVTLRSI DPFTGEKYHS LYKPAPSPEV QTRLQFNPKD
SEAQLLRQLK EYWANASSLQ DLYPEAVHIN ADQDPHTVFE SLESRLVGRL QNDA
//
