ID A0A4W5MNQ0_9TELE Unreviewed; 532 AA.
AC A0A4W5MNQ0;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 18-JUN-2025, entry version 29.
DE RecName: Full=Acetyl-CoA carboxylase kinase {ECO:0000256|ARBA:ARBA00032270};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.31 {ECO:0000256|ARBA:ARBA00012403};
DE AltName: Full=Hydroxymethylglutaryl-CoA reductase kinase {ECO:0000256|ARBA:ARBA00032865};
OS Hucho hucho (huchen).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Hucho.
OX NCBI_TaxID=62062 {ECO:0000313|Ensembl:ENSHHUP00000039249.1, ECO:0000313|Proteomes:UP000314982};
RN [1] {ECO:0000313|Proteomes:UP000314982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Macqueen D.J., Gundappa M.K.;
RT "Genome assembly of Danube salmon.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSHHUP00000039249.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[3-hydroxy-3-methylglutaryl-coenzyme A reductase] +
CC ATP = O-phospho-L-seryl-[3-hydroxy-3-methylglutaryl-coenzyme A
CC reductase] + ADP + H(+); Xref=Rhea:RHEA:23172, Rhea:RHEA-COMP:13692,
CC Rhea:RHEA-COMP:13693, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC EC=2.7.11.31; Evidence={ECO:0000256|ARBA:ARBA00047775};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[acetyl-CoA carboxylase] + ATP = O-phospho-L-seryl-
CC [acetyl-CoA carboxylase] + ADP + H(+); Xref=Rhea:RHEA:20333,
CC Rhea:RHEA-COMP:13722, Rhea:RHEA-COMP:13723, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00048417};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC H(+); Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00048679};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00047899};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000256|ARBA:ARBA00006234}.
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DR AlphaFoldDB; A0A4W5MNQ0; -.
DR Ensembl; ENSHHUT00000040787.1; ENSHHUP00000039249.1; ENSHHUG00000024389.1.
DR GeneTree; ENSGT00940000156945; -.
DR Proteomes; UP000314982; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-ARBA.
DR GO; GO:0047322; F:[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004679; F:AMP-activated protein kinase activity; IEA:UniProtKB-ARBA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:TreeGrafter.
DR GO; GO:0009896; P:positive regulation of catabolic process; IEA:UniProtKB-ARBA.
DR FunFam; 1.10.510.10:FF:000571; Maternal embryonic leucine zipper kinase; 1.
DR FunFam; 1.10.8.10:FF:000014; Non-specific serine/threonine protein kinase; 1.
DR FunFam; 3.30.200.20:FF:000136; Non-specific serine/threonine protein kinase; 1.
DR FunFam; 3.30.310.80:FF:000003; Non-specific serine/threonine protein kinase; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 1.
DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR032270; AMPK_C.
DR InterPro; IPR028375; KA1/Ssp2_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR049020; PRKAA1/2_AID.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR24346:SF104; 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-2; 1.
DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR Pfam; PF16579; AdenylateSensor; 1.
DR Pfam; PF21147; AMPK_alpha_AID; 1.
DR Pfam; PF00069; Pkinase; 2.
DR SUPFAM; SSF103243; KA1-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000314982};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 18..239
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 532 AA; 60111 MW; 2180C6C5B457CBDF CRC64;
MAERQHKHEG GRVKIGHYLL GDTLGVGTFG KVKIGEHQLT GHKVAVKILN RQKIRSLDVV
GKIKREIQNL KLFRHPHIIK LYQVISTPTD FFMMMEYVSG GELFDYICKH GRVIYQIVFL
LLFFKSNFTA CVSYLMWNRV PCSHVCSGLG DCEETSCGML YAGPEVDIWS CGVILYALLC
GTLPFDDEHV PTLFKKIRGG VFYMPEYLTR PVASLLLLML QVDPLKRASI KDIREHEWFK
QDLPGYLFPE DLSYDSTVLD EEAVREVCDK FESTESEVMS SLYSGDPQDQ LAVAYHLIID
NRRIMTQASE FYLASSPPQG SFMEDGMPLP PGVKPHPERM PPLLVDSPKA RCPLDALNTT
RAKPLAVKKS KWHLGIRSQS RPYDIMAEVY RAMRQLQYDW KVVNPYHLRV RRKNPVTDNL
VKMSLQLYQV DNRSYLLDFK SIDDDIMEAV GFKSGSSTPQ RSGSTAGLHR PRLSVDSALP
AVDLPQLSSS LPGSLCFSTV LLTSSPTSNP RQGSHTMDFF EMCASLIATL AR
//
