ID A0A2D0PXD7_ICTPU Unreviewed; 419 AA.
AC A0A2D0PXD7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Protein-serine/threonine kinase {ECO:0000256|RuleBase:RU366032};
DE EC=2.7.11.- {ECO:0000256|RuleBase:RU366032};
GN Name=pdk4 {ECO:0000313|RefSeq:XP_017310096.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017310096.1};
RN [1] {ECO:0000313|RefSeq:XP_017310096.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017310096.1};
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[pyruvate dehydrogenase E1 alpha subunit] = ADP
CC + H(+) + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha subunit];
CC Xref=Rhea:RHEA:23052, Rhea:RHEA-COMP:13689, Rhea:RHEA-COMP:13690,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.2;
CC Evidence={ECO:0000256|ARBA:ARBA00036431};
CC -!- SUBUNIT: Homodimer. Interacts with the pyruvate dehydrogenase complex
CC subunit DLAT, and is part of the multimeric pyruvate dehydrogenase
CC complex that contains multiple copies of pyruvate dehydrogenase (E1),
CC dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide
CC dehydrogenase (DLD, E3). {ECO:0000256|ARBA:ARBA00038845}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|RuleBase:RU366032}.
CC -!- SIMILARITY: Belongs to the PDK/BCKDK protein kinase family.
CC {ECO:0000256|ARBA:ARBA00006155, ECO:0000256|RuleBase:RU366032}.
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DR RefSeq; XP_017310096.1; XM_017454607.3.
DR AlphaFoldDB; A0A2D0PXD7; -.
DR STRING; 7998.ENSIPUP00000034358; -.
DR Ensembl; ENSIPUT00000035701; ENSIPUP00000034358; ENSIPUG00000023063.
DR GeneID; 108257133; -.
DR KEGG; ipu:108257133; -.
DR CTD; 5166; -.
DR OMA; EIVICQG; -.
DR OrthoDB; 3058550at2759; -.
DR Proteomes; UP000221080; Chromosome 24.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd16929; HATPase_PDK-like; 1.
DR Gene3D; 1.20.140.20; Alpha-ketoacid/pyruvate dehydrogenase kinase, N-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR036784; AK/P_DHK_N_sf.
DR InterPro; IPR018955; BCDHK/PDK_N.
DR InterPro; IPR039028; BCKD/PDK.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR PANTHER; PTHR11947:SF22; [PYRUVATE DEHYDROGENASE (ACETYL-TRANSFERRING)] KINASE ISOZYME 4, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11947; PYRUVATE DEHYDROGENASE KINASE; 1.
DR Pfam; PF10436; BCDHK_Adom3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF69012; alpha-ketoacid dehydrogenase kinase, N-terminal domain; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU366032};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glucose metabolism {ECO:0000256|ARBA:ARBA00022526};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU366032};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU366032};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU366032};
KW Pyruvate {ECO:0000313|RefSeq:XP_017310096.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 242..365
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 419 AA; 47946 MW; 6F06B0DEE60E84EB CRC64;
MKFAHMLLKN TSRFNIPKQV DRFSKFSPSP LSMKQFIDFG SANACEKTSF IFLRQELPVR
LANIMKEIDL LPDKLIGTPS VQLLHTWYTQ SLMELVDFLE KDPEDKNVLG KFTETLINVR
NRHNNVVPTM AQGVLEYKEA FGVDPVTNQN VQYFLDRFYT SRISTRMLMN QHTLIFSGST
NPAHPKHIGS IDPNCDVVEV VKDAYESSRM LCDQYYLMSP EVEIKQVNSK NPNEPVNIVY
VPSHLYHMLF ELFKNAMRAT VETHENSKYL PPIKVRVSLG HEDLTIKMSD RGGGVPLRKI
ERLFSYMYST APSPVIDNAR NAPLAGFGYG LPISRLYARY FQGDLQLYSM EGYGTSAVIY
FKALSSESVE RLPVFNKSAL RHYQTSIEAD DWSIPSSEPK KLGKYDYSVP DVRTESRVK
//