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Database: UniProt
Entry: A0A2D0PXD7_ICTPU
LinkDB: A0A2D0PXD7_ICTPU
Original site: A0A2D0PXD7_ICTPU 
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
//
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