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Protein

[3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase, mitochondrial

Gene

Bckdk

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the phosphorylation and inactivation of the branched-chain alpha-ketoacid dehydrogenase complex, the key regulatory enzyme of the valine, leucine and isoleucine catabolic pathways. Key enzyme that regulate the activity state of the BCKD complex.By similarity

Catalytic activityi

ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] = ADP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphate.

GO - Molecular functioni

  • [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase activity Source: RGD
  • ATP binding Source: HGNC
  • protein serine/threonine kinase activity Source: HGNC

GO - Biological processi

  • branched-chain amino acid catabolic process Source: HGNC
  • phosphorylation Source: HGNC
  • protein phosphorylation Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.4. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
[3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase, mitochondrial (EC:2.7.11.4)
Alternative name(s):
Branched-chain alpha-ketoacid dehydrogenase kinase
Short name:
BCKD-kinase
Short name:
BCKDHKIN
Gene namesi
Name:Bckdk
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi2198. Bckdk.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial alpha-ketoglutarate dehydrogenase complex Source: HGNC
  • mitochondrion Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030Mitochondrion1 PublicationAdd
BLAST
Chaini31 – 412382[3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase, mitochondrialPRO_0000023454Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei192 – 1921N6-acetyllysineBy similarity
Modified residuei233 – 2331N6-acetyllysineBy similarity

Post-translational modificationi

Autophosphorylated.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ00972.
PRIDEiQ00972.

PTM databases

PhosphoSiteiQ00972.

Expressioni

Gene expression databases

GenevisibleiQ00972. RN.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi248235. 1 interaction.
IntActiQ00972. 1 interaction.
STRINGi10116.ENSRNOP00000026466.

Structurei

Secondary structure

1
412
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi69 – 735Combined sources
Beta strandi74 – 763Combined sources
Beta strandi82 – 843Combined sources
Helixi85 – 11127Combined sources
Helixi114 – 1174Combined sources
Helixi120 – 13819Combined sources
Helixi145 – 16117Combined sources
Turni162 – 1643Combined sources
Helixi165 – 17612Combined sources
Helixi177 – 1793Combined sources
Helixi184 – 20926Combined sources
Beta strandi221 – 2255Combined sources
Helixi227 – 24620Combined sources
Beta strandi252 – 2576Combined sources
Beta strandi262 – 2643Combined sources
Helixi267 – 28620Combined sources
Beta strandi298 – 3047Combined sources
Beta strandi306 – 3149Combined sources
Helixi322 – 3254Combined sources
Turni326 – 3294Combined sources
Helixi369 – 37911Combined sources
Beta strandi383 – 3897Combined sources
Turni390 – 3923Combined sources
Beta strandi393 – 4019Combined sources
Beta strandi403 – 4053Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GJVX-ray2.70A31-412[»]
1GKXX-ray2.30A31-412[»]
1GKZX-ray2.20A31-412[»]
3TZ0X-ray2.50A1-412[»]
3TZ2X-ray2.85A1-412[»]
3TZ4X-ray2.25A1-412[»]
3TZ5X-ray2.40A1-412[»]
3VADX-ray2.60A1-412[»]
4DZYX-ray2.10A1-412[»]
4E00X-ray2.15A1-412[»]
4E01X-ray1.97A1-412[»]
4E02X-ray2.15A1-412[»]
4H7QX-ray2.10A1-412[»]
4H81X-ray2.05A1-412[»]
4H85X-ray2.10A1-412[»]
ProteinModelPortaliQ00972.
SMRiQ00972. Positions 68-408.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00972.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini159 – 404246Histidine kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the PDK/BCKDK protein kinase family.Curated
Contains 1 histidine kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0642.
GeneTreeiENSGT00550000074574.
HOGENOMiHOG000164315.
HOVERGENiHBG004829.
InParanoidiQ00972.
KOiK00905.
OMAiCNPTILQ.
OrthoDBiEOG7TQV0S.
PhylomeDBiQ00972.
TreeFamiTF331303.

Family and domain databases

Gene3Di1.20.140.20. 1 hit.
3.30.565.10. 1 hit.
InterProiIPR018955. BCDHK/PDK_N.
IPR003594. HATPase_C.
IPR004358. Sig_transdc_His_kin-like_C.
IPR005467. Sig_transdc_His_kinase_core.
[Graphical view]
PfamiPF10436. BCDHK_Adom3. 1 hit.
PF02518. HATPase_c. 1 hit.
[Graphical view]
PRINTSiPR00344. BCTRLSENSOR.
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF55874. SSF55874. 1 hit.
SSF69012. SSF69012. 1 hit.
PROSITEiPS50109. HIS_KIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q00972-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MILTSVLGSG PRSGSSLWPL LGSSLSLRVR STSATDTHHV ELARERSKTV
60 70 80 90 100
TSFYNQSAID VVAEKPSVRL TPTMMLYSGR SQDGSHLLKS GRYLQQELPV
110 120 130 140 150
RIAHRIKGFR SLPFIIGCNP TILHVHELYI RAFQKLTDFP PIKDQADEAQ
160 170 180 190 200
YCQLVRQLLD DHKDVVTLLA EGLRESRKHI EDEKLVRYFL DKTLTSRLGI
210 220 230 240 250
RMLATHHLAL HEDKPDFVGI ICTRLSPKKI IEKWVDFARR LCEHKYGNAP
260 270 280 290 300
RVRINGHVAA RFPFIPMPLD YILPELLKNA MRATMESHLD TPYNVPDVVI
310 320 330 340 350
TIANNDVDLI IRISDRGGGI AHKDLDRVMD YHFTTAEAST QDPRISPLFG
360 370 380 390 400
HLDMHSGGQS GPMHGFGFGL PTSRAYAEYL GGSLQLQSLQ GIGTDVYLRL
410
RHIDGREESF RI
Length:412
Mass (Da):46,474
Last modified:July 15, 1998 - v2
Checksum:iD630D3A44728927E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti110 – 12415RSLPF…PTILH → VVFLSSLVATLPYCT (PubMed:1377677).CuratedAdd
BLAST
Sequence conflicti110 – 12415RSLPF…PTILH → VVFLSSLVATLPYCT (PubMed:1496922).CuratedAdd
BLAST
Sequence conflicti222 – 2221C → S (PubMed:1377677).Curated
Sequence conflicti222 – 2221C → S (PubMed:1496922).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93271 mRNA. Translation: AAA40818.1.
U27456 mRNA. Translation: AAB60498.1.
PIRiA42924.
RefSeqiNP_062117.2. NM_019244.2.
UniGeneiRn.31976.

Genome annotation databases

EnsembliENSRNOT00000026466; ENSRNOP00000026466; ENSRNOG00000019485.
GeneIDi29603.
KEGGirno:29603.
UCSCiRGD:2198. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93271 mRNA. Translation: AAA40818.1.
U27456 mRNA. Translation: AAB60498.1.
PIRiA42924.
RefSeqiNP_062117.2. NM_019244.2.
UniGeneiRn.31976.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GJVX-ray2.70A31-412[»]
1GKXX-ray2.30A31-412[»]
1GKZX-ray2.20A31-412[»]
3TZ0X-ray2.50A1-412[»]
3TZ2X-ray2.85A1-412[»]
3TZ4X-ray2.25A1-412[»]
3TZ5X-ray2.40A1-412[»]
3VADX-ray2.60A1-412[»]
4DZYX-ray2.10A1-412[»]
4E00X-ray2.15A1-412[»]
4E01X-ray1.97A1-412[»]
4E02X-ray2.15A1-412[»]
4H7QX-ray2.10A1-412[»]
4H81X-ray2.05A1-412[»]
4H85X-ray2.10A1-412[»]
ProteinModelPortaliQ00972.
SMRiQ00972. Positions 68-408.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248235. 1 interaction.
IntActiQ00972. 1 interaction.
STRINGi10116.ENSRNOP00000026466.

PTM databases

PhosphoSiteiQ00972.

Proteomic databases

PaxDbiQ00972.
PRIDEiQ00972.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000026466; ENSRNOP00000026466; ENSRNOG00000019485.
GeneIDi29603.
KEGGirno:29603.
UCSCiRGD:2198. rat.

Organism-specific databases

CTDi10295.
RGDi2198. Bckdk.

Phylogenomic databases

eggNOGiCOG0642.
GeneTreeiENSGT00550000074574.
HOGENOMiHOG000164315.
HOVERGENiHBG004829.
InParanoidiQ00972.
KOiK00905.
OMAiCNPTILQ.
OrthoDBiEOG7TQV0S.
PhylomeDBiQ00972.
TreeFamiTF331303.

Enzyme and pathway databases

BRENDAi2.7.11.4. 5301.

Miscellaneous databases

EvolutionaryTraceiQ00972.
NextBioi609772.
PROiQ00972.

Gene expression databases

GenevisibleiQ00972. RN.

Family and domain databases

Gene3Di1.20.140.20. 1 hit.
3.30.565.10. 1 hit.
InterProiIPR018955. BCDHK/PDK_N.
IPR003594. HATPase_C.
IPR004358. Sig_transdc_His_kin-like_C.
IPR005467. Sig_transdc_His_kinase_core.
[Graphical view]
PfamiPF10436. BCDHK_Adom3. 1 hit.
PF02518. HATPase_c. 1 hit.
[Graphical view]
PRINTSiPR00344. BCTRLSENSOR.
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF55874. SSF55874. 1 hit.
SSF69012. SSF69012. 1 hit.
PROSITEiPS50109. HIS_KIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Branched-chain alpha-ketoacid dehydrogenase kinase. Molecular cloning, expression, and sequence similarity with histidine protein kinases."
    Popov K.M., Zhao Y., Shimomura Y., Kuntz M.J., Harris R.A.
    J. Biol. Chem. 267:13127-13130(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-67; 93-100; 254-260 AND 328-343.
    Tissue: Heart.
  2. "Purification, characterization, regulation and molecular cloning of mitochondrial protein kinases."
    Harris R.A., Popov K.M., Shimomura Y., Zhao Y., Jaskiewicz J., Nanaumi N., Suzuki M.
    Adv. Enzyme Regul. 32:267-284(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.
  3. "Expression and characterization of branched-chain alpha-ketoacid dehydrogenase kinase from the rat. Is it a histidine-protein kinase?"
    Davie J.R., Wynn R.M., Meng M., Huang Y.-S., Aalund G., Chuang D.T., Lau K.S.
    J. Biol. Chem. 270:19861-19867(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 31-412, SEQUENCE REVISION TO 110-124 AND 222.
    Tissue: Kidney.

Entry informationi

Entry nameiBCKD_RAT
AccessioniPrimary (citable) accession number: Q00972
Secondary accession number(s): Q64552
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 15, 1998
Last modified: June 24, 2015
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.