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Q00972

- BCKD_RAT

UniProt

Q00972 - BCKD_RAT

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Protein

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

Gene

Bckdk

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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.

Catalytic activityi

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

GO - Molecular functioni

  1. [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase activity Source: RGD
  2. ATP binding Source: HGNC
  3. protein serine/threonine kinase activity Source: HGNC

GO - Biological processi

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

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

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: Chromosome 1

Organism-specific databases

RGDi2198. Bckdk.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial alpha-ketoglutarate dehydrogenase complex Source: HGNC
  2. 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.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ00972.
PRIDEiQ00972.

PTM databases

PhosphoSiteiQ00972.

Expressioni

Gene expression databases

GenevestigatoriQ00972.

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 – 735
Beta strandi74 – 763
Beta strandi82 – 843
Helixi85 – 11127
Helixi114 – 1174
Helixi120 – 13819
Helixi145 – 16117
Turni162 – 1643
Helixi165 – 17612
Helixi177 – 1793
Helixi184 – 20926
Beta strandi221 – 2255
Helixi227 – 24620
Beta strandi252 – 2576
Beta strandi262 – 2643
Helixi267 – 28620
Beta strandi298 – 3047
Beta strandi306 – 3149
Helixi322 – 3254
Turni326 – 3294
Helixi369 – 37911
Beta strandi383 – 3897
Turni390 – 3923
Beta strandi393 – 4019
Beta strandi403 – 4053

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiTIANNDV.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
M93271 mRNA. Translation: AAA40818.1 .
U27456 mRNA. Translation: AAB60498.1 .
PIRi A42924.
RefSeqi NP_062117.2. NM_019244.2.
UniGenei Rn.31976.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GJV X-ray 2.70 A 31-412 [» ]
1GKX X-ray 2.30 A 31-412 [» ]
1GKZ X-ray 2.20 A 31-412 [» ]
3TZ0 X-ray 2.50 A 1-412 [» ]
3TZ2 X-ray 2.85 A 1-412 [» ]
3TZ4 X-ray 2.25 A 1-412 [» ]
3TZ5 X-ray 2.40 A 1-412 [» ]
3VAD X-ray 2.60 A 1-412 [» ]
4DZY X-ray 2.10 A 1-412 [» ]
4E00 X-ray 2.15 A 1-412 [» ]
4E01 X-ray 1.97 A 1-412 [» ]
4E02 X-ray 2.15 A 1-412 [» ]
4H7Q X-ray 2.10 A 1-412 [» ]
4H81 X-ray 2.05 A 1-412 [» ]
4H85 X-ray 2.10 A 1-412 [» ]
ProteinModelPortali Q00972.
SMRi Q00972. Positions 68-408.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 248235. 1 interaction.
IntActi Q00972. 1 interaction.
STRINGi 10116.ENSRNOP00000026466.

PTM databases

PhosphoSitei Q00972.

Proteomic databases

PaxDbi Q00972.
PRIDEi Q00972.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000026466 ; ENSRNOP00000026466 ; ENSRNOG00000019485 .
GeneIDi 29603.
KEGGi rno:29603.
UCSCi RGD:2198. rat.

Organism-specific databases

CTDi 10295.
RGDi 2198. Bckdk.

Phylogenomic databases

eggNOGi COG0642.
GeneTreei ENSGT00550000074574.
HOGENOMi HOG000164315.
HOVERGENi HBG004829.
InParanoidi Q00972.
KOi K00905.
OMAi TIANNDV.
OrthoDBi EOG7TQV0S.
PhylomeDBi Q00972.
TreeFami TF331303.

Miscellaneous databases

EvolutionaryTracei Q00972.
NextBioi 609772.
PROi Q00972.

Gene expression databases

Genevestigatori Q00972.

Family and domain databases

Gene3Di 1.20.140.20. 1 hit.
3.30.565.10. 1 hit.
InterProi IPR018955. BCDHK/PDK_N.
IPR003594. HATPase_C.
IPR004358. Sig_transdc_His_kin-like_C.
IPR005467. Sig_transdc_His_kinase_core.
[Graphical view ]
Pfami PF10436. BCDHK_Adom3. 1 hit.
PF02518. HATPase_c. 1 hit.
[Graphical view ]
PRINTSi PR00344. BCTRLSENSOR.
SMARTi SM00387. HATPase_c. 1 hit.
[Graphical view ]
SUPFAMi SSF55874. SSF55874. 1 hit.
SSF69012. SSF69012. 1 hit.
PROSITEi PS50109. HIS_KIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 129 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