P53395

PR
Gene name
Dbt
Protein name
Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
Names
Branched-chain alpha-keto acid dehydrogenase complex component E2, BCKAD-E2, BCKADE2, Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, Dihydrolipoamide branched chain transacylase, Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:13171
EC number
2.3.1.168: Transferring groups other than amino-acyl groups
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

9-91 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P53395

Entry ID Method Resolution Chain Position Source
AF-P53395-F1 Predicted AlphaFoldDB

32 variants for P53395

Variant ID(s) Position Change Description Diseaes Association Provenance
rs45750426 29 A>V No EVA
rs261152023 40 V>M No EVA
rs3388661572 73 G>E No EVA
rs3388658271 78 E>* No EVA
rs3388648257 97 S>I No EVA
rs3393406477 100 E>* No EVA
rs30841312 117 V>I No EVA
rs3388663534 130 Y>F No EVA
rs3388654428 150 V>I No EVA
rs3388657182 171 T>I No EVA
rs3388653350 173 A>V No EVA
rs1133575689 174 T>K No EVA
rs1132512987 175 P>L No EVA
rs3388664124 177 V>L No EVA
rs1132974662 179 R>G No EVA
rs3388657315 208 F>L No EVA
rs3388648850 224 E>G No EVA
rs3388658241 226 T>P No EVA
rs3388642276 227 P>L No EVA
rs50150450 239 T>M No EVA
rs215690986 242 A>S No EVA
rs235456382 247 F>V No EVA
rs3388663573 260 Q>* No EVA
rs3412805944 268 S>P No EVA
rs3393317120 269 A>S No EVA
rs3388661100 276 F>L No EVA
rs3388648777 279 C>F No EVA
rs3388658228 284 L>F No EVA
rs3388661143 308 M>L No EVA
rs3388648816 334 Q>H No EVA
rs3388664145 351 E>D No EVA
rs3388648208 406 G>E No EVA

No associated diseases with P53395

4 regional properties for P53395

Type Name Position InterPro Accession
domain Biotin/lipoyl attachment 64 - 139 IPR000089
domain 2-oxoacid dehydrogenase acyltransferase, catalytic domain 250 - 479 IPR001078
binding_site 2-oxo acid dehydrogenase, lipoyl-binding site 89 - 118 IPR003016
domain Peripheral subunit-binding domain 172 - 209 IPR004167

Functions

Description
EC Number 2.3.1.168 Transferring groups other than amino-acyl groups
Subcellular Localization
  • Mitochondrion matrix
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
microtubule cytoskeleton The part of the cytoskeleton (the internal framework of a cell) composed of microtubules and associated proteins.
mitochondrial alpha-ketoglutarate dehydrogenase complex Mitochondrial complex that possesses alpha-ketoglutarate dehydrogenase activity.
mitochondrial nucleoid The region of a mitochondrion to which the DNA is confined.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

4 GO annotations of molecular function

Name Definition
acetyltransferase activity Catalysis of the transfer of an acetyl group to an acceptor molecule.
dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity Catalysis of the reaction: 2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-dihydrolipoyl)lysine.
lipoic acid binding Binding to lipoic acid, 1,2-dithiolane-3-pentanoic acid.
ubiquitin protein ligase binding Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins.

1 GO annotations of biological process

Name Definition
branched-chain amino acid catabolic process The chemical reactions and pathways resulting in the breakdown of amino acids containing a branched carbon skeleton, comprising isoleucine, leucine and valine.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P11181 DBT Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial Bos taurus (Bovine) PR
P11182 DBT Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial Homo sapiens (Human) PR
Q23571 dbt-1 Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial Caenorhabditis elegans PR
Q9M7Z1 BCE2 Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial Arabidopsis thaliana (Mouse-ear cress) PR
Q5M729 At1g54220 Dihydrolipoyllysine-residue acetyltransferase component 3 of pyruvate dehydrogenase complex, mitochondrial Arabidopsis thaliana (Mouse-ear cress) PR
Q8RWN9 At3g13930 Dihydrolipoyllysine-residue acetyltransferase component 2 of pyruvate dehydrogenase complex, mitochondrial Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MAAARVLRTW SQNAVRLTCV RYFQTFNSAR VLKPKCVCSV GYPLFKYSQP RHSLRTAAVL
70 80 90 100 110 120
QGQVVQFKLS DIGEGIREVT IKEWYVKEGD TVSQFDSICE VQSDKASVTI TSRYDGVIKR
130 140 150 160 170 180
LYYNLDDIAY VGKPLIDIET EALKDSEEDV VETPAVSHDE HTHQEIKGQK TLATPAVRRL
190 200 210 220 230 240
AMENNIKLSE VVGSGKDGRI LKEDILSFLE KQTGAILPPS PKSEITPPPP QPKDRTFPTP
250 260 270 280 290 300
IAKPPVFTGK DRTEPVTGFQ KAMVKTMSAA LKIPHFGYCD EIDLTQLVKL REELKPVALA
310 320 330 340 350 360
RGIKLSFMPF FLKAASLGLL QFPILNASVD ENCQNITYKA SHNIGIAMDT ELGLIVPNVK
370 380 390 400 410 420
NVQVRSVFEI AMELNRLQKL GSSGQLGTTD LTGGTFTLSN IGSIGGTYAK PVILPPEVAI
430 440 450 460 470 480
GALGAIKALP RFDQKGDVYK AQIMNVSWSA DHRVIDGATM SRFSNLWKSY LENPAFMLLD
LK