Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q9M7Z1

Entry ID Method Resolution Chain Position Source
AF-Q9M7Z1-F1 Predicted AlphaFoldDB

35 variants for Q9M7Z1

Variant ID(s) Position Change Description Diseaes Association Provenance
ENSVATH02120145 17 S>N No 1000Genomes
tmp_3_2160405_C_T 21 V>I No 1000Genomes
tmp_3_2160374_T_A 31 Y>F No 1000Genomes
ENSVATH10534270 47 H>D No 1000Genomes
ENSVATH10534266 55 G>S No 1000Genomes
ENSVATH00310243 62 F>L No 1000Genomes
tmp_3_2160013_G_A 69 T>I No 1000Genomes
ENSVATH05787386 91 E>Q No 1000Genomes
tmp_3_2159806_G_C 107 Q>E No 1000Genomes
ENSVATH13880770 142 V>I No 1000Genomes
ENSVATH10534263 158 L>V No 1000Genomes
ENSVATH00310241 162 D>N No 1000Genomes
ENSVATH00310240 165 E>K No 1000Genomes
tmp_3_2159415_C_T 170 G>E No 1000Genomes
tmp_3_2159401_C_T 175 G>R No 1000Genomes
tmp_3_2159362_C_T 188 V>I No 1000Genomes
ENSVATH10534262 190 N>K No 1000Genomes
ENSVATH10534261 191 L>R No 1000Genomes
ENSVATH05787380 221 D>G No 1000Genomes
tmp_3_2159253_C_T 224 G>E No 1000Genomes
ENSVATH05787379 260 F>V No 1000Genomes
ENSVATH05787378 287 S>T No 1000Genomes
ENSVATH10534259 293 Q>K No 1000Genomes
tmp_3_2158954_T_G 296 K>Q No 1000Genomes
ENSVATH05787376 298 N>K No 1000Genomes
ENSVATH02120138 306 H>R No 1000Genomes
tmp_3_2158908_G_A 311 T>I No 1000Genomes
tmp_3_2158845_G_A 332 A>V No 1000Genomes
tmp_3_2158697_G_A 350 A>V No 1000Genomes
tmp_3_2158610_T_C 379 Q>R No 1000Genomes
tmp_3_2158608_G_T 380 H>N No 1000Genomes
tmp_3_2158598_G_A 383 A>V No 1000Genomes
ENSVATH10534258 389 P>R No 1000Genomes
tmp_3_2158436_C_T 437 G>E No 1000Genomes
tmp_3_2158263_C_A 467 Q>H No 1000Genomes

No associated diseases with Q9M7Z1

4 regional properties for Q9M7Z1

Type Name Position InterPro Accession
domain Biotin/lipoyl attachment 73 - 150 IPR000089
domain 2-oxoacid dehydrogenase acyltransferase, catalytic domain 251 - 480 IPR001078
binding_site 2-oxo acid dehydrogenase, lipoyl-binding site 100 - 129 IPR003016
domain Peripheral subunit-binding domain 183 - 220 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

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
mitochondrial matrix The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
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.

5 GO annotations of molecular function

Name Definition
acetyltransferase activity Catalysis of the transfer of an acetyl group to an acceptor molecule.
dihydrolipoamide branched chain acyltransferase activity Catalysis of the reaction: acyl-CoA + dihydrolipoamide = CoA + S-acyldihydrolipoamide, where the acyl group is a branched chain.
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.
zinc ion binding Binding to a zinc ion (Zn).

4 GO annotations of biological process

Name Definition
cellular response to sucrose starvation Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of sucrose.
fatty acid biosynthetic process The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.
response to absence of light Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an absence of light stimuli.
response to sucrose Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a sucrose stimulus.

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
P53395 Dbt Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial Mus musculus (Mouse) PR
Q23571 dbt-1 Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial Caenorhabditis elegans 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
MIARRIWRSH RFLRPFSSSS VCSPPFRVPE YLSQSSSSPA SRPFFVHPPT LMKWGGGSRS
70 80 90 100 110 120
WFSNEAMATD SNSGLIDVPL AQTGEGIAEC ELLKWFVKEG DSVEEFQPLC EVQSDKATIE
130 140 150 160 170 180
ITSRFKGKVA LISHSPGDII KVGETLVRLA VEDSQDSLLT TDSSEIVTLG GSKQGTENLL
190 200 210 220 230 240
GALSTPAVRN LAKDLGIDIN VITGTGKDGR VLKEDVLRFS DQKGFVTDSV SSEHAVIGGD
250 260 270 280 290 300
SVSTKASSNF EDKTVPLRGF SRAMVKTMTM ATSVPHFHFV EEINCDSLVE LKQFFKENNT
310 320 330 340 350 360
DSTIKHTFLP TLIKSLSMAL TKYPFVNSCF NAESLEIILK GSHNIGVAMA TEHGLVVPNI
370 380 390 400 410 420
KNVQSLSLLE ITKELSRLQH LAANNKLNPE DVTGGTITLS NIGAIGGKFG SPLLNLPEVA
430 440 450 460 470 480
IIALGRIEKV PKFSKEGTVY PASIMMVNIA ADHRVLDGAT VARFCCQWKE YVEKPELLML
QMR