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 Q8VCH0

Entry ID Method Resolution Chain Position Source
AF-Q8VCH0-F1 Predicted AlphaFoldDB

20 variants for Q8VCH0

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389049570 16 E>D No EVA
rs3389081185 22 Q>K No EVA
rs222635150 29 G>S No EVA
rs239541379 31 L>P No EVA
rs3389068810 44 R>L No EVA
rs252770074 55 C>G No EVA
rs217187829 58 D>N No EVA
rs3389080935 68 V>A No EVA
rs3389026781 119 V>I No EVA
rs3389090868 128 Q>H No EVA
rs240753454 169 L>Q No EVA
rs224182109 179 I>T No EVA
rs3389074725 217 G>R No EVA
rs239000945 220 H>R No EVA
rs260444212 220 H>Y No EVA
rs227253067 232 N>D No EVA
rs3389091671 237 K>R No EVA
rs3389074732 246 E>D No EVA
rs586982565 388 V>I No EVA
rs3389082616 418 V>I No EVA

No associated diseases with Q8VCH0

5 regional properties for Q8VCH0

Type Name Position InterPro Accession
active_site Thiolase, active site 403 - 416 IPR020610
conserved_site Thiolase, conserved site 367 - 383 IPR020613
active_site Thiolase, acyl-enzyme intermediate active site 119 - 137 IPR020615
domain Thiolase, N-terminal 38 - 291 IPR020616
domain Thiolase, C-terminal 300 - 420 IPR020617

Functions

Description
EC Number 2.3.1.9 Transferring groups other than amino-acyl groups
Subcellular Localization
  • Peroxisome
  • Transported into peroxisomes following association with PEX7
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
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.
peroxisome A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism.

5 GO annotations of molecular function

Name Definition
acetate CoA-transferase activity Catalysis of the reaction: acyl-CoA + acetate = a fatty acid anion + acetyl-CoA.
acetyl-CoA C-acetyltransferase activity Catalysis of the reaction: 2 acetyl-CoA = CoA + acetoacetyl-CoA.
acetyl-CoA C-acyltransferase activity Catalysis of the reaction: acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.
acetyl-CoA C-myristoyltransferase activity Catalysis of the reaction: myristoyl-CoA + acetyl-CoA = 3-oxopalmitoyl-CoA + CoA.
palmitoyl-CoA oxidase activity Catalysis of the reaction: palmitoyl-CoA + O2 = trans-2,3-dehydropalmitoyl-CoA + hydrogen peroxide.

5 GO annotations of biological process

Name Definition
bile acid metabolic process The chemical reactions and pathways involving bile acids, a group of steroid carboxylic acids occurring in bile, where they are present as the sodium salts of their amides with glycine or taurine.
fatty acid beta-oxidation A fatty acid oxidation process that results in the complete oxidation of a long-chain fatty acid. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and occurs by successive cycles of reactions during each of which the fatty acid is shortened by a two-carbon fragment removed as acetyl coenzyme A; the cycle continues until only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).
fatty acid beta-oxidation using acyl-CoA oxidase A fatty acid beta-oxidation pathway in which the initial step, which converts an acyl-CoA to a trans-2-enoyl-CoA, is catalyzed by acyl-CoA oxidase; the electrons removed by oxidation pass directly to oxygen and produce hydrogen peroxide, which is cleaved by peroxisomal catalases. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and ends when only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).
phenylacetate catabolic process The chemical reactions and pathways resulting in the breakdown of phenylacetate.
very long-chain fatty acid metabolic process The chemical reactions and pathways involving a fatty acid which has a chain length greater than C22.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P27796 POT1 3-ketoacyl-CoA thiolase, peroxisomal Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
P09110 ACAA1 3-ketoacyl-CoA thiolase, peroxisomal Homo sapiens (Human) PR
Q921H8 Acaa1a 3-ketoacyl-CoA thiolase A, peroxisomal Mus musculus (Mouse) PR
P21775 Acaa1a 3-ketoacyl-CoA thiolase A, peroxisomal Rattus norvegicus (Rat) PR
P07871 Acaa1b 3-ketoacyl-CoA thiolase B, peroxisomal Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MHRLQVVLGH LAGRPESSSA LQAAPCSAGF LQASASDVVV VHGRRTPIGR ASRGCFKDTT
70 80 90 100 110 120
PDELLSAVLT AVLQDVKLKP EQLGDISVGN VLQPGAGAIM ARIAQFLSGI PETVPLSTVN
130 140 150 160 170 180
RQCSSGLQAV ANIAGGIRNG SYDIGMACGV ESMTLSQRGN HGNISSRLLE NEKARDCLIP
190 200 210 220 230 240
MGITSENVAE RFGVSRQKQD AFALASQQKA ASAQSRGCFH AEIVPVTTTV LNDKGDKKTI
250 260 270 280 290 300
TVSQDEGVRP STTMQGLAKL KPAFKDGGST TAGNSSQVSD GAAAVLLARR SKAEELGLPI
310 320 330 340 350 360
LGVLRSYAVV GVPPDVMGIG PAYAIPAALQ KAGLTVNDID IFEINEAFAS QAVYCVEKLG
370 380 390 400 410 420
IPAEKVNPLG GAIALGHPLG CTGARQVVTL LNELKRRGRR AYGVVSMCIG TGMGAAAVFE
YPGN