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 Q921H8

Entry ID Method Resolution Chain Position Source
AF-Q921H8-F1 Predicted AlphaFoldDB

21 variants for Q921H8

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389057374 4 L>P No EVA
rs233299181 6 V>I No EVA
rs260425216 12 A>T No EVA
rs3389049636 20 A>V No EVA
rs3389081104 31 P>Q No EVA
rs3389074730 37 D>E No EVA
rs3389049649 88 V>E No EVA
rs3389080932 102 R>L No EVA
rs3389091668 149 G>W No EVA
rs247596253 179 T>I No EVA
rs3389091666 181 M>V No EVA
rs263622062 183 M>I No EVA
rs238966289 194 I>V No EVA
rs251784781 201 D>A No EVA
rs3389057442 253 T>I No EVA
rs3389080915 266 D>N No EVA
rs3389080988 375 L>P No EVA
rs3389087379 385 R>S No EVA
rs587133610 388 V>I No EVA
rs3389082364 391 L>H No EVA
rs3389070323 392 N>K No EVA

No associated diseases with Q921H8

5 regional properties for Q921H8

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 2.3.1.16 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

3 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.
peroxisomal matrix The volume contained within the membranes of a peroxisome; in many cells the matrix contains a crystalloid core largely composed of urate oxidase.
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.

8 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).
fatty acid metabolic process The chemical reactions and pathways involving fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis.
phenylacetate catabolic process The chemical reactions and pathways resulting in the breakdown of phenylacetate.
response to nutrient 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 nutrient stimulus.
response to steroid hormone 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 steroid hormone stimulus.
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
Q8VCH0 Acaa1b 3-ketoacyl-CoA thiolase B, 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 LQAAPCSARF PQASASDVVV VHGRRTPIGR ASRGGFKNTT
70 80 90 100 110 120
PDELLSAVLT AVLQDVRLKP EQLGDISVGN VLEPGAGAVM ARIAQFLSGI PETVPLSTVN
130 140 150 160 170 180
RQCSSGLQAV ANIAGGIRNG SYDIGMACGV ESMSLSGMGN PGNISSRLLE SEKARDCLTP
190 200 210 220 230 240
MGMTSENVAE RFGISRQKQD DFALASQQKA ASAQSRGCFR AEIVPVTTTV LDDKGDKKTI
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