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 O18778

Entry ID Method Resolution Chain Position Source
AF-O18778-F1 Predicted AlphaFoldDB

31 variants for O18778

Variant ID(s) Position Change Description Diseaes Association Provenance
rs473062411 3 R>Q No EVA
rs452814087 12 V>F No EVA
rs433087965 16 H>R No EVA
rs522353154 21 S>L No EVA
rs450603459 24 T>I No EVA
rs209515573 27 A>S No EVA
rs133068456 38 S>T No EVA
rs718030422 40 H>Y No EVA
rs724106506 80 R>C No EVA
rs133576003 86 E>Q No EVA
rs447863577 93 V>L No EVA
rs447863577 93 V>M No EVA
rs136371133 99 S>L No EVA
rs134434589 107 T>A No EVA
rs452959878 108 K>E No EVA
rs721743482 147 T>N No EVA
rs1117037286 150 N>S No EVA
rs110811906 154 M>I No EVA
rs209453111 165 S>F No EVA
rs42312254 188 S>N No EVA
rs382982209 201 R>Q No EVA
rs133799397 218 Q>K No EVA
rs132658757 235 G>R No EVA
rs434235338 268 R>Q No EVA
rs438210098 318 T>A No EVA
rs481652354 321 D>V No EVA
rs461526714 322 V>F No EVA
rs448102977 322 V>G No EVA
rs459185914 324 T>S No EVA
rs439158291 326 R>L No EVA
rs463601925 331 K>N No EVA

No associated diseases with O18778

No regional properties for O18778

Type Name Position InterPro Accession
No domain, repeats, and functional sites for O18778

Functions

Description
EC Number 1.14.11.18 With 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Subcellular Localization
  • Peroxisome
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
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.

3 GO annotations of molecular function

Name Definition
L-ascorbic acid binding Binding to L-ascorbic acid, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate; L-ascorbic acid is vitamin C and has co-factor and anti-oxidant activities in many species.
metal ion binding Binding to a metal ion.
phytanoyl-CoA dioxygenase activity Catalysis of the reaction: 2-oxoglutarate + O(2) + phytanoyl-CoA = 2-hydroxyphytanoyl-CoA + CO(2) + succinate.

1 GO annotations of biological process

Name Definition
fatty acid alpha-oxidation A metabolic pathway by which 3-methyl branched fatty acids are degraded. These compounds are not degraded by the normal peroxisomal beta-oxidation pathway, because the 3-methyl blocks the dehydrogenation of the hydroxyl group by hydroxyacyl-CoA dehydrogenase. The 3-methyl branched fatty acid is converted in several steps to pristenic acid, which can then feed into the beta-oxidative pathway.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
O14832 PHYH Phytanoyl-CoA dioxygenase, peroxisomal Homo sapiens (Human) PR
O35386 Phyh Phytanoyl-CoA dioxygenase, peroxisomal Mus musculus (Mouse) PR
10 20 30 40 50 60
MDRNRASARL TVLLRHLGCR SAGTIIAHHT SGVGSLASFH PQQFQYTREN NVLSLEQRKF
70 80 90 100 110 120
YEENGFLVIK NLVSDADIQR FRNEFERICR KEVKPLGLSV MRDVTITKSE YVPSEKVVSK
130 140 150 160 170 180
VQDFQEDEEL FRYCTLPEIL KYVECFTGPN IMAMHTMLIN KPPDSGKKTS RHPLHQDLHY
190 200 210 220 230 240
FPFRPSNSIV CAWTAMEHID RNNGCLVVLP GTHKGPLQPH DYPQWEGGVN IMFHGIQDYD
250 260 270 280 290 300
KNNARVHLVM EKGDTVFFHP LLIHGSGRNK SQGFRKAISC HFADANCHYI DVEGTSQENI
310 320 330
EKEVVDIVRK KYGFKDVTLK DVWTFRGRVV KGERINL