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 Q00468

Entry ID Method Resolution Chain Position Source
AF-Q00468-F1 Predicted AlphaFoldDB

No variants for Q00468

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q00468

No associated diseases with Q00468

3 regional properties for Q00468

Type Name Position InterPro Accession
domain Acyl-CoA oxidase, C-terminal 553 - 702 IPR002655
domain Acyl-CoA oxidase/dehydrogenase, middle domain 181 - 285 IPR006091
domain Acyl-coenzyme A oxidase, N-terminal 53 - 166 IPR029320

Functions

Description
EC Number 1.3.3.6 With oxygen as acceptor
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.

2 GO annotations of molecular function

Name Definition
acyl-CoA oxidase activity Catalysis of the reaction: acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + hydrogen peroxide.
FAD binding Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.

1 GO annotations of biological process

Name Definition
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).

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MALISNLKDE YDHPTKTDPD TNPKIVADII SSKEPPQPSQ DVAEERSRTD WDLKEMHEFL
70 80 90 100 110 120
EGDEAKSEEI LRLYQSIERD PILQTRPEQF DYTKNEERES VALRINQMSK YLETEPYEKF
130 140 150 160 170 180
RRRLQLMTVN DPSLGIRMLV NIGLFLNCIR GNGTQKQYDF WAKTKEAGKV KQLLRLFRYD
190 200 210 220 230 240
ELGHGFNVAG CEIFATFDEK TDQFIIDTPH IGATKWWIGG AAHSATHTVC YARLIVKDID
250 260 270 280 290 300
YGVKTFVVPL RDSTHNLLPG VAIGDIGPKL GRQGVDNGWI QFTEVRIPRF FMLQRWCKVD
310 320 330 340 350 360
RQGNVTLPPL EQLSYISLLE GRVGMATDSY RIGARYTTIA LRYAVARRQF SKGDGQPETK
370 380 390 400 410 420
LIDYTLHQRR LLPYLALTYL AALGTDKLER QHDQLLKNLD KALATNNKLL LKNTIQSTKS
430 440 450 460 470 480
MFVDSGSLKS TLTWLASDLI NEARQSCGGH GYSAYNGFGK TYGDWAVQCT WEGDNNVLGM
490 500 510 520 530 540
SAGKTIIKTV QQVLNGKQLK DSTLEFLNDA PALSSAKKAV IRIKSHVDDT DRVLKAIAGL
550 560 570 580 590 600
ISKYAKDLIP VSYQSWDSIG PQRVVLSKFR CHYYLLETFN ERLNDRIKAK SPARPHLENI
610 620 630 640 650 660
IKLYYVTNVL GPFIDEFLRF GVISPSVAKY ITTEYPQKLC AAIRPYVIGL TDSFQQPDNF
670 680 690 700 710 720
INSLIGRYDG NVYTNYLTNV TNVNDPTNYK APYSEALEAM LNRASLEERE RFEKSKAVAA
KLSQ