Q756A9

PR
Gene name
POX1 (AER358C)
Protein name
Acyl-coenzyme A oxidase
Names
Acyl-CoA oxidase
Species
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
KEGG Pathway
ago:AGOS_AER358C
EC number
1.3.3.6: With oxygen as acceptor
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-51 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q756A9

Entry ID Method Resolution Chain Position Source
AF-Q756A9-F1 Predicted AlphaFoldDB

No variants for Q756A9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q756A9

No associated diseases with Q756A9

4 regional properties for Q756A9

Type Name Position InterPro Accession
domain Acyl-CoA oxidase, C-terminal 538 - 712 IPR002655
domain Acyl-CoA oxidase/dehydrogenase, middle domain 181 - 291 IPR006091
domain Acyl-CoA dehydrogenase/oxidase C-terminal 328 - 492 IPR009075
domain Acyl-coenzyme A oxidase, N-terminal 31 - 168 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

2 GO annotations of cellular component

Name Definition
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.

4 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.
fatty acid binding Binding to a fatty acid, an aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis.
flavin adenine dinucleotide binding Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.

2 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).
lipid homeostasis Any process involved in the maintenance of an internal steady state of lipid within an organism or cell.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTKASVVDQS APAYAPKRLL AEARAASKVN IEQVFAFLEG SPEKAALTNE LLAEFAADPA
70 80 90 100 110 120
ITQGPEYYDL TKAEQREQTV KKIARLALYL ENDIKLARKQ HHKDVVRDLQ SPDAPMVTMS
130 140 150 160 170 180
DMERFEKRST LVALIDPQLA TRLGVNLSLF GNAVRGNGTD EQIKYWLQER GLIFVKGIYG
190 200 210 220 230 240
CFAMTELGHG SNVANLQTRA TYDPASDSFV IQTPDLVATK WWIGGAAHSA THSTVYARLI
250 260 270 280 290 300
VEGKDYGVKV FVVPLRNPKT MELLAGISIG DIGSKMGRDG IDNGWIQFNN VRIPREYMLS
310 320 330 340 350 360
RFTKVIPGNP PKVEMEPLLD SISGYAALLS GRVSMVLDSY RFGARFSTIA TRYAFGRQQF
370 380 390 400 410 420
GDPTNETQLI EYPLHQFRVL PQLAIIYMMA PGAMKLMDTY NSCLGELYGA GDDKKKLTTV
430 440 450 460 470 480
SARMKDLFVE SASLKATCTW LTSTLIDELR QTCGGHGYSS YNGFGKAYND WVVQCTWEGD
490 500 510 520 530 540
NNVLCLTSGK SLLKKFAGIV RGKKVTICDT SMDYLRMDYI QKVVMGGTKK VSNLSTLPDY
550 560 570 580 590 600
YQIWSVILVK YLKRCAETVR DNNDPESVSK LLVSIAKFHA FYSMLQEFHR KLASDQSHVG
610 620 630 640 650 660
DAATKEVLWK VYKLSSLYFI DKFSGEFQQL KVMSPDQMTN VQEQMLAILP EIKTHAIRLT
670 680 690 700 710 720
DAFHLPDAVI NSSIGNYDGD IYHNYFNDVT RVAAKDKAPG VPPYADMLVN FLARGDQFDN
730
LNISETSFKN LGK