Q6CKK7

PR
Gene name
POX1 (KLLA0F09933g)
Protein name
Acyl-coenzyme A oxidase
Names
Acyl-CoA oxidase
Species
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
KEGG Pathway
kla:KLLA0_F09933g
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)

1-62 (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 Q6CKK7

Entry ID Method Resolution Chain Position Source
AF-Q6CKK7-F1 Predicted AlphaFoldDB

No variants for Q6CKK7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6CKK7

No associated diseases with Q6CKK7

3 regional properties for Q6CKK7

Type Name Position InterPro Accession
domain Acyl-CoA oxidase, C-terminal 535 - 713 IPR002655
domain Acyl-CoA oxidase/dehydrogenase, middle domain 181 - 291 IPR006091
domain Acyl-coenzyme A oxidase, N-terminal 30 - 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

1 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.

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
MTRQSTVDQN QSTYNAKNFI TKERQESKLD IDQLNVFLEN GEQEAKLTHD LIEEIINDPI
70 80 90 100 110 120
LKTDTDHYDI TKSQEREITA RRIARLSLYM EHDVKTKQRE FKDDLVKNLE RKDSKLLTNK
130 140 150 160 170 180
DLSIFDRRLS LVANIDPGLS TRIGVHLGLF GNCIKGNGTD EQIHYWLQEK GALLLKGIYG
190 200 210 220 230 240
CFAMTELGHG SNVAQLQTTA TYDPSSDTFK INTPDLLATK WWIGGAAHSA THTTAYARLI
250 260 270 280 290 300
VNGKDYGVKT FVVPLRDEKT LNLLPGIMIG DIGAKMGRDG IDNGWIQFKN VVIPRQFMLQ
310 320 330 340 350 360
RFTKVIPGSP PKVQTQPLLD QISGYSALLS GRVNMVMDSF RFGSKFAIIA TRYAVGRQQF
370 380 390 400 410 420
GPEGNETQLI DYPLHQYRVL PQLALCYLVA PTAHKLMGTY ISTLMELHQA GADKAKLINV
430 440 450 460 470 480
SNKLKDLFID SASLKATNTW LVAKLIDDLR QTCGGHGYSS YNGFGKGYND WVVQCTWEGD
490 500 510 520 530 540
NNILSLTSAK SIVKKFADIS RGKNTTVTTD SLKYLTPQFI GKSLSKDLTF KFDNKKDFTE
550 560 570 580 590 600
IWAVMIIRLI HHVVELISKG TKIDSLSKTL VQISKFHAIH SMLLTYQDKL NNESEASVKD
610 620 630 640 650 660
AYTKGYLWKL YELFSLYFID QHLGEFLLLK VVTSDQMSQV LQPRLLQLLP EIRKECIALT
670 680 690 700 710 720
DAFKLPDAMI NAPIGYYDGD IYHNYFNEVT NNNKLEPDGA GRPPYYPLLT SMLGRDDFQN
730
RLGGSFESET LDSLLK