Q8HXY7

PR
Gene name
ACADVL
Protein name
Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
Names
VLCAD
Species
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
KEGG Pathway
EC number
1.3.8.9: With a flavin as acceptor
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-104 (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 Q8HXY7

Entry ID Method Resolution Chain Position Source
AF-Q8HXY7-F1 Predicted AlphaFoldDB

No variants for Q8HXY7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8HXY7

No associated diseases with Q8HXY7

3 regional properties for Q8HXY7

Type Name Position InterPro Accession
domain Oxoglutarate/iron-dependent dioxygenase 152 - 256 IPR005123
domain Non-haem dioxygenase N-terminal domain 3 - 104 IPR026992
domain Isopenicillin N synthase-like, Fe(2+) 2OG dioxygenase domain 163 - 256 IPR044861

Functions

Description
EC Number 1.3.8.9 With a flavin as acceptor
Subcellular Localization
  • Mitochondrion inner membrane ; Peripheral membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
extrinsic component of mitochondrial inner membrane The component of mitochondrial inner membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region.

4 GO annotations of molecular function

Name Definition
acyl-CoA dehydrogenase activity Catalysis of the reaction: acyl-CoA + oxidized
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.
identical protein binding Binding to an identical protein or proteins.
very-long-chain-acyl-CoA dehydrogenase activity Catalysis of the reaction: a very-long-chain 2,3-saturated fatty acyl-CoA + H+ + oxidized = a very-long-chain (2E)-enoyl-CoA + reduced

1 GO annotations of biological process

Name Definition
fatty acid beta-oxidation using acyl-CoA dehydrogenase A fatty acid beta-oxidation pathway in which the initial step of each oxidation cycle, which converts an acyl-CoA to a trans-2-enoyl-CoA, is catalyzed by acyl-CoA dehydrogenase; the electrons removed by oxidation pass through the respiratory chain to oxygen and leave H2O as the product. 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
MQAARIAPSL GRQLLRFGGG SSRPTALLGQ PWPGPARRPY AGGAAQLALD KSDSHLSDAL
70 80 90 100 110 120
NKAKPAKAES KSFAVAMFKG QLTTDQVFPY PSVLNQEQTE FLKELVEPVS RFFEEVNDPA
130 140 150 160 170 180
KNDTLEMVEE TTLQGLKELG AFGLQVPSEL GGVGLCNTQY ARLVEIVGMH DLAVGITLGA
190 200 210 220 230 240
HQSIGFKGIL LFGTKAQKEK YLPKLASGET LAAFCLTEPS SGSDAASIRT SAVPSPCGKY
250 260 270 280 290 300
YTLNGSKLWI SNGGLADIFT VFAKTPVTDP ATGAVKEKIT AFVVERGFGG VTHGPPEKKM
310 320 330 340 350 360
GIKASNTAEV LFDGVRVPSE NVLGEVGSGF KVAMHILNNG RFGMAAALAG TMRGIITKAV
370 380 390 400 410 420
DYATNRIQFG EKIHNFGLIQ EKLARMVMLQ YVTESMAYMV SANMDQGSTD FQIEAAISKI
430 440 450 460 470 480
FGSEAAWKVT DECIQIMGGM GFMKEPGVER VLRDLRIFRI FEGTNDILRL FVALQGCMDK
490 500 510 520 530 540
GKELSGLGSA LKNPFGNAGL LLGEAGKQLR RRAGLGSGLS LSGIVHPELS RSGELAVQAL
550 560 570 580 590 600
EQFATVVEAK LIKHKKGIVN EQFLLQRLAD GAIDLYAMVV VLSRASRSLS EGHHTAQHEK
610 620 630 640 650
MLCDTWCIEA AARIREGMAA LQSDPRQHEL YRNFKSISKA LVERGGVVTN NPLGF