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 Q39659

Entry ID Method Resolution Chain Position Source
AF-Q39659-F1 Predicted AlphaFoldDB

No variants for Q39659

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q39659

No associated diseases with Q39659

4 regional properties for Q39659

Type Name Position InterPro Accession
domain 3-hydroxyacyl-CoA dehydrogenase, C-terminal 495 - 588 IPR006108
domain 3-hydroxyacyl-CoA dehydrogenase, NAD binding 314 - 492 IPR006176
conserved_site 3-hydroxyacyl-CoA dehydrogenase, conserved site 492 - 516 IPR006180
conserved_site Enoyl-CoA hydratase/isomerase, conserved site 106 - 126 IPR018376

Functions

Description
EC Number 1.1.1.35 With NAD(+) or NADP(+) as acceptor
Subcellular Localization
  • Glyoxysome
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
glyoxysome A specialized form of peroxisome that contains the enzymes of the glyoxylate pathway. The glyoxysome is found in some plant cells, notably the cells of germinating seeds.

6 GO annotations of molecular function

Name Definition
3-hydroxyacyl-CoA dehydratase activity Catalysis of the reaction: alkene-CoA + H2O = alcohol-CoA. Substrates are crotonoyl-CoA (producing 3-hydroxyacyl-CoA) and 2,3-didehydro-pimeloyl-CoA (producing 3-hydroxypimeloyl-CoA).
3-hydroxyacyl-CoA dehydrogenase activity Catalysis of the reaction: (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H(+).
3-hydroxybutyryl-CoA epimerase activity Catalysis of the reaction: (S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA.
delta(3)-delta(2)-enoyl-CoA isomerase activity Catalysis of the reactions: a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA or a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA.
enoyl-CoA hydratase activity Catalysis of the reaction: (3S)-3-hydroxyacyl-CoA = trans-2-enoyl-CoA + H2O.
NAD+ binding Binding to the oxidized form, NAD, of nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions.

1 GO annotations of biological process

Name Definition
fatty acid beta-oxidation A fatty acid oxidation process that results in the complete oxidation of a long-chain fatty acid. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and occurs by successive cycles of reactions during each of which the fatty acid is shortened by a two-carbon fragment removed as acetyl coenzyme A; the cycle continues until only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q08426 EHHADH Peroxisomal bifunctional enzyme Homo sapiens (Human) PR
P42126 ECI1 Enoyl-CoA delta isomerase 1, mitochondrial Homo sapiens (Human) PR
P23965 Eci1 Enoyl-CoA delta isomerase 1, mitochondrial Rattus norvegicus (Rat) PR
Q8W1L6 MFP Peroxisomal fatty acid beta-oxidation multifunctional protein Oryza sativa subsp japonica (Rice) PR
Q9ZPI5 MFP2 Peroxisomal fatty acid beta-oxidation multifunctional protein MFP2 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MGSNAKGRTV MEVGTDGVAI ITIINPPVNS LSFDVLFSLR DSYEQALRRD DVKAIVVTGA
70 80 90 100 110 120
KGKFSGGFDI TAFGVLQGGK GEQPNVRNIS IEMITDIFEA ARKPAVAAID GLALGGGLEV
130 140 150 160 170 180
AMACHARIST PTAQLGLPEL QLGIIPGFGG TQRLPRLVGL SKALEMMLTS KPIKGQEAHS
190 200 210 220 230 240
LGLVDAIVPP EELINTARRW ALEILERRRP WVHSLHRTDK LESLAEARKI FNLARAQAKK
250 260 270 280 290 300
QYPNLKHTIA CIDAVETGVV SGPRAGLWKE AEEFQGLLHS DTCKSLIHIF FAQRSTTKVP
310 320 330 340 350 360
GVTDLGLVPR QIKKVAIVGG GLMGSGIATA LILSNYHVVL KEVNDKFLQA GIDRVRANLQ
370 380 390 400 410 420
SRVKKGNMTN EKFEKSISLL KGVLNYESFK DVDMVIEAVI ENVSLKQQIF SDLEKYCPPH
430 440 450 460 470 480
CMLATNTSTI DLELIGERIK SRDRIIGAHF FSPAHIMPLL EIVRTKHTAA QVIVDLLDVG
490 500 510 520 530 540
KNIKKTPVVV GNCTGFAVNR MFFPYSQAAI LLAEHGVDPY QIDRAISKFG MPMGPFRLCD
550 560 570 580 590 600
LVGFGVAAAT ASQFVQAFPE RTYKSMLIPL MQEDKNAGES TRKGFYVYDK NRKAGPNPEL
610 620 630 640 650 660
KKYIEKARNS SGVSVDPKLT KLPEKDIVEM IFFPVVNEAC RVLAEGIAVK AADLDIAGVM
670 680 690 700 710 720
GMGFPSYRGG LMFWADSLGS NYIYSRLEEW SKQYGGFFKP CGYLAERAVQ GATLSAPGGH
AKPRM