Q8W1L6
Gene name |
MFP (Os02g0274100, LOC_Os02g17390, P0413A11.18) |
Protein name |
Peroxisomal fatty acid beta-oxidation multifunctional protein |
Names |
MFP |
Species |
Oryza sativa subsp japonica (Rice) |
KEGG Pathway |
osa:4328997 |
EC number |
1.1.1.35: With NAD(+) or NADP(+) as acceptor |
Protein Class |
|
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 Q8W1L6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8W1L6-F1 | Predicted | AlphaFoldDB |
No variants for Q8W1L6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q8W1L6 | |||||
No associated diseases with Q8W1L6
4 regional properties for Q8W1L6
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | 3-hydroxyacyl-CoA dehydrogenase, C-terminal | 492 - 585 | IPR006108 |
| domain | 3-hydroxyacyl-CoA dehydrogenase, NAD binding | 311 - 489 | IPR006176 |
| conserved_site | 3-hydroxyacyl-CoA dehydrogenase, conserved site | 489 - 513 | IPR006180 |
| conserved_site | Enoyl-CoA hydratase/isomerase, conserved site | 103 - 123 | IPR018376 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.1.1.35 | With NAD(+) or NADP(+) as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| microtubule | Any of the long, generally straight, hollow tubes of internal diameter 12-15 nm and external diameter 24 nm found in a wide variety of eukaryotic cells; each consists (usually) of 13 protofilaments of polymeric tubulin, staggered in such a manner that the tubulin monomers are arranged in a helical pattern on the microtubular surface, and with the alpha/beta axes of the tubulin subunits parallel to the long axis of the tubule; exist in equilibrium with pool of tubulin monomers and can be rapidly assembled or disassembled in response to physiological stimuli; concerned with force generation, e.g. in the spindle. |
| 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. |
8 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. |
| microtubule binding | Binding to a microtubule, a filament composed of tubulin monomers. |
| mRNA binding | Binding to messenger RNA (mRNA), an intermediate molecule between DNA and protein. mRNA includes UTR and coding sequences, but does not contain introns. |
| 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 |
|---|---|---|---|---|
| Q39659 | Glyoxysomal fatty acid beta-oxidation multifunctional protein MFP-a | Cucumis sativus (Cucumber) | PR | |
| P42126 | ECI1 | Enoyl-CoA delta isomerase 1, mitochondrial | Homo sapiens (Human) | PR |
| Q08426 | EHHADH | Peroxisomal bifunctional enzyme | Homo sapiens (Human) | PR |
| P23965 | Eci1 | Enoyl-CoA delta isomerase 1, mitochondrial | Rattus norvegicus (Rat) | PR |
| Q9ZPI5 | MFP2 | Peroxisomal fatty acid beta-oxidation multifunctional protein MFP2 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAGAIRVTME | VGADGVAVVT | ICNPPVNALH | PIIIQGLKEK | YAEAMDRDDV | KAIVLTGAGG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KFCGGFDINV | FTEVHKTGNV | SLMPDVSVEL | VSNLMEAGKK | PSVAAIQGLA | LGGGLELTMG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| CHARISTPEA | QLGLPELTLG | IIPGFGGTQR | LPRLVGLPKA | IEMMLQSKFI | TAKEGKEGGL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VDALCSPDEL | IKMSRLWALE | IANYRKPWIR | SLARTDRLGS | LSEARSVLNS | ARQQAKKVAA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NLPQHQACLD | VMEEGVLCGG | HAGVLKEAKV | FKELVLSPTS | KALVHAFFAQ | RLTTKVPGVT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DVQLKPRKIR | KVAVIGGGLM | GSGIATALLV | SNTSVVLKEV | NPQFLQRGQK | MIAANLEGLV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KRGSLTKDKM | NKAMSLLKGA | LDYSDFKDVD | MVIEAVIEKI | PLKQSIFSDL | EKVCPPHCIL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ATNTSTIDLN | VVGEKTNSQD | RIIGAHFFSP | AHIMPLLEIV | RTEKTSPQAI | LDLITVGKMI |
| 490 | 500 | 510 | 520 | 530 | 540 |
| KKVPVVVGNC | TGFAVNRTFF | PYTQGSHLLV | SIGIDVFRID | RVISSFGMPM | GPFQLQDLAG |
| 550 | 560 | 570 | 580 | 590 | 600 |
| YGVALAVKDI | YAAAFGTRNL | DSNLVDLMVQ | NGRQGKSNGK | GYYLYEKGGK | PKPDPSVQVV |
| 610 | 620 | 630 | 640 | 650 | 660 |
| IDEYRRCAKT | MPGGKPVTLS | DQDILEMIFF | PVVNEACRVM | DENVVIRASD | LDIASILGMG |
| 670 | 680 | 690 | 700 | 710 | 720 |
| FPKFRGGLVF | WADTIGAPYI | HSKLSKWTEI | YGDFFKPSSY | LEDRAKRSLP | LSAPNATQQA |
| SSRSRM |