P77399
Gene name |
fadJ (yfcX, b2341, JW2338) |
Protein name |
Fatty acid oxidation complex subunit alpha |
Names |
|
Species |
Escherichia coli (strain K12) |
KEGG Pathway |
eco:b2341 |
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
No variants for P77399
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P77399 | |||||
No associated diseases with P77399
4 regional properties for P77399
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | 3-hydroxyacyl-CoA dehydrogenase, C-terminal | 492 - 586 | IPR006108-1 |
| domain | 3-hydroxyacyl-CoA dehydrogenase, C-terminal | 618 - 703 | IPR006108-2 |
| domain | 3-hydroxyacyl-CoA dehydrogenase, NAD binding | 311 - 489 | IPR006176 |
| conserved_site | 3-hydroxyacyl-CoA dehydrogenase, conserved site | 489 - 513 | IPR006180 |
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 |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| fatty acid beta-oxidation multienzyme complex | A multienzyme complex possessing three kinds of enzymes that catalyze the chain reactions in the fatty acid beta-oxidation cycle, enoyl-CoA hydratase (ECH), 3-hydroxyacyl-CoA dehydrogenase (HACD), and acetyl-CoA C-acyltransferase (KACT). |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| 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. |
| enoyl-CoA hydratase activity | Catalysis of the reaction: (3S)-3-hydroxyacyl-CoA = trans-2-enoyl-CoA + H2O. |
| long-chain-3-hydroxyacyl-CoA dehydrogenase activity | Catalysis of the reaction: (S)-3-hydroxyacyl-CoA + NAD(P)+ = 3-oxoacyl-CoA + NAD(P)H + H+, where the acyl group is a long-chain fatty acid residue. A long-chain fatty acid is a fatty acid with a chain length between C13 and C22. |
| 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). |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEMTSAFTLN | VRLDNIAVIT | IDVPGEKMNT | LKAEFASQVR | AIIKQLRENK | ELRGVVFVSA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KPDNFIAGAD | INMIGNCKTA | QEAEALARQG | QQLMAEIHAL | PIQVIAAIHG | ACLGGGLELA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LACHGRVCTD | DPKTVLGLPE | VQLGLLPGSG | GTQRLPRLIG | VSTALEMILT | GKQLRAKQAL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KLGLVDDVVP | HSILLEAAVE | LAKKERPSSR | PLPVRERILA | GPLGRALLFK | MVGKKTEHKT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QGNYPATERI | LEVVETGLAQ | GTSSGYDAEA | RAFGELAMTP | QSQALRSIFF | ASTDVKKDPG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SDAPPAPLNS | VGILGGGLMG | GGIAYVTACK | AGIPVRIKDI | NPQGINHALK | YSWDQLEGKV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RRRHLKASER | DKQLALISGT | TDYRGFAHRD | LIIEAVFENL | ELKQQMVAEV | EQNCAAHTIF |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ASNTSSLPIG | DIAAHATRPE | QVIGLHFFSP | VEKMPLVEII | PHAGTSAQTI | ATTVKLAKKQ |
| 490 | 500 | 510 | 520 | 530 | 540 |
| GKTPIVVRDK | AGFYVNRILA | PYINEAIRML | TQGERVEHID | AALVKFGFPV | GPIQLLDEVG |
| 550 | 560 | 570 | 580 | 590 | 600 |
| IDTGTKIIPV | LEAAYGERFS | APANVVSSIL | NDDRKGRKNG | RGFYLYGQKG | RKSKKQVDPA |
| 610 | 620 | 630 | 640 | 650 | 660 |
| IYPLIGTQGQ | GRISAPQVAE | RCVMLMLNEA | VRCVDEQVIR | SVRDGDIGAV | FGIGFPPFLG |
| 670 | 680 | 690 | 700 | 710 | |
| GPFRYIDSLG | AGEVVAIMQR | LATQYGSRFT | PCERLVEMGA | RGESFWKTTA | TDLQ |