B7I3P1
Gene name |
fadB |
Protein name |
Fatty acid oxidation complex subunit alpha |
Names |
|
Species |
Acinetobacter baumannii (strain AB0057) |
KEGG Pathway |
abn:AB57_0387 |
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 B7I3P1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B7I3P1-F1 | Predicted | AlphaFoldDB |
No variants for B7I3P1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B7I3P1 | |||||
No associated diseases with B7I3P1
4 regional properties for B7I3P1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | 3-hydroxyacyl-CoA dehydrogenase, C-terminal | 498 - 593 | IPR006108 |
| domain | 3-hydroxyacyl-CoA dehydrogenase, NAD binding | 318 - 496 | IPR006176 |
| conserved_site | 3-hydroxyacyl-CoA dehydrogenase, conserved site | 495 - 519 | IPR006180 |
| conserved_site | Enoyl-CoA hydratase/isomerase, conserved site | 107 - 127 | 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 | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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. |
| 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). |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MIHAGNAITV | QMLADGIAEF | RFDLQGESVN | KFNRATIEDF | KAAIAAVKAN | NDIKGLVVTS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GKSTFIVGAD | ITEFGQNFAQ | GEKAIVDWLM | PVHEIFNSFE | DLDLPKVAAI | NGMALGGGFE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| MCLVCDYRVM | SEAAQVGLPE | IKLGIYPGFG | GSVRLSRLIG | IDNAVEWMAM | ATPKKPAAAL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KDGAVDAVVA | ADKLLDAATD | LVKQAISGRL | NWKAKRQEKL | EAVKLNPLEQ | MMAFNTAKGA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VLAKANPAQY | PAPKLLLDSL | QAGASLARDE | ALKAEAEGFA | KAAVTPQAEA | LIGLFINDQV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VKKASKQHEK | GAHPVNQAAV | LGAGIMGGGI | AYQAASKGTP | IIMKDIGNPQ | LALGMKEANN |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LLTKQVERKK | MKPVQMGETL | ARIRPTLSYE | EFKEVDIVIE | AVTENPKVKE | IVLAETEKNV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| RENTIIASNT | STISITRLAK | ALQRPENFVG | MHFFNPVHMM | PLVEVIRGEK | TSEEAIATTV |
| 490 | 500 | 510 | 520 | 530 | 540 |
| VLAQKMGKTP | IVVNDCPGFL | VNRVLFPYFG | AFDLLVKDGA | DFQQIDNVMS | KFGWPMGPAY |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LIDVVGIDTG | VHGAEVMAEG | FPDRMKPDYK | GAIEAMYEAK | RLGQKNDVGF | YKYELDKKGK |
| 610 | 620 | 630 | 640 | 650 | 660 |
| KAKTVDPTAY | EVIAPFVTGE | KREFDNQEII | DRMMLALCNE | TVRCLEDNIV | ATASEADMAM |
| 670 | 680 | 690 | 700 | 710 | |
| IMGIGFPPFR | GGPCRYIDQT | GVAEYVALCD | KYAHLGKAYE | APQMLRDMAA | NNKKFYG |