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Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Pseudomonas fragi
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate.UniRule annotation

Catalytic activityi

(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.UniRule annotation
(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O.UniRule annotation
(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA.UniRule annotation
(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.UniRule annotation

Pathwayi: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei120Important for catalytic activityUniRule annotation1
Sitei140Important for catalytic activityUniRule annotation1
Binding sitei297Substrate1 Publication1
Binding sitei325NAD; via amide nitrogen1 Publication1
Binding sitei344NAD1 Publication1
Binding sitei408NAD1 Publication1
Binding sitei430NAD1 Publication1
Active sitei451For 3-hydroxyacyl-CoA dehydrogenase activityUniRule annotation1
Binding sitei454NAD1 Publication1
Binding sitei501Substrate1 Publication1
Binding sitei660Substrate1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi401 – 403NAD1 Publication3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase, Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid degradation, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid oxidation complex subunit alphaUniRule annotation
Including the following 2 domains:
Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimeraseUniRule annotation (EC:4.2.1.17UniRule annotation, EC:5.1.2.3UniRule annotation, EC:5.3.3.8UniRule annotation)
3-hydroxyacyl-CoA dehydrogenaseUniRule annotation (EC:1.1.1.35UniRule annotation)
Gene namesi
Name:fadBUniRule annotation
Synonyms:faoA
OrganismiPseudomonas fragi
Taxonomic identifieri296 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001092761 – 715Fatty acid oxidation complex subunit alphaAdd BLAST715

Expressioni

Inductioni

By palmitic acid.1 Publication

Interactioni

Subunit structurei

Heterotetramer of two alpha chains (FadB) and two beta chains (FadA).UniRule annotation1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
fadAP287903EBI-1039318,EBI-1039311

Protein-protein interaction databases

DIPiDIP-29089N.
IntActiP28793. 1 interactor.

Structurei

Secondary structure

1715
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 12Combined sources7
Helixi14 – 16Combined sources3
Beta strandi17 – 22Combined sources6
Beta strandi27 – 29Combined sources3
Helixi34 – 49Combined sources16
Beta strandi55 – 67Combined sources13
Helixi71 – 77Combined sources7
Helixi82 – 100Combined sources19
Beta strandi106 – 110Combined sources5
Helixi117 – 123Combined sources7
Beta strandi125 – 131Combined sources7
Beta strandi135 – 137Combined sources3
Helixi139 – 143Combined sources5
Turni148 – 150Combined sources3
Helixi151 – 159Combined sources9
Helixi161 – 170Combined sources10
Beta strandi173 – 175Combined sources3
Helixi176 – 181Combined sources6
Beta strandi184 – 189Combined sources6
Helixi191 – 193Combined sources3
Helixi194 – 206Combined sources13
Beta strandi207 – 210Combined sources4
Helixi212 – 216Combined sources5
Helixi217 – 220Combined sources4
Helixi227 – 245Combined sources19
Helixi250 – 262Combined sources13
Helixi267 – 282Combined sources16
Helixi285 – 308Combined sources24
Beta strandi315 – 320Combined sources6
Helixi323 – 335Combined sources13
Beta strandi340 – 343Combined sources4
Helixi347 – 365Combined sources19
Turni366 – 368Combined sources3
Helixi372 – 381Combined sources10
Beta strandi382 – 388Combined sources7
Helixi391 – 393Combined sources3
Beta strandi395 – 399Combined sources5
Helixi405 – 416Combined sources12
Beta strandi424 – 427Combined sources4
Beta strandi430 – 432Combined sources3
Helixi434 – 437Combined sources4
Helixi438 – 440Combined sources3
Helixi444 – 446Combined sources3
Beta strandi447 – 451Combined sources5
Turni456 – 458Combined sources3
Beta strandi461 – 466Combined sources6
Helixi472 – 484Combined sources13
Beta strandi488 – 494Combined sources7
Turni496 – 499Combined sources4
Helixi500 – 516Combined sources17
Helixi521 – 531Combined sources11
Helixi537 – 544Combined sources8
Helixi546 – 559Combined sources14
Helixi561 – 564Combined sources4
Helixi571 – 577Combined sources7
Turni583 – 586Combined sources4
Beta strandi587 – 592Combined sources6
Beta strandi599 – 603Combined sources5
Helixi607 – 612Combined sources6
Helixi613 – 615Combined sources3
Helixi624 – 644Combined sources21
Beta strandi647 – 650Combined sources4
Helixi651 – 661Combined sources11
Helixi666 – 668Combined sources3
Helixi671 – 678Combined sources8
Helixi680 – 689Combined sources10
Helixi690 – 693Combined sources4
Helixi695 – 697Combined sources3
Helixi701 – 708Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WDKX-ray2.50A/B1-715[»]
1WDLX-ray3.50A/B1-715[»]
1WDMX-ray3.80A/B1-715[»]
2D3TX-ray3.40A/B1-715[»]
ProteinModelPortaliP28793.
SMRiP28793.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28793.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 190Enoyl-CoA hydratase/isomeraseUniRule annotationAdd BLAST190
Regioni312 – 7153-hydroxyacyl-CoA dehydrogenaseUniRule annotationAdd BLAST404

Sequence similaritiesi

In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.UniRule annotation
In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.UniRule annotation

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
HAMAPiMF_01621. FadB. 1 hit.
InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR012799. FadB.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH_1. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF51735. SSF51735. 1 hit.
SSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR02437. FadB. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P28793-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIYEGKAITV TALESGIVEL KFDLKGESVN KFNRLTLNEL RQAVDAIKAD
60 70 80 90 100
ASVKGVIVSS GKDVFIVGAD ITEFVENFKL PDAELIAGNL EANKIFSDFE
110 120 130 140 150
DLNVPTVAAI NGIALGGGLE MCLAADFRVM ADSAKIGLPE VKLGIYPGFG
160 170 180 190 200
GTVRLPRLIG VDNAVEWIAS GKENRAEDAL KVSAVDAVVT ADKLGAAALD
210 220 230 240 250
LIKRAISGEL DYKAKRQPKL EKLKLNAIEQ MMAFETAKGF VAGQAGPNYP
260 270 280 290 300
APVEAIKTIQ KAANFGRDKA LEVEAAGFAK LAKTSASNCL IGLFLNDQEL
310 320 330 340 350
KKKAKVYDKI AKDVKQAAVL GAGIMGGGIA YQSASKGTPI LMKDINEHGI
360 370 380 390 400
EQGLAEAAKL LVGRVDKGRM TPAKMAEVLN GIRPTLSYGD FGNVDLVVEA
410 420 430 440 450
VVENPKVKQA VLAEVENHVR EDAILASNTS TISISLLAKA LKRPENFVGM
460 470 480 490 500
HFFNPVHMMP LVEVIRGEKS SDLAVATTVA YAKKMGKNPI VVNDCPGFLV
510 520 530 540 550
NRVLFPYFGG FAKLVSAGVD FVRIDKVMEK FGWPMGPAYL MDVVGIDTGH
560 570 580 590 600
HGRDVMAEGF PDRMKDDRRS AIDALYEAKR LGQKNGKGFY AYEADKKGKQ
610 620 630 640 650
KKLVDSSVLE VLKPIVYEQR DVTDEDIINW MMIPLCLETV RCLEDGIVET
660 670 680 690 700
AAEADMGLVY GIGFPLFRGG ALRYIDSIGV AEFVALADQY AELGALYHPT
710
AKLREMAKNG QSFFG
Length:715
Mass (Da):77,137
Last modified:December 1, 1992 - v1
Checksum:iF22727CDEF7F3DB5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10390 Genomic DNA. Translation: BAA01227.1.
PIRiJX0199.

Genome annotation databases

GeneIDi24444371.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10390 Genomic DNA. Translation: BAA01227.1.
PIRiJX0199.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WDKX-ray2.50A/B1-715[»]
1WDLX-ray3.50A/B1-715[»]
1WDMX-ray3.80A/B1-715[»]
2D3TX-ray3.40A/B1-715[»]
ProteinModelPortaliP28793.
SMRiP28793.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29089N.
IntActiP28793. 1 interactor.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24444371.

Enzyme and pathway databases

UniPathwayiUPA00659.

Miscellaneous databases

EvolutionaryTraceiP28793.

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
HAMAPiMF_01621. FadB. 1 hit.
InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR012799. FadB.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH_1. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF51735. SSF51735. 1 hit.
SSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR02437. FadB. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFADB_PSEFR
AccessioniPrimary (citable) accession number: P28793
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: November 2, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.