Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P28793

- FADB_PSEFR

UniProt

P28793 - FADB_PSEFR

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Pseudomonas fragi
Status
Reviewed - 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei120 – 1201Important for catalytic activityUniRule annotation
Sitei140 – 1401Important for catalytic activityUniRule annotation
Binding sitei297 – 2971Substrate
Binding sitei325 – 3251NAD; via amide nitrogen
Binding sitei344 – 3441NAD
Binding sitei408 – 4081NAD
Active sitei451 – 4511For 3-hydroxyacyl-CoA dehydrogenase activityUniRule annotation
Binding sitei454 – 4541NAD
Binding sitei501 – 5011Substrate
Binding sitei660 – 6601Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi401 – 4033NAD
Nucleotide bindingi428 – 4303NAD

GO - Molecular functioni

  1. 3-hydroxyacyl-CoA dehydrogenase activity Source: UniProtKB-HAMAP
  2. 3-hydroxybutyryl-CoA epimerase activity Source: UniProtKB-HAMAP
  3. coenzyme binding Source: InterPro
  4. dodecenoyl-CoA delta-isomerase activity Source: UniProtKB-HAMAP
  5. enoyl-CoA hydratase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. fatty acid beta-oxidation Source: UniProtKB-UniPathway
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

  1. fatty acid beta-oxidation multienzyme complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 715715Fatty acid oxidation complex subunit alphaPRO_0000109276Add
BLAST

Expressioni

Inductioni

By palmitic acid.1 Publication

Interactioni

Subunit structurei

Heterotetramer of two alpha chains (FadB) and two beta chains (FadA).1 PublicationUniRule annotation

Binary interactionsi

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

Protein-protein interaction databases

DIPiDIP-29089N.
IntActiP28793. 1 interaction.

Structurei

Secondary structure

1
715
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 127
Helixi14 – 163
Beta strandi17 – 226
Beta strandi27 – 293
Helixi34 – 4916
Beta strandi55 – 6713
Helixi71 – 777
Helixi82 – 10019
Beta strandi106 – 1105
Helixi117 – 1237
Beta strandi125 – 1317
Beta strandi135 – 1373
Helixi139 – 1435
Turni148 – 1503
Helixi151 – 1599
Helixi161 – 17010
Beta strandi173 – 1753
Helixi176 – 1816
Beta strandi184 – 1896
Helixi191 – 1933
Helixi194 – 20613
Beta strandi207 – 2104
Helixi212 – 2165
Helixi217 – 2204
Helixi227 – 24519
Helixi250 – 26213
Helixi267 – 28216
Helixi285 – 30824
Beta strandi315 – 3206
Helixi323 – 33513
Beta strandi340 – 3434
Helixi347 – 36519
Turni366 – 3683
Helixi372 – 38110
Beta strandi382 – 3887
Helixi391 – 3933
Beta strandi395 – 3995
Helixi405 – 41612
Beta strandi424 – 4274
Beta strandi430 – 4323
Helixi434 – 4374
Helixi438 – 4403
Helixi444 – 4463
Beta strandi447 – 4515
Turni456 – 4583
Beta strandi461 – 4666
Helixi472 – 48413
Beta strandi488 – 4947
Turni496 – 4994
Helixi500 – 51617
Helixi521 – 53111
Helixi537 – 5448
Helixi546 – 55914
Helixi561 – 5644
Helixi571 – 5777
Turni583 – 5864
Beta strandi587 – 5926
Beta strandi599 – 6035
Helixi607 – 6126
Helixi613 – 6153
Helixi624 – 64421
Beta strandi647 – 6504
Helixi651 – 66111
Helixi666 – 6683
Helixi671 – 6788
Helixi680 – 68910
Helixi690 – 6934
Helixi695 – 6973
Helixi701 – 7088

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 1-715.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28793.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 190190Enoyl-CoA hydratase/isomeraseUniRule annotationAdd
BLAST
Regioni312 – 7154043-hydroxyacyl-CoA dehydrogenaseUniRule annotationAdd
BLAST

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.
InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR013328. DH_multihelical.
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 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
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:
EMBL
GenBank
DDBJ
Links Updated
D10390 Genomic DNA. Translation: BAA01227.1.
PIRiJX0199.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D10390 Genomic DNA. Translation: BAA01227.1 .
PIRi JX0199.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WDK X-ray 2.50 A/B 1-715 [» ]
1WDL X-ray 3.50 A/B 1-715 [» ]
1WDM X-ray 3.80 A/B 1-715 [» ]
2D3T X-ray 3.40 A/B 1-715 [» ]
ProteinModelPortali P28793.
SMRi P28793. Positions 1-715.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-29089N.
IntActi P28793. 1 interaction.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00659 .

Miscellaneous databases

EvolutionaryTracei P28793.

Family and domain databases

Gene3Di 1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
HAMAPi MF_01621. FadB.
InterProi IPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR013328. DH_multihelical.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR012799. FadB.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view ]
SUPFAMi SSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.
TIGRFAMsi TIGR02437. FadB. 1 hit.
PROSITEi PS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Primary structures of the genes, faoA and faoB, from Pseudomonas fragi B-0771 which encode the two subunits of the HDT multienzyme complex involved in fatty acid beta-oxidation."
    Sato S., Hayashi M., Imamura S., Ozeki Y., Kawaguchi A.
    J. Biochem. 111:8-15(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: B-0771.
  2. "Transcription of the faoAB operon which encodes the HDT multienzyme complex involved in fatty acid beta-oxidation in Pseudomonas fragi B-0771."
    Sato S., Ozeki Y., Kawaguchi A.
    J. Biochem. 115:286-292(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  3. "Structural basis for channelling mechanism of a fatty acid beta-oxidation multienzyme complex."
    Ishikawa M., Tsuchiya D., Oyama T., Tsunaka Y., Morikawa K.
    EMBO J. 23:2745-2754(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEXES WITH NAD AND ACYL-COENZYME A, SUBUNIT.

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: October 29, 2014
This is version 106 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

External Data

Dasty 3