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P28793

- FADB_PSEFR

UniProt

P28793 - FADB_PSEFR

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

3D structure databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10390 Genomic DNA. Translation: BAA01227.1 .
PIRi JX0199.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 107 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