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Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Enterobacter cloacae
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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

Pathway:ifatty 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)LengthDescriptionGraphical viewFeature identifierActions
Sitei119 – 1191Important for catalytic activityUniRule annotation
Sitei139 – 1391Important for catalytic activityUniRule annotation
Binding sitei296 – 2961SubstrateUniRule annotation
Binding sitei324 – 3241NAD; via amide nitrogenUniRule annotation
Binding sitei343 – 3431NADUniRule annotation
Binding sitei407 – 4071NADUniRule annotation
Active sitei450 – 4501For 3-hydroxyacyl-CoA dehydrogenase activityUniRule annotation
Binding sitei453 – 4531NADUniRule annotation
Binding sitei500 – 5001SubstrateUniRule annotation
Binding sitei660 – 6601SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi400 – 4023NADUniRule annotation
Nucleotide bindingi427 – 4293NADUniRule annotation

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
OrganismiEnterobacter cloacae
Taxonomic identifieri550 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEnterobacterEnterobacter cloacae complex

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 729729Fatty acid oxidation complex subunit alphaPRO_0000109266Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi716541.ECL_04951.

Structurei

3D structure databases

ProteinModelPortaliQ9F0Y7.
SMRiQ9F0Y7. Positions 1-714.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 189189Enoyl-CoA hydratase/isomeraseUniRule annotationAdd
BLAST
Regioni311 – 7294193-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. 2 hits.
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.
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. 2 hits.
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.

Q9F0Y7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLYKGDTLYL NWLEDGIAEL VFDAPGSVNK LDTATVASLG QALDVLEKQP
60 70 80 90 100
ELKGMLLRSN KAAFIVGADI TEFLSLFLVP EEQLSQWLHF ANSVFNRLED
110 120 130 140 150
LPVPTISAVN GYALGGGCEC VLATDYRLAT PDLRIGLPET RLGIMPGFGG
160 170 180 190 200
SVRMPRMLGA DSAMEIIAAG KDVGAEQAQK IGLVDGVVKP EKLVEGALAI
210 220 230 240 250
LRQAINGDLD WKAKRQPKLE PLKLSKIEAT MSFTIAKGMV MQTAGKHYPA
260 270 280 290 300
PITAVKTIEA AARLGRDEAL KLENQSFVPL AHTNEARALV GIFLNDQFVK
310 320 330 340 350
GKARQLTKNV ETPKHAAVLG AGIMGGGIAY QSAWKGVPVV MKDISEKSLT
360 370 380 390 400
LGMTEAAKLL NKQLERGKID GLKLAGVIST IQPVLEYSGF DRVDVVVEAV
410 420 430 440 450
VENPKVKKAV LAETEDKVRP ETVLASNTST IPISELASVL KRPENFCGMH
460 470 480 490 500
FFNPVHRMPL VEVIRGEKTS DETIAKVVAW ASKMGKTPIV VNDCPGFFVN
510 520 530 540 550
RVLFPYFAGF SQLLRDGADF RKIDKVMEKQ FGWPMGPAYL LDVVGIDTAH
560 570 580 590 600
HAQAVMAAGF PQRMQKDYRD AIDALFDANR FGQKNGLGFW RYKENSKGKP
610 620 630 640 650
KKEEDAVVDG LLADVSQPKR DFTDDEIIAR MMIPMINEVV RCLEEGIIAS
660 670 680 690 700
PAEADMALVY GLGFPPFHGG AFRWLDTLGS ARYLDMAQQY QHLGPLYEVP
710 720
EGLRNKARHN EPYYPAVEPA RPVGELKTA
Length:729
Mass (Da):79,759
Last modified:March 1, 2001 - v1
Checksum:i68EBD8FD10AC7204
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF191029 Genomic DNA. Translation: AAG17183.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF191029 Genomic DNA. Translation: AAG17183.1.

3D structure databases

ProteinModelPortaliQ9F0Y7.
SMRiQ9F0Y7. Positions 1-714.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi716541.ECL_04951.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00659.

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 2 hits.
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.
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. 2 hits.
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]
ProtoNetiSearch...

Publicationsi

  1. "Fatty acid competition as a mechanism by which Enterobacter cloacae suppresses Pythium ultimum sporangium germination and damping-off."
    van Dijk K., Nelson E.B.
    Appl. Environ. Microbiol. 66:5340-5347(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: A-11 / 501R3.

Entry informationi

Entry nameiFADB_ENTCL
AccessioniPrimary (citable) accession number: Q9F0Y7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: March 1, 2001
Last modified: July 22, 2015
This is version 78 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

Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.