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P21177

- FADB_ECOLI

UniProt

P21177 - FADB_ECOLI

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Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Escherichia coli (strain K12)
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.5 PublicationsUniRule 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

Kineticsi

  1. KM=53 µM for crotonyl-CoA (for enoyl-CoA hydratase activity)3 Publications
  2. KM=8.7 mM for L-3-hydroxy-4-trans-decenoyl-CoA (for enoyl-CoA hydratase activity)3 Publications
  3. KM=38 mM for D-3-hydroxy-4-trans-decenoyl-CoA (for enoyl-CoA hydratase activity)3 Publications
  4. KM=5.8 µM for 3-cis-tetradecenoyl-CoA (for Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase activity)3 Publications
  5. KM=69 µM for acetoacetyl-CoA (for 3-hydroxyacyl-CoA dehydrogenase activity)3 Publications
  6. KM=2.0 µM for NADH (for 3-hydroxyacyl-CoA dehydrogenase activity)3 Publications

Pathwayi

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 nitrogenCurated
Binding sitei343 – 3431NADUniRule annotation
Binding sitei407 – 4071NADUniRule annotation
Active sitei450 – 4501For 3-hydroxyacyl-CoA dehydrogenase activity2 PublicationsUniRule 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

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

GO - Biological processi

  1. fatty acid beta-oxidation Source: EcoCyc
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

BioCyciEcoCyc:FADB-MONOMER.
ECOL316407:JW3822-MONOMER.
MetaCyc:FADB-MONOMER.
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:oldB
Ordered Locus Names:b3846, JW3822
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10279. fadB.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi116 – 1161G → F: Absence of both enoyl-CoA hydratase and 3-hydroxyacyl-CoA epimerase activities. Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase is only slightly affected. 1 Publication
Mutagenesisi322 – 3221G → A: 10-fold increase in KM for NADH. 1 Publication
Mutagenesisi450 – 4501H → A or Q: Almost complete loss of 3-hydroxyacyl-CoA dehydrogenase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 729729Fatty acid oxidation complex subunit alphaPRO_0000109268Add
BLAST

Proteomic databases

PaxDbiP21177.
PRIDEiP21177.

Expressioni

Inductioni

Repressed by FadR in the absence of LCFAs (fatty acids of, at least, 12 carbon atoms). When LCFAs are present in the medium, they are converted to long-chain acyl-CoAs which bind to FadR resulting in its release from the DNA and thus derepression of the transcription.

Gene expression databases

GenevestigatoriP21177.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-9560N.
IntActiP21177. 7 interactions.
STRINGi511145.b3846.

Structurei

3D structure databases

ProteinModelPortaliP21177.
SMRiP21177. Positions 1-727.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 189189Enoyl-CoA hydratase/isomeraseAdd
BLAST
Regioni311 – 7294193-hydroxyacyl-CoA dehydrogenaseAdd
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

Phylogenomic databases

eggNOGiCOG1250.
HOGENOMiHOG000261344.
InParanoidiP21177.
KOiK01825.
OMAiNPIVVND.
OrthoDBiEOG6M9F0M.
PhylomeDBiP21177.

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.
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. 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.

P21177-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLYKGDTLYL DWLEDGIAEL VFDAPGSVNK LDTATVASLG EAIGVLEQQS
60 70 80 90 100
DLKGLLLRSN KAAFIVGADI TEFLSLFLVP EEQLSQWLHF ANSVFNRLED
110 120 130 140 150
LPVPTIAAVN GYALGGGCEC VLATDYRLAT PDLRIGLPET KLGIMPGFGG
160 170 180 190 200
SVRMPRMLGA DSALEIIAAG KDVGADQALK IGLVDGVVKA EKLVEGAKAV
210 220 230 240 250
LRQAINGDLD WKAKRQPKLE PLKLSKIEAT MSFTIAKGMV AQTAGKHYPA
260 270 280 290 300
PITAVKTIEA AARFGREEAL NLENKSFVPL AHTNEARALV GIFLNDQYVK
310 320 330 340 350
GKAKKLTKDV ETPKQAAVLG AGIMGGGIAY QSAWKGVPVV MKDINDKSLT
360 370 380 390 400
LGMTEAAKLL NKQLERGKID GLKLAGVIST IHPTLDYAGF DRVDIVVEAV
410 420 430 440 450
VENPKVKKAV LAETEQKVRQ DTVLASNTST IPISELANAL ERPENFCGMH
460 470 480 490 500
FFNPVHRMPL VEIIRGEKSS DETIAKVVAW ASKMGKTPIV VNDCPGFFVN
510 520 530 540 550
RVLFPYFAGF SQLLRDGADF RKIDKVMEKQ FGWPMGPAYL LDVVGIDTAH
560 570 580 590 600
HAQAVMAAGF PQRMQKDYRD AIDALFDANR FGQKNGLGFW RYKEDSKGKP
610 620 630 640 650
KKEEDAAVED LLAEVSQPKR DFSEEEIIAR MMIPMVNEVV RCLEEGIIAT
660 670 680 690 700
PAEADMALVY GLGFPPFHGG AFRWLDTLGS AKYLDMAQQY QHLGPLYEVP
710 720
EGLRNKARHN EPYYPPVEPA RPVGDLKTA
Length:729
Mass (Da):79,594
Last modified:August 1, 1992 - v2
Checksum:i6F1055E402F6B129
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti518 – 5181A → R in AAA23750. (PubMed:1699931)Curated
Sequence conflicti664 – 6641F → L in CAB40809. (PubMed:2204034)Curated
Sequence conflicti666 – 6661P → A in CAB40809. (PubMed:2204034)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M59368 Genomic DNA. Translation: AAA23750.1.
X52837 Genomic DNA. Translation: CAB40809.1.
M74164 Genomic DNA. Translation: AAA62777.1.
M87049 Genomic DNA. Translation: AAA67643.1.
U00096 Genomic DNA. Translation: AAC76849.1.
AP009048 Genomic DNA. Translation: BAE77457.1.
PIRiA39592.
RefSeqiNP_418288.1. NC_000913.3.
YP_491598.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76849; AAC76849; b3846.
BAE77457; BAE77457; BAE77457.
GeneIDi12934454.
948336.
KEGGiecj:Y75_p3334.
eco:b3846.
PATRICi32123189. VBIEscCol129921_3960.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M59368 Genomic DNA. Translation: AAA23750.1 .
X52837 Genomic DNA. Translation: CAB40809.1 .
M74164 Genomic DNA. Translation: AAA62777.1 .
M87049 Genomic DNA. Translation: AAA67643.1 .
U00096 Genomic DNA. Translation: AAC76849.1 .
AP009048 Genomic DNA. Translation: BAE77457.1 .
PIRi A39592.
RefSeqi NP_418288.1. NC_000913.3.
YP_491598.1. NC_007779.1.

3D structure databases

ProteinModelPortali P21177.
SMRi P21177. Positions 1-727.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9560N.
IntActi P21177. 7 interactions.
STRINGi 511145.b3846.

Proteomic databases

PaxDbi P21177.
PRIDEi P21177.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76849 ; AAC76849 ; b3846 .
BAE77457 ; BAE77457 ; BAE77457 .
GeneIDi 12934454.
948336.
KEGGi ecj:Y75_p3334.
eco:b3846.
PATRICi 32123189. VBIEscCol129921_3960.

Organism-specific databases

EchoBASEi EB0275.
EcoGenei EG10279. fadB.

Phylogenomic databases

eggNOGi COG1250.
HOGENOMi HOG000261344.
InParanoidi P21177.
KOi K01825.
OMAi NPIVVND.
OrthoDBi EOG6M9F0M.
PhylomeDBi P21177.

Enzyme and pathway databases

UniPathwayi UPA00659 .
BioCyci EcoCyc:FADB-MONOMER.
ECOL316407:JW3822-MONOMER.
MetaCyc:FADB-MONOMER.

Miscellaneous databases

PROi P21177.

Gene expression databases

Genevestigatori P21177.

Family and domain databases

Gene3Di 1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 2 hits.
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. 2 hits.
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

« Hide 'large scale' publications
  1. "Primary sequence of the Escherichia coli fadBA operon, encoding the fatty acid-oxidizing multienzyme complex, indicates a high degree of homology to eucaryotic enzymes."
    Dirusso C.C.
    J. Bacteriol. 172:6459-6468(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Nucleotide sequence of the fadA gene. Primary structure of 3-ketoacyl-coenzyme A thiolase from Escherichia coli and the structural organization of the fadAB operon."
    Yang S.-Y., Yang X.-Y.H., Healy-Louie G., Schulz H., Elzinga M.
    J. Biol. Chem. 265:10424-10429(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10.
    Strain: K12.
  3. "Nucleotide sequence of the fadA and fadB genes from Escherichia coli."
    Nakahigashi K., Inokuchi H.
    Nucleic Acids Res. 18:4937-4937(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Nucleotide sequence of the promoter and fadB gene of the fadBA operon and primary structure of the multifunctional fatty acid oxidation protein from Escherichia coli."
    Yang X.Y.H., Schulz H., Elzinga M., Yang S.Y.
    Biochemistry 30:6788-6795(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes."
    Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.
    Science 257:771-778(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  7. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  8. "Five different enzymatic activities are associated with the multienzyme complex of fatty acid oxidation from Escherichia coli."
    Pramanik A., Pawar S., Antonian E., Schulz H.
    J. Bacteriol. 137:469-473(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  9. "Epimerization of 3-hydroxy-4-trans-decenoyl coenzyme A by a dehydration/hydration mechanism catalyzed by the multienzyme complex of fatty acid oxidation from Escherichia coli."
    Smeland T.E., Cuebas D., Schulz H.
    J. Biol. Chem. 266:23904-23908(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN EPIMERASE AND HYDRATASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  10. "Association of both enoyl coenzyme A hydratase and 3-hydroxyacyl coenzyme A epimerase with an active site in the amino-terminal domain of the multifunctional fatty acid oxidation protein from Escherichia coli."
    Yang S.Y., Elzinga M.
    J. Biol. Chem. 268:6588-6592(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN EPIMERASE AND HYDRATASE, CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF GLY-116, BIOPHYSICOCHEMICAL PROPERTIES.
  11. "Histidine-450 is the catalytic residue of L-3-hydroxyacyl coenzyme A dehydrogenase associated with the large alpha-subunit of the multienzyme complex of fatty acid oxidation from Escherichia coli."
    He X.Y., Yang S.Y.
    Biochemistry 35:9625-9630(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A DEHYDROGENASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, NAD-BINDING, MUTAGENESIS OF GLY-322 AND HIS-450.
  12. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  13. "A new Escherichia coli metabolic competency: growth on fatty acids by a novel anaerobic beta-oxidation pathway."
    Campbell J.W., Morgan-Kiss R.M., Cronan J.E. Jr.
    Mol. Microbiol. 47:793-805(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ANAEROBIC BETA-OXIDATION PATHWAY.
    Strain: K12 / MG1655 / ATCC 47076.

Entry informationi

Entry nameiFADB_ECOLI
AccessioniPrimary (citable) accession number: P21177
Secondary accession number(s): Q2M8E9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: August 1, 1992
Last modified: October 29, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3