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A4TR27 (FADB_YERPP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Fatty acid oxidation complex subunit alpha

Including the following 2 domains:

  1. Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase
    EC=4.2.1.17
    EC=5.1.2.3
    EC=5.3.3.8
  2. 3-hydroxyacyl-CoA dehydrogenase
    EC=1.1.1.35
Gene names
Name:fadB
Ordered Locus Names:YPDSF_3386
OrganismYersinia pestis (strain Pestoides F) [Complete proteome] [HAMAP]
Taxonomic identifier386656 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia

Protein attributes

Sequence length729 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the formation of an hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities By similarity. HAMAP MF_01621

Catalytic activity

(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH. HAMAP MF_01621

(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O. HAMAP MF_01621

(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA. HAMAP MF_01621

(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA. HAMAP MF_01621

Pathway

Lipid metabolism; fatty acid beta-oxidation. HAMAP MF_01621

Subunit structure

Heterotetramer of two alpha chains (fadB) and two beta chains (fadA) By similarity.

Sequence similarities

In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.

In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 729729Fatty acid oxidation complex subunit alpha HAMAP MF_01621
PRO_1000069586

Regions

Nucleotide binding400 – 4023NAD By similarity
Nucleotide binding427 – 4293NAD By similarity
Region1 – 189189Enoyl-CoA hydratase/isomerase By similarity
Region311 – 7294193-hydroxyacyl-CoA dehydrogenase By similarity

Sites

Binding site2961Substrate By similarity
Binding site3241NAD; via amide nitrogen By similarity
Binding site3431NAD By similarity
Binding site4071NAD By similarity
Binding site4531NAD By similarity
Binding site5001Substrate By similarity
Binding site6601Substrate By similarity
Site1191Important for catalytic activity By similarity
Site1391Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A4TR27 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 2C534B2963B09491

FASTA72978,826
        10         20         30         40         50         60 
MLYQSETLQL HWLENGIAEL VFDAPGSVNK LDTKTVANLG EALNVLEKQS ELKGLLLRSA 

        70         80         90        100        110        120 
KTALIVGADI TEFLSLFNAP PEKLHQWLVF ANTIFNRLED LPVPTISAIN GYALGGGCEC 

       130        140        150        160        170        180 
ILATDFRIAS PEARIGLPET KLGIMPGFGG SVRLPRLLGA DSALEIIATG KDVTANDALK 

       190        200        210        220        230        240 
IGLVDAVVDP EKLVGSALTM LKQAIDGKLD WQAARRPKLE PLKLNPTEAA MCFTIAKGRV 

       250        260        270        280        290        300 
MQVAGKHYPA PLTAVKTIEA AAKFGRTEAL NLETNSFVPL AGSNEARALV GIFLNDQYVK 

       310        320        330        340        350        360 
AQAKKLSKGV AAPKLAAVLG AGIMGGGIAY QSALKSVPVI MKDINENSLD LGMNEAAKLL 

       370        380        390        400        410        420 
NKQLERGKVD GLKMASILAT IRPTLDYAGI ERAQVIVEAV VENPKVKAAV LAEVEALIGE 

       430        440        450        460        470        480 
DTVLASNTST IPIDQLAKSL KRPENFCGMH FFNPVHRMPL VEIIRGAKTS DKTLAAVVAY 

       490        500        510        520        530        540 
ATQMGKTPIV VNDCPGFFVN RVLFPYLAGF GMLVRDGGDF HQIDKVMEKQ FGWPMGPAYL 

       550        560        570        580        590        600 
LDVVGIDTAH HAQAVMAAGF PERMNKDYRD AVDVMFDNQR FGQKNGQGFY RYTQDAKGKP 

       610        620        630        640        650        660 
RKENDEQVDK LLAEISQPLQ EFSDEDIIAR TMIPMINEVV RCLEEGIIAS AAEGDMALVY 

       670        680        690        700        710        720 
GLGFPPFHGG VFRYLDTLGS ANYVEMAQRY AHLGALYHVP AGLRAKAEHN ESYYPVAAAL 


LDVSTNQPA

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References

[1]"Complete sequence of chromosome of Yersinia pestis Pestoides F."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Di Bartolo G., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Worsham P., Chu M., Bearden S., Garcia E., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pestoides F.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000668 Genomic DNA. Translation: ABP41739.1.
RefSeqYP_001164712.1. NC_009381.1.

3D structure databases

ProteinModelPortalA4TR27.
SMRA4TR27. Positions 1-714.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4TR27.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5062579.
GenomeReviewsGene locus YPDSF_3386 in contig CP000668_GR.
KEGGypp:YPDSF_3386.
PATRIC18616741. VBIYerPes122972_4239.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHBG691737.
OMAFGEQKAF.
ProtClustDBPRK11730.

Enzyme and pathway databases

BioCycYPES386656:YPDSF_3386-MONOMER.

Family and domain databases

HAMAPMF_01621. FadB.
[Tree]
InterProIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR001753. Crotonase_core.
IPR013328. DH_multihelical.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR012799. FadB.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
G3DSA:1.10.1040.10. Opine_DH. 2 hits.
KOK01825.
PfamPF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMSSF48179. 6DGDH_C_like. 2 hits.
TIGRFAMsTIGR02437. FadB. 1 hit.
PROSITEPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADB_YERPP
AccessionPrimary (citable) accession number: A4TR27
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 15, 2007
Last modified: January 25, 2012
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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