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Q5R5M8 (ECHP_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxisomal bifunctional enzyme

Short name=PBE
Short name=PBFE

Including the following 2 domains:

  1. Enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase
    EC=4.2.1.17
    EC=5.3.3.8
  2. 3-hydroxyacyl-CoA dehydrogenase
    EC=1.1.1.35
Gene names
Name:EHHADH
Synonyms:ECHD
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length723 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

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

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

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

Enzyme regulation

Enzyme activity enhanced by acetylation By similarity.

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Subunit structure

Monomer By similarity.

Subcellular location

Peroxisome By similarity.

Post-translational modification

Acetylated, leading to enhanced enzyme activity. Acetylation is enhanced by up to 80% after treatment either with trichostin A (TCA) or with nicotinamide (NAM) with highest increase on Lys-346. Acetylation and enzyme activity increased by about 1.5% on addition of fatty acids 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 – 723723Peroxisomal bifunctional enzyme
PRO_0000353181

Regions

Region1 – 282282Enoyl-CoA hydratase / isomerase
Region283 – 5722903-hydroxyacyl-CoA dehydrogenase
Motif721 – 7233Microbody targeting signal By similarity

Sites

Binding site1011Substrate; via amide nitrogen By similarity
Site1041Important for catalytic activity By similarity
Site1241Important for catalytic activity By similarity

Amino acid modifications

Modified residue381N6-succinyllysine By similarity
Modified residue1651N6-acetyllysine; alternate By similarity
Modified residue1651N6-succinyllysine; alternate By similarity
Modified residue1711N6-acetyllysine By similarity
Modified residue2191N6-acetyllysine; alternate By similarity
Modified residue2191N6-succinyllysine; alternate By similarity
Modified residue2501N6-acetyllysine By similarity
Modified residue2801N6-succinyllysine By similarity
Modified residue2901N6-succinyllysine By similarity
Modified residue3461N6-acetyllysine By similarity
Modified residue3501N6-acetyllysine By similarity
Modified residue4641N6-acetyllysine By similarity
Modified residue5321N6-succinyllysine By similarity
Modified residue5771N6-succinyllysine By similarity
Modified residue5841N6-acetyllysine; alternate By similarity
Modified residue5841N6-succinyllysine; alternate By similarity
Modified residue5911N6-acetyllysine; alternate By similarity
Modified residue5911N6-succinyllysine; alternate By similarity
Modified residue7101N6-acetyllysine; alternate By similarity
Modified residue7101N6-succinyllysine; alternate By similarity
Modified residue7221N6-succinyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5R5M8 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 8CAE3A1578A147C6

FASTA72379,481
        10         20         30         40         50         60 
MAEYTRLHNA LALIRLRNPP VNAISTALLR DIKEGLQKAV IDHTIKAIVI CGAEGKFSAG 

        70         80         90        100        110        120 
ADIHGFSAPR TFGFTLGHVV DEIQRNEKPV VAAIQGMAFG GGLELALGCH YRIAHSEAQV 

       130        140        150        160        170        180 
GLPEVTLGLL PGARGTQLLP RLIGVPAALD LITSGRHILA DEALKLGILD KVVNSDPVEE 

       190        200        210        220        230        240 
AIRFAQRVSD QPLESRRLCN KPIQSLPNMD TIFSEALLKM RRQHPGCLAQ EACVRAVQAA 

       250        260        270        280        290        300 
VQYPYEVGVK KEEELFLYLF QSGQARALQY AFLAERKANK WSTPSGASWK TASARPVSSV 

       310        320        330        340        350        360 
GVVGLGTMGR GIVISFARAR IPVIAVDSDK NQLATANKMI TSVLEKEASK MQQSGHPWSG 

       370        380        390        400        410        420 
PKPRLTSSMK ELGGVDLVIE AVFEEMSLKK QVFAELSAIC KPEAFLCTNT SALDVDEIAS 

       430        440        450        460        470        480 
STDRPHLVIG THFFSPAHVM KLLEVIPSQY SSPTTIATVM NLSKKIKKIG VVVGNCFGFV 

       490        500        510        520        530        540 
GNRMLNPYYN QAYFLLEEGS KPEEVDQVLE EFGFKMGPFR VSDLAGLDVG WKSRKGQGLT 

       550        560        570        580        590        600 
GPTLPPGTPA RKRGNRRYCP IPDVLCELGR FGQKTGKGWY QYDKPLGRIH KADPWLSKFL 

       610        620        630        640        650        660 
SQYRETHHIE PRTISQDEIL ERCLYSLINE AFRILGEGIA ASPEHIDVVY LHGYGWPRHK 

       670        680        690        700        710        720 
GGPMFYASTV GLPTVLEKLQ KYYRQNPDIP QLEPSDYLKK LASQGNPPQK EWQSLAGSPS 


SKL 

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References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR860829 mRNA. Translation: CAH92938.1.
RefSeqNP_001127606.1. NM_001134134.1.

3D structure databases

ProteinModelPortalQ5R5M8.
SMRQ5R5M8. Positions 262-717.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5R5M8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100174685.
KEGGpon:100174685.

Organism-specific databases

CTD1962.

Phylogenomic databases

HOGENOMHOG000261347.
HOVERGENHBG104990.
InParanoidQ5R5M8.
KOK07514.

Enzyme and pathway databases

UniPathwayUPA00659.

Family and domain databases

Gene3D1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
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_superfam.
IPR013328. DH_multihelical.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMSSF48179. SSF48179. 2 hits.
PROSITEPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameECHP_PONAB
AccessionPrimary (citable) accession number: Q5R5M8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 4, 2008
Last sequence update: December 21, 2004
Last modified: March 19, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways