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Reviewed, UniProtKB/Swiss-Prot Q5R5M8 (ECHP_PONAB)

Last modified December 15, 2009. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peroxisomal bifunctional enzyme
      Short name=PBE
      Short name=PBFE
Including the following 2 domains:
    1- Recommended name:
            Enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase
              EC=4.2.1.17
              EC=5.3.3.8
    2- Recommended name:
            3-hydroxyacyl-CoA dehydrogenase
              EC=1.1.1.35
Gene names
Name: EHHADH
Synonyms: ECHD
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length723 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Subunit structure

Monomer By similarity.

Subcellular location

Peroxisome 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

Initiator methionine11Removed By similarity
Chain2 – 723722Peroxisomal bifunctional enzyme
PRO_0000353181

Regions

Region2 – 282281Enoyl-CoA hydratase / isomerase
Region283 – 5722903-hydroxyacyl-CoA dehydrogenase
Motif721 – 7233Microbody targeting signal By similarity

Sites

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

Amino acid modifications

Modified residue3591Phosphoserine By similarity
Modified residue5841N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5R5M8-1 [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.
UniGenePab.18109

3D structure databases

HSSPHSSP built from PDB template 1ZCJ based on UniProtKB P07896.
SMRQ5R5M8. Positions 262-717.
ModBaseSearch...

Genome annotation databases

GeneID100174685.

Organism-specific databases

CTD100174685.

Phylogenomic databases

HOVERGENQ5R5M8.
InParanoidQ5R5M8.

Family and domain databases

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.
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.
PfamPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
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: December 15, 2009
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents