Reviewed, UniProtKB/Swiss-Prot Q5R5M8 (ECHP_PONAB)

Names and origin

Protein names

Recommended 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

Organism

Pongo abelii (Sumatran orangutan)

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

Sequence length	723 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Peroxisome
Ligand	NAD
Molecular function	Isomerase Lyase Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-hydroxyacyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: EC coenzyme binding Inferred from electronic annotation. Source: InterPro dodecenoyl-CoA delta-isomerase activity Inferred from electronic annotation. Source: EC enoyl-CoA hydratase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 723	722	Peroxisomal bifunctional enzyme		PRO_0000353181
Regions
	Region	2 – 282	281	Enoyl-CoA hydratase / isomerase
	Region	283 – 572	290	3-hydroxyacyl-CoA dehydrogenase
	Motif	721 – 723	3	Microbody targeting signal By similarity
Sites
	Binding site	101	1	Substrate; via amide nitrogen By similarity
	Site	124	1	Important for catalytic activity By similarity
Amino acid modifications
	Modified residue	359	1	Phosphoserine By similarity
	Modified residue	584	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5R5M8-1 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: 8CAE3A1578A147C6	FASTA	723	79,481
	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

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.
RefSeq	NP_001127606.1.
UniGene	Pab.18109
3D structure databases
HSSP	HSSP built from PDB template 1ZCJ based on UniProtKB P07896.
SMR	Q5R5M8. Positions 262-717.
ModBase	Search...
Genome annotation databases
GeneID	100174685.
Organism-specific databases
CTD	100174685.
Phylogenomic databases
HOVERGEN	Q5R5M8.
InParanoid	Q5R5M8.
Family and domain databases
InterPro	IPR006180. 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]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 2 hits.
Pfam	PF00725. 3HCDH. 2 hits. PF02737. 3HCDH_N. 1 hit. PF00378. ECH. 1 hit. [Graphical view]
PROSITE	PS00067. 3HCDH. 1 hit. PS00166. ENOYL_COA_HYDRATASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ECHP_PONAB

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)