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Protein

Ethylmalonyl-CoA decarboxylase

Gene

ECHDC1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Decarboxylases ethylmalonyl-CoA decarboxylase, a potentially toxic metabolite, to form butyryl-CoA, suggesting it might be involved in metabolite proofreading. Also has methylmalonyl-CoA decarboxylase activity at lower level (By similarity).By similarity

Catalytic activityi

(S)-ethylmalonyl-CoA = butanoyl-CoA + CO2.
(S)-methylmalonyl-CoA = propanoyl-CoA + CO2.

GO - Molecular functioni

  1. carboxy-lyase activity Source: UniProtKB
  2. methylmalonyl-CoA decarboxylase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Names & Taxonomyi

Protein namesi
Recommended name:
Ethylmalonyl-CoA decarboxylase (EC:4.1.1.94)
Alternative name(s):
Enoyl-CoA hydratase domain-containing protein 1
Methylmalonyl-CoA decarboxylase (EC:4.1.1.41)
Short name:
MMCD
Gene namesi
Name:ECHDC1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

Cytoplasmcytosol By similarity

GO - Cellular componenti

  1. cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 306306Ethylmalonyl-CoA decarboxylasePRO_0000273245Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei216 – 2161N6-acetyllysine; alternateBy similarity
Modified residuei216 – 2161N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ2HJD5.
PRIDEiQ2HJD5.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000005072.

Structurei

3D structure databases

ProteinModelPortaliQ2HJD5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1024.
HOGENOMiHOG000007808.
HOVERGENiHBG054783.
InParanoidiQ2HJD5.
KOiK18426.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
PfamiPF00378. ECH. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 1 hit.
PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2HJD5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MELKQEMASL LKTSPNAVKK RLLHQIGLSL YNTSHGFHEE EVKKKLEQFP
60 70 80 90 100
GGSIDLQKEN SGIGILTLNN PSKMNAFSGV MMLQLLEKVI ELENWTEGKG
110 120 130 140 150
LIIRGAKNTF SSGSDLNAVK ALGTPEDGMA VCMFMQNTLT RFMRLPLISV
160 170 180 190 200
ALVQGRALGG GAEVTTACDF RLMTTESEIR FVHKEMGIIP SWGGATRLVE
210 220 230 240 250
IIGGRQALKV LSGALKLDSE KALNIGMVDD ILPSSDETEC LKEAQEWLQQ
260 270 280 290 300
FIKGPPEVIR ALKKSVSSCK ELCLEEALQR ERDILGTVWG GPANLEAVAR

KGKFNK
Length:306
Mass (Da):33,542
Last modified:March 21, 2006 - v1
Checksum:i380866BE4ED86C88
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti176 – 1761E → Q in AAX46345. (PubMed:16305752)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021498 mRNA. Translation: AAX46345.1.
DAAA02025518 Genomic DNA. No translation available.
BC105549 mRNA. Translation: AAI05550.1.
RefSeqiNP_001030492.1. NM_001035415.1.
UniGeneiBt.10238.

Genome annotation databases

GeneIDi536284.
KEGGibta:536284.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021498 mRNA. Translation: AAX46345.1.
DAAA02025518 Genomic DNA. No translation available.
BC105549 mRNA. Translation: AAI05550.1.
RefSeqiNP_001030492.1. NM_001035415.1.
UniGeneiBt.10238.

3D structure databases

ProteinModelPortaliQ2HJD5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000005072.

Proteomic databases

PaxDbiQ2HJD5.
PRIDEiQ2HJD5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi536284.
KEGGibta:536284.

Organism-specific databases

CTDi55862.

Phylogenomic databases

eggNOGiCOG1024.
HOGENOMiHOG000007808.
HOVERGENiHBG054783.
InParanoidiQ2HJD5.
KOiK18426.

Miscellaneous databases

NextBioi20876922.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
PfamiPF00378. ECH. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 1 hit.
PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Hereford.
  3. NIH - Mammalian Gene Collection (MGC) project
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Ascending colon.

Entry informationi

Entry nameiECHD1_BOVIN
AccessioniPrimary (citable) accession number: Q2HJD5
Secondary accession number(s): F1MDK4, Q58DU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: March 21, 2006
Last modified: January 7, 2015
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.