UniProtKB - Q920F5 (DCMC_RAT)
Malonyl-CoA decarboxylase, mitochondrial
Mlycd
Functioni
Catalytic activityi
Activity regulationi
Kineticsi
- KM=0.36 mM for malonyl-CoA1 Publication
: acetyl-CoA biosynthesis Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes acetyl-CoA from malonyl-CoA.Proteins known to be involved in this subpathway in this organism are:
- Malonyl-CoA decarboxylase, mitochondrial (Mlycd)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetyl-CoA from malonyl-CoA, the pathway acetyl-CoA biosynthesis and in Metabolic intermediate biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 210 | Essential for catalytic activity | 1 | |
Active sitei | 328 | Proton acceptorBy similarity | 1 | |
Binding sitei | 328 | Malonyl-CoABy similarity | 1 | |
Active sitei | 422 | Proton donorBy similarity | 1 | |
Binding sitei | 422 | Malonyl-CoABy similarity | 1 |
GO - Molecular functioni
- identical protein binding Source: RGD
- malonyl-CoA decarboxylase activity Source: RGD
GO - Biological processi
- acetyl-CoA biosynthetic process Source: RGD
- fatty acid biosynthetic process Source: UniProtKB
- fatty acid oxidation Source: RGD
- malonyl-CoA catabolic process Source: UniProtKB
- positive regulation of fatty acid oxidation Source: UniProtKB
- regulation of fatty acid beta-oxidation Source: RGD
- regulation of fatty acid oxidation Source: RGD
- regulation of glucose metabolic process Source: UniProtKB
- response to ischemia Source: UniProtKB
Keywordsi
Molecular function | Decarboxylase, Lyase |
Biological process | Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism |
Enzyme and pathway databases
Reactomei | R-RNO-390247, Beta-oxidation of very long chain fatty acids R-RNO-9033241, Peroxisomal protein import |
SABIO-RKi | Q920F5 |
UniPathwayi | UPA00340;UER00710 |
Names & Taxonomyi
Protein namesi | Recommended name: Malonyl-CoA decarboxylase, mitochondrialCurated (EC:4.1.1.93 Publications)Short name: MCD |
Gene namesi | Name:MlycdImported |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 620234, Mlycd |
Subcellular locationi
Peroxisome
- Peroxisome By similarity
- Peroxisome matrix 1 Publication
Mitochondrion
- Mitochondrion matrix 1 Publication
Other locations
- Cytoplasm 1 Publication
Note: Enzymatically active in all three subcellular compartments.
Cytosol
- cytosol Source: RGD
Mitochondrion
- mitochondrial matrix Source: UniProtKB
- mitochondrion Source: RGD
Peroxisome
- peroxisomal matrix Source: UniProtKB
- peroxisome Source: UniProtKB
Other locations
- cytoplasm Source: UniProtKB
Keywords - Cellular componenti
Cytoplasm, Mitochondrion, PeroxisomePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 210 | K → M: Abolishes catalytic activity. 1 Publication | 1 | |
Mutagenesisi | 308 | K → M: 40% reduction in catalytic activity. 1 Publication | 1 | |
Mutagenesisi | 388 | K → M: 40% reduction in catalytic activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transit peptidei | 1 – 38 | MitochondrionSequence analysisAdd BLAST | 38 | |
ChainiPRO_0000021092 | 39 – 492 | Malonyl-CoA decarboxylase, mitochondrialAdd BLAST | 454 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 58 | N6-acetyllysine1 Publication | 1 | |
Modified residuei | 167 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 167 | N6-succinyllysine; alternateBy similarity | 1 | |
Disulfide bondi | 205 | InterchainSequence analysis | ||
Modified residuei | 210 | N6-acetyllysine1 Publication | 1 | |
Modified residuei | 221 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 316 | N6-acetyllysine1 Publication | 1 | |
Modified residuei | 385 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 385 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 388 | N6-acetyllysine1 Publication | 1 | |
Modified residuei | 441 | N6-acetyllysine1 Publication | 1 | |
Modified residuei | 471 | N6-acetyllysineBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, Disulfide bondProteomic databases
jPOSTi | Q920F5 |
PaxDbi | Q920F5 |
PRIDEi | Q920F5 |
PTM databases
iPTMneti | Q920F5 |
PhosphoSitePlusi | Q920F5 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSRNOG00000014522, Expressed in heart and 22 other tissues |
Genevisiblei | Q920F5, RN |
Interactioni
Subunit structurei
Homotetramer. Dimer of dimers. The two subunits within a dimer display conformational differences suggesting that at any given moment, only one of the two subunits is competent for malonyl-CoA binding and catalytic activity. Under oxidizing conditions, can form disulfide-linked homotetramers (in vitro). Associates with the peroxisomal targeting signal receptor PEX5 (By similarity).
By similarityGO - Molecular functioni
- identical protein binding Source: RGD
Protein-protein interaction databases
IntActi | Q920F5, 1 interactor |
STRINGi | 10116.ENSRNOP00000019923 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 39 – 189 | Alpha-helical domainBy similarityAdd BLAST | 151 | |
Regioni | 190 – 492 | Catalytic domainBy similarityAdd BLAST | 303 | |
Regioni | 298 – 304 | Malonyl-CoA bindingBy similarity | 7 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 490 – 492 | Microbody targeting signalSequence analysis | 3 |
Keywords - Domaini
Transit peptidePhylogenomic databases
eggNOGi | KOG3018, Eukaryota |
GeneTreei | ENSGT00390000005410 |
HOGENOMi | CLU_023433_0_0_1 |
InParanoidi | Q920F5 |
OMAi | QSEFPHM |
OrthoDBi | 1436590at2759 |
PhylomeDBi | Q920F5 |
TreeFami | TF312959 |
Family and domain databases
Gene3Di | 1.20.140.90, 1 hit 3.40.630.150, 1 hit |
InterProi | View protein in InterPro IPR038917, Malonyl_CoA_deC IPR007956, Malonyl_CoA_deC_C IPR042303, Malonyl_CoA_deC_C_sf IPR035372, MCD_N IPR038351, MCD_N_sf |
PANTHERi | PTHR28641, PTHR28641, 1 hit |
Pfami | View protein in Pfam PF05292, MCD, 1 hit PF17408, MCD_N, 1 hit |
s (2)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsialternative initiation. AlignAdd to basketThis isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MRGLGPSLRA RRLLPLRYPP RPPGPRGPRL CSGLTASAMD ELLRRAVPPT
60 70 80 90 100
PAYELREKTP APAEGQCADF VSFYGGLAEA AQRAELLGRL AQGFGVDHGQ
110 120 130 140 150
VAEQSAGVLQ LRQQSREAAV LLQAEDRLRY ALVPRYRGLF HHISKLDGGV
160 170 180 190 200
RFLVQLRADL LEAQALKLVE GPHVREMNGV LKSMLSEWFS SGFLNLERVT
210 220 230 240 250
WHSPCEVLQK ISECEAVHPV KNWMDMKRRV GPYRRCYFFS HCSTPGDPLV
260 270 280 290 300
VLHVALTGDI SNNIQSIVKE CPPSETEEKN RIAAAVFYSI SLTQQGLQGV
310 320 330 340 350
ELGTFLIKRV VKELQKEFPH LGAFSSLSPI PGFTKWLLGL LNVQGKEYGR
360 370 380 390 400
NELFTDSECK EIAEVTGDPV HESLKGLLSS GEWAKSEKLA QALQGPLMRL
410 420 430 440 450
CAWYLYGEKH RGYALNPVAN FHLQNGAVMW RINWMADSSL KGLTSSCGLM
460 470 480 490
VNYRYYLEET GPNSISYLGS KNIKASEQIL SLVAQFQSNS KL
The sequence of this isoform differs from the canonical sequence as follows:
1-38: Missing.
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 213 | E → D in CAB46681 (PubMed:10229677).Curated | 1 | |
Sequence conflicti | 218 | H → Q in CAB46681 (PubMed:10229677).Curated | 1 | |
Sequence conflicti | 301 | E → G in CAB46681 (PubMed:10229677).Curated | 1 | |
Sequence conflicti | 412 | Missing in CAB46681 (PubMed:10229677).Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_018818 | 1 – 38 | Missing in isoform Cytoplasmic+peroxisomal. CuratedAdd BLAST | 38 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AJ007704 mRNA Translation: CAB46681.1 AF304865 mRNA Translation: AAL09352.1 BC061845 mRNA Translation: AAH61845.1 |
RefSeqi | NP_445929.1, NM_053477.1 |
Genome annotation databases
Ensembli | ENSRNOT00000019923; ENSRNOP00000019923; ENSRNOG00000014522 [Q920F5-1] |
GeneIDi | 85239 |
KEGGi | rno:85239 |
UCSCi | RGD:620234, rat [Q920F5-1] |
Keywords - Coding sequence diversityi
Alternative initiationSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AJ007704 mRNA Translation: CAB46681.1 AF304865 mRNA Translation: AAL09352.1 BC061845 mRNA Translation: AAH61845.1 |
RefSeqi | NP_445929.1, NM_053477.1 |
3D structure databases
SMRi | Q920F5 |
ModBasei | Search... |
Protein-protein interaction databases
IntActi | Q920F5, 1 interactor |
STRINGi | 10116.ENSRNOP00000019923 |
PTM databases
iPTMneti | Q920F5 |
PhosphoSitePlusi | Q920F5 |
Proteomic databases
jPOSTi | Q920F5 |
PaxDbi | Q920F5 |
PRIDEi | Q920F5 |
Protocols and materials databases
ABCDi | Q920F5, 4 sequenced antibodies |
Genome annotation databases
Ensembli | ENSRNOT00000019923; ENSRNOP00000019923; ENSRNOG00000014522 [Q920F5-1] |
GeneIDi | 85239 |
KEGGi | rno:85239 |
UCSCi | RGD:620234, rat [Q920F5-1] |
Organism-specific databases
CTDi | 23417 |
RGDi | 620234, Mlycd |
Phylogenomic databases
eggNOGi | KOG3018, Eukaryota |
GeneTreei | ENSGT00390000005410 |
HOGENOMi | CLU_023433_0_0_1 |
InParanoidi | Q920F5 |
OMAi | QSEFPHM |
OrthoDBi | 1436590at2759 |
PhylomeDBi | Q920F5 |
TreeFami | TF312959 |
Enzyme and pathway databases
UniPathwayi | UPA00340;UER00710 |
Reactomei | R-RNO-390247, Beta-oxidation of very long chain fatty acids R-RNO-9033241, Peroxisomal protein import |
SABIO-RKi | Q920F5 |
Miscellaneous databases
PROi | PR:Q920F5 |
Gene expression databases
Bgeei | ENSRNOG00000014522, Expressed in heart and 22 other tissues |
Genevisiblei | Q920F5, RN |
Family and domain databases
Gene3Di | 1.20.140.90, 1 hit 3.40.630.150, 1 hit |
InterProi | View protein in InterPro IPR038917, Malonyl_CoA_deC IPR007956, Malonyl_CoA_deC_C IPR042303, Malonyl_CoA_deC_C_sf IPR035372, MCD_N IPR038351, MCD_N_sf |
PANTHERi | PTHR28641, PTHR28641, 1 hit |
Pfami | View protein in Pfam PF05292, MCD, 1 hit PF17408, MCD_N, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | DCMC_RAT | |
Accessioni | Q920F5Primary (citable) accession number: Q920F5 Secondary accession number(s): Q9WUY2 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 7, 2005 |
Last sequence update: | December 1, 2001 | |
Last modified: | December 2, 2020 | |
This is version 120 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways