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P12617

- DCMC_ANSAN

UniProt

P12617 - DCMC_ANSAN

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Protein

Malonyl-CoA decarboxylase, mitochondrial

Gene

MLYCD

Organism
Anser anser anser (Western graylag goose)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of malonyl-CoA to acetyl-CoA. In the fatty acid biosynthesis MCD selectively removes malonyl-CoA and thus assures that methyl-malonyl-CoA is the only chain elongating substrate for fatty acid synthase and that fatty acids with multiple methyl side chains are produced.

Catalytic activityi

Malonyl-CoA = acetyl-CoA + CO2.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei222 – 2221Essential for catalytic activityBy similarity
Active sitei340 – 3401Proton acceptorBy similarity
Active sitei434 – 4341Proton donorBy similarity

GO - Molecular functioni

  1. malonyl-CoA decarboxylase activity Source: UniProtKB

GO - Biological processi

  1. acetyl-CoA biosynthetic process Source: UniProtKB
  2. fatty acid biosynthetic process Source: UniProtKB-KW
  3. malonyl-CoA catabolic process Source: UniProtKB
  4. positive regulation of fatty acid oxidation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

UniPathwayiUPA00340; UER00710.

Names & Taxonomyi

Protein namesi
Recommended name:
Malonyl-CoA decarboxylase, mitochondrial (EC:4.1.1.9)
Short name:
MCD
Gene namesi
Name:MLYCD
OrganismiAnser anser anser (Western graylag goose)
Taxonomic identifieri8844 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeAnseriformesAnatidaeAnser

Subcellular locationi

Mitochondrion 1 Publication. Cytoplasm 1 Publication. Peroxisome 1 Publication
Note: Mitochondrial in liver. Cytoplasmic in uropygial gland.

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB
  2. peroxisome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5050MitochondrionSequence AnalysisAdd
BLAST
Chaini51 – 504454Malonyl-CoA decarboxylase, mitochondrialPRO_0000021086Add
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni51 – 201151Alpha-helical domainBy similarityAdd
BLAST
Regioni202 – 504303Catalytic domainBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi502 – 5043Microbody targeting signalSequence Analysis

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOVERGENiHBG000825.

Family and domain databases

InterProiIPR007956. Malonyl_CoA_deC.
[Graphical view]
PfamiPF05292. MCD. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative promoter usage. Align

Isoform Mitochondrial (identifier: P12617-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRGLRRGLSR LGPRLGPWAV PRSLRRVLRA AGPWRGQSSA GSVSERGGAS
60 70 80 90 100
MEEVLSRSVP LLPPYETKEK APPPAERRSA EFVRYYRGLE AGSRRAELLG
110 120 130 140 150
CLARDFGADH GRVAEFSAKV LQAREQEREQ GALLQAEDRV RYYLTPRYRA
160 170 180 190 200
LFQHLGRLEG GLRFLVELRG DLVEGLAAKA VDGPHVKEMS GVLKNMLSEW
210 220 230 240 250
FSTGFLNLER VTWQSPCEVL QKISDSEAVH PVRNWVDLKR RVGPYRRCYF
260 270 280 290 300
FSHCAIPGEP LIILHVALTS DISSSIQSIV KDVESLETED AEKITTAIFY
310 320 330 340 350
SISLAQQGLQ GVELGNHLIK RVVKELQKDL PQIEAFSSLS PIPGFTKWLV
360 370 380 390 400
GLLSSQTKEL GRNELFTESE RQEISEITED STTETLKKLL TNSEWVKSEK
410 420 430 440 450
LVKALHSPLM RLCAWYLYGE KHRGYALNPV ANFHLQNGAE LWRINWMGDT
460 470 480 490 500
SPRGIAASCG MMVNYRYFLE DTASNSAAYL GTKHIKASEQ VLSFVSQFQQ

NSKL
Length:504
Mass (Da):56,690
Last modified:November 1, 1995 - v2
Checksum:i683991C1F9773DF4
GO
Isoform Cytoplasmic+peroxisomal (identifier: P12617-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-50: Missing.

Show »
Length:454
Mass (Da):51,368
Checksum:i06251394595673F1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti124 – 13613Missing AA sequence (PubMed:2914961)CuratedAdd
BLAST
Sequence conflicti140 – 1401V → L in AAA49317. (PubMed:2914961)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5050Missing in isoform Cytoplasmic+peroxisomal. 1 PublicationVSP_018815Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L21171 mRNA. Translation: AAA49317.1. Sequence problems.
PIRiA33313.
S27113.

Keywords - Coding sequence diversityi

Alternative promoter usage

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L21171 mRNA. Translation: AAA49317.1 . Sequence problems.
PIRi A33313.
S27113.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG000825.

Enzyme and pathway databases

UniPathwayi UPA00340 ; UER00710 .

Family and domain databases

InterProi IPR007956. Malonyl_CoA_deC.
[Graphical view ]
Pfami PF05292. MCD. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cytoplasmic accumulation of a normally mitochondrial malonyl-CoA decarboxylase by the use of an alternate transcription start site."
    Courchesne-Smith C., Jang S.-H., Shi Q., Dewille J., Sasaki G., Kolattukudy P.E.
    Arch. Biochem. Biophys. 298:576-586(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MITOCHONDRIAL AND CYTOPLASMIC+PEROXISOMAL), ALTERNATIVE PROMOTER USAGE, SUBCELLULAR LOCATION.
    Tissue: Uropygial gland.
  2. "Molecular cloning, nucleotide sequence, and tissue distribution of malonyl-CoA decarboxylase."
    Jang S.-H., Cheesbrough T.M., Kolattukudy P.E.
    J. Biol. Chem. 264:3500-3505(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 74-504, PARTIAL PROTEIN SEQUENCE.
    Tissue: Uropygial gland.

Entry informationi

Entry nameiDCMC_ANSAN
AccessioniPrimary (citable) accession number: P12617
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 1, 1995
Last modified: October 29, 2014
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways

External Data

Dasty 3