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O95822

- DCMC_HUMAN

UniProt

O95822 - DCMC_HUMAN

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Protein

Malonyl-CoA decarboxylase, mitochondrial

Gene

MLYCD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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. In peroxisomes it may be involved in degrading intraperoxisomal malonyl-CoA, which is generated by the peroxisomal beta-oxidation of odd chain-length dicarboxylic fatty acids. Plays a role in the metabolic balance between glucose and lipid oxidation in muscle independent of alterations in insulin signaling. May play a role in controlling the extent of ischemic injury by promoting glucose oxidation.4 Publications

Catalytic activityi

Malonyl-CoA = acetyl-CoA + CO2.5 Publications

Enzyme regulationi

Malonyl-CoA decarboxylase activity does not require any cofactors or divalent metal ions. Formation of interchain disulfide bonds leads to positive cooperativity between active sites and increases the affinity for malonyl-CoA and the catalytic efficiency (in vitro).2 Publications

Kineticsi

kcat is 19 sec(-1) with malonyl-CoA for malonyl-CoA decarboxylase mitochondrial form, PubMed:15003260. kcat is 28 sec(-1) with malonyl-CoA for Malonyl-CoA decarboxylase cytoplasmic+peroxisomal form, PubMed:15003260. The catalytic efficiency for malonyl-CoA is at least 1.09-fold higher with the malonyl-CoA decarboxylase cytoplasmic+peroxisomal form, PubMed:15003260.

  1. KM=0.36 mM for malonyl-CoA (Malonyl-CoA decarboxylase mitochondrial form), PubMed:150032603 Publications
  2. KM=0.83 mM for malonyl-CoA (Malonyl-CoA decarboxylase mitochondrial form), PubMed:234825653 Publications
  3. KM=0.22 mM for malonyl-CoA (Malonyl-CoA decarboxylase cytoplasmic+peroxisomal form), PubMed:104551073 Publications
  4. KM=0.33 mM for malonyl-CoA (Malonyl-CoA decarboxylase cytoplasmic+peroxisomal form), PubMed:150032603 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei211 – 2111Essential for catalytic activityBy similarity
Active sitei329 – 3291Proton acceptor1 Publication
Binding sitei329 – 3291Malonyl-CoACurated
Active sitei423 – 4231Proton donor1 Publication
Binding sitei423 – 4231Malonyl-CoACurated

GO - Molecular functioni

  1. malonyl-CoA decarboxylase activity Source: UniProtKB
  2. receptor binding Source: UniProtKB

GO - Biological processi

  1. acetyl-CoA biosynthetic process Source: UniProtKB
  2. cellular lipid metabolic process Source: Reactome
  3. fatty acid biosynthetic process Source: UniProtKB
  4. malonyl-CoA catabolic process Source: UniProtKB
  5. positive regulation of fatty acid oxidation Source: UniProtKB
  6. regulation of glucose metabolic process Source: UniProtKB
  7. response to ischemia Source: UniProtKB
  8. small molecule metabolic process Source: Reactome
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

ReactomeiREACT_16957. Peroxisomal lipid metabolism.
SABIO-RKO95822.
UniPathwayiUPA00340; UER00710.

Names & Taxonomyi

Protein namesi
Recommended name:
Malonyl-CoA decarboxylase, mitochondrial (EC:4.1.1.9)
Short name:
MCD
Gene namesi
Name:MLYCD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:7150. MLYCD.

Subcellular locationi

Cytoplasm 1 Publication. Mitochondrion matrix 1 Publication. Peroxisome 1 Publication. Peroxisome matrix By similarity
Note: Enzymatically active in all three subcellular compartments.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. mitochondrial matrix Source: UniProtKB
  3. mitochondrion Source: UniProtKB
  4. peroxisomal matrix Source: UniProtKB
  5. peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Peroxisome

Pathology & Biotechi

Involvement in diseasei

Malonyl-CoA decarboxylase deficiency (MLYCD deficiency) [MIM:248360]: Autosomal recessive disease characterized by abdominal pain, chronic constipation, episodic vomiting, metabolic acidosis and malonic aciduria.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi206 – 2061C → S: Abolishes formation of disulfide-linked homotetramers. Abolishes the cooperative enzyme kinetics that are seen under oxidative conditions. 1 Publication
Mutagenesisi243 – 2431C → S: Does not abolish formation of disulfide-linked homotetramers. No effect on development of cooperative enzyme kinetics in response to oxidative conditions. 1 Publication
Mutagenesisi290 – 2901S → F: 2-fold reduction in catalytic activity. 1 Publication
Mutagenesisi302 – 3021E → G: Decreases catalytic activity. Increases affinity for malonyl-CoA. 1 Publication
Mutagenesisi329 – 3291S → A: 110-fold reduction in catalytic activity. 1 Publication
Mutagenesisi423 – 4231H → N: 7-fold reduction in catalytic activity. 1 Publication
Mutagenesisi456 – 4561Y → S: 3.5-fold reduction in catalytic activity. 1 Publication

Organism-specific databases

MIMi248360. phenotype.
Orphaneti943. Malonic aciduria.
PharmGKBiPA30861.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3939MitochondrionSequence AnalysisAdd
BLAST
Chaini40 – 493454Malonyl-CoA decarboxylase, mitochondrialPRO_0000021088Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei59 – 591N6-acetyllysineBy similarity
Modified residuei168 – 1681N6-acetyllysine; alternateBy similarity
Modified residuei168 – 1681N6-succinyllysine; alternateBy similarity
Disulfide bondi206 – 206InterchainSequence Analysis
Modified residuei211 – 2111N6-acetyllysineBy similarity
Modified residuei222 – 2221N6-succinyllysineBy similarity
Modified residuei389 – 3891N6-acetyllysineBy similarity
Modified residuei472 – 4721N6-acetyllysineBy similarity

Post-translational modificationi

Acetylation at Lys-472 activates malonyl-CoA decarboxylase activity. Deacetylation at Lys-472 by SIRT4 represses activity, leading to promote lipogenesis (By similarity).By similarity
Interchain disulfide bonds may form in peroxisomes (Potential). Interchain disulfide bonds are not expected to form in the reducing environment of the cytoplasm and mitochondria.Curated

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

MaxQBiO95822.
PaxDbiO95822.
PRIDEiO95822.

PTM databases

PhosphoSiteiO95822.

Expressioni

Tissue specificityi

Expressed in fibroblasts and hepatoblastoma cells (at protein level). Expressed strongly in heart, liver, skeletal muscle, kidney and pancreas. Expressed in myotubes. Expressed weakly in brain, placenta, spleen, thymus, testis, ovary and small intestine.2 Publications

Gene expression databases

BgeeiO95822.
CleanExiHS_MLYCD.
GenevestigatoriO95822.

Organism-specific databases

HPAiHPA031625.

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 PEX5.2 Publications

Protein-protein interaction databases

BioGridi116989. 2 interactions.
DIPiDIP-60405N.
STRINGi9606.ENSP00000262430.

Structurei

Secondary structure

1
493
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi40 – 478Combined sources
Helixi54 – 563Combined sources
Helixi67 – 7610Combined sources
Helixi81 – 9414Combined sources
Helixi99 – 11214Combined sources
Turni114 – 1163Combined sources
Helixi119 – 13214Combined sources
Helixi138 – 1458Combined sources
Beta strandi147 – 1493Combined sources
Helixi150 – 16617Combined sources
Helixi173 – 18917Combined sources
Helixi192 – 1943Combined sources
Beta strandi195 – 2006Combined sources
Helixi206 – 2149Combined sources
Helixi224 – 2307Combined sources
Beta strandi235 – 2428Combined sources
Beta strandi250 – 26011Combined sources
Helixi266 – 2694Combined sources
Beta strandi285 – 29410Combined sources
Helixi296 – 2983Combined sources
Turni299 – 3013Combined sources
Helixi303 – 31816Combined sources
Beta strandi324 – 3274Combined sources
Helixi334 – 3418Combined sources
Beta strandi348 – 3503Combined sources
Helixi357 – 36711Combined sources
Helixi374 – 3796Combined sources
Turni380 – 3823Combined sources
Helixi383 – 3864Combined sources
Helixi388 – 3936Combined sources
Helixi395 – 40713Combined sources
Beta strandi414 – 4174Combined sources
Helixi418 – 4258Combined sources
Beta strandi429 – 4346Combined sources
Helixi441 – 4477Combined sources
Beta strandi451 – 4555Combined sources
Helixi458 – 4603Combined sources
Helixi461 – 47111Combined sources
Helixi478 – 4869Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YGWX-ray2.80A/B40-490[»]
4F0XX-ray3.29A/B/C/D/E/F/G/H39-493[»]
ProteinModelPortaliO95822.
SMRiO95822. Positions 39-493.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni40 – 190151Alpha-helical domainAdd
BLAST
Regioni191 – 493303Catalytic domainAdd
BLAST
Regioni299 – 3057Malonyl-CoA bindingCurated

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi491 – 4933Microbody targeting signalSequence Analysis

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1593.
GeneTreeiENSGT00390000005410.
HOGENOMiHOG000141409.
HOVERGENiHBG000825.
InParanoidiO95822.
KOiK01578.
OMAiLDEGREQ.
OrthoDBiEOG76X5ZZ.
PhylomeDBiO95822.
TreeFamiTF312959.

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 initiation. Align

Note: A single transcription start site has been demonstrated in Rat.

Isoform Mitochondrial (identifier: O95822-1) [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
MRGFGPGLTA RRLLPLRLPP RPPGPRLASG QAAGALERAM DELLRRAVPP
60 70 80 90 100
TPAYELREKT PAPAEGQCAD FVSFYGGLAE TAQRAELLGR LARGFGVDHG
110 120 130 140 150
QVAEQSAGVL HLRQQQREAA VLLQAEDRLR YALVPRYRGL FHHISKLDGG
160 170 180 190 200
VRFLVQLRAD LLEAQALKLV EGPDVREMNG VLKGMLSEWF SSGFLNLERV
210 220 230 240 250
TWHSPCEVLQ KISEAEAVHP VKNWMDMKRR VGPYRRCYFF SHCSTPGEPL
260 270 280 290 300
VVLHVALTGD ISSNIQAIVK EHPPSETEEK NKITAAIFYS ISLTQQGLQG
310 320 330 340 350
VELGTFLIKR VVKELQREFP HLGVFSSLSP IPGFTKWLLG LLNSQTKEHG
360 370 380 390 400
RNELFTDSEC KEISEITGGP INETLKLLLS SSEWVQSEKL VRALQTPLMR
410 420 430 440 450
LCAWYLYGEK HRGYALNPVA NFHLQNGAVL WRINWMADVS LRGITGSCGL
460 470 480 490
MANYRYFLEE TGPNSTSYLG SKIIKASEQV LSLVAQFQKN SKL
Length:493
Mass (Da):55,003
Last modified:December 1, 2000 - v3
Checksum:i8F061CA38908E8FC
GO
Isoform Cytoplasmic+peroxisomal (identifier: O95822-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: Missing.

Note: May be produced by alternative initiation at Met-40 of isoform mitochondrial. Alternatively, represents a proteolytic processed form of the mitochondrial form.

Show »
Length:454
Mass (Da):50,946
Checksum:i41C79B2AC6DB3554
GO

Sequence cautioni

The sequence AAD16177.2 differs from that shown. Reason: Frameshift at positions 23, 28, 297 and 308. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821A → D in AAD16177. (PubMed:10417274)Curated
Sequence conflicti119 – 1191A → S in AAD48994. (PubMed:9869665)Curated
Sequence conflicti127 – 1271D → V in AAD48994. (PubMed:9869665)Curated
Sequence conflicti192 – 1921S → P in AAD34631. (PubMed:10455107)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3939Missing in isoform Cytoplasmic+peroxisomal. 3 PublicationsVSP_047649Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF097832 mRNA. Translation: AAD16177.2. Frameshift.
AF153679 mRNA. Translation: AAD34631.1.
AF090834 mRNA. Translation: AAD48994.1.
AC009119 Genomic DNA. No translation available.
BC000286 mRNA. Translation: AAH00286.1.
BC052592 mRNA. Translation: AAH52592.1.
CCDSiCCDS42206.1. [O95822-1]
RefSeqiNP_036345.2. NM_012213.2. [O95822-1]
UniGeneiHs.644610.

Genome annotation databases

EnsembliENST00000262430; ENSP00000262430; ENSG00000103150. [O95822-1]
GeneIDi23417.
KEGGihsa:23417.
UCSCiuc002fgz.3. human. [O95822-1]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF097832 mRNA. Translation: AAD16177.2 . Frameshift.
AF153679 mRNA. Translation: AAD34631.1 .
AF090834 mRNA. Translation: AAD48994.1 .
AC009119 Genomic DNA. No translation available.
BC000286 mRNA. Translation: AAH00286.1 .
BC052592 mRNA. Translation: AAH52592.1 .
CCDSi CCDS42206.1. [O95822-1 ]
RefSeqi NP_036345.2. NM_012213.2. [O95822-1 ]
UniGenei Hs.644610.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YGW X-ray 2.80 A/B 40-490 [» ]
4F0X X-ray 3.29 A/B/C/D/E/F/G/H 39-493 [» ]
ProteinModelPortali O95822.
SMRi O95822. Positions 39-493.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116989. 2 interactions.
DIPi DIP-60405N.
STRINGi 9606.ENSP00000262430.

Chemistry

BindingDBi O95822.
ChEMBLi CHEMBL4698.

PTM databases

PhosphoSitei O95822.

Proteomic databases

MaxQBi O95822.
PaxDbi O95822.
PRIDEi O95822.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262430 ; ENSP00000262430 ; ENSG00000103150 . [O95822-1 ]
GeneIDi 23417.
KEGGi hsa:23417.
UCSCi uc002fgz.3. human. [O95822-1 ]

Organism-specific databases

CTDi 23417.
GeneCardsi GC16P083932.
H-InvDB HIX0173296.
HGNCi HGNC:7150. MLYCD.
HPAi HPA031625.
MIMi 248360. phenotype.
606761. gene.
neXtProti NX_O95822.
Orphaneti 943. Malonic aciduria.
PharmGKBi PA30861.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1593.
GeneTreei ENSGT00390000005410.
HOGENOMi HOG000141409.
HOVERGENi HBG000825.
InParanoidi O95822.
KOi K01578.
OMAi LDEGREQ.
OrthoDBi EOG76X5ZZ.
PhylomeDBi O95822.
TreeFami TF312959.

Enzyme and pathway databases

UniPathwayi UPA00340 ; UER00710 .
Reactomei REACT_16957. Peroxisomal lipid metabolism.
SABIO-RK O95822.

Miscellaneous databases

ChiTaRSi MLYCD. human.
GenomeRNAii 23417.
NextBioi 45627.
PROi O95822.
SOURCEi Search...

Gene expression databases

Bgeei O95822.
CleanExi HS_MLYCD.
Genevestigatori O95822.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL), CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
  2. "MCD encodes peroxisomal and cytoplasmic forms of malonyl-CoA decarboxylase and is mutated in malonyl-CoA decarboxylase deficiency."
    Sacksteder K.A., Morrell J.C., Wanders R.J.A., Matalon R., Gould S.J.
    J. Biol. Chem. 274:24461-24468(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
    Tissue: Heart.
  3. "Cloning and mutational analysis of human malonyl-coenzyme A decarboxylase."
    Gao J., Waber L., Bennett M.J., Gibson K.M., Cohen J.C.
    J. Lipid Res. 40:178-182(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL), CATALYTIC ACTIVITY.
  4. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS MITOCHONDRIAL AND CYTOPLASMIC+PEROXISOMAL).
    Tissue: Eye and Lung.
  6. Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
  7. "Malonyl CoenzymeA decarboxylase regulates lipid and glucose metabolism in human skeletal muscle."
    Bouzakri K., Austin R., Rune A., Lassman M.E., Garcia-Roves P.M., Berger J.P., Krook A., Chibalin A.V., Zhang B.B., Zierath J.R.
    Diabetes 57:1508-1516(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  8. "A proteome-wide perspective on peroxisome targeting signal 1(PTS1)-Pex5p affinities."
    Ghosh D., Berg J.M.
    J. Am. Chem. Soc. 132:3973-3979(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH PEX5.
  9. "Structural asymmetry and disulphide bridges among subunits modulate the activity of human Malonyl-CoA Decarboxylase."
    Aparicio D., Perez R., Carpena X., Diaz M., Ferrer J.C., Loewen P.C., Fita I.
    J. Biol. Chem. 288:11907-11919(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 39-493 IN COMPLEX WITH LIGAND REPRESENTING COENZYME A, CATALYTIC ACTIVITY, FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISULFIDE BONDS, MUTAGENESIS OF CYS-206; CYS-243 AND GLU-302, IDENTIFICATION BY MASS SPECTROMETRY.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 40-490, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-290; SER-329; HIS-423 AND TYR-456.

Entry informationi

Entry nameiDCMC_HUMAN
AccessioniPrimary (citable) accession number: O95822
Secondary accession number(s): Q9UNU5, Q9Y3F2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: November 26, 2014
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3