DCMC_ANSAN
ID DCMC_ANSAN Reviewed; 504 AA.
AC P12617;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Malonyl-CoA decarboxylase, mitochondrial;
DE Short=MCD;
DE EC=4.1.1.9;
DE Flags: Precursor;
GN Name=MLYCD;
OS Anser anser anser (Western greylag goose).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anserinae; Anser.
OX NCBI_TaxID=8844;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MITOCHONDRIAL AND
RP CYTOPLASMIC+PEROXISOMAL), ALTERNATIVE PROMOTER USAGE, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Uropygial gland;
RX PubMed=1416987; DOI=10.1016/0003-9861(92)90452-3;
RA Courchesne-Smith C., Jang S.-H., Shi Q., Dewille J., Sasaki G.,
RA Kolattukudy P.E.;
RT "Cytoplasmic accumulation of a normally mitochondrial malonyl-CoA
RT decarboxylase by the use of an alternate transcription start site.";
RL Arch. Biochem. Biophys. 298:576-586(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 74-504, AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Uropygial gland;
RX PubMed=2914961; DOI=10.1016/s0021-9258(18)94094-9;
RA Jang S.-H., Cheesbrough T.M., Kolattukudy P.E.;
RT "Molecular cloning, nucleotide sequence, and tissue distribution of
RT malonyl-CoA decarboxylase.";
RL J. Biol. Chem. 264:3500-3505(1989).
CC -!- FUNCTION: Catalyzes the conversion of malonyl-CoA to acetyl-CoA. In the
CC fatty acid biosynthesis MCD selectively removes malonyl-CoA and thus
CC assures that methyl-malonyl-CoA is the only chain elongating substrate
CC for fatty acid synthase and that fatty acids with multiple methyl side
CC chains are produced. {ECO:0000250|UniProtKB:O95822}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + malonyl-CoA = acetyl-CoA + CO2; Xref=Rhea:RHEA:18781,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384; EC=4.1.1.9;
CC Evidence={ECO:0000250|UniProtKB:O95822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18782;
CC Evidence={ECO:0000250|UniProtKB:O95822};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis;
CC acetyl-CoA from malonyl-CoA: step 1/1.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:1416987}.
CC Cytoplasm {ECO:0000269|PubMed:1416987}. Peroxisome
CC {ECO:0000269|PubMed:1416987}. Note=Mitochondrial in liver. Cytoplasmic
CC in uropygial gland.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=Mitochondrial;
CC IsoId=P12617-1; Sequence=Displayed;
CC Name=Cytoplasmic+peroxisomal;
CC IsoId=P12617-2; Sequence=VSP_018815;
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DR EMBL; L21171; AAA49317.1; ALT_SEQ; mRNA.
DR PIR; A33313; A33313.
DR PIR; S27113; S27113.
DR AlphaFoldDB; P12617; -.
DR SMR; P12617; -.
DR UniPathway; UPA00340; UER00710.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0050080; F:malonyl-CoA decarboxylase activity; ISS:UniProtKB.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:2001294; P:malonyl-CoA catabolic process; ISS:UniProtKB.
DR GO; GO:0046321; P:positive regulation of fatty acid oxidation; ISS:UniProtKB.
DR Gene3D; 1.20.140.90; -; 1.
DR Gene3D; 3.40.630.150; -; 1.
DR InterPro; IPR038917; Malonyl_CoA_deC.
DR InterPro; IPR007956; Malonyl_CoA_deC_C.
DR InterPro; IPR042303; Malonyl_CoA_deC_C_sf.
DR InterPro; IPR035372; MCD_N.
DR InterPro; IPR038351; MCD_N_sf.
DR PANTHER; PTHR28641; PTHR28641; 1.
DR Pfam; PF05292; MCD; 1.
DR Pfam; PF17408; MCD_N; 1.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Cytoplasm; Decarboxylase;
KW Direct protein sequencing; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Lyase; Mitochondrion; Peroxisome;
KW Transit peptide.
FT TRANSIT 1..50
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 51..504
FT /note="Malonyl-CoA decarboxylase, mitochondrial"
FT /id="PRO_0000021086"
FT REGION 51..201
FT /note="Alpha-helical domain"
FT /evidence="ECO:0000250"
FT REGION 202..504
FT /note="Catalytic domain"
FT /evidence="ECO:0000250"
FT MOTIF 502..504
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 340
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 434
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT SITE 222
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..50
FT /note="Missing (in isoform Cytoplasmic+peroxisomal)"
FT /evidence="ECO:0000303|PubMed:1416987"
FT /id="VSP_018815"
FT CONFLICT 124..136
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="V -> L (in Ref. 2; AAA49317)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 504 AA; 56690 MW; 683991C1F9773DF4 CRC64;
MRGLRRGLSR LGPRLGPWAV PRSLRRVLRA AGPWRGQSSA GSVSERGGAS MEEVLSRSVP
LLPPYETKEK APPPAERRSA EFVRYYRGLE AGSRRAELLG CLARDFGADH GRVAEFSAKV
LQAREQEREQ GALLQAEDRV RYYLTPRYRA LFQHLGRLEG GLRFLVELRG DLVEGLAAKA
VDGPHVKEMS GVLKNMLSEW FSTGFLNLER VTWQSPCEVL QKISDSEAVH PVRNWVDLKR
RVGPYRRCYF FSHCAIPGEP LIILHVALTS DISSSIQSIV KDVESLETED AEKITTAIFY
SISLAQQGLQ GVELGNHLIK RVVKELQKDL PQIEAFSSLS PIPGFTKWLV GLLSSQTKEL
GRNELFTESE RQEISEITED STTETLKKLL TNSEWVKSEK LVKALHSPLM RLCAWYLYGE
KHRGYALNPV ANFHLQNGAE LWRINWMGDT SPRGIAASCG MMVNYRYFLE DTASNSAAYL
GTKHIKASEQ VLSFVSQFQQ NSKL
