MCD_CERSP
ID MCD_CERSP Reviewed; 548 AA.
AC D3JV03;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=(2S)-methylsuccinyl-CoA dehydrogenase {ECO:0000303|PubMed:19703103};
DE Short=MCD {ECO:0000303|PubMed:19703103};
DE EC=1.3.8.12 {ECO:0000269|PubMed:19703103};
GN Name=mcd {ECO:0000303|PubMed:19703103};
OS Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=1063;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE, COFACTOR, SUBUNIT, AND
RP SUBSTRATE SPECIFICITY.
RC STRAIN=2.4.1;
RX PubMed=19703103; DOI=10.1111/j.1365-2958.2009.06837.x;
RA Erb T.J., Fuchs G., Alber B.E.;
RT "(2S)-Methylsuccinyl-CoA dehydrogenase closes the ethylmalonyl-CoA pathway
RT for acetyl-CoA assimilation.";
RL Mol. Microbiol. 73:992-1008(2009).
CC -!- FUNCTION: Involved in the ethylmalonyl-CoA pathway, a new acetyl-CoA
CC assimilation strategy that operates in a number of bacteria and
CC replaces the glyoxylate cycle. Catalyzes the oxidation of (2S)-
CC methylsuccinyl-CoA to yield mesaconyl-(C1)-CoA. Highly specific for
CC (S)-methylsuccinyl-CoA. {ECO:0000269|PubMed:19703103}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-methylsuccinyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = 2-methylfumaryl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:45028, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:75635, ChEBI:CHEBI:84866; EC=1.3.8.12;
CC Evidence={ECO:0000269|PubMed:19703103};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:19703103};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:19703103};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20 uM for (2S)-methylsuccinyl-CoA {ECO:0000269|PubMed:19703103};
CC Vmax=6 umol/min/mg enzyme {ECO:0000269|PubMed:19703103};
CC pH dependence:
CC Optimum pH is 9.2. {ECO:0000269|PubMed:19703103};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19703103}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to utilize
CC acetate or acetoacetate as sole carbon source, but grow on succinate or
CC propionate plus bicarbonate. {ECO:0000269|PubMed:19703103}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; GU320611; ADC44452.1; -; Genomic_DNA.
DR AlphaFoldDB; D3JV03; -.
DR SMR; D3JV03; -.
DR BioCyc; MetaCyc:MON-19169; -.
DR BRENDA; 1.3.8.12; 5383.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0052890; F:oxidoreductase activity, acting on the CH-CH group of donors, with a flavin as acceptor; IDA:UniProtKB.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Oxidoreductase.
FT CHAIN 1..548
FT /note="(2S)-methylsuccinyl-CoA dehydrogenase"
FT /id="PRO_0000435827"
FT ACT_SITE 532
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P15651"
FT BINDING 282..291
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P15651"
FT BINDING 291
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15651"
FT BINDING 315..317
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P15651"
FT BINDING 409..412
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15651"
FT BINDING 437
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P15651"
FT BINDING 505..509
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P15651"
FT BINDING 534..536
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P15651"
SQ SEQUENCE 548 AA; 59772 MW; 6D573DBB5CED31EB CRC64;
MTGQPLLGDL LTLASDALPE VEALFETARS ALKERVTTDG KVSSKALEEE QFAAHALSWL
ATYVESLRQM RAWAGRLETE GRFGEMEALI LQIAFGEYLA QIRGGIPMSQ TETARVQDIG
IELGHPGEAV RRLIQAGNTP AARARLVALM RDNHGRATFG ASGLDEELEM IRDQFRRFAD
ERVAPHAHGW HMRDELIPME IVEALAEMGV FGLTIPEEFG GFGLSKASMV VVSEELSRGY
IGVGSLGTRS EIAAELILCG GTDAQKAAWL PKLASGEILP TAVFTEPNTG SDLGSLRTRA
VKDGDEWVVH GNKTWITHAA RTHVMTLLAR TDLETTDYRG LSMFLAEKVP GTDADPFPTP
GMTGGEIEVL GYRGMKEYEI GFDGFRVKAE NLLGGVEGQG FKQLMQTFES ARIQTAARAI
GVAQNALEVG MQYAEERKQF GKALIEFPRV AGKLAMMAVE IMVARQLTYH SAWEKDHGQR
CDLEAGMAKL LGARVAWAAA DNALQIHGGN GFALEYQISR ILCDARILNI FEGAAEIQAQ
VIARRLLD
