ID   MMDE_VEIPA              Reviewed;          55 AA.
AC   Q57490;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Methylmalonyl-CoA decarboxylase subunit epsilon {ECO:0000305};
DE            EC=7.2.4.3 {ECO:0000269|PubMed:2920730, ECO:0000269|PubMed:6852015, ECO:0000269|PubMed:7601825};
GN   Name=mmdE {ECO:0000303|PubMed:8227015};
GN   ORFNames=FNLLGLLA_00683 {ECO:0000312|EMBL:CAB1275125.1},
GN   HMPREF1865_00704 {ECO:0000312|EMBL:KXB86196.1};
OS   Veillonella parvula (Staphylococcus parvulus).
OC   Bacteria; Firmicutes; Negativicutes; Veillonellales; Veillonellaceae;
OC   Veillonella.
OX   NCBI_TaxID=29466;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-7, AND SUBUNIT.
RX   PubMed=8227015; DOI=10.1016/s0021-9258(19)74504-9;
RA   Huder J.B., Dimroth P.;
RT   "Sequence of the sodium ion pump methylmalonyl-CoA decarboxylase from
RT   Veillonella parvula.";
RL   J. Biol. Chem. 268:24564-24571(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DNF00876;
RA   Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA   O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA   Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SKV38;
RA   Beloin C.;
RL   Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=7070502; DOI=10.1038/296584a0;
RA   Hilpert W., Dimroth P.;
RT   "Conversion of the chemical energy of methylmalonyl-CoA decarboxylation
RT   into a Na+ gradient.";
RL   Nature 296:584-585(1982).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=ATCC 17745;
RX   PubMed=6852015; DOI=10.1111/j.1432-1033.1983.tb07403.x;
RA   Hilpert W., Dimroth P.;
RT   "Purification and characterization of a new sodium-transport decarboxylase.
RT   Methylmalonyl-CoA decarboxylase from Veillonella alcalescens.";
RL   Eur. J. Biochem. 132:579-587(1983).
RN   [6]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 17745;
RX   PubMed=6692834; DOI=10.1111/j.1432-1033.1984.tb07953.x;
RA   Hilpert W., Dimroth P.;
RT   "Reconstitution of Na+ transport from purified methylmalonyl-CoA
RT   decarboxylase and phospholipid vesicles.";
RL   Eur. J. Biochem. 138:579-583(1984).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   DOI=10.1016/0014-5793(86)80177-6;
RA   Rohde M., Dakena P., Mayer F., Dimroth P.;
RT   "Morphological properties of proteoliposomes reconstituted with the Na+
RT   pump methylmalonyl-CoA decarboxylase from Veillonella alcalescens.";
RL   FEBS Lett. 195:280-284(1986).
RN   [8]
RP   FUNCTION.
RX   PubMed=3609308; DOI=10.1016/0014-5793(87)80888-8;
RA   Hoffmann A., Dimroth P.;
RT   "Stereochemistry of the methylmalonyl-CoA decarboxylation reaction.";
RL   FEBS Lett. 220:121-125(1987).
RN   [9]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 17745;
RX   PubMed=2920730; DOI=10.1111/j.1432-1033.1989.tb14596.x;
RA   Hoffmann A., Hilpert W., Dimroth P.;
RT   "The carboxyltransferase activity of the sodium-ion-translocating
RT   methylmalonyl-CoA decarboxylase of Veillonella alcalescens.";
RL   Eur. J. Biochem. 179:645-650(1989).
RN   [10]
RP   FUNCTION.
RC   STRAIN=ATCC 17745;
RX   PubMed=1991479; DOI=10.1111/j.1432-1033.1991.tb15678.x;
RA   Hilpert W., Dimroth P.;
RT   "On the mechanism of sodium ion translocation by methylmalonyl-CoA
RT   decarboxylase from Veillonella alcalescens.";
RL   Eur. J. Biochem. 195:79-86(1991).
RN   [11]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=7601825; DOI=10.1128/jb.177.13.3623-3630.1995;
RA   Huder J.B., Dimroth P.;
RT   "Expression of the sodium ion pump methylmalonyl-coenzyme A-decarboxylase
RT   from Veillonella parvula and of mutated enzyme specimens in Escherichia
RT   coli.";
RL   J. Bacteriol. 177:3623-3630(1995).
CC   -!- FUNCTION: Subunit of the sodium ion pump methylmalonyl-CoA
CC       decarboxylase, which converts the chemical energy of a decarboxylation
CC       reaction into an electrochemical gradient of Na(+) ions across the
CC       cytoplasmic membrane, thereby creating a sodium ion motive force that
CC       is used for ATP synthesis (PubMed:7070502, PubMed:6852015,
CC       PubMed:3609308, PubMed:2920730, PubMed:1991479, PubMed:7601825). The
CC       epsilon subunit seems not important for the catalysis of either
CC       decarboxylation or Na(+) transport, but it improves binding of the
CC       alpha subunit and plays an important role in stabilizing the
CC       methylmalonyl-CoA-decarboxylase enzyme complex (PubMed:7601825). Can
CC       also convert malonyl-CoA into acetyl-CoA (PubMed:6852015,
CC       PubMed:2920730). {ECO:0000269|PubMed:1991479,
CC       ECO:0000269|PubMed:2920730, ECO:0000269|PubMed:3609308,
CC       ECO:0000269|PubMed:6852015, ECO:0000269|PubMed:7070502,
CC       ECO:0000269|PubMed:7601825}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-methylmalonyl-CoA + H(+)(out) + Na(+)(in) = CO2 +
CC         Na(+)(out) + propanoyl-CoA; Xref=Rhea:RHEA:21396, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:29101, ChEBI:CHEBI:57327,
CC         ChEBI:CHEBI:57392; EC=7.2.4.3; Evidence={ECO:0000269|PubMed:2920730,
CC         ECO:0000269|PubMed:6852015, ECO:0000269|PubMed:7601825};
CC   -!- ACTIVITY REGULATION: Completely inhibited by avidin.
CC       {ECO:0000269|PubMed:6852015, ECO:0000269|PubMed:7601825}.
CC   -!- SUBUNIT: The methylmalonyl-CoA decarboxylase is composed of five
CC       subunits: the carboxyltransferase alpha subunit (MmdA), the tunnel beta
CC       subunit (MmdB), the biotin-containing gamma subunit (MmdC), and the
CC       delta (MmdD) and epsilon (MmdE) subunits. {ECO:0000269|PubMed:7601825,
CC       ECO:0000269|PubMed:8227015}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:6692834,
CC       ECO:0000269|PubMed:6852015, ECO:0000269|PubMed:7070502,
CC       ECO:0000269|Ref.7}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the gene does not abolish
CC       methylmalonyl-CoA-decarboxylase or Na(+) transport activity, but it
CC       affects the stability of the complex, especially the binding of the
CC       alpha subunit. Mutant lacking this gene plus the 3'-terminal half of
CC       the mmdD gene lacks methylmalonyl-CoA decarboxylase activity.
CC       {ECO:0000269|PubMed:7601825}.
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DR   EMBL; L22208; AAC36822.1; -; Unassigned_DNA.
DR   EMBL; Z24754; CAA80874.1; -; Genomic_DNA.
DR   EMBL; LSDP01000020; KXB86196.1; -; Genomic_DNA.
DR   EMBL; LR778174; CAB1275125.1; -; Genomic_DNA.
DR   PIR; C49094; C49094.
DR   TCDB; 3.B.1.1.2; the na(+)-transporting carboxylic acid decarboxylase (nat-dc) family.
DR   EnsemblBacteria; KXB86196; KXB86196; HMPREF1865_00704.
DR   PATRIC; fig|29466.15.peg.692; -.
DR   Proteomes; UP000070604; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Ion transport; Membrane; Sodium;
KW   Sodium transport; Translocase; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8227015"
FT   CHAIN           2..55
FT                   /note="Methylmalonyl-CoA decarboxylase subunit epsilon"
FT                   /id="PRO_0000453531"
SQ   SEQUENCE   55 AA;  5889 MW;  0FA6EC78ACC7070F CRC64;
     MSNATTTNGK APSQDVVAVI VGALAAMGYS ADQIAHIRPI VSYNWKMEGR LRGNR