ID   MMDD_VEIPA              Reviewed;         115 AA.
AC   Q56724; Q56723;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Methylmalonyl-CoA decarboxylase subunit delta {ECO:0000305};
DE            EC=7.2.4.3 {ECO:0000269|PubMed:2920730, ECO:0000269|PubMed:6852015, ECO:0000269|PubMed:7601825};
GN   Name=mmdD {ECO:0000303|PubMed:8227015};
OS   Veillonella parvula (Staphylococcus parvulus).
OC   Bacteria; Firmicutes; Negativicutes; Veillonellales; Veillonellaceae;
OC   Veillonella.
OX   NCBI_TaxID=29466;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], 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   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   [3]
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   [4]
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   [5]
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   [6]
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   [7]
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   [8]
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   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBUNIT.
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       delta subunit is required for catalytic activity as well as for the
CC       proper assembly of the individual subunits to an enzyme complex
CC       (PubMed:7601825). Can also convert malonyl-CoA into acetyl-CoA
CC       (PubMed:6852015, 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.5}; Single-pass membrane protein {ECO:0000255}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:8227015}.
CC   -!- SIMILARITY: Belongs to the OadG family. {ECO:0000305}.
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DR   EMBL; L22208; AAC36821.1; -; Unassigned_DNA.
DR   EMBL; Z24754; CAA80873.1; -; Genomic_DNA.
DR   PIR; B49094; B49094.
DR   RefSeq; WP_004696485.1; NZ_LT906445.1.
DR   SMR; Q56724; -.
DR   TCDB; 3.B.1.1.2; the na(+)-transporting carboxylic acid decarboxylase (nat-dc) family.
DR   OMA; IIMLINM; -.
DR   BioCyc; MetaCyc:MON-21720; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015081; F:sodium ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0036376; P:sodium ion export across plasma membrane; IEA:InterPro.
DR   InterPro; IPR005899; Na_pump_deCOase.
DR   Pfam; PF04277; OAD_gamma; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Ion transport; Membrane; Sodium; Sodium transport;
KW   Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..115
FT                   /note="Methylmalonyl-CoA decarboxylase subunit delta"
FT                   /id="PRO_0000453539"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          46..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   115 AA;  11951 MW;  3F873586E596EC26 CRC64;
     MEGQAVTTNP WLIMAINMTV VFAVLIALGI LMEIVHLIDP TKKKKEAPAA TAPVATPTAT
     PVAPANASAQ NEDEVVAAIV GAIVAMGYSS EQIASIRPTA TSAKWRLEGR LSGRG