ID   MMDA_PROMO              Reviewed;         517 AA.
AC   O54028;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   29-SEP-2021, sequence version 2.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Methylmalonyl-CoA decarboxylase subunit alpha {ECO:0000305};
DE            EC=7.2.4.3 {ECO:0000269|PubMed:9428714};
GN   Name=mmdA {ECO:0000303|PubMed:9428714};
OS   Propionigenium modestum.
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Propionigenium.
OX   NCBI_TaxID=2333;
RN   [1]
RP   PROTEIN SEQUENCE OF 1-31, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-516,
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=DSM 2376 / Gra Succ2;
RX   PubMed=9428714; DOI=10.1111/j.1432-1033.1997.0590a.x;
RA   Bott M., Pfister K., Burda P., Kalbermatter O., Woehlke G., Dimroth P.;
RT   "Methylmalonyl-CoA decarboxylase from Propionigenium modestum--cloning and
RT   sequencing of the structural genes and purification of the enzyme
RT   complex.";
RL   Eur. J. Biochem. 250:590-599(1997).
CC   -!- FUNCTION: Carboxyltransferase subunit of the sodium ion pump
CC       methylmalonyl-CoA decarboxylase, which converts the chemical energy of
CC       a decarboxylation reaction into an electrochemical gradient of Na(+)
CC       ions across the cytoplasmic membrane, thereby creating a sodium ion
CC       motive force that is used for ATP synthesis (PubMed:9428714). The alpha
CC       subunit catalyzes the Na(+)-independent carboxyltransfer from
CC       methylmalonyl-CoA to the prosthetic biotin group located on the gamma
CC       subunit (By similarity). {ECO:0000250|UniProtKB:Q57079,
CC       ECO:0000269|PubMed:9428714}.
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:9428714};
CC   -!- SUBUNIT: The methylmalonyl-CoA decarboxylase is composed of four
CC       subunits: the carboxyltransferase alpha subunit (MmdA), the tunnel beta
CC       subunit (MmdB), the biotin-containing gamma subunit (MmdC) and the
CC       delta subunit (MmdD). {ECO:0000269|PubMed:9428714}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9428714}.
CC   -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000305}.
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DR   EMBL; AJ002015; CAA05137.1; -; Genomic_DNA.
DR   PIR; T44982; T44982.
DR   SMR; O54028; -.
DR   KEGG; ag:CAA05137; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR   GO; GO:0004492; F:methylmalonyl-CoA decarboxylase activity; IEA:RHEA.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR034733; AcCoA_carboxyl.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   InterPro; IPR005783; MemalonylCoA_decase_suA.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   SUPFAM; SSF52096; SSF52096; 2.
DR   TIGRFAMs; TIGR01117; mmdA; 1.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
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:9428714"
FT   CHAIN           2..517
FT                   /note="Methylmalonyl-CoA decarboxylase subunit alpha"
FT                   /id="PRO_0000453532"
FT   DOMAIN          4..260
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT   DOMAIN          271..513
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
SQ   SEQUENCE   517 AA;  56111 MW;  ACDAE666051AF4EF CRC64;
     MSVAAKKIQD LQKKKEKIAL GGGIKRIEKQ HASGKMTARE RLAYLFDEGT FVEMDAFVQH
     RCTNFGMDKQ DLPSESVVTG YGMVDGRVVY AFSQDFTVTG GALGEMHAKK ICKAMDMAGK
     VGAPVVGLND SGGARIQEAV DALSGYGDIF YRNSIYSGVV PQISAILGPC AGGAVYSPAL
     TDFIFMVDQT SQMFITGPQV IKTVTGEEVT AEQLGGAMTH NSTSGCAQFI SQDDKACIDD
     IRRLISFLPS NNMEKAPEFG CEDDLNIQFP ELDALMPDNP NKAYNMFDVI TKIVDNGDYM
     EYQPHYSKNI ITCFARVNGK SVGIIANQPQ VMAGCLDIDS GDKCAKFIRT CDAFNIPLLT
     IVDVPGFLPG VTQEYGGIIR HGAKILYAYS EATVPKVTLI TRKAYGGAYV AMCSKSLGAD
     VVLAWPTAEI AVMGPAGAVN IIFRKDIKDA KDPAATTKQK LDEYTTEFAN PYQAARRGLV
     DDVIEPKTSR QRIVDAFNML EGKREKLPAK KHGNIPL