MMDC_VEIPA
ID MMDC_VEIPA Reviewed; 129 AA.
AC Q57111;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Methylmalonyl-CoA decarboxylase subunit gamma {ECO:0000305};
DE EC=7.2.4.3 {ECO:0000269|PubMed:2920730, ECO:0000269|PubMed:6852015, ECO:0000269|PubMed:7601825};
GN Name=mmdC {ECO:0000303|PubMed:8227015};
GN ORFNames=D3219_04680 {ECO:0000312|EMBL:RIW10324.1},
GN DWV36_05390 {ECO:0000312|EMBL:RGX04057.1},
GN HMPREF1865_00703 {ECO:0000312|EMBL:KXB86195.1};
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 1-23, 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=AF04-47;
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KHUD_VP2;
RA Lee J.-H., Moon J.-H., Shin S.-Y.;
RT "Genome sequence of Veillonella parvula isolated from periodontal Korean
RT patients.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
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: Biotin-containing 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:7070502,
CC PubMed:6852015, PubMed:3609308, PubMed:2920730, PubMed:1991479,
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 -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01066};
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.8}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L22208; AAC36823.1; -; Unassigned_DNA.
DR EMBL; Z24754; CAA80875.1; -; Genomic_DNA.
DR EMBL; LSDP01000020; KXB86195.1; -; Genomic_DNA.
DR EMBL; QSBH01000003; RGX04057.1; -; Genomic_DNA.
DR EMBL; QYAA01000006; RIW10324.1; -; Genomic_DNA.
DR PIR; D49094; D49094.
DR RefSeq; WP_004696481.1; NZ_QYAA01000006.1.
DR SMR; Q57111; -.
DR STRING; 29466.GCA_002005185_01892; -.
DR TCDB; 3.B.1.1.2; the na(+)-transporting carboxylic acid decarboxylase (nat-dc) family.
DR EnsemblBacteria; KXB86195; KXB86195; HMPREF1865_00703.
DR PATRIC; fig|29466.15.peg.691; -.
DR BioCyc; MetaCyc:MON-21719; -.
DR Proteomes; UP000070604; Unassembled WGS sequence.
DR Proteomes; UP000283535; Unassembled WGS sequence.
DR Proteomes; UP000285055; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR011053; Single_hybrid_motif.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PE 1: Evidence at protein level;
KW Biotin; Cell membrane; Direct protein sequencing; Ion transport; Membrane;
KW Sodium; Sodium transport; Translocase; Transport.
FT CHAIN 1..129
FT /note="Methylmalonyl-CoA decarboxylase subunit gamma"
FT /id="PRO_0000453535"
FT DOMAIN 51..129
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT REGION 24..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..52
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 95
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
SQ SEQUENCE 129 AA; 12687 MW; 205642A393380DCE CRC64;
MKKFNVTVNG TAYDVEVNEV KAAAPAAAPK AAPAAAPAPK AAPAPAPAPA AAAAPVPAGA
ETVKAPMPGK ILSVAVSAGQ AVKKGETLLI LEAMKMQNEI AAPHDAVVSE VRVSANQTVS
TGDDMVVLG
