MMDA_VEIPA
ID MMDA_VEIPA Reviewed; 509 AA.
AC Q57079;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Methylmalonyl-CoA decarboxylase subunit alpha {ECO:0000305};
DE EC=7.2.4.3 {ECO:0000269|PubMed:2920730, ECO:0000269|PubMed:6852015, ECO:0000269|PubMed:7601825};
DE AltName: Full=Carboxyltransferase {ECO:0000305};
GN Name=mmdA {ECO:0000303|PubMed:8227015};
GN ORFNames=CYK26_07570 {ECO:0000312|EMBL:PKZ92514.1},
GN DWV36_05400 {ECO:0000312|EMBL:RGX04059.1},
GN FNLLGLLA_00681 {ECO:0000312|EMBL:CAB1275121.1},
GN GL281_04675 {ECO:0000312|EMBL:MTH56717.1},
GN HMPREF1865_00706 {ECO:0000312|EMBL:KXB86198.1};
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 1-11, AND SUBUNIT.
RC STRAIN=ATCC 17745;
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=UMB0371;
RA Thomas-White K., Wolfe A.J.;
RT "Phylogenetic diversity of female urinary microbiome.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BIOML-A2;
RX PubMed=31477907; DOI=10.1038/s41591-019-0559-3;
RA Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X.,
RA Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D.,
RA Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J.,
RA Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A.,
RA Xavier R.J., Alm E.J.;
RT "A library of human gut bacterial isolates paired with longitudinal
RT multiomics data enables mechanistic microbiome research.";
RL Nat. Med. 25:1442-1452(2019).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKV38;
RA Beloin C.;
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND SUBCELLULAR 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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
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: 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. The alpha subunit
CC catalyzes the Na(+)-independent carboxyltransfer from methylmalonyl-CoA
CC to the prosthetic biotin group located on the gamma subunit
CC (PubMed:7070502, PubMed:6852015, PubMed:3609308, PubMed:2920730,
CC PubMed:1991479, PubMed:7601825). Can also convert malonyl-CoA into
CC acetyl-CoA (PubMed:6852015, PubMed:2920730).
CC {ECO:0000269|PubMed:1991479, ECO:0000269|PubMed:2920730,
CC ECO:0000269|PubMed:3609308, ECO:0000269|PubMed:6852015,
CC ECO:0000269|PubMed:7070502, 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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7 uM for (S)-methylmalonyl-CoA {ECO:0000269|PubMed:6852015};
CC KM=35 uM for malonyl-CoA {ECO:0000269|PubMed:6852015};
CC KM=0.6 mM for Na(+) {ECO:0000269|PubMed:6852015};
CC pH dependence:
CC Optimum pH is 6.4-7.0. {ECO:0000269|PubMed:6852015};
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 (PubMed:8227015,
CC PubMed:7601825). Interacts with the gamma subunit (PubMed:7601825).
CC {ECO:0000269|PubMed:7601825, 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.10}.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000305}.
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; AAC36820.1; -; Unassigned_DNA.
DR EMBL; Z24754; CAA80872.1; -; Genomic_DNA.
DR EMBL; LSDP01000020; KXB86198.1; -; Genomic_DNA.
DR EMBL; PKHW01000004; PKZ92514.1; -; Genomic_DNA.
DR EMBL; QSBH01000003; RGX04059.1; -; Genomic_DNA.
DR EMBL; WMKL01000003; MTH56717.1; -; Genomic_DNA.
DR EMBL; LR778174; CAB1275121.1; -; Genomic_DNA.
DR PIR; A49094; A49094.
DR RefSeq; WP_004696486.1; NZ_WMKM01000002.1.
DR SMR; Q57079; -.
DR STRING; 29466.GCA_002005185_01895; -.
DR TCDB; 3.B.1.1.2; the na(+)-transporting carboxylic acid decarboxylase (nat-dc) family.
DR EnsemblBacteria; KXB86198; KXB86198; HMPREF1865_00706.
DR EnsemblBacteria; PKZ92514; PKZ92514; CYK26_07570.
DR GeneID; 57850530; -.
DR PATRIC; fig|29466.15.peg.694; -.
DR BioCyc; MetaCyc:MON-21717; -.
DR Proteomes; UP000070604; Unassembled WGS sequence.
DR Proteomes; UP000234458; Unassembled WGS sequence.
DR Proteomes; UP000283535; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016874; F:ligase activity; IEA:InterPro.
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 CHAIN 1..509
FT /note="Methylmalonyl-CoA decarboxylase subunit alpha"
FT /id="PRO_0000453533"
FT DOMAIN 4..260
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 267..503
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
SQ SEQUENCE 509 AA; 55101 MW; B9F85266A422B03B CRC64;
MATVQEKIEL LHEKLAKVKA GGGEKRVEKQ HAQGKMTARE RLAKLFDDNS FVELDQFVKH
RCVNFGQEKK ELPGEGVVTG YGTIDGRLVY AFAQDFTVEG GSLGEMHAAK IVKVQRLAMK
MGAPIVGIND SGGARIQEAV DALAGYGKIF FENTNASGVI PQISVIMGPC AGGAVYSPAL
TDFIYMVKNT SQMFITGPAV IKSVTGEEVT AEDLGGAMAH NSVSGVAHFA AENEDDCIAQ
IRYLLGFLPS NNMEDAPLVD TGDDPTREDE SLNSLLPDNS NMPYDMKDVI AATVDNGEYY
EVQPFYATNI ITCFARFDGQ SVGIIANQPK VMAGCLDINA SDKSSRFIRF CDAFNIPIVN
FVDVPGFLPG TNQEWGGIIR HGAKMLYAYS EATVPKITVI TRKAYGGSYL AMCSQDLGAD
QVYAWPTSEI AVMGPAGAAN IIFKKDEDKD AKTAKYVEEF ATPYKAAERG FVDVVIEPKQ
TRPAVINALA MLASKRENRA PKKHGNIPL
