MMDB_VEIPA
ID MMDB_VEIPA Reviewed; 373 AA.
AC Q57286;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Methylmalonyl-CoA decarboxylase subunit beta {ECO:0000305};
DE EC=7.2.4.3 {ECO:0000269|PubMed:2920730, ECO:0000269|PubMed:6852015, ECO:0000269|PubMed:7601825};
GN Name=mmdB {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, BIOPHYSICOCHEMICAL
RP PROPERTIES, 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 [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: Tunnel 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. The beta subunit catalyzes the
CC decarboxylation of the carboxybiotin carrier protein and the coupled
CC export of Na(+) ions (PubMed:7070502, PubMed:6852015, PubMed:3609308,
CC PubMed:2920730, PubMed:1991479, PubMed:7601825). Can also convert
CC malonyl-CoA into 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. {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}; Multi-pass membrane protein {ECO:0000255}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:8227015}.
CC -!- SIMILARITY: Belongs to the GcdB/MmdB/OadB family. {ECO:0000305}.
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DR EMBL; L22208; AAC36824.1; -; Unassigned_DNA.
DR EMBL; Z24754; CAA80876.1; -; Genomic_DNA.
DR PIR; E49094; E49094.
DR RefSeq; WP_004696480.1; NZ_LT906445.1.
DR SMR; Q57286; -.
DR TCDB; 3.B.1.1.2; the na(+)-transporting carboxylic acid decarboxylase (nat-dc) family.
DR OMA; PMIADPK; -.
DR BioCyc; MetaCyc:MON-21718; -.
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:0018801; F:glutaconyl-CoA decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR005661; OadB_MmdB.
DR PANTHER; PTHR35806; PTHR35806; 1.
DR Pfam; PF03977; OAD_beta; 1.
DR PIRSF; PIRSF015658; MmdB_OadB; 1.
DR TIGRFAMs; TIGR01109; Na_pump_decarbB; 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..373
FT /note="Methylmalonyl-CoA decarboxylase subunit beta"
FT /id="PRO_0000453537"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 373 AA; 38730 MW; 69D02C1E659CC486 CRC64;
MEAFAVAIQS VINDSGFLAF TTGNAIMILV GLILLYLAFA REFEPLLLGP IAFGCLLANI
PRNGFEEGVM ALISAGISQE IFPPLIFLGV GAMTDFGPLI ANPKTLLLGA AAQIGVFAAL
GGAMMLGFTA QEAAAIGIIG GADGPTSIYL ATKLAPHLLG AIAVAAYSYM SLVPLIQPPV
MKLFTTQKER EIVMEQLREV TRFEKIVFPI VATIFISLLL PSITSLLGML MLGNLFRESG
VTDRLSDTSQ NALINTVTIF LATGTGLTMS AEHFLSLETI KIILLGLFAF ICGTAGGVLF
GKLMSLVDGG KTNPLIGSAG VSAVPMAARV SQVVGAKANP ANFLLMHAMG PNVAGVIGTA
VAAGTMLAML SNH
