MADB_MALRU
ID MADB_MALRU Reviewed; 401 AA.
AC O06923;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Carboxybiotin decarboxylase;
DE EC=7.2.4.1 {ECO:0000269|PubMed:11902724};
DE AltName: Full=Carboxybiotin protein decarboxylase;
GN Name=madB;
OS Malonomonas rubra.
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Desulfuromonadaceae; Malonomonas.
OX NCBI_TaxID=57040;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=9128730; DOI=10.1111/j.1432-1033.1997.00103.x;
RA Berg M., Hilbi H., Dimroth P.;
RT "Sequence of a gene cluster from Malonomonas rubra encoding components of
RT the malonate decarboxylase Na+ pump and evidence for their function.";
RL Eur. J. Biochem. 245:103-115(1997).
RN [2]
RP CATALYTIC ACTIVITY.
RX PubMed=11902724; DOI=10.1046/j.1365-2958.1997.4611824.x;
RA Dimroth P., Hilbi H.;
RT "Enzymic and genetic basis for bacterial growth on malonate.";
RL Mol. Microbiol. 25:3-10(1997).
CC -!- FUNCTION: Beta subunit of the biotin-dependent malonate decarboxylase
CC multienzyme complex (EC 7.2.4.4). Acts as an integral membrane-bound
CC carboxybiotin protein decarboxylase by releasing the carboxyl group of
CC the carboxylated biotin carrier MADF. The free energy of the
CC decarboxylation reaction is used to pump Na(+) out of the cell.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + n Na(+)(in) =
CC CO2 + N(6)-biotinyl-L-lysyl-[protein] + n Na(+)(out);
CC Xref=Rhea:RHEA:43336, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:83144, ChEBI:CHEBI:83145; EC=7.2.4.1;
CC Evidence={ECO:0000269|PubMed:11902724};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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DR EMBL; U87980; AAC45399.1; -; Genomic_DNA.
DR AlphaFoldDB; O06923; -.
DR SMR; O06923; -.
DR TCDB; 3.B.1.1.4; the na(+)-transporting carboxylic acid decarboxylase (nat-dc) family.
DR KEGG; ag:AAC45399; -.
DR BioCyc; MetaCyc:MON-14257; -.
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:0015451; F:decarboxylation-driven active transmembrane transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR GO; GO:0006814; P:sodium ion transport; IEA:InterPro.
DR InterPro; IPR017558; Malonate_biotin.
DR InterPro; IPR005661; OadB_MmdB.
DR PANTHER; PTHR35806; PTHR35806; 1.
DR Pfam; PF03977; OAD_beta; 1.
DR PIRSF; PIRSF015658; MmdB_OadB; 1.
DR TIGRFAMs; TIGR03136; malonate_biotin; 1.
DR TIGRFAMs; TIGR01109; Na_pump_decarbB; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..401
FT /note="Carboxybiotin decarboxylase"
FT /id="PRO_0000424275"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 401 AA; 43024 MW; 5E69B195E29748CD CRC64;
MEQLMSLFPA ISTLFTQDPV ISITRIALII FGFFLSYFGF KRTLEPLIMV PMGLGMIAIN
AGVLFLEAGV VGTIHLDPLV SEPSVLVNLM QVNWLQPVYN FTFSNGLIAC IVFFGIGAMS
DISFILIRPW ASIIVALFAE MGTFATLIIG IKMGLLPNEA AAVATIGGAD GPMVLFASLI
LAKDLFVPIA IIAYLYLSLT YAGYPYLIKL LVPKKYRGLE VEMDFPEVSQ RSKFVFSVLA
CMLLCLLLPV ASPLILSFFL GIAIKEAQIE PFQNLLETTL TYGSTLFLGL LLGALCEAKT
ILDPKISLIV VLGITALLIS GIGGVLGGWI VYWFSKGKFN PVIGIAGVSC LPTTAKIAQK
TVTEENPYAV ILPLAMGAGV CGLIVSAIAT GVFISTLFLL N