BCCP_PROFR
ID BCCP_PROFR Reviewed; 123 AA.
AC P02904;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Methylmalonyl-CoA carboxyltransferase 1.3S subunit;
DE EC=2.1.3.1;
DE AltName: Full=Biotin carboxyl carrier protein of transcarboxylase;
DE AltName: Full=Transcarboxylase, 1.3S subunit;
OS Propionibacterium freudenreichii subsp. shermanii.
OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC Propionibacterium.
OX NCBI_TaxID=1752;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3898065; DOI=10.1073/pnas.82.17.5617;
RA Murtif V.L., Bahler C.R., Samols D.;
RT "Cloning and expression of the 1.3S biotin-containing subunit of
RT transcarboxylase.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:5617-5621(1985).
RN [2]
RP PROTEIN SEQUENCE, AND BIOTINYLATION AT LYS-89.
RX PubMed=40985; DOI=10.1016/s0021-9258(19)86529-8;
RA Maloy W.L., Bowien B.U., Zwolinski G.K., Kumar G.K., Wood H.G.,
RA Ericsson L.H., Walsh K.A.;
RT "Amino acid sequence of the biotinyl subunit from transcarboxylase.";
RL J. Biol. Chem. 254:11615-11622(1979).
RN [3]
RP MUTAGENESIS OF ALA-87; MET-88 AND MET-90, AND SUBUNIT STRUCTURE.
RX PubMed=1526981; DOI=10.1016/s0021-9258(19)36977-7;
RA Shenoy B.C., Xie Y., Park V.L., Kumar G.K., Beegen H., Wood H.G.,
RA Samols D.;
RT "The importance of methionine residues for the catalysis of the biotin
RT enzyme, transcarboxylase. Analysis by site-directed mutagenesis.";
RL J. Biol. Chem. 267:18407-18412(1992).
RN [4]
RP STRUCTURE BY NMR.
RX PubMed=9398186; DOI=10.1021/bi971674y;
RA Reddy D.V., Shenoy B.C., Carey P.R., Soennichsen F.D.;
RT "Absence of observable biotin-protein interactions in the 1.3S subunit of
RT transcarboxylase: an NMR study.";
RL Biochemistry 36:14676-14682(1997).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=10704200; DOI=10.1021/bi9925367;
RA Reddy D.V., Shenoy B.C., Carey P.R., Soennichsen F.D.;
RT "High resolution solution structure of the 1.3S subunit of transcarboxylase
RT from Propionibacterium shermanii.";
RL Biochemistry 39:2509-2516(2000).
CC -!- FUNCTION: The biotinyl 1.3S subunit serves as a carboxyl carrier
CC between the substrate-binding sites on the 12S and 5S subunits.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-methylmalonyl-CoA + pyruvate = oxaloacetate + propanoyl-
CC CoA; Xref=Rhea:RHEA:20764, ChEBI:CHEBI:15361, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:57327, ChEBI:CHEBI:57392; EC=2.1.3.1;
CC -!- SUBUNIT: Transcarboxylase is composed of three subunits: 1.3S, 5S, and
CC 12S. The core of the enzyme is composed of six 12S subunits. On each
CC side of the core there are three pairs of 5S subunits. Each 5S dimer is
CC attached to the core by two 1.3S subunits. Thus the total number of
CC chains is 30 (6 + 12 + 12). {ECO:0000269|PubMed:1526981}.
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DR EMBL; M11738; AAA25674.1; -; Genomic_DNA.
DR PIR; A03401; BKIP.
DR RefSeq; WP_013161729.1; NZ_OVTV01000165.1.
DR PDB; 1DCZ; NMR; -; A=47-123.
DR PDB; 1DD2; NMR; -; A=47-123.
DR PDB; 1O78; NMR; -; A=1-9, A=51-123.
DR PDBsum; 1DCZ; -.
DR PDBsum; 1DD2; -.
DR PDBsum; 1O78; -.
DR AlphaFoldDB; P02904; -.
DR BMRB; P02904; -.
DR SMR; P02904; -.
DR OMA; AIHVGPG; -.
DR BioCyc; MetaCyc:MON-12431; -.
DR EvolutionaryTrace; P02904; -.
DR GO; GO:0047154; F:methylmalonyl-CoA carboxytransferase activity; IEA:UniProtKB-EC.
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 3D-structure; Biotin; Direct protein sequencing; Transferase.
FT CHAIN 1..123
FT /note="Methylmalonyl-CoA carboxyltransferase 1.3S subunit"
FT /id="PRO_0000146809"
FT DOMAIN 46..123
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT MOD_RES 89
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066,
FT ECO:0000269|PubMed:40985"
FT MUTAGEN 87
FT /note="A->M: Reduces activity 10-fold; when associated with
FT L-88."
FT /evidence="ECO:0000269|PubMed:1526981"
FT MUTAGEN 88
FT /note="M->A,C,T,L: Reduces activity at least 10-fold."
FT /evidence="ECO:0000269|PubMed:1526981"
FT MUTAGEN 90
FT /note="M->L: No effect."
FT /evidence="ECO:0000269|PubMed:1526981"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:1DCZ"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:1DCZ"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:1DCZ"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:1DCZ"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:1DCZ"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:1DCZ"
SQ SEQUENCE 123 AA; 12367 MW; D0980C2065EA9A89 CRC64;
MKLKVTVNGT AYDVDVDVDK SHENPMGTIL FGGGTGGAPA PRAAGGAGAG KAGEGEIPAP
LAGTVSKILV KEGDTVKAGQ TVLVLEAMKM ETEINAPTDG KVEKVLVKER DAVQGGQGLI
KIG
