12S_PROFR
ID 12S_PROFR Reviewed; 524 AA.
AC Q8GBW6; Q05617;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 4.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Methylmalonyl-CoA carboxyltransferase 12S subunit;
DE EC=2.1.3.1 {ECO:0000269|PubMed:8366018};
DE AltName: Full=Transcarboxylase 12S subunit {ECO:0000303|PubMed:8366018};
OS Propionibacterium freudenreichii subsp. shermanii.
OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC Propionibacterium.
OX NCBI_TaxID=1752;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-6; 13-39; 56-63;
RP 71-112; 199-213; 252-280; 351-372; 395-405 AND 500-516, FUNCTION, CATALYTIC
RP ACTIVITY, AND SUBUNIT.
RC STRAIN=St33;
RX PubMed=8366018; DOI=10.1128/jb.175.17.5301-5308.1993;
RA Thornton C.G., Kumar G.K., Haase F.C., Phillips N.F.B., Woo S.B.,
RA Park V.M., Magner W.J., Shenoy B.C., Wood H.G., Samols D.;
RT "Primary structure of the monomer of the 12S subunit of transcarboxylase as
RT deduced from DNA and characterization of the product expressed in
RT Escherichia coli.";
RL J. Bacteriol. 175:5301-5308(1993).
RN [2] {ECO:0007744|PDB:1ON3, ECO:0007744|PDB:1ON9}
RP NUCLEOTIDE SEQUENCE [MRNA], AND X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=12743028; DOI=10.1093/emboj/cdg244;
RA Hall P.R., Wang Y.-F., Rivera-Hainaj R.E., Zheng X., Pusztai-Carey M.,
RA Carey P.R., Yee V.C.;
RT "Transcarboxylase 12S crystal structure: hexamer assembly and substrate
RT binding to a multienzyme core.";
RL EMBO J. 22:2334-2347(2003).
CC -!- FUNCTION: The 12S subunit specifically catalyzes the transfer of the
CC carboxyl group of methylmalonyl CoA to the biotin of the 1.3S subunit
CC forming propanoyl-CoA and carboxylated 1.3S-biotin.
CC {ECO:0000269|PubMed:8366018}.
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 Evidence={ECO:0000269|PubMed:8366018};
CC -!- SUBUNIT: Homohexamer (PubMed:8366018, PubMed:12743028).
CC Transcarboxylase is composed of three subunits: 1.3S, 5S, and 12S. The
CC core of the enzyme is composed of six 12S subunits. On each side of the
CC core there are three pairs of 5S subunits. Each 5S dimer is attached to
CC the core by two 1.3S subunits. Thus the total number of chains is 30 (6
CC + 12 + 12) (Probable). {ECO:0000269|PubMed:12743028,
CC ECO:0000269|PubMed:8366018, ECO:0000305}.
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DR EMBL; L04196; AAA25676.1; -; Genomic_DNA.
DR EMBL; AJ535715; CAD59919.1; -; mRNA.
DR PIR; A48665; A48665.
DR PDB; 1ON3; X-ray; 1.90 A; A/B/C/D/E/F=2-518.
DR PDB; 1ON9; X-ray; 2.00 A; A/B/C/D/E/F=2-518.
DR PDBsum; 1ON3; -.
DR PDBsum; 1ON9; -.
DR AlphaFoldDB; Q8GBW6; -.
DR SMR; Q8GBW6; -.
DR DrugBank; DB04045; (R)-methylmalonyl-CoA.
DR DrugBank; DB04183; Methylmalonic Acid.
DR PRIDE; Q8GBW6; -.
DR BioCyc; MetaCyc:MON-12429; -.
DR BRENDA; 2.1.3.1; 5032.
DR EvolutionaryTrace; Q8GBW6; -.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR GO; GO:0047154; F:methylmalonyl-CoA carboxytransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR InterPro; IPR034733; AcCoA_carboxyl.
DR InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR PRINTS; PR01070; ACCCTRFRASEB.
DR SUPFAM; SSF52096; SSF52096; 2.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8366018"
FT CHAIN 2..524
FT /note="Methylmalonyl-CoA carboxyltransferase 12S subunit"
FT /id="PRO_0000146817"
FT DOMAIN 13..268
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 274..506
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT REGION 13..506
FT /note="Carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT CONFLICT 35
FT /note="R -> L (in Ref. 1; AAA25676)"
FT /evidence="ECO:0000305"
FT CONFLICT 113..126
FT /note="GETQSTKVVETMEQ -> WRDAVHEGRRDDGT (in Ref. 1;
FT AAA25676)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="Missing (in Ref. 1; AAA25676)"
FT /evidence="ECO:0000305"
FT CONFLICT 181..182
FT /note="GG -> C (in Ref. 1; AAA25676)"
FT /evidence="ECO:0000305"
FT CONFLICT 227..236
FT /note="AHMAISGNIH -> PIWPSRAIY (in Ref. 1; AAA25676)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="Missing (in Ref. 1; AAA25676)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="A -> R (in Ref. 1; AAA25676)"
FT /evidence="ECO:0000305"
FT CONFLICT 406..432
FT /note="VVLRKAYGGSYLAMCNRDLGADAVYAW -> CLATPTAAPTWPCATVTLVPT
FT PCTPV (in Ref. 1; AAA25676)"
FT /evidence="ECO:0000305"
FT CONFLICT 474..482
FT /note="AFNTPYVAA -> GSTRRTWR (in Ref. 1; AAA25676)"
FT /evidence="ECO:0000305"
FT CONFLICT 519..524
FT /note="HGNFPC -> PWKLPLLSEEEIMADEEEKDLMIATLNKRVASLESELGSLQS
FT DTQGVTEDVLTAISAVAAYLGNDGSAEVVHFAPSPNWVREGRRALQNHSIR (in
FT Ref. 1; AAA25676)"
FT /evidence="ECO:0000305"
FT HELIX 13..28
FT /evidence="ECO:0007829|PDB:1ON3"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:1ON3"
FT HELIX 33..41
FT /evidence="ECO:0007829|PDB:1ON3"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:1ON3"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1ON3"
FT TURN 73..78
FT /evidence="ECO:0007829|PDB:1ON3"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:1ON3"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:1ON3"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:1ON3"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:1ON3"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:1ON3"
FT HELIX 114..130
FT /evidence="ECO:0007829|PDB:1ON3"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:1ON3"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:1ON3"
FT HELIX 149..165
FT /evidence="ECO:0007829|PDB:1ON3"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:1ON3"
FT STRAND 171..181
FT /evidence="ECO:0007829|PDB:1ON3"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:1ON3"
FT HELIX 185..189
FT /evidence="ECO:0007829|PDB:1ON3"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:1ON3"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:1ON3"
FT HELIX 206..213
FT /evidence="ECO:0007829|PDB:1ON3"
FT HELIX 219..223
FT /evidence="ECO:0007829|PDB:1ON3"
FT HELIX 225..230
FT /evidence="ECO:0007829|PDB:1ON3"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:1ON3"
FT HELIX 242..254
FT /evidence="ECO:0007829|PDB:1ON3"
FT HELIX 277..281
FT /evidence="ECO:0007829|PDB:1ON3"
FT HELIX 294..300
FT /evidence="ECO:0007829|PDB:1ON3"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:1ON3"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:1ON3"
FT STRAND 317..324
FT /evidence="ECO:0007829|PDB:1ON3"
FT STRAND 327..334
FT /evidence="ECO:0007829|PDB:1ON3"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:1ON3"
FT HELIX 345..360
FT /evidence="ECO:0007829|PDB:1ON3"
FT STRAND 365..371
FT /evidence="ECO:0007829|PDB:1ON3"
FT HELIX 378..382
FT /evidence="ECO:0007829|PDB:1ON3"
FT HELIX 385..398
FT /evidence="ECO:0007829|PDB:1ON3"
FT STRAND 403..412
FT /evidence="ECO:0007829|PDB:1ON3"
FT HELIX 413..417
FT /evidence="ECO:0007829|PDB:1ON3"
FT TURN 418..420
FT /evidence="ECO:0007829|PDB:1ON3"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:1ON3"
FT STRAND 427..431
FT /evidence="ECO:0007829|PDB:1ON3"
FT STRAND 436..440
FT /evidence="ECO:0007829|PDB:1ON3"
FT HELIX 442..449
FT /evidence="ECO:0007829|PDB:1ON3"
FT HELIX 451..456
FT /evidence="ECO:0007829|PDB:1ON3"
FT STRAND 457..459
FT /evidence="ECO:0007829|PDB:1ON9"
FT HELIX 460..475
FT /evidence="ECO:0007829|PDB:1ON3"
FT HELIX 478..483
FT /evidence="ECO:0007829|PDB:1ON3"
FT STRAND 486..490
FT /evidence="ECO:0007829|PDB:1ON3"
FT HELIX 493..495
FT /evidence="ECO:0007829|PDB:1ON3"
FT HELIX 496..506
FT /evidence="ECO:0007829|PDB:1ON3"
FT HELIX 507..509
FT /evidence="ECO:0007829|PDB:1ON3"
SQ SEQUENCE 524 AA; 56397 MW; C04354D5FD92C2DB CRC64;
MAENNNLKLA STMEGRVEQL AEQRQVIEAG GGERRVEKQH SQGKQTARER LNNLLDPHSF
DEVGAFRKHR TTLFGMDKAV VPADGVVTGR GTILGRPVHA ASQDFTVMGG SAGETQSTKV
VETMEQALLT GTPFLFFYDS GGARIQEGID SLSGYGKMFF ANVKLSGVVP QIAIIAGPCA
GGASYSPALT DFIIMTKKAH MFITGPQVIK SVTGEDVTAD ELGGAEAHMA ISGNIHFVAE
DDDAAELIAK KLLSFLPQNN TEEASFVNPN NDVSPNTELR DIVPIDGKKG YDVRDVIAKI
VDWGDYLEVK AGYATNLVTA FARVNGRSVG IVANQPSVMS GCLDINASDK AAEFVNFCDS
FNIPLVQLVD VPGFLPGVQQ EYGGIIRHGA KMLYAYSEAT VPKITVVLRK AYGGSYLAMC
NRDLGADAVY AWPSAEIAVM GAEGAANVIF RKEIKAADDP DAMRAEKIEE YQNAFNTPYV
AAARGQVDDV IDPADTRRKI ASALEMYATK RQTRPAKKHG NFPC
