ACCD6_MYCTO
ID ACCD6_MYCTO Reviewed; 473 AA.
AC P9WQH4; L0TBQ7; P63407; Q10506;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=Biotin-dependent acetyl-/propionyl-coenzyme A carboxylase beta6 subunit {ECO:0000250|UniProtKB:P9WQH5};
DE AltName: Full=Acetyl-CoA carboxylase {ECO:0000250|UniProtKB:P9WQH5};
DE Short=ACC {ECO:0000250|UniProtKB:P9WQH5};
DE EC=2.1.3.15 {ECO:0000250|UniProtKB:P9WQH5};
DE AltName: Full=Propionyl-CoA carboxylase {ECO:0000250|UniProtKB:P9WQH5};
DE Short=PCC {ECO:0000250|UniProtKB:P9WQH5};
DE EC=2.1.3.- {ECO:0000250|UniProtKB:P9WQH5};
GN Name=accD6; OrderedLocusNames=MT2307;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Component of a biotin-dependent acyl-CoA carboxylase complex.
CC This subunit transfers the CO2 from carboxybiotin to the CoA ester
CC substrate. When associated with the alpha3 subunit AccA3, is involved
CC in the carboxylation of acetyl-CoA and propionyl-CoA.
CC {ECO:0000250|UniProtKB:P9WQH5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-
CC CoA + N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:54728,
CC Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145; EC=2.1.3.15;
CC Evidence={ECO:0000250|UniProtKB:P9WQH5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54729;
CC Evidence={ECO:0000250|UniProtKB:P9WQH5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-carboxybiotinyl-L-lysyl-[protein] + propanoyl-CoA =
CC methylmalonyl-CoA + N(6)-biotinyl-L-lysyl-[protein];
CC Xref=Rhea:RHEA:66612, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC ChEBI:CHEBI:57392, ChEBI:CHEBI:59916, ChEBI:CHEBI:83144,
CC ChEBI:CHEBI:83145; Evidence={ECO:0000250|UniProtKB:P9WQH5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66613;
CC Evidence={ECO:0000250|UniProtKB:P9WQH5};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:P9WQH5}.
CC -!- PATHWAY: Lipid metabolism; mycolic acid biosynthesis.
CC {ECO:0000250|UniProtKB:P9WQH5}.
CC -!- SUBUNIT: The biotin-dependent acyl-CoA carboxylase complex is composed
CC of AccA3, which contains the biotin carboxylase (BC) and biotin
CC carboxyl carrier protein (BCCP) domains, and AccD6, which contains the
CC carboxyl transferase (CT) domain. {ECO:0000250|UniProtKB:P9WQH5}.
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; AE000516; AAK46591.1; -; Genomic_DNA.
DR PIR; C70779; C70779.
DR RefSeq; WP_003900487.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WQH4; -.
DR SMR; P9WQH4; -.
DR PRIDE; P9WQH4; -.
DR EnsemblBacteria; AAK46591; AAK46591; MT2307.
DR GeneID; 45426227; -.
DR KEGG; mtc:MT2307; -.
DR PATRIC; fig|83331.31.peg.2484; -.
DR HOGENOM; CLU_018822_6_2_11; -.
DR UniPathway; UPA00094; -.
DR UniPathway; UPA00915; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
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 Pfam; PF01039; Carboxyl_trans; 1.
DR SUPFAM; SSF52096; SSF52096; 2.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Transferase.
FT CHAIN 1..473
FT /note="Biotin-dependent acetyl-/propionyl-coenzyme A
FT carboxylase beta6 subunit"
FT /id="PRO_0000426775"
FT DOMAIN 1..224
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 225..473
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
SQ SEQUENCE 473 AA; 50136 MW; 94AD7EBD88F233C3 CRC64;
MTIMAPEAVG ESLDPRDPLL RLSNFFDDGS VELLHERDRS GVLAAAGTVN GVRTIAFCTD
GTVMGGAMGV EGCTHIVNAY DTAIEDQSPI VGIWHSGGAR LAEGVRALHA VGQVFEAMIR
ASGYIPQISV VVGFAAGGAA YGPALTDVVV MAPESRVFVT GPDVVRSVTG EDVDMASLGG
PETHHKKSGV CHIVADDELD AYDRGRRLVG LFCQQGHFDR SKAEAGDTDI HALLPESSRR
AYDVRPIVTA ILDADTPFDE FQANWAPSMV VGLGRLSGRT VGVLANNPLR LGGCLNSESA
EKAARFVRLC DAFGIPLVVV VDVPGYLPGV DQEWGGVVRR GAKLLHAFGE CTVPRVTLVT
RKTYGGAYIA MNSRSLNATK VFAWPDAEVA VMGAKAAVGI LHKKKLAAAP EHEREALHDQ
LAAEHERIAG GVDSALDIGV VDEKIDPAHT RSKLTEALAQ APARRGRHKN IPL
