ID   ACCD3_MYCTO             Reviewed;         495 AA.
AC   P9WQH8; L0T824; P63405; Q10561;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Probable biotin-dependent acyl-coenzyme A carboxylase beta3 subunit {ECO:0000250|UniProtKB:P9WQH9};
DE            EC=2.1.3.- {ECO:0000250|UniProtKB:O53578};
GN   Name=accD3; OrderedLocusNames=MT0927;
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. {ECO:0000250|UniProtKB:O53578}.
CC   -!- SUBUNIT: The biotin-dependent acyl-CoA carboxylase complex is composed
CC       of an AccA protein, which contains the biotin carboxylase (BC) and
CC       biotin carboxyl carrier protein (BCCP) domains, and an AccD protein,
CC       which contains the carboxyl transferase (CT) domain.
CC       {ECO:0000250|UniProtKB:O53578}.
CC   -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK45174.1; -; Genomic_DNA.
DR   PIR; E70783; E70783.
DR   RefSeq; WP_003404691.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WQH8; -.
DR   SMR; P9WQH8; -.
DR   EnsemblBacteria; AAK45174; AAK45174; MT0927.
DR   GeneID; 45424867; -.
DR   KEGG; mtc:MT0927; -.
DR   PATRIC; fig|83331.31.peg.996; -.
DR   HOGENOM; CLU_015486_2_1_11; -.
DR   Proteomes; UP000001020; Chromosome.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Transferase.
FT   CHAIN           1..495
FT                   /note="Probable biotin-dependent acyl-coenzyme A
FT                   carboxylase beta3 subunit"
FT                   /id="PRO_0000426773"
FT   DOMAIN          1..236
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT   DOMAIN          242..470
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
SQ   SEQUENCE   495 AA;  51772 MW;  156C96E927FF950C CRC64;
     MSRITTDQLR HAVLDRGSFV SWDSEPLAVP VADSYARELA AARAATGADE SVQTGEGRVF
     GRRVAVVACE FDFLGGSIGV AAAERITAAV ERATAERLPL LASPSSGGTR MQEGTVAFLQ
     MVKIAAAIQL HNQARLPYLV YLRHPTTGGV FASWGSLGHL TVAEPGALIG FLGPRVYELL
     YGDPFPSGVQ TAENLRRHGI IDGVVALDRL RPMLDRALTV LIDAPEPLPA PQTPAPVPDV
     PTWDSVVASR RPDRPGVRQL LRHGATDRVL LSGTDQGEAA TTLLALARFG GQPTVVLGQQ
     RAVGGGGSTV GPAALREARR GMALAAELCL PLVLVIDAAG PALSAAAEQG GLAGQIAHCL
     AELVTLDTPT VSILLGQGSG GPALAMLPAD RVLAALHGWL APLPPEGASA IVFRDTAHAA
     ELAAAQGIRS ADLLKSGIVD TIVPEYPDAA DEPIEFALRL SNAIAAEVHA LRKIPAPERL
     ATRLQRYRRI GLPRD