ID   ACCD3_MYCTU             Reviewed;         495 AA.
AC   P9WQH9; 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 37.
DE   RecName: Full=Probable biotin-dependent acyl-coenzyme A carboxylase beta3 subunit {ECO:0000305};
DE            EC=2.1.3.- {ECO:0000250|UniProtKB:O53578};
GN   Name=accD3; OrderedLocusNames=Rv0904c; ORFNames=MTCY31.32c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=12657046; DOI=10.1046/j.1365-2958.2003.03425.x;
RA   Sassetti C.M., Boyd D.H., Rubin E.J.;
RT   "Genes required for mycobacterial growth defined by high density
RT   mutagenesis.";
RL   Mol. Microbiol. 48:77-84(2003).
RN   [3]
RP   INDUCTION.
RC   STRAIN=H37Rv;
RX   PubMed=17114269; DOI=10.1128/jb.01019-06;
RA   Daniel J., Oh T.J., Lee C.M., Kolattukudy P.E.;
RT   "AccD6, a member of the Fas II locus, is a functional carboxyltransferase
RT   subunit of the acyl-coenzyme A carboxylase in Mycobacterium tuberculosis.";
RL   J. Bacteriol. 189:911-917(2007).
RN   [4]
RP   IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX   PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA   Raman K., Yeturu K., Chandra N.;
RT   "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT   through an interactome, reactome and genome-scale structural analysis.";
RL   BMC Syst. Biol. 2:109-109(2008).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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   -!- INDUCTION: Does not show significant changes in expression throughout
CC       M.tuberculosis growth phases. {ECO:0000269|PubMed:17114269}.
CC   -!- DISRUPTION PHENOTYPE: Not essential for growth.
CC       {ECO:0000269|PubMed:12657046}.
CC   -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC       {ECO:0000269|PubMed:19099550}.
CC   -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000305}.
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DR   EMBL; AL123456; CCP43652.1; -; Genomic_DNA.
DR   PIR; E70783; E70783.
DR   RefSeq; NP_215419.1; NC_000962.3.
DR   RefSeq; WP_003404691.1; NZ_NVQJ01000001.1.
DR   AlphaFoldDB; P9WQH9; -.
DR   SMR; P9WQH9; -.
DR   STRING; 83332.Rv0904c; -.
DR   PaxDb; P9WQH9; -.
DR   DNASU; 885279; -.
DR   GeneID; 45424867; -.
DR   GeneID; 885279; -.
DR   KEGG; mtu:Rv0904c; -.
DR   TubercuList; Rv0904c; -.
DR   eggNOG; COG0777; Bacteria.
DR   eggNOG; COG0825; Bacteria.
DR   OMA; RNPTMGG; -.
DR   PhylomeDB; P9WQH9; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071768; P:mycolic acid biosynthetic process; IMP:MTBBASE.
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   Reference proteome; Transferase.
FT   CHAIN           1..495
FT                   /note="Probable biotin-dependent acyl-coenzyme A
FT                   carboxylase beta3 subunit"
FT                   /id="PRO_0000199773"
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