ID   ACCD2_MYCTU             Reviewed;         529 AA.
AC   O86318; I6Y5A8; L0T826;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Probable biotin-dependent acyl-coenzyme A carboxylase beta2 subunit {ECO:0000305};
DE            EC=2.1.3.- {ECO:0000250|UniProtKB:I6YDK7};
GN   Name=accD2; OrderedLocusNames=Rv0974c {ECO:0000312|EMBL:CCP43723.1};
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   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   [3]
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:I6YDK7}.
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:I6YDK7}.
CC   -!- INDUCTION: Does not show significant changes in expression throughout
CC       M.tuberculosis growth phases. {ECO:0000269|PubMed:17114269}.
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; AL123456; CCP43723.1; -; Genomic_DNA.
DR   RefSeq; NP_215489.1; NC_000962.3.
DR   RefSeq; WP_010886097.1; NZ_NVQJ01000001.1.
DR   AlphaFoldDB; O86318; -.
DR   SMR; O86318; -.
DR   STRING; 83332.Rv0974c; -.
DR   PaxDb; O86318; -.
DR   PRIDE; O86318; -.
DR   DNASU; 886064; -.
DR   GeneID; 886064; -.
DR   KEGG; mtu:Rv0974c; -.
DR   PATRIC; fig|83332.111.peg.1081; -.
DR   TubercuList; Rv0974c; -.
DR   eggNOG; COG4799; Bacteria.
DR   OMA; QGGIIKH; -.
DR   PhylomeDB; O86318; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:1905202; C:methylcrotonoyl-CoA carboxylase complex; IBA:GO_Central.
DR   GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006552; P:leucine catabolic process; IBA:GO_Central.
DR   GO; GO:0071768; P:mycolic acid biosynthetic process; IMP:MTBBASE.
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   InterPro; IPR045190; MCCB/AccD1-like.
DR   PANTHER; PTHR22855; PTHR22855; 1.
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   1: Evidence at protein level;
KW   Reference proteome; Transferase.
FT   CHAIN           1..529
FT                   /note="Probable biotin-dependent acyl-coenzyme A
FT                   carboxylase beta2 subunit"
FT                   /id="PRO_0000452369"
FT   DOMAIN          20..271
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT   DOMAIN          270..520
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
SQ   SEQUENCE   529 AA;  56256 MW;  0556A3ED4AB08F4F CRC64;
     MLQSTLDPNA SAYDEAAATM SGKLDEINAE LAKALAGGGP KYVDRHHARG NLTPRERIEL
     LVDPDSPFLE LSPLAAYGSN FQIGASLVTG IGAVCGVECM IVANDPTVKG GTSNPWTLRK
     ILRANQIAFE NRLPVISLVE SGGADLPTQK EIFIPGGQMF RDLTRLSAAG IPTIALVFGN
     STAGGAYVPG MSDHVVMIKE RSKVFLAGPP LVKMATGEES DDESLGGAEM HARISGLADY
     FALDELDAIR IGRRIVARLN WIKQGPAPAP VTEPLFDAEE LIGIVPPDLR IPFDPREVIA
     RIVDGSEFDE FKPLYGSSLV TGWARLHGYP LGILANARGV LFSEESQKAT QFIQLANRAD
     TPLLFLHNTT GYMVGKDYEE GGMIKHGSMM INAVSNSTVP HISLLIGASY GAGHYGMCGR
     AYDPRFLFAW PSAKSAVMGG AQLSGVLSIV ARAAAEARGQ QVDEAADAAM RAAVEGQIEA
     ESLPLVLSGM LYDDGVIDPR DTRTVLGMCL SAIANGPIKG TSNFGVFRM