ACCD5_MYCTO
ID ACCD5_MYCTO Reviewed; 548 AA.
AC P9WQH6; L0TF57; P96885;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Biotin-dependent acetyl-/propionyl-coenzyme A carboxylase beta5 subunit {ECO:0000250|UniProtKB:P9WQH7};
DE AltName: Full=Acetyl-CoA carboxylase {ECO:0000250|UniProtKB:P9WQH7};
DE Short=ACC {ECO:0000250|UniProtKB:P9WQH7};
DE EC=2.1.3.15 {ECO:0000250|UniProtKB:P9WQH7};
DE AltName: Full=Propionyl-CoA carboxylase {ECO:0000250|UniProtKB:P9WQH7};
DE Short=PCC {ECO:0000250|UniProtKB:P9WQH7};
DE EC=2.1.3.- {ECO:0000250|UniProtKB:P9WQH7};
GN Name=accD5; Synonyms=pccB; OrderedLocusNames=MT3379.1;
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:P9WQH7}.
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:P9WQH7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54729;
CC Evidence={ECO:0000250|UniProtKB:P9WQH7};
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:P9WQH7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66613;
CC Evidence={ECO:0000250|UniProtKB:P9WQH7};
CC -!- PATHWAY: Lipid metabolism; mycolic acid biosynthesis.
CC {ECO:0000250|UniProtKB:P9WQH7}.
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 AccD5, which contains the
CC carboxyl transferase (CT) domain. {ECO:0000250|UniProtKB:P9WQH7}.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000305}.
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DR EMBL; AE000516; AAK47722.1; -; Genomic_DNA.
DR PIR; A70980; A70980.
DR RefSeq; WP_003917758.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WQH6; -.
DR SMR; P9WQH6; -.
DR PRIDE; P9WQH6; -.
DR EnsemblBacteria; AAK47722; AAK47722; MT3379.1.
DR KEGG; mtc:MT3379.1; -.
DR PATRIC; fig|83331.31.peg.3637; -.
DR HOGENOM; CLU_018822_6_2_11; -.
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:0071704; P:organic substance metabolic process; IEA:UniProt.
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 Transferase.
FT CHAIN 1..548
FT /note="Biotin-dependent acetyl-/propionyl-coenzyme A
FT carboxylase beta5 subunit"
FT /id="PRO_0000426774"
FT DOMAIN 25..281
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 295..541
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 548 AA; 59296 MW; 8D0A51EE9AE09F52 CRC64;
MTSVTDRSAH SAERSTEHTI DIHTTAGKLA ELHKRREESL HPVGEDAVEK VHAKGKLTAR
ERIYALLDED SFVELDALAK HRSTNFNLGE KRPLGDGVVT GYGTIDGRDV CIFSQDATVF
GGSLGEVYGE KIVKVQELAI KTGRPLIGIN DGAGARIQEG VVSLGLYSRI FRNNILASGV
IPQISLIMGA AAGGHVYSPA LTDFVIMVDQ TSQMFITGPD VIKTVTGEEV TMEELGGAHT
HMAKSGTAHY AASGEQDAFD YVRELLSYLP PNNSTDAPRY QAAAPTGPIE ENLTDEDLEL
DTLIPDSPNQ PYDMHEVITR LLDDEFLEIQ AGYAQNIVVG FGRIGGRPVG IVANQPTHFA
GCLDINASEK AARFVRTCDC FNIPIVMLVD VPGFLPGTDQ EYNGIIRRGA KLLYAYGEAT
VPKITVITRK AYGGAYCVMG SKDMGCDVNL AWPTAQIAVM GASGAVGFVY RQQLAEAAAN
GEDIDKLRLR LQQEYEDTLV NPYVAAERGY VDAVIPPSHT RGYIGTALRL LERKIAQLPP
KKHGNVPL
