ACCD5_MYCLE
ID ACCD5_MYCLE Reviewed; 549 AA.
AC P53002;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=ML0731; ORFNames=B1308_C1_125;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7489918; DOI=10.1016/0378-1119(95)00427-8;
RA Doukhan L., Predich M., Nair G., Dussurget O., Mandic-Mulec I., Cole S.T.,
RA Smith D.R., Smith I.;
RT "Genomic organization of the mycobacterial sigma gene cluster.";
RL Gene 165:67-70(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; U00012; AAA85917.1; -; Genomic_DNA.
DR EMBL; AL583919; CAC30240.1; -; Genomic_DNA.
DR PIR; D87000; D87000.
DR RefSeq; NP_301571.1; NC_002677.1.
DR RefSeq; WP_010907895.1; NC_002677.1.
DR AlphaFoldDB; P53002; -.
DR SMR; P53002; -.
DR STRING; 272631.ML0731; -.
DR EnsemblBacteria; CAC30240; CAC30240; CAC30240.
DR KEGG; mle:ML0731; -.
DR PATRIC; fig|272631.5.peg.1328; -.
DR Leproma; ML0731; -.
DR eggNOG; COG4799; Bacteria.
DR HOGENOM; CLU_018822_6_2_11; -.
DR OMA; YAYAECT; -.
DR UniPathway; UPA00915; -.
DR Proteomes; UP000000806; 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 Reference proteome; Transferase.
FT CHAIN 1..549
FT /note="Biotin-dependent acetyl-/propionyl-coenzyme A
FT carboxylase beta5 subunit"
FT /id="PRO_0000199798"
FT DOMAIN 25..281
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 295..542
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
SQ SEQUENCE 549 AA; 59396 MW; 949FAA54101E76CB CRC64;
MTSVTDHSAH SMERAAEHTI NIHTTAGKLA ELHKRTEEAL HPVGAAAFEK VHAKGKFTAR
ERIYALLDDD SFVELDALAR HRSTNFGLGE NRPVGDGVVT GYGTIDGRDV CIFSQDVTVF
GGSLGEVYGE KIVKVQELAI KTGRPLIGIN DGAGARIQEG VVSLGLYSRI FRNNILASGV
IPQISLIMGA AAGGHVYSPA LTDFVVMVDQ TSQMFITGPD VIKTVTGEDV TMEELGGAHT
HMAKSGTAHY VASGEQDAFD WVRDVLSYLP SNNFTDAPRY SKPVPHGSIE DNLTAKDLEL
DTLIPDSPNQ PYDMHEVVTR LLDEEEFLEV QAGYATNIVV GLGRIDDRPV GIVANQPIQF
AGCLDINASE KAARFVRVCD CFNIPIVMLV DVPGFLPGTE QEYDGIIRRG AKLLFAYGEA
TVPKITVITR KAYGGAYCVM GSKNMGCDVN LAWPTAQIAV MGASGAVGFV YRKELAQAAK
NGANVDELRL QLQQEYEDTL VNPYIAAERG YVDAVIPPSH TRGYIATALH LLERKIAHLP
PKKHGNIPL
