ACCA2_BURTA
ID ACCA2_BURTA Reviewed; 322 AA.
AC Q2T4M6;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha 2 {ECO:0000255|HAMAP-Rule:MF_00823};
DE Short=ACCase subunit alpha 2 {ECO:0000255|HAMAP-Rule:MF_00823};
DE Short=Acetyl-CoA carboxylase carboxyltransferase subunit alpha 2 {ECO:0000255|HAMAP-Rule:MF_00823};
DE EC=2.1.3.15 {ECO:0000255|HAMAP-Rule:MF_00823};
GN Name=accA-2 {ECO:0000303|PubMed:29914944};
GN Synonyms=thaC {ECO:0000303|PubMed:20853892}; OrderedLocusNames=BTH_II1679;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
RN [2]
RP NOMENCLATURE.
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=20853892; DOI=10.1021/ja105003g;
RA Ishida K., Lincke T., Behnken S., Hertweck C.;
RT "Induced biosynthesis of cryptic polyketide metabolites in a Burkholderia
RT thailandensis quorum sensing mutant.";
RL J. Am. Chem. Soc. 132:13966-13968(2010).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=29914944; DOI=10.1128/aac.00463-18;
RA Wozniak C.E., Lin Z., Schmidt E.W., Hughes K.T., Liou T.G.;
RT "Thailandamide, a Fatty Acid Synthesis Antibiotic That Is Coexpressed with
RT a Resistant Target Gene.";
RL Antimicrob. Agents Chemother. 62:0-0(2018).
RN [4]
RP FUNCTION.
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=29975047; DOI=10.1021/acs.biochem.8b00678;
RA Wu Y., Seyedsayamdost M.R.;
RT "The Polyene Natural Product Thailandamide A Inhibits Fatty Acid
RT Biosynthesis in Gram-Positive and Gram-Negative Bacteria.";
RL Biochemistry 57:4247-4251(2018).
CC -!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex.
CC First, biotin carboxylase catalyzes the carboxylation of biotin on its
CC carrier protein (BCCP) and then the CO(2) group is transferred by the
CC carboxyltransferase to acetyl-CoA to form malonyl-CoA.
CC {ECO:0000255|HAMAP-Rule:MF_00823}.
CC -!- FUNCTION: Confers resistance to the endogenous polyketide antibiotic
CC thailandamide. Can replace the endogenous gene in S.typhimurium,
CC conferring slow growth and resistance to thailandamide
CC (PubMed:29914944). Can also replace the endogenous gene in E.coli,
CC conferring resistance to thailandamide (PubMed:29975047).
CC {ECO:0000269|PubMed:29914944, ECO:0000269|PubMed:29975047}.
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:0000255|HAMAP-Rule:MF_00823};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00823}.
CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of biotin
CC carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two
CC subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta
CC (AccD). {ECO:0000255|HAMAP-Rule:MF_00823}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00823}.
CC -!- DISRUPTION PHENOTYPE: Becomes sensitive to thailandamide antibiotic.
CC {ECO:0000269|PubMed:29914944}.
CC -!- MISCELLANEOUS: Thailandamide is a polyketide that is toxic to human
CC cell lines but also has antibacterial activity on E.coli, S.typhimurium
CC and S.aureus. It probably acts on acetyl-CoA carboxylase in the fatty
CC acid synthesis pathway, which is rarely found to be an antibiotic
CC target. These data suggest it might be a good starting point for
CC engineering of novel antibiotics. {ECO:0000305|PubMed:29914944,
CC ECO:0000305|PubMed:29975047}.
CC -!- SIMILARITY: Belongs to the AccA family. {ECO:0000255|HAMAP-
CC Rule:MF_00823}.
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DR EMBL; CP000085; ABC35022.1; -; Genomic_DNA.
DR RefSeq; WP_011401357.1; NZ_CP008786.1.
DR AlphaFoldDB; Q2T4M6; -.
DR SMR; Q2T4M6; -.
DR PRIDE; Q2T4M6; -.
DR EnsemblBacteria; ABC35022; ABC35022; BTH_II1679.
DR GeneID; 66550328; -.
DR KEGG; bte:BTH_II1679; -.
DR HOGENOM; CLU_015486_0_2_4; -.
DR OMA; LWKDAKY; -.
DR OrthoDB; 886663at2; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000001930; Chromosome II.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR HAMAP; MF_00823; AcetylCoA_CT_alpha; 1.
DR InterPro; IPR001095; Acetyl_CoA_COase_a_su.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR PANTHER; PTHR42853; PTHR42853; 1.
DR Pfam; PF03255; ACCA; 1.
DR PRINTS; PR01069; ACCCTRFRASEA.
DR SUPFAM; SSF52096; SSF52096; 1.
DR TIGRFAMs; TIGR00513; accA; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; ATP-binding; Cytoplasm; Fatty acid biosynthesis;
KW Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..322
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit alpha 2"
FT /id="PRO_0000452509"
FT DOMAIN 37..294
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
SQ SEQUENCE 322 AA; 36187 MW; ED214B60533A7358 CRC64;
MTNVTYLDFE KAIGELDAKI DALRCSEDES AIDLSEEINR LSARSEKLTK ELYERLTPWQ
IVQVARHPAR PYTLDYVNFI FTDFHELHGD RSYADDQSIV GGLARFNDRP CVVVGHQKGR
NTKERAMRNF GYPRPEGYRK ALRLFKLAEK FRLPIFTFID TPGAWPGIDA EEHNQSEAIG
RNLMEMASLQ TPIITTVIGE GGSGGALAIG VGDVSIMLQF STYSVISPES CSSILWKNPN
YAEQAANALG LTAHRLKALG LIDKIANEPV GGAHRDPQQM ALMLKRVLQE SLRNVESLDA
KQLLVRRHER LMHYGKFRET AV
