ACCA1_BURTA
ID ACCA1_BURTA Reviewed; 323 AA.
AC Q2SX76;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha 1 {ECO:0000255|HAMAP-Rule:MF_00823};
DE Short=ACCase subunit alpha 1 {ECO:0000255|HAMAP-Rule:MF_00823};
DE Short=Acetyl-CoA carboxylase carboxyltransferase subunit alpha 1 {ECO:0000255|HAMAP-Rule:MF_00823};
DE EC=2.1.3.15 {ECO:0000255|HAMAP-Rule:MF_00823};
GN Name=accA-1 {ECO:0000303|PubMed:16336651}; OrderedLocusNames=BTH_I1943;
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 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).
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: Does not confer resistance to the endogenous polyketide
CC antibiotic thailandamide, does not confer resistance to thailandamide
CC when expressed in S.typhimurium. {ECO:0000269|PubMed:29914944}.
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: Remains resistant to thailandamide.
CC {ECO:0000269|PubMed:29914944}.
CC -!- SIMILARITY: Belongs to the AccA family. {ECO:0000255|HAMAP-
CC Rule:MF_00823}.
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DR EMBL; CP000086; ABC36311.1; -; Genomic_DNA.
DR RefSeq; WP_009890295.1; NZ_CP008785.1.
DR AlphaFoldDB; Q2SX76; -.
DR SMR; Q2SX76; -.
DR PRIDE; Q2SX76; -.
DR EnsemblBacteria; ABC36311; ABC36311; BTH_I1943.
DR KEGG; bte:BTH_I1943; -.
DR HOGENOM; CLU_015486_0_2_4; -.
DR OMA; TPWQRVQ; -.
DR OrthoDB; 886663at2; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000001930; Chromosome I.
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 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 ATP-binding; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW Ligase; Lipid biosynthesis; Lipid metabolism; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..323
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit alpha 1"
FT /id="PRO_0000452508"
FT DOMAIN 39..293
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
SQ SEQUENCE 323 AA; 35677 MW; A3C80786D7D5D453 CRC64;
MKTTFLDFEQ PIAELEAKIE ELRFVQDDSV VDISEEIERL SKKSQQLTKD LYAHLTPWQV
SQIARHPQRP YTLDYVSELF TDFHELHGDR AFADDLSIVG GLARFNGHAC MVIGHQKGRD
TKERAARNFG MPRPEGYRKA ERLMRVAEKF GLPIFTFIDT PGAYPGVGAE ERGQSEAIGH
NLYVMAELKT PIIATVIGEG GSGGALAIAV ADTVMMLQFS TYSVISPEGC ASILWKSAAK
APEAAEALGL TAHRLKALGL IDKIVNEPLG GAHRDPKGTA ALLRRALGDS LRQFQGMSVD
ALRERRFERL MAYGKYKETT ARA
