ACCA_BACSU
ID ACCA_BACSU Reviewed; 325 AA.
AC O34847;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00823};
DE Short=ACCase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00823};
DE Short=Acetyl-CoA carboxylase carboxyltransferase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00823};
DE EC=2.1.3.15 {ECO:0000255|HAMAP-Rule:MF_00823};
GN Name=accA {ECO:0000255|HAMAP-Rule:MF_00823}; OrderedLocusNames=BSU29200;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP ACTIVITY REGULATION, ANTIBIOTIC RESISTANCE, AND MUTAGENESIS OF GLY-199.
RX PubMed=15066985; DOI=10.1074/jbc.m402989200;
RA Freiberg C., Brunner N.A., Schiffer G., Lampe T., Pohlmann J., Brands M.,
RA Raabe M., Haebich D., Ziegelbauer K.;
RT "Identification and characterization of the first class of potent bacterial
RT acetyl-CoA carboxylase inhibitors with antibacterial activity.";
RL J. Biol. Chem. 279:26066-26073(2004).
RN [4]
RP ANTIBIOTIC RESISTANCE, AND MUTAGENESIS OF GLU-227.
RC STRAIN=3610;
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 -!- 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 -!- ACTIVITY REGULATION: Inhibited by pyrrolidine dione antibiotics
CC moiramide B (CPD1) and CPD2. {ECO:0000269|PubMed:15066985}.
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 -!- SIMILARITY: Belongs to the AccA family. {ECO:0000255|HAMAP-
CC Rule:MF_00823}.
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; AF008220; AAC00341.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14880.1; -; Genomic_DNA.
DR PIR; G69580; G69580.
DR RefSeq; NP_390798.1; NC_000964.3.
DR RefSeq; WP_003229417.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O34847; -.
DR SMR; O34847; -.
DR STRING; 224308.BSU29200; -.
DR PaxDb; O34847; -.
DR PRIDE; O34847; -.
DR DNASU; 936367; -.
DR EnsemblBacteria; CAB14880; CAB14880; BSU_29200.
DR GeneID; 936367; -.
DR KEGG; bsu:BSU29200; -.
DR PATRIC; fig|224308.179.peg.3171; -.
DR eggNOG; COG0825; Bacteria.
DR InParanoid; O34847; -.
DR OMA; TPWQRVQ; -.
DR PhylomeDB; O34847; -.
DR BioCyc; BSUB:BSU29200-MON; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000001570; Chromosome.
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 1: Evidence at protein level;
KW Antibiotic resistance; ATP-binding; Cytoplasm; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..325
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit alpha"
FT /id="PRO_0000146773"
FT DOMAIN 38..292
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT MUTAGEN 199
FT /note="G->S: Resistant to the pyrrolidine dione antibiotic
FT CPD2."
FT /evidence="ECO:0000269|PubMed:15066985"
FT MUTAGEN 227
FT /note="E->K: Resistance to polyketide antibiotic
FT thailandamide."
FT /evidence="ECO:0000269|PubMed:29975047"
SQ SEQUENCE 325 AA; 36334 MW; 9B177DEE4A5B5864 CRC64;
MAPRLEFEKP VIELQTKIAE LKKFTQDSDM DLSAEIERLE DRLAKLQDDI YKNLKPWDRV
QIARLADRPT TLDYIEHLFT DFFECHGDRA YGDDEAIVGG IAKFHGLPVT VIGHQRGKDT
KENLVRNFGM PHPEGYRKAL RLMKQADKFN RPIICFIDTK GAYPGRAAEE RGQSEAIAKN
LFEMAGLRVP VICIVIGEGG SGGALGLGVG NHLHMLENST YSVISPEGAA ALLWKDSSLA
KKAAETMKIT APDLKELGII DHMIKEVKGG AHHDVKLQAS YMDETLKQSL KTLLKLSEEE
LVQQRYEKYK AIGKVSVEDQ YIGVN
