ACCA_PSEAE
ID ACCA_PSEAE Reviewed; 316 AA.
AC Q9HXZ2;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=PA3639;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP CHARACTERIZATION OF ACTIVITY REGULATION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
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).
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 antibiotic
CC moiramide B (CPD1); in vivo the effects are not seen unless the efflux
CC MexAB-OprM system is inactive.
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}.
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DR EMBL; AE004091; AAG07027.1; -; Genomic_DNA.
DR PIR; D83192; D83192.
DR RefSeq; NP_252329.1; NC_002516.2.
DR RefSeq; WP_003109333.1; NZ_QZGE01000001.1.
DR AlphaFoldDB; Q9HXZ2; -.
DR SMR; Q9HXZ2; -.
DR STRING; 287.DR97_4300; -.
DR PaxDb; Q9HXZ2; -.
DR PRIDE; Q9HXZ2; -.
DR DNASU; 880489; -.
DR EnsemblBacteria; AAG07027; AAG07027; PA3639.
DR GeneID; 880489; -.
DR KEGG; pae:PA3639; -.
DR PATRIC; fig|208964.12.peg.3808; -.
DR PseudoCAP; PA3639; -.
DR HOGENOM; CLU_015486_0_2_6; -.
DR InParanoid; Q9HXZ2; -.
DR OMA; TPWQRVQ; -.
DR PhylomeDB; Q9HXZ2; -.
DR BioCyc; PAER208964:G1FZ6-3709-MON; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000002438; 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 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 ATP-binding; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..316
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit alpha"
FT /id="PRO_0000223806"
FT DOMAIN 39..293
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
SQ SEQUENCE 316 AA; 34947 MW; 914D9418A79FB484 CRC64;
MNPNFLDFEQ PIADLQAKIE ELRLVGNDNA LNISDEISRL QDKSKALTEN IFGNLSSWQI
AQLARHPKRP YTLDYIGYLF SDFEELHGDR HFADDPAIVG GVARLDGSPV MVIGHQKGRE
VREKVRRNFG MPRPEGYRKA CRLMEMAERF KMPILTFIDT PGAYPGIDAE ERGQSEAIAW
NLRVMARLKT PIIATVIGEG GSGGALAIGV CDQLNMLQYS TYSVISPEGC ASILWKTAEK
APEAAEAMGI TAERLKGLGI VDKVIDEPLG GAHRDPASMA ESIRGELLAQ LKMLQGLEMG
ELLERRYDRL MSYGAP
