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ACCA_RHILW
ID   ACCA_RHILW              Reviewed;         317 AA.
AC   B5ZSI8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=Rleg2_3599;
OS   Rhizobium leguminosarum bv. trifolii (strain WSM2304).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395492;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM2304;
RX   PubMed=21304679; DOI=10.4056/sigs.44642;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA   Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA   Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA   Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv trifolii strain
RT   WSM2304, an effective microsymbiont of the South American clover Trifolium
RT   polymorphum.";
RL   Stand. Genomic Sci. 2:66-76(2010).
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   -!- 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; CP001191; ACI56866.1; -; Genomic_DNA.
DR   RefSeq; WP_003589922.1; NC_011369.1.
DR   AlphaFoldDB; B5ZSI8; -.
DR   SMR; B5ZSI8; -.
DR   STRING; 395492.Rleg2_3599; -.
DR   EnsemblBacteria; ACI56866; ACI56866; Rleg2_3599.
DR   KEGG; rlt:Rleg2_3599; -.
DR   eggNOG; COG0825; Bacteria.
DR   HOGENOM; CLU_015486_0_2_5; -.
DR   OMA; TPWQRVQ; -.
DR   OrthoDB; 886663at2; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000008330; 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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Nucleotide-binding; Transferase.
FT   CHAIN           1..317
FT                   /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT                   subunit alpha"
FT                   /id="PRO_1000134511"
FT   DOMAIN          40..293
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
SQ   SEQUENCE   317 AA;  34595 MW;  DD9956FF689A0217 CRC64;
     MHNYLDFEKP ISDLEGKIIE LKKLATEDES IDTTDEIGRL EVRVREAIVE IYSKLNPWQK
     TQVARHPQRP HFVDYAKTLF QEFTPLAGDR KFSEDAAIQA GLARFRGQPV AVVGQEKGND
     TKTRLKHNFG SPRPEGYRKA IRILEMADRF GLPVISLVDT AGAYPGVGAE ERGQAEAIAR
     STEMCLGVKV PLVSVVIGEG GSGGAIAIAT GNKVYMLEHS IYSVISPEGA ASILWRDSTR
     AREAATNMKI TAEDLKSLGV IDGIISEPLG GAHRDPDSVI AATGDVIANA LGEMASRSGE
     QLRNERRQKF LNMGRNL
 
 
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