ACCDA_FRASN
ID ACCDA_FRASN Reviewed; 614 AA.
AC A8L4H3;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunits beta/alpha;
DE Short=ACCase subunits beta/alpha;
DE Short=Acetyl-CoA carboxylase carboxyltransferase subunits beta/alpha;
DE EC=2.1.3.15;
GN Name=accD; Synonyms=accA, accDA; OrderedLocusNames=Franean1_3951;
OS Frankia sp. (strain EAN1pec).
OC Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia;
OC unclassified Frankia.
OX NCBI_TaxID=298653;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EAN1pec;
RX PubMed=17151343; DOI=10.1101/gr.5798407;
RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA Benson D.R.;
RT "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT reflect host range and host plant biogeography.";
RL Genome Res. 17:7-15(2007).
CC -!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex.
CC Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its
CC carrier protein (BCCP) and then the CO(2) group is transferred by the
CC transcarboxylase to acetyl-CoA to form malonyl-CoA (By similarity).
CC {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1.
CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterotetramer composed of biotin
CC carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two
CC subunits of ACCase subunit beta/alpha. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AccD/PCCB family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the AccA family.
CC {ECO:0000305}.
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DR EMBL; CP000820; ABW13341.1; -; Genomic_DNA.
DR RefSeq; WP_020461476.1; NC_009921.1.
DR AlphaFoldDB; A8L4H3; -.
DR SMR; A8L4H3; -.
DR STRING; 298653.Franean1_3951; -.
DR PRIDE; A8L4H3; -.
DR EnsemblBacteria; ABW13341; ABW13341; Franean1_3951.
DR KEGG; fre:Franean1_3951; -.
DR eggNOG; COG0777; Bacteria.
DR eggNOG; COG0825; Bacteria.
DR HOGENOM; CLU_015486_3_2_11; -.
DR OMA; RVLMCAN; -.
DR OrthoDB; 504557at2; -.
DR UniPathway; UPA00655; UER00711.
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:0008270; F:zinc ion binding; 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 HAMAP; MF_01395; AcetylCoA_CT_beta; 1.
DR InterPro; IPR034733; AcCoA_carboxyl.
DR InterPro; IPR001095; Acetyl_CoA_COase_a_su.
DR InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR PANTHER; PTHR42853; PTHR42853; 1.
DR Pfam; PF03255; ACCA; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR PRINTS; PR01070; ACCCTRFRASEB.
DR SUPFAM; SSF52096; SSF52096; 2.
DR TIGRFAMs; TIGR00513; accA; 1.
DR TIGRFAMs; TIGR00515; accD; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Metal-binding; Nucleotide-binding;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..614
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunits beta/alpha"
FT /id="PRO_0000389901"
FT DOMAIN 18..287
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 311..556
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT ZN_FING 22..44
FT /note="C4-type"
FT /evidence="ECO:0000250"
FT REGION 1..250
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit beta"
FT /evidence="ECO:0000250"
FT REGION 18..556
FT /note="Carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT REGION 251..614
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit alpha"
FT /evidence="ECO:0000250"
FT REGION 272..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 614 AA; 63112 MW; 3670D4F11A7E042A CRC64;
MTASATRQRP EADLGTAEWL VCDGCRRMIY GRRFARGGHV CPECGWHARL TATQRIALLL
DEGSVEVVDT PVTAADPLQF VDTRPYADRL RSARTSTGLT EAVVVARGRI EGCPVVTAVM
DFRFLGGSLG AAVGEAITGA CEIALRERTP LLLVTASGGA RMQEGALSLM QMAKTAQAIG
QLDEAGILTV SLITDPTFGG VAASFATLTD VIVAEPGARL GFAGARVIEQ TIRQTLPPGF
QTAEFLLEHG VVDLISPRGQ LRPTLARLLG VATRRPGTAP VTPGDGHSAG DGRGAGDSRG
ASHGGDGVVR DPARLADRHP WEAVRLARRL GRPSTLDYIG ALVEDWTELH GDRAATDCPA
MVAGLGRLDG TPVVVIGTQK GHTATELAAR SYGMPSPGGY RKAARVMRLA AKLGLPVITL
IDTAGAHPGL EAEQNGQAVA IAENLRLMAG LPVPVVAVVT GEGGSGGALA LAVANRVLMC
ANAIYSVISP EGCAAILWKD PAAGPDAAAA LRVDARALLA AGIVDGVVPE PDGGADVDPL
AATDALRAAL TGALAELAPL DPPTLVTARR ARFRRFGTPA PAGGAAPAPV VPAARPPLGA
GRTHADLDDA RRAS
