ACCDA_FRAAA
ID ACCDA_FRAAA Reviewed; 609 AA.
AC Q0RKW5;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=FRAAL3196;
OS Frankia alni (strain ACN14a).
OC Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=326424;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACN14a;
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; CT573213; CAJ61840.1; -; Genomic_DNA.
DR RefSeq; WP_011604345.1; NC_008278.1.
DR AlphaFoldDB; Q0RKW5; -.
DR SMR; Q0RKW5; -.
DR STRING; 326424.FRAAL3196; -.
DR KEGG; fal:FRAAL3196; -.
DR eggNOG; COG0777; Bacteria.
DR eggNOG; COG0825; Bacteria.
DR HOGENOM; CLU_015486_2_0_11; -.
DR OMA; RVLMCAN; -.
DR OrthoDB; 504557at2; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000000657; 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: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; 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 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 Reference proteome; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..609
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunits beta/alpha"
FT /id="PRO_0000359114"
FT DOMAIN 39..308
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 314..559
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT ZN_FING 43..65
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 1..271
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit beta"
FT /evidence="ECO:0000250"
FT REGION 39..559
FT /note="Carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT REGION 272..582
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit alpha"
FT /evidence="ECO:0000250"
FT REGION 582..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 609 AA; 64294 MW; 2CF7B04E826734EA CRC64;
MTLEATAIEA TAIEATGIEA TGITATAIEP TPRRSPGSSW LLCGGCGTML YERRFAREGR
VCADCSWHAP MTIQQRLDLL LDADSARPVD VPAIDGDPLE FTDTRPYRDR LRDARASTGL
DEAAACVRGT IDGNPVVVVV MDFRFLGGSL GATVGEVFTR GAELALRERT PLLTVTASGG
ARMQEGAIAL MQMAKTSQAL GQLDEAGILT VSLITDPTFG GVAASFATLA DVIIAEPGAR
LGFAGRRVIE QTIRQTLPED FQTAEFLLTH GVVDLISPRR ELRANLARLL SVSSRRADGI
PRQAGRPDRA VVTDPEQLAR RDAWESVRAA RRLGRPTTLD YAAMILEDFT ELRGDRMSAD
CPALVAGLGR LDGVPVAVLG TQKGHTADEL RYRNFGMPTP AGYRKSARVM RLAAKLGLPV
ITLIDTAGAY PGVEAEEQAQ AVAIAENLRL MAGLPVPVVA VVTGEGGSGG ALALAFADRV
LMCANAVYSV ISAEGCAAIL WKNPAAAPTA AAALRVDARE LLRLGVVDGV IPEPDGGADA
DPAGTAARLR EALRGALADL LPLDQMNLVT RRRARFRQFG VATPAPATAP AASDDAHESQ
TDRSVEATR
