ACCDA_SACEN
ID ACCDA_SACEN Reviewed; 568 AA.
AC A4F5Q5;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=SACE_0026;
OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Saccharopolyspora.
OX NCBI_TaxID=405948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC 2338;
RX PubMed=17369815; DOI=10.1038/nbt1297;
RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA Haydock S.F., Leadlay P.F.;
RT "Complete genome sequence of the erythromycin-producing bacterium
RT Saccharopolyspora erythraea NRRL23338.";
RL Nat. Biotechnol. 25:447-453(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; AM420293; CAL99379.1; -; Genomic_DNA.
DR RefSeq; WP_009945664.1; NZ_PDBV01000001.1.
DR AlphaFoldDB; A4F5Q5; -.
DR SMR; A4F5Q5; -.
DR STRING; 405948.SACE_0026; -.
DR EnsemblBacteria; CAL99379; CAL99379; SACE_0026.
DR KEGG; sen:SACE_0026; -.
DR eggNOG; COG0777; Bacteria.
DR eggNOG; COG0825; Bacteria.
DR HOGENOM; CLU_015486_2_1_11; -.
DR OMA; RVLMCAN; -.
DR OrthoDB; 504557at2; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000006728; 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; 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 InterPro; IPR041010; Znf-ACC.
DR PANTHER; PTHR42853; PTHR42853; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR Pfam; PF17848; zf-ACC; 1.
DR PRINTS; PR01069; ACCCTRFRASEA.
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..568
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunits beta/alpha"
FT /id="PRO_0000359116"
FT DOMAIN 21..290
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 286..536
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT ZN_FING 25..47
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 1..253
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit beta"
FT /evidence="ECO:0000250"
FT REGION 21..536
FT /note="Carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT REGION 254..559
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit alpha"
FT /evidence="ECO:0000250"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 28
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"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 568 AA; 60536 MW; 9DA032BBC18AB6F7 CRC64;
MAEPARTLAQ DPRLADADQV RWTRCPNCRS LVYLRRLRRN GHVCPDCAHH MRMGVHDRIE
SLLDAGSFER FGADVAPVDV LGFTDSRPYT ERLAQAQRRS GSNEAVLCGT GTIDGAPLVV
AALDFGFLGG SVGGVTGELV ARAARTALDR RTPLVLVCAS GGARMQEGTI SLMQMAKTSQ
EVARLHEAGV LVVSIGTDPT YGGVTASFGM LGDVVVAEPG ARIGFAGPQV IRQTIRQELP
AGFQTAEYLR DAGMVDLVVP RHELRAHLAR LLRVHSGGTA APAAERGYRT RPRPAADRDA
SEVLHAARDI GRPSTSDYCA RIFEDFVELH GDRVSGDDPA VVAGIGTLGG RPVVVVGHQK
GHETAELVQR NFGMPQPAGY HKARRMMDYA ERFGFPLVTF VDTPGAHPGV DAEQRGQGTA
IAECISRMAR LKVPAVSVVT GEGGSGGALA LGVGNRVLVL ENAYYSVISP EGCSTILWGT
AERTSQAAEQ LRITAEDLLR LGVVDGVVDE PAGGAQQDHA AMASRLAAAL RASIGELSEL
DGDALLDQRR RRFDRFGDPD HSDSEVQP
