(data stored in ACNUC1104 zone)

SWISSPROT: 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   11-DEC-2019, entry version 86.
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}.
DR   EMBL; AM420293; CAL99379.1; -; Genomic_DNA.
DR   RefSeq; WP_009945664.1; NZ_PDBV01000001.1.
DR   SMR; A4F5Q5; -.
DR   STRING; 405948.SACE_0026; -.
DR   PRIDE; A4F5Q5; -.
DR   EnsemblBacteria; CAL99379; CAL99379; SACE_0026.
DR   KEGG; sen:SACE_0026; -.
DR   eggNOG; ENOG4105D8K; Bacteria.
DR   eggNOG; COG0777; LUCA.
DR   eggNOG; COG0825; LUCA.
DR   HOGENOM; HOG000244564; -.
DR   KO; K01962; -.
DR   KO; K01963; -.
DR   OMA; RVLMCAN; -.
DR   OrthoDB; 504557at2; -.
DR   BioCyc; SERY405948:SACE_RS00125-MONOMER; -.
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;
DR   PRODOM; A4F5Q5.
DR   SWISS-2DPAGE; A4F5Q5.
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   METAL           25
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250"
FT   METAL           28
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250"
FT   METAL           44
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250"
FT   METAL           47
FT                   /note="Zinc"
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
//

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