ID   ACCD_CLOBJ              Reviewed;         289 AA.
AC   C1FNJ8;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   01-MAY-2013, entry version 26.
DE   RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta;
DE            Short=ACCase subunit beta;
DE            Short=Acetyl-CoA carboxylase carboxyltransferase subunit beta;
DE            EC=6.4.1.2;
GN   Name=accD; OrderedLocusNames=CLM_4087;
OS   Clostridium botulinum (strain Kyoto / Type A2).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=536232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kyoto / Type A2;
RA   Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C.,
RA   Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G.,
RA   Brettin T.S.;
RT   "Genome sequence of Clostridium botulinum A2 Kyoto.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC)
CC       complex. Biotin carboxylase (BC) catalyzes the carboxylation of
CC       biotin on its carrier protein (BCCP) and then the CO(2) group is
CC       transferred by the transcarboxylase to acetyl-CoA to form malonyl-
CC       CoA (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate
CC       + malonyl-CoA.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
CC       from acetyl-CoA: step 1/1.
CC   -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of
CC       biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC)
CC       and two subunits each of ACCase subunit alpha (AccA) and ACCase
CC       subunit beta (AccD) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the AccD/PCCB family.
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DR   EMBL; CP001581; ACO86209.1; -; Genomic_DNA.
DR   RefSeq; YP_002806139.1; NC_012563.1.
DR   ProteinModelPortal; C1FNJ8; -.
DR   SMR; C1FNJ8; 31-287.
DR   STRING; 536232.CLM_4087; -.
DR   EnsemblBacteria; ACO86209; ACO86209; CLM_4087.
DR   GeneID; 7765864; -.
DR   KEGG; cby:CLM_4087; -.
DR   PATRIC; 19384555; VBICloBot91161_3851.
DR   eggNOG; COG0777; -.
DR   HOGENOM; HOG000021671; -.
DR   KO; K01963; -.
DR   OMA; GLWIKCP; -.
DR   ProtClustDB; CLSK883536; -.
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:HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:HAMAP.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:HAMAP.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_01395; AcetylCoA_CT_beta; 1; -.
DR   InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
DR   InterPro; IPR000022; Carboxyl_trans.
DR   InterPro; IPR011762; COA_CT_N.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   PRINTS; PR01070; ACCCTRFRASEB.
DR   TIGRFAMs; TIGR00515; accD; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
KW   Metal-binding; Nucleotide-binding; Zinc; Zinc-finger.
FT   CHAIN         1    289       Acetyl-coenzyme A carboxylase carboxyl
FT                                transferase subunit beta.
FT                                /FTId=PRO_0000389724.
FT   ZN_FING      38     60       C4-type (By similarity).
FT   METAL        38     38       Zinc (By similarity).
FT   METAL        41     41       Zinc (By similarity).
FT   METAL        57     57       Zinc (By similarity).
FT   METAL        60     60       Zinc (By similarity).
SQ   SEQUENCE   289 AA;  32653 MW;  7BFEC395F73D7CF6 CRC64;
     MLKNLFRKTK YITVSQKNIG NYKRENTPTI PDGMWVKCNK CGEILYQNDL EKNYMVCNLC
     GNHFRIGVKE RIKYLFDKDT FKEWDYKIKT ENPLDFKGYD EKIEHIKEKT NLSEAVTTGK
     GKIAGMEVVV CIMDSKFMMG SMGSVVGEKI TRAIERAIEL RLPVIIFTAS GGARMQEGIL
     SLMQMAKVSS ALAKLDEEGL LYICVLTDPT TGGVTASFAM LGDIILAEPD ALIGFAGKRV
     IEQTINEKLP EDFQKSEFLL EHGFIDKIVP RSDLRKVLAK LINMHQNSF
//