ID ACCD_STRR6 Reviewed; 288 AA.
AC Q7CRB7; Q7D4F5; Q9FBB8;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 29-MAY-2013, entry version 60.
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=spr0386;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10910344; DOI=10.1038/35018162;
RA Heath R.J., Rock C.O.;
RT "A triclosan-resistant bacterial enzyme.";
RL Nature 406:145-146(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/JB.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E.,
RA LeBlanc D.J., Lee L.N., Lefkowitz E.J., Lu J., Matsushima P.,
RA McAhren S.M., McHenney M., McLeaster K., Mundy C.W., Nicas T.I.,
RA Norris F.H., O'Gara M., Peery R.B., Robertson G.T., Rockey P.,
RA Sun P.-M., Winkler M.E., Yang Y., Young-Bellido M., Zhao G.,
RA Zook C.A., Baltz R.H., Jaskunas S.R., Rosteck P.R. Jr., Skatrud P.L.,
RA Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
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; AF197933; AAF98280.1; -; Genomic_DNA.
DR EMBL; AE007317; AAK99190.1; -; Genomic_DNA.
DR RefSeq; NP_357980.1; NC_003098.1.
DR ProteinModelPortal; Q7CRB7; -.
DR SMR; Q7CRB7; 30-287.
DR STRING; 171101.spr0386; -.
DR EnsemblBacteria; AAK99190; AAK99190; spr0386.
DR GeneID; 934669; -.
DR KEGG; spr:spr0386; -.
DR PATRIC; 19700611; VBIStrPne107296_0427.
DR eggNOG; COG0777; -.
DR HOGENOM; HOG000021671; -.
DR KO; K01963; -.
DR OMA; GLWIKCP; -.
DR ProtClustDB; PRK05654; -.
DR BioCyc; SPNE171101:GJC8-394-MONOMER; -.
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; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1 288 Acetyl-coenzyme A carboxylase carboxyl
FT transferase subunit beta.
FT /FTId=PRO_0000389872.
FT ZN_FING 37 58 C4-type (By similarity).
FT METAL 37 37 Zinc (By similarity).
FT METAL 40 40 Zinc (By similarity).
FT METAL 55 55 Zinc (By similarity).
FT METAL 58 58 Zinc (By similarity).
SQ SEQUENCE 288 AA; 31786 MW; 42C29A8FC7BF21D5 CRC64;
MALFSKKDKY IRINPNRSVR EKPQAKPEVP DELFSQCPGC KHTIYQKDLG SERICPHCSY
TFRISAQERL ALTIDMGTFK ELFTGIESKD PLHFPGYQKK LASMREKTGL HEAVVTGTAL
IKGQTVALGI MDSNFIMASM GTVVGEKITR LFEYATVEKL PVVLFTASGG ARMQEGIMSL
MQMAKISAAV KRHSNAGLFY LTILTDPTTG GVTASFAMEG DIILAEPQSL VGFAGRRVIE
NTVRESLPED FQKAEFLLEH GFVDAIVKRR DLPDTIASLV RLHGGSPR
//
