(data stored in ACNUC7421 zone)

SWISSPROT: Q13S22_PARXL

ID   Q13S22_PARXL            Unreviewed;       290 AA.
AC   Q13S22;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   07-JUN-2017, entry version 78.
DE   RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta {ECO:0000256|HAMAP-Rule:MF_01395};
DE            Short=ACCase subunit beta {ECO:0000256|HAMAP-Rule:MF_01395};
DE            Short=Acetyl-CoA carboxylase carboxyltransferase subunit beta {ECO:0000256|HAMAP-Rule:MF_01395};
DE            EC=6.4.1.2 {ECO:0000256|HAMAP-Rule:MF_01395};
GN   Name=accD {ECO:0000256|HAMAP-Rule:MF_01395};
GN   ORFNames=Bxe_B2878 {ECO:0000313|EMBL:ABE33117.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33117.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33117.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33117.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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. {ECO:0000256|HAMAP-Rule:MF_01395}.
CC   -!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate
CC       + malonyl-CoA. {ECO:0000256|HAMAP-Rule:MF_01395}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01395};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01395};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
CC       from acetyl-CoA: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01395}.
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). {ECO:0000256|HAMAP-Rule:MF_01395,
CC       ECO:0000256|SAAS:SAAS00753290}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01395,
CC       ECO:0000256|SAAS:SAAS00710105}.
CC   -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000256|HAMAP-
CC       Rule:MF_01395}.
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DR   EMBL; CP000271; ABE33117.1; -; Genomic_DNA.
DR   RefSeq; WP_011490500.1; NZ_CP008762.1.
DR   ProteinModelPortal; Q13S22; -.
DR   STRING; 266265.Bxe_B2878; -.
DR   EnsemblBacteria; ABE33117; ABE33117; Bxe_B2878.
DR   GeneID; 4006757; -.
DR   KEGG; bxb:DR64_5208; -.
DR   KEGG; bxe:Bxe_B2878; -.
DR   PATRIC; fig|266265.5.peg.4811; -.
DR   eggNOG; ENOG4107QTG; Bacteria.
DR   eggNOG; COG0777; LUCA.
DR   HOGENOM; HOG000021670; -.
DR   KO; K01963; -.
DR   OMA; PEGLWIK; -.
DR   OrthoDB; POG091H04JK; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000001817; Chromosome 2.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_01395; AcetylCoA_CT_beta; 1.
DR   InterPro; IPR034733; AcCoA_carboxyl.
DR   InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom.
DR   InterPro; IPR011762; COA_CT_N.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   PRINTS; PR01070; ACCCTRFRASEB.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   TIGRFAMs; TIGR00515; accD; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13S22.
DR   SWISS-2DPAGE; Q13S22.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01395};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01395,
KW   ECO:0000256|SAAS:SAAS00709970};
KW   Fatty acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01395};
KW   Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01395};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01395};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01395};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01395};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01395};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01395};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Transferase {ECO:0000313|EMBL:ABE33117.1};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01395};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_01395}.
FT   DOMAIN       27    290       CoA carboxyltransferase N-terminal.
FT                                {ECO:0000259|PROSITE:PS50980}.
FT   ZN_FING      31     53       C4-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_01395}.
FT   METAL        31     31       Zinc. {ECO:0000256|HAMAP-Rule:MF_01395}.
FT   METAL        34     34       Zinc. {ECO:0000256|HAMAP-Rule:MF_01395}.
FT   METAL        50     50       Zinc. {ECO:0000256|HAMAP-Rule:MF_01395}.
FT   METAL        53     53       Zinc. {ECO:0000256|HAMAP-Rule:MF_01395}.
SQ   SEQUENCE   290 AA;  31975 MW;  2697378EC9AF6B9F CRC64;
     MSWLDKLLPP KIKQTDPKNR KGIPEGLWIK CPSCEAVLYR NDVEANLHVC PKCDHHMRIG
     ARERLDGLLD PEGRYEIGQE IVPVDALKFK DSRKYPDRLK EAMDDTDETD AMVVMGGAIH
     TLPVVVACFE FSFMGGSMGS VVGERFVRGA QNALEQKVPF ICFTASGGAR MQESLLSLMQ
     MAKTTAMLTK LAEARLPFIS VLTDPTMGGV SASFAFLGDV VIAEPKALIG FAGPRVIEQT
     VREKLPEGFQ RAEFLLTKGA IDMIVDRRKL REEIAQLMAL LSHQPADAVA
//

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