(data stored in ACNUC7421 zone)

SWISSPROT: ACCD_RHOPS

ID   ACCD_RHOPS              Reviewed;         322 AA.
AC   Q13EQ0;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 74.
DE   RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395};
DE            Short=ACCase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395};
DE            Short=Acetyl-CoA carboxylase carboxyltransferase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395};
DE            EC=2.1.3.15 {ECO:0000255|HAMAP-Rule:MF_01395};
GN   Name=accD {ECO:0000255|HAMAP-Rule:MF_01395};
GN   OrderedLocusNames=RPD_0199;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) 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. {ECO:0000255|HAMAP-Rule:MF_01395}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] =
CC         malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein];
CC         Xref=Rhea:RHEA:54728, Rhea:RHEA-COMP:10505, Rhea:RHEA-
CC         COMP:10506, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384,
CC         ChEBI:CHEBI:83144, ChEBI:CHEBI:83145; EC=2.1.3.15;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01395};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
CC       from acetyl-CoA: step 1/1. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01395}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01395}.
CC   -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000255|HAMAP-
CC       Rule:MF_01395}.
DR   EMBL; CP000283; ABE37439.1; -; Genomic_DNA.
DR   RefSeq; WP_011500631.1; NC_007958.1.
DR   SMR; Q13EQ0; -.
DR   STRING; 316057.RPD_0199; -.
DR   EnsemblBacteria; ABE37439; ABE37439; RPD_0199.
DR   KEGG; rpd:RPD_0199; -.
DR   eggNOG; ENOG4108IDZ; Bacteria.
DR   eggNOG; COG0777; LUCA.
DR   HOGENOM; HOG000021670; -.
DR   KO; K01963; -.
DR   OMA; PEGLWIK; -.
DR   OrthoDB; 504557at2; -.
DR   BioCyc; RPAL316057:RPD_RS01010-MONOMER; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000001818; 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:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
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_sf.
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; Q13EQ0.
DR   SWISS-2DPAGE; Q13EQ0.
KW   ATP-binding; Complete proteome; Cytoplasm; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
KW   Nucleotide-binding; Transferase.
FT   CHAIN         1    322       Acetyl-coenzyme A carboxylase carboxyl
FT                                transferase subunit beta.
FT                                /FTId=PRO_0000389836.
FT   DOMAIN       24    293       CoA carboxyltransferase N-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01136}.
SQ   SEQUENCE   322 AA;  35253 MW;  E9D9B231B8BE0388 CRC64;
     MNWLTNVVRP KIRNILRRET PENLWIKCPD TGQLVFYKDV EQNQFVIPGS NYHMRMGALA
     RLRSVFDNET WYDVALPEVT ADPLKFRDER KYADRIKDAR TKTGAHDAVK VGYGKLEGLG
     VVAAVQDFDF MGGSLGMAAG EAIIRGLELA VEKHAPFIMF AASGGARMQE GILSLMQMPR
     TTVAVQMLRE AGLPYIVVLT NPTTGGVTAS YAMLGDIQLA EPGALIGFAG ARVIEQTIRE
     KLPDGFQRAE YLRDHGMVDM VVHRHELRPT LARLCRILTK TPLPAVEEIA ASDDAAQDAE
     AAAATEIVVT PPEAPSPTAP QA
//

If you have problems or comments...

PBIL Back to PBIL home page