(data stored in ACNUC7421 zone)

HOGENOM: IDLOI1_1_PE1012

ID   IDLOI1_1_PE1012                      STANDARD;      PRT;   292 AA.
AC   IDLOI1_1_PE1012; Q5QUD9;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit
DE   beta; Short=ACCase subunit beta; Short=Acetyl-CoA carboxylase
DE   carboxyltransferase subunit beta; EC=6.4.1 2; (IDLOI1_1.PE1012).
GN   Name=accD; OrderedLocusNames=IL1016;
OS   IDIOMARINA LOIHIENSIS L2TR.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=283942;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS IDLOI1_1.PE1012.
CC       Idiomarina loihiensis L2TR chromosome, complete genome.
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:ACCD_IDILO
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.
CC   -!- GENE_FAMILY: HOG000021670 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q5QUD9; -.
DR   EMBL; AE017340; AAV81856.1; -; Genomic_DNA.
DR   RefSeq; YP_155405.1; NC_006512.1.
DR   ProteinModelPortal; Q5QUD9; -.
DR   SMR; Q5QUD9; 23-282.
DR   GeneID; 3174064; -.
DR   GenomeReviews; AE017340_GR; IL1016.
DR   KEGG; ilo:IL1016; -.
DR   NMPDR; fig|283942.3.peg.784; -.
DR   OMA; FQTSEYL; -.
DR   ProtClustDB; CLSK742217; -.
DR   BioCyc; ILOI283942:IL1016-MON; -.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
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.
DR   HOGENOMDNA; IDLOI1_1.PE1012; -.
KW   ATP-binding; Complete proteome; Cytoplasm; Fatty acid biosynthesis;
KW   Ligase; Lipid synthesis; Metal-binding; Nucleotide-binding; Zinc;
KW   Zinc-finger.
SQ   SEQUENCE   292 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSWIERILAK PKINKRRGVP EGVWSKCTAC GNIIYKADLE RSLNVCPKCD HHMRVTGRSR
     LDIFLDKDNR EEIGTDLEPK DVLRFKDSKK YKDRIAAAQK STGENDALIA EKGTVKGVPL
     VAVAFDFNFM GGSMASVVGA KFVLAAEVCL KHRIPLVCFS ASGGARMQEA LMSLMQMAKT
     SAALARMSEE GLPFISILTD PTMGGVSASL AMLGDIHIAE PKALIGFAGP RVIEQTVRQT
     LPEGFQRAEF LLEHGAIDMI TDRRDMRDTV ARLLAKMQNL PSTEATEVSV NE
//

If you have problems or comments...

PBIL Back to PBIL home page