ID Q2EUT0_ECOLX Unreviewed; 296 AA.
AC Q2EUT0;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=AccD {ECO:0000313|EMBL:ABD19992.1};
DE Flags: Fragment;
GN Name=accD {ECO:0000313|EMBL:ABD19992.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:ABD19992.1};
RN [1] {ECO:0000313|EMBL:ABD19992.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=1708 {ECO:0000313|EMBL:ABD19994.1}, 44738
RC {ECO:0000313|EMBL:ABD19993.1}, and 44825
RC {ECO:0000313|EMBL:ABD19992.1};
RX PubMed=17160643; DOI=10.1007/s00239-006-0052-8;
RA Yang J., Nie H., Chen L., Zhang X., Yang F., Xu X., Zhu Y., Yu J., Jin Q.;
RT "Revisiting the molecular evolutionary history of Shigella spp.";
RL J. Mol. Evol. 64:71-79(2007).
CC -!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex.
CC Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its
CC carrier protein (BCCP) and then the CO(2) group is transferred by the
CC transcarboxylase to acetyl-CoA to form malonyl-CoA.
CC {ECO:0000256|ARBA:ARBA00025280}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; DQ362291; ABD19992.1; -; Genomic_DNA.
DR EMBL; DQ362292; ABD19993.1; -; Genomic_DNA.
DR EMBL; DQ362293; ABD19994.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2EUT0; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; 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; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011762; COA_CT_N.
DR InterPro; IPR041010; Znf-ACC.
DR NCBIfam; TIGR00515; accD; 1.
DR PANTHER; PTHR42995; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC; 1.
DR PANTHER; PTHR42995:SF5; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR Pfam; PF17848; zf-ACC; 1.
DR PRINTS; PR01070; ACCCTRFRASEB.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 21..290
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABD19992.1"
FT NON_TER 296
FT /evidence="ECO:0000313|EMBL:ABD19992.1"
SQ SEQUENCE 296 AA; 32434 MW; 8E4469D5697B48B8 CRC64;
WIERIKSNIT PTRKASIPEG VWTKCDSCGQ VLYRAELERN LEVCPKCDHH MRMTARNRLH
SLLDEGSLVE LGSELEPKDV LKFRDSKKYK DRLASAQKET GEKDALVVMK GTLYGMPVVA
AAFEFAFMGG SMGSVVGARF VRAVEQALED NCPLICFSAS GGARMQEALM SLMQMAKTSA
ALAKMQERGL PYISVLTDPT MGGVSASFAM LGDLNIAEPK ALIGFAGPRV IEQTVREKLP
PGFQRSEFLI EKGAIDMIVR RPEMRLKLAS ILAKLMNLPA PNPEAPREGV VVPPVP
//
