ID   A6XI75_9MAGN            Unreviewed;       290 AA.
AC   A6XI75;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Acetyl co-A carboxylase {ECO:0000313|EMBL:ABI18049.1};
DE   Flags: Fragment;
GN   Name=accD {ECO:0000313|EMBL:ABI18049.1};
OS   Heisteria cauliflora.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:ABI18049.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Santalales; Erythropalaceae; Heisteria.
OX   NCBI_TaxID=397389 {ECO:0000313|EMBL:ABI18049.1};
RN   [1] {ECO:0000313|EMBL:ABI18049.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Malecot V.R., Nickrent D.L.;
RT   "Phylogenetic relationships of basal Santalales, particularly Olacaceae,
RT   based on nuclear and chloroplast sequences.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of biotin
CC       carboxyl carrier protein, biotin carboxylase and 2 subunits each of
CC       ACCase subunit alpha and ACCase plastid-coded subunit beta (accD).
CC       {ECO:0000256|ARBA:ARBA00011842}.
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DR   EMBL; DQ790264; ABI18049.1; -; Genomic_DNA.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
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:InterPro.
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   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   PRINTS; PR01070; ACCCTRFRASEB.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chloroplast {ECO:0000313|EMBL:ABI18049.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Plastid {ECO:0000313|EMBL:ABI18049.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          95..290
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   REGION          56..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABI18049.1"
FT   NON_TER         290
FT                   /evidence="ECO:0000313|EMBL:ABI18049.1"
SQ   SEQUENCE   290 AA;  32634 MW;  192A9923DA9CAB0A CRC64;
     NDPYYDHYVY DTKYSWNNHI NSCIDSYLHS QIRIDSYILS GXXXXXXXXX XXXXXXXXXS
     RERGSSGIRT STNGSDLTIR ESSNDLDTAQ NYRHLWVQCE NCYGLNYKKF FKSKMKICEQ
     CGYHLKMSSS DRIELLIDPG TWDPMDEDMV SLDPIEFHSE EELYKDRIDS YQRKTGLTEA
     VQTGIGQLNG IPIAIGVMDF QFMGGSMGSV VGEKITRLIE YATNKFLPLI IVCASGGARM
     QEGSLSLMQM AKISSALYDY QSNKKLFYVS ILTSPTTGGV TASFGMLGDI
//