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Database: UniProt
Entry: B5D6J1_PINPI
LinkDB: B5D6J1_PINPI
Original site: B5D6J1_PINPI 
ID   B5D6J1_PINPI            Unreviewed;       100 AA.
AC   B5D6J1;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Acetyl-CoA carboxylase beta subunit {ECO:0000313|EMBL:CAP03189.1};
DE   Flags: Fragment;
GN   Name=accD {ECO:0000313|EMBL:CAP03189.1};
OS   Pinus pinea (Italian stone pine).
OG   Plastid {ECO:0000313|EMBL:CAP03189.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Pinus.
OX   NCBI_TaxID=3346 {ECO:0000313|EMBL:CAP03189.1};
RN   [1] {ECO:0000313|EMBL:CAP03189.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=22111 {ECO:0000313|EMBL:CAP03189.1}, 22112
RC   {ECO:0000313|EMBL:CAP03190.1}, and L27 {ECO:0000313|EMBL:CAP03216.1};
RA   Kelly L.J.;
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAP03189.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=22111 {ECO:0000313|EMBL:CAP03189.1}, 22112
RC   {ECO:0000313|EMBL:CAP03190.1}, and L27 {ECO:0000313|EMBL:CAP03216.1};
RA   Cowan R.;
RT   "DNA Barcoding of Land Plants.";
RL   Submitted (SEP-2008) 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; AM883236; CAP03189.1; -; Genomic_DNA.
DR   EMBL; AM883237; CAP03190.1; -; Genomic_DNA.
DR   EMBL; AM883263; CAP03216.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5D6J1; -.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR   GO; GO:0009536; C:plastid; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Plastid {ECO:0000313|EMBL:CAP03189.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..100
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAP03189.1"
FT   NON_TER         100
FT                   /evidence="ECO:0000313|EMBL:CAP03189.1"
SQ   SEQUENCE   100 AA;  10607 MW;  879FE3213F4C6D1A CRC64;
     SMGSVVGEKI TRLIERATAE SLPLILVCAS GGARMQEGSF SLMQMAKIAS ALYIHQKEKK
     LLYISILTSP TTGGVTASFG MLGDIIIAEP KAYIAFAGKR
//
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