GenomeNet

Database: UniProt
Entry: A0A059ASE0_EUCGR
LinkDB: A0A059ASE0_EUCGR
Original site: A0A059ASE0_EUCGR 
ID   A0A059ASE0_EUCGR        Unreviewed;       452 AA.
AC   A0A059ASE0;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=CoA carboxyltransferase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS50980};
GN   ORFNames=EUGRSUZ_I02537 {ECO:0000313|EMBL:KCW56872.1};
OS   Eucalyptus grandis (Flooded gum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW56872.1};
RN   [1] {ECO:0000313|EMBL:KCW56872.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW56872.1};
RA   Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT   "The genome of Eucalyptus grandis.";
RL   Submitted (JUL-2013) 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; KK198761; KCW56872.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059ASE0; -.
DR   STRING; 71139.A0A059ASE0; -.
DR   EnsemblPlants; KCW56872; KCW56872; EUGRSUZ_I02537.
DR   Gramene; KCW56872; KCW56872; EUGRSUZ_I02537.
DR   InParanoid; A0A059ASE0; -.
DR   OMA; KMNICEH; -.
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:InterPro.
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   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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          184..452
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
SQ   SEQUENCE   452 AA;  51346 MW;  00E16AE549222F21 CRC64;
     MGKWWFNSML YKGKLEYRCG LSKSIDRFGN PIEKTSVSED PVRNDTYKKI HSWSESSSYS
     NATHLVGVRG VRNFIFDDTL LVRDSNRNIY SIYFDITNQI FEIDNDPSLL SERESSFFSY
     RTYVYLKEGS KNDDPPCDHS MYDIKYSWNN HITSCIHSYL GSQICIESSI LSSSDNSSDS
     YISSYIYGEY SNERGSSSKI LKSKMNICDQ CGYHLKMSSS DRIELSIDPS TWDPMDEDMV
     SLDPIEFHLE EEPYKDRIDS YQRKTGLTDA VQTGTSRLND IPIAIGVMDF QFMGGSMGCV
     VGEKIIHLIE YATNKFLPLI LVCASGGARM QEGSLSLMQM AKIFAALYDY QSHKKLFYIS
     ILTSPTTGGV TASFGRLGDI IIVEPNAYIA FASKRVIEQT LNKLVPEGSQ AAEYLFHKGL
     FNPIVPRNPL KGVLSELFKL HTFFSFELKF TY
//
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