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Database: UniProt
Entry: K4K8P1_9ROSI
LinkDB: K4K8P1_9ROSI
Original site: K4K8P1_9ROSI 
ID   K4K8P1_9ROSI            Unreviewed;       284 AA.
AC   K4K8P1;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=AccD {ECO:0000313|EMBL:AFU94620.1};
DE   Flags: Fragment;
GN   Name=accD {ECO:0000313|EMBL:AFU94620.1};
OS   Clusia rosea.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AFU94620.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Clusiaceae; Clusieae; Clusia.
OX   NCBI_TaxID=156476 {ECO:0000313|EMBL:AFU94620.1};
RN   [1] {ECO:0000313|EMBL:AFU94620.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23045684; DOI=10.1073/pnas.1205818109;
RA   Xi Z., Ruhfel B.R., Schaefer H., Amorim A.M., Sugumaran M., Wurdack K.J.,
RA   Endress P.K., Matthews M.L., Stevens P.F., Mathews S., Davis C.C.;
RT   "Phylogenomics and a posteriori data partitioning resolve the Cretaceous
RT   angiosperm radiation Malpighiales.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:17519-17524(2012).
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; JX662494; AFU94620.1; -; 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   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   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   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   Chloroplast {ECO:0000313|EMBL:AFU94620.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Plastid {ECO:0000313|EMBL:AFU94620.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          6..284
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFU94620.1"
FT   NON_TER         284
FT                   /evidence="ECO:0000313|EMBL:AFU94620.1"
SQ   SEQUENCE   284 AA;  31701 MW;  3AB59F3957A10BBD CRC64;
     QKYRHLWVQC EICYGLNYKK XFWKSRMNIC EQCGYHLKMS SSDRIELSID PGTWDXXXXX
     XXXXXXXPIN EDMVSLDPIE FHSYKDRIDS YQRKTGLTEA VQTGTGQLNG IPVAIGVMDF
     QFMGGSMGSV VGEKITRLIE YAANKFLPLI LVCASGGARM QEGSLSLMQM AKISSALYDY
     XXXXXQSNKK LFYVSILTSP TTGGVTASFG MLGDIIIAEP NAYIAFAGKR VIEQTLNKTV
     PEGSQAAEFL FHKGLFDPIV PRNPLKGVLN ELFQLHVFFX XPLN
//
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