ID Q6QBP0_CASSA Unreviewed; 537 AA.
AC Q6QBP0;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic {ECO:0000256|HAMAP-Rule:MF_01395};
DE Short=ACCase subunit beta {ECO:0000256|HAMAP-Rule:MF_01395};
DE Short=Acetyl-CoA carboxylase carboxyltransferase subunit beta {ECO:0000256|HAMAP-Rule:MF_01395};
DE EC=2.1.3.15 {ECO:0000256|HAMAP-Rule:MF_01395};
GN Name=accD {ECO:0000256|HAMAP-Rule:MF_01395,
GN ECO:0000313|EMBL:AAS55872.1};
OS Castanea sativa (Sweet chestnut).
OG Plastid; Chloroplast {ECO:0000313|EMBL:AAS55872.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Fagaceae; Castanea.
OX NCBI_TaxID=21020 {ECO:0000313|EMBL:AAS55872.1};
RN [1] {ECO:0000313|EMBL:AAS55872.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15660155; DOI=10.1371/journal.pbio.0030014;
RA Knapp M., Stockler K., Havell D., Delsuc F., Sebastiani F., Lockhart P.J.;
RT "Relaxed molecular clock provides evidence for long-distance dispersal of
RT Nothofagus (southern beech).";
RL PLoS Biol. 3:38-43(2005).
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. {ECO:0000256|HAMAP-
CC Rule:MF_01395}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-
CC CoA + N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:54728,
CC Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145; EC=2.1.3.15;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01395};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01395};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01395};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01395}.
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}.
CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of biotin
CC carboxyl carrier protein, biotin carboxylase and two subunits each of
CC ACCase subunit alpha and ACCase plastid-coded subunit beta (accD).
CC {ECO:0000256|HAMAP-Rule:MF_01395}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000256|HAMAP-
CC Rule:MF_01395}.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000256|HAMAP-
CC Rule:MF_01395}.
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DR EMBL; AY548965; AAS55872.1; -; Genomic_DNA.
DR UniPathway; UPA00655; UER00711.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
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, ECO:0000256|HAMAP-
KW Rule:MF_01395}; Chloroplast {ECO:0000313|EMBL:AAS55872.1};
KW Fatty acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01395};
KW Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01395};
KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01395};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01395};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01395};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01395}; Plastid {ECO:0000313|EMBL:AAS55872.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01395}; Zinc {ECO:0000256|HAMAP-Rule:MF_01395};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_01395}.
FT DOMAIN 249..520
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT ZN_FING 253..275
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT REGION 50..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT BINDING 272
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT BINDING 275
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
SQ SEQUENCE 537 AA; 61063 MW; 46C0F615D0758F16 CRC64;
MTIHLLYFSC KYVQQGFMEK GWFNSMLSKK KELEYGYGLS KSMGSLGSIE NTSVSEDPIR
NDIDKNTLSG SDSDNSSYNN VDHLVGVRDI HNFVPDDTFL VRDNNRDSYF ICFDIENQIF
EIDNAHSFLS ELESSFSNSR NFCYLNSVSN SDDPHYDPYI YDTKYSWNKH ITSCIDSYFR
SQICIDSYIL SGIVNYNDNY ISSYIFDESR NSSETQSSSI KTSPAGSELT ITETENSNDL
DFTQKYRHLW VQCENCYGLN YKKFFKSKMN ICEXCGHHLK MSSSDRIELL IDPGTWVPMD
EDMVSVDTIE FPLEEESYKD RIDSYQRKTG LTEAVQTGTG QLNGIPIAIG VMDFQFMGGS
MGSVVGEKIT RLIEYATNRF LPLILVCASG GARMQEGSLS LMQMAKIASA LYDYQSKKKL
FYVSILTSPT TGGVTASFGM LGDIIIAEPN AYIAFAGKRV IEQTLNTTVP EGSQTAEYLF
HKGQFDLIVP RNLLKDVLSE LFQLHAFFSL NQNSIKWILN KKKNILINQN INYYFFL
//
