ACCD_PHAAO
ID ACCD_PHAAO Reviewed; 497 AA.
AC Q3BAN3;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01395};
DE Short=ACCase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395};
DE Short=Acetyl-CoA carboxylase carboxyltransferase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395};
DE EC=2.1.3.15 {ECO:0000255|HAMAP-Rule:MF_01395};
GN Name=accD {ECO:0000255|HAMAP-Rule:MF_01395};
OS Phalaenopsis aphrodite subsp. formosana (Moth orchid).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC Epidendroideae; Vandeae; Aeridinae; Phalaenopsis.
OX NCBI_TaxID=308872;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Taisugar TS-97;
RX PubMed=16207935; DOI=10.1093/molbev/msj029;
RA Chang C.-C., Lin H.-C., Lin I.-P., Chow T.-Y., Chen H.-H., Chen W.-H.,
RA Cheng C.-H., Lin C.-Y., Liu S.-M., Chang C.-C., Chaw S.-M.;
RT "The chloroplast genome of Phalaenopsis aphrodite (Orchidaceae):
RT comparative analysis of evolutionary rate with that of grasses and its
RT phylogenetic implications.";
RL Mol. Biol. Evol. 23:279-291(2006).
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:0000255|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:0000255|HAMAP-Rule:MF_01395};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01395};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01395};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000255|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:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000255|HAMAP-
CC Rule:MF_01395}.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000255|HAMAP-
CC Rule:MF_01395}.
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DR EMBL; AY916449; AAW82509.1; -; Genomic_DNA.
DR RefSeq; YP_358585.1; NC_007499.1.
DR AlphaFoldDB; Q3BAN3; -.
DR SMR; Q3BAN3; -.
DR PRIDE; Q3BAN3; -.
DR GeneID; 3741688; -.
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.
DR InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011762; COA_CT_N.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR PRINTS; PR01070; ACCCTRFRASEB.
DR SUPFAM; SSF52096; SSF52096; 1.
DR TIGRFAMs; TIGR00515; accD; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Metal-binding; Nucleotide-binding;
KW Plastid; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..497
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit beta, chloroplastic"
FT /id="PRO_0000359160"
FT DOMAIN 225..497
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT ZN_FING 229..251
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
SQ SEQUENCE 497 AA; 56240 MW; 73219EE052AF8561 CRC64;
MKKYWFNSML SNKKLEQKCG LSKSMDGLDA LGHTSGSEET IRKDADKKIP SWDSYSFSNI
HYLNSLFDRR NLWSLISDHT FLVRNSNGDT YSVYFDIENQ IFDIDNASSF LSELPSYLKS
GSNNSNYYYS YYSMYDTQSN WNNHINSCID SYLRFEISLN SDIYSDIDSY ISSFICTEST
SSIENCTEST SSIENGNSSI KTSSSYFNRI EKSNDFDLNT KYKQLWVQCE NCYGLNYKKF
FSSKMNICEY CGYHLKMSSS DRIELFIDPG TWEPMDEDMV SIDPIEFHSI DPIEFHSEEE
PYIDRISFYQ TKTGLTEAVQ TGVGQLNSIP IAIGVMDFQF MGGSMGSVVG EKITRLIEYA
TNRSLPVIIV CASGGARMQE GALSLMQMAK ISSASYDYQS NKKLFFVSIL TSPTTGGVTA
SFGMLGDIII AEPNAYIAFA GKRVIEQTLK KTVPDGLQVA EYLFHKGLFD PIVPRNPLKG
VLNELFQLHG FLPLNQD
