ACCD_EPIVI
ID ACCD_EPIVI Reviewed; 493 AA.
AC P30064;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta {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}; Synonyms=dedB, ycf11, zfpA;
OS Epifagus virginiana (Beechdrops) (Orobanche virginiana).
OG Plastid; Non-photosynthetic plastid.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Orobanchaceae; Orobancheae; Epifagus.
OX NCBI_TaxID=4177;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=1332054; DOI=10.1073/pnas.89.22.10648;
RA Wolfe K.H., Morden C.W., Palmer J.D.;
RT "Function and evolution of a minimal plastid genome from a
RT nonphotosynthetic parasitic plant.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:10648-10652(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1404416; DOI=10.1007/bf00161168;
RA Wolfe K.H., Morden C.W., Ems S.C., Palmer J.D.;
RT "Rapid evolution of the plastid translational apparatus in a
RT nonphotosynthetic plant: loss or accelerated sequence evolution of tRNA and
RT ribosomal protein genes.";
RL J. Mol. Evol. 35:304-317(1992).
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 stroma {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000255|HAMAP-
CC Rule:MF_01395}.
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DR EMBL; M81884; AAA65854.1; -; Genomic_DNA.
DR PIR; S78384; S78384.
DR RefSeq; NP_054380.1; NC_001568.1.
DR AlphaFoldDB; P30064; -.
DR SMR; P30064; -.
DR GeneID; 801404; -.
DR UniPathway; UPA00655; UER00711.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR GO; GO:0009532; C:plastid 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; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Metal-binding; Nucleotide-binding;
KW Plastid; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..493
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit beta"
FT /id="PRO_0000199784"
FT DOMAIN 231..493
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT ZN_FING 235..257
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 254
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
SQ SEQUENCE 493 AA; 56560 MW; 2CB0529471558036 CRC64;
MERWRFSLMV FNNKLKHEYG IKKSLDSVSS IENTIENKDS NSKPNIKGRA QNIRSCGGRD
NYSYNNIIYL FGVEYNRNLI PNDTFLFRDN KGDSFYISFN IENHIFEIDI NFSCLSELEI
ERYFYSYHGF DYFNFNNGSA IEDYLYNHYM YDTPSNNHIT SCIESYLQSQ ICVNPSIISD
SSDSYIFGCF DKRRTHNESR RSGIRNRAQS SYLTIRESFN NLDSTKKYKH LWVQCENCYG
LNYKKFLKSK INLCEQCGYH FKMSSSERIE VLVDPDTWYP MDEDMSSLDP IEFHSEEEPY
KDRIYSYQKR TGLTEAVQTG LGQLNGIPIA IGVMDFQFMG GSMGSVVGEK ITRLIEYATN
KILPLIIVCA SGGARMQEGS LSLMQMAKIS SALFDYQSNK KLLYVSILTS PTTGGVTASF
GMLGDIIIAE PNSYIAFAGK RVIEQTLHKI VPEGSQAAEY LFQKGLFDLI IPRNLLKSVL
GELFKLHAFF PLN
