ACCD_CRYJA
ID ACCD_CRYJA Reviewed; 700 AA.
AC B1VKF0;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 55.
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 Cryptomeria japonica (Japanese cedar) (Cupressus japonica).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers II; Cupressales; Cupressaceae;
OC Cryptomeria.
OX NCBI_TaxID=3369;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18570682; DOI=10.1186/1471-2229-8-70;
RA Hirao T., Watanabe A., Kurita M., Kondo T., Takata K.;
RT "Complete nucleotide sequence of the Cryptomeria japonica D. Don.
RT chloroplast genome and comparative chloroplast genomics: diversified
RT genomic structure of coniferous species.";
RL BMC Plant Biol. 8:70-70(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Wogon-Sugi, and cv. Yaku-Sugi;
RX PubMed=19449186; DOI=10.1007/s00294-009-0247-9;
RA Hirao T., Watanabe A., Kurita M., Kondo T., Takata K.;
RT "A frameshift mutation of the chloroplast matK coding region is associated
RT with chlorophyll deficiency in the Cryptomeria japonica virescent mutant
RT Wogon-Sugi.";
RL Curr. Genet. 55:311-321(2009).
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; AP009377; BAG16661.1; -; Genomic_DNA.
DR EMBL; AP010966; BAH73287.1; -; Genomic_DNA.
DR EMBL; AP010967; BAH73368.1; -; Genomic_DNA.
DR RefSeq; YP_001806663.1; NC_010548.1.
DR AlphaFoldDB; B1VKF0; -.
DR SMR; B1VKF0; -.
DR GeneID; 6166625; -.
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; 2.
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..700
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit beta, chloroplastic"
FT /id="PRO_0000389903"
FT DOMAIN 445..700
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT ZN_FING 34..56
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
SQ SEQUENCE 700 AA; 81325 MW; 6D69A2EFF60F1682 CRC64;
MCEENENKDS EYIETTPVEN GYNSERFKHL WFLCENCETL IYKKSLLEQK GVCAECGATL
QMTSSERIEL LIDNGTWRSI NTKLSSIDVL EKKHTTFDIK MVRKVSILLY KVISGKYFYK
EFFKNKYYNK ALRILVAYNN TLVNILKVAL GSKFIKYLNL DSKETIKILQ DIIDTGLKTA
QFALFEIRKK IKNEFYRFAL LNKAFENKQI SSLLAQNLED RRDDESEIIS IEFDRMAFRV
QTFLILESLL KLNTQLADVK EQLLSQDKFL KAVATSLVKK ELYFPEDKRK TRKIKKIFPF
YPGTDPETDY FLWLRTHMAI SLMERYLVLK EFKYWFRNRY CGLLEEEFPR FGSDILIEYV
KKQDRYESYN MIDHIMQDDL HTSTNSVELF QQINLLFHHK NNEKDCDNNF LSYTENTKGI
YFCLLEIMKQ FSTLTLDSKD KFPKKKGRDT KDTEDIEDID EEDIEEEYPL TYDSLTKEEK
EYVDANIELI KSTFNLGKEE FIETEEQSYQ DYNTSYQKET GLPDAIQTGV GEINGISVAL
GVMDFQFMGG SMGSVVGEKI TRLIQFATEN FLPLILVCAS GGARMQEGSF SLMQMNKIAA
MLHTYQKEKN LLYISVLTSP TTGGVTASFG MLANVTIVEP NAYIAFAGKR VIEQTLNQIV
DDEDQISDSL FDFGMFDSMV PRALLKNVLS ETIEIYMYGD
