ACCD_CARPA
ID ACCD_CARPA Reviewed; 497 AA.
AC B1A944;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 59.
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 Carica papaya (Papaya).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Caricaceae; Carica.
OX NCBI_TaxID=3649;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. SunUp;
RX PubMed=18432245; DOI=10.1038/nature06856;
RA Ming R., Hou S., Feng Y., Yu Q., Dionne-Laporte A., Saw J.H., Senin P.,
RA Wang W., Ly B.V., Lewis K.L., Salzberg S.L., Feng L., Jones M.R.,
RA Skelton R.L., Murray J.E., Chen C., Qian W., Shen J., Du P., Eustice M.,
RA Tong E., Tang H., Lyons E., Paull R.E., Michael T.P., Wall K., Rice D.W.,
RA Albert H., Wang M.L., Zhu Y.J., Schatz M., Nagarajan N., Acob R.A.,
RA Guan P., Blas A., Wai C.M., Ackerman C.M., Ren Y., Liu C., Wang J.,
RA Wang J., Na J.K., Shakirov E.V., Haas B., Thimmapuram J., Nelson D.,
RA Wang X., Bowers J.E., Gschwend A.R., Delcher A.L., Singh R., Suzuki J.Y.,
RA Tripathi S., Neupane K., Wei H., Irikura B., Paidi M., Jiang N., Zhang W.,
RA Presting G., Windsor A., Navajas-Perez R., Torres M.J., Feltus F.A.,
RA Porter B., Li Y., Burroughs A.M., Luo M.C., Liu L., Christopher D.A.,
RA Mount S.M., Moore P.H., Sugimura T., Jiang J., Schuler M.A., Friedman V.,
RA Mitchell-Olds T., Shippen D.E., dePamphilis C.W., Palmer J.D., Freeling M.,
RA Paterson A.H., Gonsalves D., Wang L., Alam M.;
RT "The draft genome of the transgenic tropical fruit tree papaya (Carica
RT papaya Linnaeus).";
RL Nature 452:991-996(2008).
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; EU431223; ABY86791.1; -; Genomic_DNA.
DR RefSeq; YP_001671692.1; NC_010323.1.
DR AlphaFoldDB; B1A944; -.
DR SMR; B1A944; -.
DR GeneID; 5878364; -.
DR KEGG; cpap:5878364; -.
DR OrthoDB; 623889at2759; -.
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_0000359127"
FT DOMAIN 230..497
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT ZN_FING 234..256
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
SQ SEQUENCE 497 AA; 56379 MW; BE9D60307C0BC438 CRC64;
MEKSWFNSML SKGEVEYRCG LSKSMDSLGP IENTSISEDP VINDPDKNIY NSIWGESSSY
YSNVDHLVGA KDIRNFISDD TFLVRDSNRD SYSIYFDIEN NNFEIDNDHS FLSELESFFY
SYRNSSYMNN RSKSDDPHYD PYMYDTKYSW TNHINSCIDS YLRSQICIDS SILSGSDNYN
DSYIYNYICS ESGKSSESEN SNIRTNTNRS DLTIKESSND LDITQKYRHL WVQCENCYGL
NYKKFLKSKM NICEQCGYYL KMSSSDRIEL LVDPGTWNPM DENMVSLDPI EFHSEEEPYK
DRIDSYQRKT GLTEAVQTGT GQLNGIPIAL GVMDFQFMGG SMGSVVGEKI TRLIEYATNE
FLPLIIVCAS GGARMQEGSL SLMQMAKISS ALYDYQSNKK LFYVSILTSP TTGGVTASFG
MLGDIIIAEP NAYIAFAGKR VIEQTLNKTV PEGSQAAEYL FHKGLFDSIV PRNPLKGVLS
ELFQLHGFFP LNQNSIK
