ACCD_CUSRE
ID ACCD_CUSRE Reviewed; 497 AA.
AC P31562; A7M977;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 108.
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=ycf11, zfpA;
OS Cuscuta reflexa (Southern Asian dodder).
OG Plastid.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Convolvulaceae; Cuscuteae; Cuscuta;
OC Cuscuta subgen. Monogynella.
OX NCBI_TaxID=4129;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Heberhausen G.;
RL Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING.
RX PubMed=17714582; DOI=10.1186/1471-2229-7-45;
RA Funk H.T., Berg S., Krupinska K., Maier U.-G., Krause K.;
RT "Complete DNA sequences of the plastid genomes of two parasitic flowering
RT plant species, Cuscuta reflexa and Cuscuta gronovii.";
RL BMC Plant Biol. 7:45-45(2007).
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.
CC -!- RNA EDITING: Modified_positions=258 {ECO:0000269|PubMed:17714582};
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000255|HAMAP-
CC Rule:MF_01395}.
CC -!- CAUTION: Young tissue from this organism is photosynthetic and contains
CC some thylakoids, although the photosynthetic activity does not exceed
CC the light compensation point. {ECO:0000305}.
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DR EMBL; X69803; CAA49462.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AM711640; CAM98405.1; ALT_SEQ; Genomic_DNA.
DR PIR; S31477; S31477.
DR RefSeq; YP_001430119.1; NC_009766.1.
DR AlphaFoldDB; P31562; -.
DR SMR; P31562; -.
DR GeneID; 5536593; -.
DR UniPathway; UPA00655; UER00711.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR GO; GO:0009536; C:plastid; 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 2: Evidence at transcript level;
KW ATP-binding; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Metal-binding; Nucleotide-binding;
KW Plastid; RNA editing; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..497
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit beta"
FT /id="PRO_0000199783"
FT DOMAIN 217..489
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT ZN_FING 221..243
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
SQ SEQUENCE 497 AA; 56481 MW; E97910C4E8D9E988 CRC64;
MERREGGRDN SSCSNVNQLF GVKDSESLLY DDVFIVRDRN GDSYFAYWDI EKNTFLSEPF
YSYRSRNSSY LPKIKAFMSE DRSQIHEVKN GFRSEDHSKI NKINGVENLF HNYNMNVLTD
DYNFKMGMNG FHRPQSKIHI NRFIDSYLQS QICIATTPGS GSDNDSYIHG SRVYGESESY
TRSEGRSSSI RTRTKGVELT LRERPGILDR TKKYMYLWLQ CDNCYGLNYK KVLKSKMTIC
EQCGYHLQMS SSDRIELLID PGTWDPMDED MVSRDPIKFD SGGGEAYKDR LYFYQRKTGL
TEAVQTGIGQ LNGIPVAIGV MDFKFMGGSM GSVVGEKITR LIEHATNKFL PLIIVSASGG
ARMQEGSLSL MQMAKISSAL YDYQSNKRLV YVSILTSPTA GGVTASFGML GDIIIVEPRA
YVAFAGKRVI EQTLNQTIPN DSQEAEFLFH KGLFDLIIPR HLLKSVISEL FTLHDLFPLN
QNSNQYSQYR ALLNPIF
