ACCD_SOYBN
ID ACCD_SOYBN Reviewed; 432 AA.
AC P49158; Q2PMS4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 3.
DT 03-AUG-2022, entry version 109.
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 Glycine max (Soybean) (Glycine hispida).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Resnik; TISSUE=Leaf;
RA Reverdatto S.V., Beilinson V., Nielsen N.C.;
RT "The rps16, accD, psaI, ORF 203, ORF 151, ORF 103, ORF 229 and petA gene
RT cluster in the chloroplast genome of soybean.";
RL (er) Plant Gene Register PGR95-051(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. PI 437654;
RX PubMed=16247559; DOI=10.1007/s11103-005-8882-0;
RA Saski C., Lee S.-B., Daniell H., Wood T.C., Tomkins J., Kim H.-G.,
RA Jansen R.K.;
RT "Complete chloroplast genome sequence of Glycine max and comparative
RT analyses with other legume genomes.";
RL Plant Mol. Biol. 59:309-322(2005).
RN [3]
RP RNA EDITING.
RC STRAIN=cv. Enrei;
RX PubMed=11078738; DOI=10.1074/jbc.m008166200;
RA Sasaki Y., Kozaki A., Ohmori A., Iguchi H., Nagano Y.;
RT "Chloroplast RNA editing required for functional acetyl-CoA carboxylase in
RT plants.";
RL J. Biol. Chem. 276:3937-3940(2001).
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 -!- RNA EDITING: Modified_positions=206 {ECO:0000269|PubMed:11078738};
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000255|HAMAP-
CC Rule:MF_01395}.
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DR EMBL; U26948; AAA80643.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DQ317523; ABC25134.1; ALT_SEQ; Genomic_DNA.
DR PIR; T06341; T06341.
DR RefSeq; YP_538774.1; NC_007942.1.
DR AlphaFoldDB; P49158; -.
DR SMR; P49158; -.
DR STRING; 3847.GLYMA15G39765.1; -.
DR PRIDE; P49158; -.
DR GeneID; 3989306; -.
DR KEGG; gmx:3989306; -.
DR InParanoid; P49158; -.
DR OrthoDB; 623889at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000008827; Chloroplast.
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 2: Evidence at transcript level;
KW ATP-binding; Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Metal-binding; Nucleotide-binding;
KW Plastid; Reference proteome; RNA editing; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..432
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit beta, chloroplastic"
FT /id="PRO_0000199794"
FT DOMAIN 165..432
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT ZN_FING 169..191
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT REGION 127..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT CONFLICT 115
FT /note="Y -> N (in Ref. 1; AAA80643)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="D -> N (in Ref. 1; AAA80643)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="F -> S (in Ref. 1; AAA80643)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 432 AA; 48993 MW; 8F2BE2C4AD25322C CRC64;
MEKWWFNSML FNRKLEYRCE LSKSMDSLGP IENTSLREDP KILTDIEKKI HRDLDYLEME
GFFSSDLNTV SKNDDDHYMY ETQFSFNNNI TSFIDSCIES FNLGDIDKYN DIYFYSYIFL
KGRNCSESDN SSTSIITSTN DTNDSDSTIG ESSNNLDESQ KYKHLWLECE NCYGLNYKKF
FKSKMNICEY CGYHLKMGSS DRIELLIDSG TWNPMDEDMV SLDPIEFHSE EEPYKDRIDS
YQRKTGLTEA VQTGTGQLNG IPVAIGIMDF QFMGGSMGSA VGEKITRLVE YATNQLLPLI
LVCASGGARM QEGSLSLIQM AKISSALYDY QKNKKLFYVS ILTSPTTGGV TASFGMLGDI
IIAEPNAYIA FAGKRVIEQT LNKAVPEGSQ AAEYLFHKGL FDSIVPRNLL KGVLSELFQF
HNFFSLTKND KA
