ACCD_PEA
ID ACCD_PEA Reviewed; 590 AA.
AC P18823;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 3.
DT 03-AUG-2022, entry version 107.
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}; Synonyms=ycf11, zfpA;
OS Pisum sativum (Garden pea).
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; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=cv. Alaska;
RX PubMed=1807835; DOI=10.1007/bf00317074;
RA Nagano Y., Matsuno R., Sasaki Y.;
RT "Sequence and transcriptional analysis of the gene cluster trnQ-zfpA-psaI-
RT ORF231-petA in pea chloroplasts.";
RL Curr. Genet. 20:431-436(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 220-590.
RC STRAIN=cv. Alaska;
RX PubMed=2505231; DOI=10.1093/nar/17.15.6217;
RA Sasaki Y., Nagano Y., Morioka S., Ishikawa H., Matsuno R.;
RT "A chloroplast gene encoding a protein with one zinc finger.";
RL Nucleic Acids Res. 17:6217-6227(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-590.
RC STRAIN=cv. Alaska;
RX PubMed=1913879; DOI=10.1007/bf00309603;
RA Smith A.G., Wilson R.J., Kaethner T.M., Willey D.L., Gray J.C.;
RT "Pea chloroplast genes encoding a 4 kDa polypeptide of photosystem I and a
RT putative enzyme of C1 metabolism.";
RL Curr. Genet. 19:403-410(1991).
RN [4]
RP PROTEIN SEQUENCE OF 1-17, RNA EDITING, AND ACTIVITY REGULATION BY REDOX
RP CONTROL.
RC STRAIN=cv. Alaska;
RX PubMed=10744768; DOI=10.1074/jbc.275.14.10702;
RA Kozaki A., Kamada K., Nagano Y., Iguchi H., Sasaki Y.;
RT "Recombinant carboxyltransferase responsive to redox of pea plastidic
RT acetyl-CoA carboxylase.";
RL J. Biol. Chem. 275:10702-10708(2000).
RN [5]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND RNA EDITING.
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).
RN [6]
RP ACTIVITY REGULATION BY REDOX CONTROL, DISULFIDE BOND, AND MUTAGENESIS OF
RP CYS-230; CYS-233; CYS-249; CYS-252; CYS-442 AND CYS-466.
RX PubMed=11546765; DOI=10.1074/jbc.m103525200;
RA Kozaki A., Mayumi K., Sasaki Y.;
RT "Thiol-disulfide exchange between nuclear-encoded and chloroplast-encoded
RT subunits of pea acetyl-CoA carboxylase.";
RL J. Biol. Chem. 276:39919-39925(2001).
RN [7]
RP SUBCELLULAR LOCATION, SUBUNIT, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Little Marvel;
RX PubMed=12054435; DOI=10.1016/s0003-9861(02)00025-5;
RA Thelen J.J., Ohlrogge J.B.;
RT "The multisubunit acetyl-CoA carboxylase is strongly associated with the
RT chloroplast envelope through non-ionic interactions to the
RT carboxyltransferase subunits.";
RL Arch. Biochem. Biophys. 400:245-257(2002).
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; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC -!- ACTIVITY REGULATION: Activated by reductants such as dithiothreitol
CC (DTT), and by thioredoxin in vivo, following exposure to light.
CC {ECO:0000269|PubMed:10744768, ECO:0000269|PubMed:11546765}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=151 nmol/min/mg enzyme {ECO:0000269|PubMed:11078738};
CC Note=Unedited protein has no activity.;
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 inner membrane
CC {ECO:0000305|PubMed:12054435}; Peripheral membrane protein
CC {ECO:0000305|PubMed:12054435}; Stromal side
CC {ECO:0000305|PubMed:12054435}.
CC -!- DEVELOPMENTAL STAGE: Activity was highest in chloroplasts isolated from
CC young, actively dividing leaves. {ECO:0000269|PubMed:12054435}.
CC -!- RNA EDITING: Modified_positions=267 {ECO:0000269|PubMed:10744768,
CC 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; X56315; CAA39754.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X56315; CAA39756.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X56315; CAA39755.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X15268; CAA33339.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X54750; CAA38546.1; ALT_SEQ; Genomic_DNA.
DR PIR; S17920; S17920.
DR RefSeq; YP_003587558.1; NC_014057.1.
DR AlphaFoldDB; P18823; -.
DR SMR; P18823; -.
DR GeneID; 9073106; -.
DR UniPathway; UPA00655; UER00711.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-UniRule.
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 1: Evidence at protein level;
KW ATP-binding; Chloroplast; Direct protein sequencing; Disulfide bond;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Metal-binding; Nucleotide-binding; Plastid;
KW Plastid inner membrane; RNA editing; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..590
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit beta, chloroplastic"
FT /id="PRO_0000199789"
FT DOMAIN 226..590
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT ZN_FING 230..252
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT REGION 292..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT DISULFID 442
FT /note="Interchain (with C-317 in alpha subunit)"
FT /evidence="ECO:0000305|PubMed:11546765"
FT MUTAGEN 230
FT /note="C->A: Almost complete loss of carboxyltransferase
FT activity in E.coli."
FT /evidence="ECO:0000269|PubMed:11546765"
FT MUTAGEN 233
FT /note="C->A: Almost complete loss of carboxyltransferase
FT activity in E.coli."
FT /evidence="ECO:0000269|PubMed:11546765"
FT MUTAGEN 249
FT /note="C->A: Almost complete loss of carboxyltransferase
FT activity in E.coli."
FT /evidence="ECO:0000269|PubMed:11546765"
FT MUTAGEN 252
FT /note="C->A: Complete loss of carboxyltransferase activity
FT in E.coli."
FT /evidence="ECO:0000269|PubMed:11546765"
FT MUTAGEN 442
FT /note="C->A: Loss of redox control, but also considerable
FT loss of carboxyltransferase activity in E.coli."
FT /evidence="ECO:0000269|PubMed:11546765"
FT MUTAGEN 466
FT /note="C->A: Retains 50% carboxyltransferase activity in
FT the presence of DTT in E.coli."
FT /evidence="ECO:0000269|PubMed:11546765"
SQ SEQUENCE 590 AA; 67143 MW; 66EE291425EBEC49 CRC64;
MINEDPSSLT DMDNNIDSWK NNSENSSYSH ADSLADVSNI DNLLSDKIFS IRDSNSNIYD
IYYAYDTNDT NITKYKWTNN INRCIESYLR SQICEDIDFN SDICDKVQRT IIILIRSTND
TNDISDTNDI SDTNDTNDTN AIYDPFDISD TNDTNEIYDP FFILDINDTN DTNDIYGIYD
PDDIYETNIK DICERYSEIY PRNREKSTFV PIDYSDPNCM EKLARLWVQC ETCYGLNFKQ
FFRPKMNICE HCGEHLKMSS SDRIDLLIDR DTWNPMDEDM VSVDPIKFDS IKELGSEEES
SKDRLDEDML SPDPIELDSE EESSKDRVDS EEEKDQSYID RLDSYQEKTG LPETVQTGTD
QREEIHPLFE DIMNQLDLYL QTAKNRVDSE EEKDQSYIDR LDSYQEKTGL PEAVQTGTGQ
LNGIPLALAV MDSEFIAGSM GCVVGEKITR LIEYATNLLL PLIIVCASGG ARMQEGSLSL
MQMAKISSAL YNYQINQKLF YVAILTSPTT GGVTASFGML GDIIIAEPNA TIAFAGKRVI
EQLLNKEVPE GSQSADLLFD RGLLDAVVPR HLLKEFLTEL FQFHGFVPLT
