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Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic (ACCase subunit beta) (Acetyl-CoA carboxylase carboxyltransferase subunit beta) (EC 6.4.1.2)

 ACCD_PEA                Reviewed;         590 AA.
P18823;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
24-NOV-2009, sequence version 3.
22-NOV-2017, entry version 93.
RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01395};
Short=ACCase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395};
Short=Acetyl-CoA carboxylase carboxyltransferase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395};
EC=6.4.1.2 {ECO:0000255|HAMAP-Rule:MF_01395};
Name=accD {ECO:0000255|HAMAP-Rule:MF_01395}; Synonyms=ycf11, zfpA;
Pisum sativum (Garden pea).
Plastid; Chloroplast.
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Fabeae; Pisum.
NCBI_TaxID=3888;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
STRAIN=cv. Alaska;
PubMed=1807835; DOI=10.1007/BF00317074;
Nagano Y., Matsuno R., Sasaki Y.;
"Sequence and transcriptional analysis of the gene cluster trnQ-zfpA-
psaI-ORF231-petA in pea chloroplasts.";
Curr. Genet. 20:431-436(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 220-590.
STRAIN=cv. Alaska;
PubMed=2505231; DOI=10.1093/nar/17.15.6217;
Sasaki Y., Nagano Y., Morioka S., Ishikawa H., Matsuno R.;
"A chloroplast gene encoding a protein with one zinc finger.";
Nucleic Acids Res. 17:6217-6227(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-590.
STRAIN=cv. Alaska;
PubMed=1913879; DOI=10.1007/BF00309603;
Smith A.G., Wilson R.J., Kaethner T.M., Willey D.L., Gray J.C.;
"Pea chloroplast genes encoding a 4 kDa polypeptide of photosystem I
and a putative enzyme of C1 metabolism.";
Curr. Genet. 19:403-410(1991).
[4]
PROTEIN SEQUENCE OF 1-17, RNA EDITING, AND ENZYME REGULATION BY REDOX
CONTROL.
STRAIN=cv. Alaska;
PubMed=10744768; DOI=10.1074/jbc.275.14.10702;
Kozaki A., Kamada K., Nagano Y., Iguchi H., Sasaki Y.;
"Recombinant carboxyltransferase responsive to redox of pea plastidic
acetyl-CoA carboxylase.";
J. Biol. Chem. 275:10702-10708(2000).
[5]
BIOPHYSICOCHEMICAL PROPERTIES, AND RNA EDITING.
PubMed=11078738; DOI=10.1074/jbc.M008166200;
Sasaki Y., Kozaki A., Ohmori A., Iguchi H., Nagano Y.;
"Chloroplast RNA editing required for functional acetyl-CoA
carboxylase in plants.";
J. Biol. Chem. 276:3937-3940(2001).
[6]
ENZYME REGULATION BY REDOX CONTROL, DISULFIDE BOND, AND MUTAGENESIS OF
CYS-230; CYS-233; CYS-249; CYS-252; CYS-442 AND CYS-466.
PubMed=11546765; DOI=10.1074/jbc.M103525200;
Kozaki A., Mayumi K., Sasaki Y.;
"Thiol-disulfide exchange between nuclear-encoded and chloroplast-
encoded subunits of pea acetyl-CoA carboxylase.";
J. Biol. Chem. 276:39919-39925(2001).
[7]
SUBCELLULAR LOCATION, SUBUNIT, AND DEVELOPMENTAL STAGE.
STRAIN=cv. Little Marvel;
PubMed=12054435; DOI=10.1016/S0003-9861(02)00025-5;
Thelen J.J., Ohlrogge J.B.;
"The multisubunit acetyl-CoA carboxylase is strongly associated with
the chloroplast envelope through non-ionic interactions to the
carboxyltransferase subunits.";
Arch. Biochem. Biophys. 400:245-257(2002).
-!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC)
complex. Biotin carboxylase (BC) catalyzes the carboxylation of
biotin on its carrier protein (BCCP) and then the CO(2) group is
transferred by the transcarboxylase to acetyl-CoA to form malonyl-
CoA. {ECO:0000255|HAMAP-Rule:MF_01395}.
-!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate
+ malonyl-CoA. {ECO:0000255|HAMAP-Rule:MF_01395}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
Note=Binds 1 zinc ion per subunit. {ECO:0000305};
-!- ENZYME REGULATION: Activated by reductants such as dithiothreitol
(DTT), and by thioredoxin in vivo, following exposure to light.
{ECO:0000269|PubMed:10744768, ECO:0000269|PubMed:11546765}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
Vmax=151 nmol/min/mg enzyme {ECO:0000269|PubMed:11078738};
Note=Unedited protein has no activity.;
-!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
from acetyl-CoA: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01395}.
-!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of
biotin carboxyl carrier protein, biotin carboxylase and 2 subunits
each of ACCase subunit alpha and ACCase plastid-coded subunit beta
(accD). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
{ECO:0000305|PubMed:12054435}; Peripheral membrane protein
{ECO:0000305|PubMed:12054435}; Stromal side
{ECO:0000305|PubMed:12054435}.
-!- DEVELOPMENTAL STAGE: Activity was highest in chloroplasts isolated
from young, actively dividing leaves.
{ECO:0000269|PubMed:12054435}.
-!- RNA EDITING: Modified_positions=267 {ECO:0000269|PubMed:10744768,
ECO:0000269|PubMed:11078738};
-!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000255|HAMAP-
Rule:MF_01395}.
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EMBL; X56315; CAA39754.1; ALT_SEQ; Genomic_DNA.
EMBL; X56315; CAA39756.1; ALT_SEQ; Genomic_DNA.
EMBL; X56315; CAA39755.1; ALT_SEQ; Genomic_DNA.
EMBL; X15268; CAA33339.1; ALT_SEQ; Genomic_DNA.
EMBL; X54750; CAA38546.1; ALT_SEQ; Genomic_DNA.
PIR; S17920; S17920.
RefSeq; YP_003587558.1; NC_014057.1.
SMR; P18823; -.
PRIDE; P18823; -.
GeneID; 9073106; -.
UniPathway; UPA00655; UER00711.
GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
HAMAP; MF_01395; AcetylCoA_CT_beta; 1.
InterPro; IPR034733; AcCoA_carboxyl.
InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
InterPro; IPR011762; COA_CT_N.
Pfam; PF01039; Carboxyl_trans; 1.
PRINTS; PR01070; ACCCTRFRASEB.
SUPFAM; SSF52096; SSF52096; 4.
PROSITE; PS50980; COA_CT_NTER; 1.
1: Evidence at protein level;
ATP-binding; Chloroplast; Direct protein sequencing; Disulfide bond;
Fatty acid biosynthesis; Fatty acid metabolism; Ligase;
Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
Nucleotide-binding; Plastid; Plastid inner membrane; RNA editing;
Zinc; Zinc-finger.
CHAIN 1 590 Acetyl-coenzyme A carboxylase carboxyl
transferase subunit beta, chloroplastic.
/FTId=PRO_0000199789.
DOMAIN 226 590 CoA carboxyltransferase N-terminal.
{ECO:0000255|PROSITE-ProRule:PRU01136}.
ZN_FING 230 252 C4-type. {ECO:0000255|HAMAP-
Rule:MF_01395}.
METAL 230 230 Zinc. {ECO:0000305}.
METAL 233 233 Zinc. {ECO:0000305}.
METAL 249 249 Zinc. {ECO:0000305}.
METAL 252 252 Zinc. {ECO:0000305}.
DISULFID 442 442 Interchain (with C-317 in alpha subunit).
{ECO:0000305|PubMed:11546765}.
MUTAGEN 230 230 C->A: Almost complete loss of
carboxyltransferase activity in E.coli.
{ECO:0000269|PubMed:11546765}.
MUTAGEN 233 233 C->A: Almost complete loss of
carboxyltransferase activity in E.coli.
{ECO:0000269|PubMed:11546765}.
MUTAGEN 249 249 C->A: Almost complete loss of
carboxyltransferase activity in E.coli.
{ECO:0000269|PubMed:11546765}.
MUTAGEN 252 252 C->A: Complete loss of
carboxyltransferase activity in E.coli.
{ECO:0000269|PubMed:11546765}.
MUTAGEN 442 442 C->A: Loss of redox control, but also
considerable loss of carboxyltransferase
activity in E.coli.
{ECO:0000269|PubMed:11546765}.
MUTAGEN 466 466 C->A: Retains 50% carboxyltransferase
activity in the presence of DTT in
E.coli. {ECO:0000269|PubMed:11546765}.
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


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