ACCA_PEA
ID ACCA_PEA Reviewed; 875 AA.
AC Q41008; Q9MBB4;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha, chloroplastic;
DE Short=ACCase subunit alpha;
DE Short=Acetyl-CoA carboxylase carboxyltransferase subunit alpha;
DE EC=2.1.3.15;
DE AltName: Full=pIEP96;
DE Flags: Precursor;
GN Name=ACCA;
OS Pisum sativum (Garden pea).
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 [MRNA], VARIANTS SER-313; LEU-452 AND GLU-631, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Miranda;
RX PubMed=7766898; DOI=10.1007/bf00020890;
RA Hirsch S., Soll J.;
RT "Import of a new chloroplast inner envelope protein is greatly stimulated
RT by potassium phosphate.";
RL Plant Mol. Biol. 27:1173-1181(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 51-875, PROTEIN SEQUENCE OF 51-62, AND
RP ACTIVITY REGULATION.
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 [3]
RP BIOPHYSICOCHEMICAL PROPERTIES.
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 [4]
RP ACTIVITY REGULATION, DISULFIDE BOND, AND MUTAGENESIS OF CYS-297 AND
RP CYS-317.
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 [5]
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 First, biotin carboxylase catalyzes the carboxylation of biotin on its
CC carrier protein (BCCP) and then the CO(2) group is transferred by the
CC carboxyltransferase to acetyl-CoA to form malonyl-CoA (By similarity).
CC {ECO:0000250}.
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 -!- 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 -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1.
CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of biotin
CC carboxyl carrier protein, biotin carboxylase and two subunits each of
CC ACCase subunit alpha and ACCase plastid-coded subunit beta (accD).
CC {ECO:0000305|PubMed:12054435}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000305|PubMed:12054435, ECO:0000305|PubMed:7766898}; Peripheral
CC membrane protein {ECO:0000305|PubMed:12054435,
CC ECO:0000305|PubMed:7766898}; Stromal side {ECO:0000305|PubMed:12054435,
CC ECO:0000305|PubMed:7766898}.
CC -!- DEVELOPMENTAL STAGE: Activity is highest in chloroplasts isolated from
CC young, actively dividing leaves (at protein level).
CC {ECO:0000269|PubMed:12054435}.
CC -!- SIMILARITY: Belongs to the AccA family. {ECO:0000305}.
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DR EMBL; Z31559; CAA83434.1; -; mRNA.
DR EMBL; AB029556; BAA94752.1; -; mRNA.
DR PIR; S56667; S56667.
DR AlphaFoldDB; Q41008; -.
DR SMR; Q41008; -.
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:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_00823; AcetylCoA_CT_alpha; 1.
DR InterPro; IPR001095; Acetyl_CoA_COase_a_su.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR PANTHER; PTHR42853; PTHR42853; 2.
DR Pfam; PF03255; ACCA; 1.
DR PRINTS; PR01069; ACCCTRFRASEA.
DR SUPFAM; SSF52096; SSF52096; 1.
DR TIGRFAMs; TIGR00513; accA; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chloroplast; Coiled coil; Direct protein sequencing;
KW Disulfide bond; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Nucleotide-binding;
KW Plastid; Plastid inner membrane; Transferase; Transit peptide.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:10744768"
FT CHAIN 51..875
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit alpha, chloroplastic"
FT /id="PRO_0000389652"
FT DOMAIN 128..380
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT REGION 845..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 664..705
FT /evidence="ECO:0000255"
FT COMPBIAS 845..869
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 317
FT /note="Interchain (with C-442 in beta subunit)"
FT /evidence="ECO:0000305|PubMed:11546765"
FT VARIANT 313
FT /note="M -> S (in strain: cv. Miranda)"
FT /evidence="ECO:0000269|PubMed:7766898"
FT VARIANT 452
FT /note="F -> L (in strain: cv. Miranda)"
FT /evidence="ECO:0000269|PubMed:7766898"
FT VARIANT 631
FT /note="V -> E (in strain: cv. Miranda)"
FT /evidence="ECO:0000269|PubMed:7766898"
FT MUTAGEN 297
FT /note="C->A: Loss of 30% of carboxyltransferase activity in
FT E.coli."
FT /evidence="ECO:0000269|PubMed:11546765"
FT MUTAGEN 317
FT /note="C->A: Loss of redox control, also 20% loss of
FT carboxyltransferase activity in E.coli."
FT /evidence="ECO:0000269|PubMed:11546765"
SQ SEQUENCE 875 AA; 96421 MW; 61CE277A9FC3E7C9 CRC64;
MASSSATLVG STASDLLRSS TTGFTGVPLR TLGRAGLVLK RRDLTVSVTA KLRKVKRREY
PWSSNPDPNM KGGRLRHLST FQPLKQPPKP VILEFEKPLI NMEKKINDFR KVAEKTGVDL
SDQILALEAK YQKALVELYT NLTPIQRVTV ARHPNRPTFL DHMYNMTEKF VELHGDREGY
DDPAIAAGLG SIDGKTYMFI GHQKGRDTKE NIKRNFAMPT PHGYRKALRL MEYADHHGFP
IVTFIDTPGA FADLKSEQLG QGEAIAHNLR SMFALKVPVI SIVIGEGGSG GALAIGCANK
LLMLENSVFF VAMPEACGAI LWKSNKAAPK AAERLKITAS ALLDLEIADG IIPEPLAGAH
TDPSWMSQQI KIAINEAMDE LTKLSTEDLI KDRMHKFRKL GVDGIQEGIP LVPSKKVNTK
KREIGVPPKR QEVPIPDSQI EAEIEKLKKA IFEGEDSSAA KKNPGSQIGS AIDKLKGLFL
EGKDSSAAKK TPGSQIVAEL DKLKGLYLEA KDSSAAKVPG SQIVAEIEKL KNSIFEDEDS
SSAVLPEKIP GSEIAVEIAK LKKNILEGKD SSSEPSKLDL DKTIETLKRE VNREFSEAVK
AAGLTKTLTK LRGEISKAKA GNQPLTPLLK VEIKSFNQRL SAAPNSRKLL KKRGLLREVT
KVKLLLDKNK AATRKQELKK KSDEHKEAAR LEQELKKKFD EVMDTPRIKE KYEALRSEVR
RVDASSGSGL DDELKKKIIE FNKEVDLELA TAVKSVGLEV ESVKPGHGWN KSSVPEIEEL
NKDVQKEIEI VANSSPNVKR LIEQLKLEVA KSGGKPDSES KSRIDALTQQ IKKSLAEAVD
SPSLKEKYEN LTRPAGDTLT DDKLREKVGV NRNFS
