RRAA3_ARATH
ID RRAA3_ARATH Reviewed; 166 AA.
AC Q9FH13; Q53XH2;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase 3;
DE Short=HMG aldolase 3;
DE EC=4.1.3.17;
DE AltName: Full=Oxaloacetate decarboxylase;
DE Short=OAA decarboxylase;
DE EC=4.1.1.112;
DE AltName: Full=Regulator of ribonuclease activity homolog 3;
DE AltName: Full=RraA-like protein 3;
GN OrderedLocusNames=At5g56260; ORFNames=K24C1.7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-
CC oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a
CC secondary oxaloacetate (OAA) decarboxylase activity due to the common
CC pyruvate enolate transition state formed following C-C bond cleavage in
CC the retro-aldol and decarboxylation reactions (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxy-4-methyl-2-oxoglutarate = 2 pyruvate;
CC Xref=Rhea:RHEA:22748, ChEBI:CHEBI:15361, ChEBI:CHEBI:58276;
CC EC=4.1.3.17;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxaloacetate = CO2 + pyruvate; Xref=Rhea:RHEA:15641,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:16526; EC=4.1.1.112;
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC Note=Divalent metal cation. {ECO:0000250};
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class II aldolase/RraA-like family.
CC {ECO:0000305}.
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DR EMBL; AB023029; BAB09117.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96742.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69380.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69381.1; -; Genomic_DNA.
DR EMBL; BT010892; AAR24670.1; -; mRNA.
DR EMBL; BT010934; AAR24712.1; -; mRNA.
DR RefSeq; NP_001331062.1; NM_001345190.1.
DR RefSeq; NP_001331063.1; NM_001345193.1.
DR RefSeq; NP_200437.1; NM_125009.4.
DR AlphaFoldDB; Q9FH13; -.
DR SMR; Q9FH13; -.
DR BioGRID; 20969; 1.
DR IntAct; Q9FH13; 1.
DR STRING; 3702.AT5G56260.1; -.
DR iPTMnet; Q9FH13; -.
DR PaxDb; Q9FH13; -.
DR PRIDE; Q9FH13; -.
DR ProteomicsDB; 228202; -.
DR DNASU; 835725; -.
DR EnsemblPlants; AT5G56260.1; AT5G56260.1; AT5G56260.
DR EnsemblPlants; AT5G56260.2; AT5G56260.2; AT5G56260.
DR EnsemblPlants; AT5G56260.5; AT5G56260.5; AT5G56260.
DR GeneID; 835725; -.
DR Gramene; AT5G56260.1; AT5G56260.1; AT5G56260.
DR Gramene; AT5G56260.2; AT5G56260.2; AT5G56260.
DR Gramene; AT5G56260.5; AT5G56260.5; AT5G56260.
DR KEGG; ath:AT5G56260; -.
DR Araport; AT5G56260; -.
DR TAIR; locus:2156430; AT5G56260.
DR eggNOG; ENOG502S32I; Eukaryota.
DR HOGENOM; CLU_072626_4_1_1; -.
DR InParanoid; Q9FH13; -.
DR PhylomeDB; Q9FH13; -.
DR PRO; PR:Q9FH13; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FH13; baseline and differential.
DR Genevisible; Q9FH13; AT.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0047443; F:4-hydroxy-4-methyl-2-oxoglutarate aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008428; F:ribonuclease inhibitor activity; IEA:InterPro.
DR GO; GO:0051252; P:regulation of RNA metabolic process; IEA:InterPro.
DR CDD; cd16841; RraA_family; 1.
DR InterPro; IPR010203; RraA.
DR InterPro; IPR005493; RraA/RraA-like.
DR InterPro; IPR036704; RraA/RraA-like_sf.
DR Pfam; PF03737; RraA-like; 1.
DR SUPFAM; SSF89562; SSF89562; 1.
DR TIGRFAMs; TIGR01935; NOT-MenG; 1.
PE 1: Evidence at protein level;
KW Acetylation; Lyase; Metal-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..166
FT /note="Putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase
FT 3"
FT /id="PRO_0000209654"
FT BINDING 81..84
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 166 AA; 17567 MW; 88C1CD8CE4FBB73C CRC64;
MAAFATAEAC DSNAELISNG DLRALHPIFK IYGQRRCFSG PIVTLKVFED NVLVRNQLET
KGEGGVLVID GGGSMRCALV GGNLGQLAQN NGWSGIVVNG CVRDVDEIND CDVGVRALGS
NPLKSTKKGH GEKNVPVHIG GTLIRDGEWL YADSDGILIS KTELSV
