MMSA_ARATH
ID MMSA_ARATH Reviewed; 607 AA.
AC Q0WM29; Q9SI43;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial;
DE Short=MM-ALDH;
DE Short=MMSDH;
DE Short=Malonate-semialdehyde dehydrogenase [acylating];
DE EC=1.2.1.27;
DE AltName: Full=Aldehyde dehydrogenase family 6 member B2;
DE Flags: Precursor;
GN Name=ALDH6B2; OrderedLocusNames=At2g14170; ORFNames=F15N24.6, T22C12.10;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] OF 294-607.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NOMENCLATURE.
RX PubMed=15358267; DOI=10.1016/j.tplants.2004.06.004;
RA Kirch H.-H., Bartels D., Wei Y., Schnable P.S., Wood A.J.;
RT "The ALDH gene superfamily of Arabidopsis.";
RL Trends Plant Sci. 9:371-377(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP LEU-98.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methyl-3-oxopropanoate + CoA + H2O + NAD(+) = H(+) +
CC hydrogencarbonate + NADH + propanoyl-CoA; Xref=Rhea:RHEA:20804,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57700, ChEBI:CHEBI:57945; EC=1.2.1.27;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:25732537}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q0WM29-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
CC -!- CAUTION: In contrast to other members of the family, the conserved Glu
CC residue in position 94 is replaced by an Arg. Its activity is therefore
CC unsure. {ECO:0000305}.
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DR EMBL; AC007197; AAD25855.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06286.1; -; Genomic_DNA.
DR EMBL; AK230004; BAF01828.1; -; mRNA.
DR PIR; H84514; H84514.
DR RefSeq; NP_179032.1; NM_126989.2. [Q0WM29-1]
DR AlphaFoldDB; Q0WM29; -.
DR SMR; Q0WM29; -.
DR BioGRID; 1263; 3.
DR STRING; 3702.AT2G14170.1; -.
DR MetOSite; Q0WM29; -.
DR PaxDb; Q0WM29; -.
DR PRIDE; Q0WM29; -.
DR ProteomicsDB; 237159; -. [Q0WM29-1]
DR EnsemblPlants; AT2G14170.1; AT2G14170.1; AT2G14170. [Q0WM29-1]
DR GeneID; 815903; -.
DR Gramene; AT2G14170.1; AT2G14170.1; AT2G14170. [Q0WM29-1]
DR KEGG; ath:AT2G14170; -.
DR Araport; AT2G14170; -.
DR TAIR; locus:2059456; AT2G14170.
DR eggNOG; KOG2449; Eukaryota.
DR InParanoid; Q0WM29; -.
DR OrthoDB; 608999at2759; -.
DR PhylomeDB; Q0WM29; -.
DR BioCyc; ARA:AT2G14170-MON; -.
DR PRO; PR:Q0WM29; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q0WM29; baseline and differential.
DR Genevisible; Q0WM29; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0018478; F:malonate-semialdehyde dehydrogenase (acetylating) activity; IBA:GO_Central.
DR GO; GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (acylating) activity; IBA:GO_Central.
DR GO; GO:0006210; P:thymine catabolic process; IBA:GO_Central.
DR GO; GO:0006574; P:valine catabolic process; IBA:GO_Central.
DR CDD; cd07085; ALDH_F6_MMSDH; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR010061; MeMal-semiAld_DH.
DR PANTHER; PTHR43866; PTHR43866; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR01722; MMSDH; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Mitochondrion; NAD; Oxidoreductase;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..98
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 99..607
FT /note="Methylmalonate-semialdehyde dehydrogenase
FT [acylating], mitochondrial"
FT /id="PRO_0000256067"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 391
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 335..340
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 260
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 607 AA; 65927 MW; 0257A3606B31165C CRC64;
MVRVKQKNLE SYRSNGTYPP TWRNPTTSFA PDQHRVSIHS SLKSKTKRRR LYKEADDNTK
LRSSSSTTTT TTTMLLRISG NNLRPLRPQF LALRSSWLST SPEQSTQPQM PPRVPNLIGG
SFVESQSSSF IDVINPATQE VVSKVPLTTN EEFKAAVSAA KQAFPLWRNT PITTRQRVML
KFQELIRKNM DKLAMNITTE QGKTLKDSHG DIFRGLEVVE HACGMATLQM GEYLPNVSNG
VDTYSIREPL GVCAGICPFN FPAMIPLWMF PVAVTCGNTF ILKPSEKDPG ASVILAELAM
EAGLPDGVLN IVHGTNDTVN AICDDEDIRA VSFVGSNTAG MHIYARAAAK GKRIQSNMGA
KNHGLVLPDA NIDATLNALL AAGFGAAGQR CMALSTVVFV GDAKSWEDKL VERAKALKVT
CGSEPDADLG PVISKQAKER ICRLIQSGVD DGAKLLLDGR DIVVPGYEKG NFIGPTILSG
VTPDMECYKE EIFGPVLVCM QANSFDEAIS IINKNKYGNG AAIFTSSGAA ARKFQMDIEA
GQIGINVPIP VPLPFFSFTG NKASFAGDLN FYGKAGVDFF TQIKTVTQQW KDIPTSVSLA
MPTSQKQ
