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   16-JUN-2009, entry version 25.
DE   RecName: Full=Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial;
DE            Short=MMSDH;
DE            Short=MM-ALDH;
DE            EC=1.2.1.27;
DE   AltName: Full=Aldehyde dehydrogenase family 6 member B2;
DE   Flags: Precursor;
GN   Name=ALDH6B2; OrderedLocusNames=At2g14170;
GN   ORFNames=F15N24.6, T22C12.10;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=20083487; 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.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
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.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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).
CC   -!- CATALYTIC ACTIVITY: 2-methyl-3-oxopropanoate + CoA + H(2)O +
CC       NAD(+) = propanoyl-CoA + HCO(3)(-) + NADH.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (Potential).
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   -!- CAUTION: In contrast to other members of the family, the conserved
CC       Glu residue in position 94 is replaced by an Arg. Its activity is
CC       therefore unsure.
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DR   EMBL; AC007197; AAD25855.1; -; Genomic_DNA.
DR   EMBL; AK230004; BAF01828.1; -; mRNA.
DR   IPI; IPI00518167; -.
DR   PIR; H84514; H84514.
DR   RefSeq; NP_179032.1; -.
DR   UniGene; At.43851; -.
DR   HSSP; P51977; 1BXS.
DR   PRIDE; Q0WM29; -.
DR   GeneID; 815903; -.
DR   GenomeReviews; CT485783_GR; AT2G14170.
DR   NMPDR; fig|3702.1.peg.8445; -.
DR   GeneFarm; 4385; -.
DR   TAIR; At2g14170; -.
DR   OMA; Q0WM29; IISNVKP.
DR   BRENDA; 1.2.1.27; 302.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (...; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IDA:TAIR.
DR   GO; GO:0006573; P:valine metabolic process; IEA:InterPro.
DR   InterPro; IPR016160; Ald_DH_CS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH.
DR   InterPro; IPR010061; MeMal-semiAld_DH.
DR   Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
DR   PANTHER; PTHR11699; Aldehyde_dehyd; 1.
DR   PANTHER; PTHR11699:SF27; MMSDH; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   TIGRFAMs; TIGR01722; MMSDH; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Complete proteome; Mitochondrion; NAD;
KW   Oxidoreductase; Transit peptide.
FT   TRANSIT       1     24       Mitochondrion (Potential).
FT   CHAIN        25    607       Methylmalonate-semialdehyde dehydrogenase
FT                                [acylating], mitochondrial.
FT                                /FTId=PRO_0000256067.
FT   NP_BIND     335    340       NAD (By similarity).
FT   ACT_SITE    391    391       Nucleophile (By similarity).
FT   SITE        260    260       Transition state stabilizer (By
FT                                similarity).
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
//