ID   MMSA_DROPS              Reviewed;         520 AA.
AC   Q29HB2;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=Probable methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial;
DE            Short=MMSDH;
DE            Short=Malonate-semialdehyde dehydrogenase [acylating];
DE            EC=1.2.1.27;
DE            EC=1.2.1.18;
DE   Flags: Precursor;
GN   ORFNames=GA14712;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P.,
RA   Couronne O., Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J.,
RA   van Batenburg M.F., Howells S.L., Scherer S.E., Sodergren E.,
RA   Matthews B.B., Crosby M.A., Schroeder A.J., Ortiz-Barrientos D.,
RA   Rives C.M., Metzker M.L., Muzny D.M., Scott G., Steffen D.,
RA   Wheeler D.A., Worley K.C., Havlak P., Durbin K.J., Egan A., Gill R.,
RA   Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y., Waldron L.,
RA   Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura:
RT   chromosomal, gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
CC   -!- FUNCTION: Plays a role in valine and pyrimidine metabolism. Binds
CC       fatty acyl-CoA (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2-methyl-3-oxopropanoate + CoA + H(2)O +
CC       NAD(+) = propanoyl-CoA + HCO(3)(-) + NADH.
CC   -!- CATALYTIC ACTIVITY: 3-oxopropanoate + CoA + NAD(P)(+) = acetyl-CoA
CC       + CO(2) + NAD(P)H.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL31846.1; Type=Erroneous gene model prediction;
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DR   EMBL; CH379064; EAL31846.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001354791.1; -.
DR   GeneID; 4815188; -.
DR   KEGG; dpo:Dpse_GA14712; -.
DR   FlyBase; FBgn0074739; Dpse\GA14712.
DR   OMA; Q29HB2; IISNVKP.
DR   BRENDA; 1.2.1.18; 190795.
DR   BRENDA; 1.2.1.27; 190795.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0000062; F:acyl-CoA binding; ISS:UniProtKB.
DR   GO; GO:0018478; F:malonate-semialdehyde dehydrogenase (acetyl...; ISS:UniProtKB.
DR   GO; GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (...; ISS:UniProtKB.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0019859; P:thymine metabolic process; ISS:UniProtKB.
DR   GO; GO:0006573; P:valine metabolic process; ISS:UniProtKB.
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   3: Inferred from homology;
KW   Complete proteome; Mitochondrion; NAD; Oxidoreductase;
KW   Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    520       Probable methylmalonate-semialdehyde
FT                                dehydrogenase [acylating], mitochondrial.
FT                                /FTId=PRO_0000312824.
FT   NP_BIND     195    199       NAD (Potential).
FT   NP_BIND     247    252       NAD (Potential).
FT   ACT_SITE    303    303       Nucleophile (By similarity).
FT   BINDING     403    403       NAD (Potential).
SQ   SEQUENCE   520 AA;  56064 MW;  E8336961D816B35D CRC64;
     MAFLRAIGAE ARYLTQRAYS SAAPTTKLFI DGKFVESKTK EWIDVHDPAT NKVVTRVPKA
     TQDEMQTALE SNKKAFRSWS NQSILTRQAV MFKLQALIKE NMGELAKNIT KEQGKTLADA
     EGDVLRGLQV VEHCCSIPSL QMGETVANVA RDMDTYSLVM PLGVTAGIAP FNFPAMIPLW
     MFPVAITTGN TMLLKPSERV PGATMLLMEL LNEAGCPPGV VNVIHGQHDA VNFICDAPAI
     KAVSFVGSDQ AGKYIYERAG KNGKRVQSNM GAKNHGVILS DANKENTLNQ LAGAAFGAAG
     QRCMALSTAV FVGDAQGWIP DLVERAQKLK VNAGHVPGTD VGPVISAASR QRINDLIESG
     VKEGAKLILD GRKISVPGFE DGYFVGPTIL SDVTPSMKCY TEEIFGPVLV ILKADNLDDA
     IDIVNANPYG NGTAVFTTNG AAARKFVNEI DAGQVGVNVP IPVPLPMFSF TGTRGSFRGD
     HHFYGKQGIK FYTQTKTVTQ LWRETDVNHT QAAVAMPTMK
//