ID   MMSA_CAEEL              Reviewed;         523 AA.
AC   P52713;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JUN-2009, entry version 70.
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   Name=alh-8; ORFNames=F13D12.4;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
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.
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DR   EMBL; Z49127; CAA88946.1; -; Genomic_DNA.
DR   PIR; T20828; T20828.
DR   RefSeq; NP_001022078.1; -.
DR   UniGene; Cel.17786; -.
DR   HSSP; Q28399; 1O9J.
DR   DIP; DIP:25038N; -.
DR   IntAct; P52713; 1.
DR   PRIDE; P52713; -.
DR   Ensembl; F13D12.4; Caenorhabditis elegans.
DR   GeneID; 174800; -.
DR   KEGG; cel:F13D12.4; -.
DR   WormBase; WBGene00000114; alh-8.
DR   WormPep; F13D12.4; CE02183.
DR   OMA; P52713; AIFVGES.
DR   BRENDA; 1.2.1.18; 672.
DR   BRENDA; 1.2.1.27; 672.
DR   NextBio; 885562; -.
DR   ArrayExpress; P52713; -.
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   2: Evidence at transcript level;
KW   Complete proteome; Mitochondrion; NAD; Oxidoreductase;
KW   Transit peptide.
FT   TRANSIT       1     22       Mitochondrion (By similarity).
FT   CHAIN        23    523       Probable methylmalonate-semialdehyde
FT                                dehydrogenase [acylating], mitochondrial.
FT                                /FTId=PRO_0000007191.
FT   NP_BIND     199    203       NAD (Potential).
FT   NP_BIND     251    256       NAD (Potential).
FT   ACT_SITE    307    307       Nucleophile (By similarity).
FT   BINDING     407    407       NAD (Potential).
SQ   SEQUENCE   523 AA;  56462 MW;  2871499FE3267A29 CRC64;
     MLSRLARVQP KCQQLAHFST SKSAAAAPTV KLWIDGQAVE SKTTDFVELT NPATNEVIAM
     VPNATQAEMQ AAVDSAKNAF NTWKNTSPLT RQQCMFKLQA LIKRDMKKLA ESITIEQGKT
     LPDAEGDVSR GLQVVEHACS VPSLMMGETL PNVSRDMDTH SYRIPLGVTA GICPFNFPAM
     IPLWMFPVAL ATGNTMVIKP SEQDPGAAQL LVELAKEAGV PDGCVNIIHG QHSAVNFICD
     NPDIKAISFV GGDAAGKHIY ERGAKNGKRV QSNMGAKNHG VIMADANKEQ TLNQLTAAAF
     GAAGQRCMAL TTAVLVGEAR AWLPELVEKA KNLKVNAGWK PDTDIGPLIS KQSKARVLRL
     IESAKKEGAQ VPLDGSNITV PGFENGNFVG PTILAGVKPN MTCYREEIFG PVLVVMEAEN
     LNEAIEIINN NPYGNGTAIF TSNGATARKF TNEVDVGQIG INVPIPVPLP MFSFTGSRGS
     FLGDLNFYGK AGIQFYTQWK TVTQYWNESL TELKPQMSFP QLK
//