MMSA_CAEEL
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 03-AUG-2022, entry version 167.
DE RecName: Full=Probable methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial;
DE Short=MMSDH;
DE Short=Malonate-semialdehyde dehydrogenase [acylating];
DE EC=1.2.1.18;
DE EC=1.2.1.27;
DE Flags: Precursor;
GN Name=alh-8; ORFNames=F13D12.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX 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 investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Plays a role in valine and pyrimidine metabolism. Binds fatty
CC acyl-CoA (By similarity). {ECO:0000250}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxopropanoate + CoA + NAD(+) = acetyl-CoA + CO2 + NADH;
CC Xref=Rhea:RHEA:22992, ChEBI:CHEBI:16526, ChEBI:CHEBI:33190,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.18;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxopropanoate + CoA + NADP(+) = acetyl-CoA + CO2 + NADPH;
CC Xref=Rhea:RHEA:22988, ChEBI:CHEBI:16526, ChEBI:CHEBI:33190,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.2.1.18;
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; Z49127; CAA88946.1; -; Genomic_DNA.
DR PIR; T20828; T20828.
DR RefSeq; NP_001022078.1; NM_001026907.2.
DR AlphaFoldDB; P52713; -.
DR SMR; P52713; -.
DR BioGRID; 40105; 60.
DR DIP; DIP-25038N; -.
DR STRING; 6239.F13D12.4a.3; -.
DR World-2DPAGE; 0011:P52713; -.
DR World-2DPAGE; 0020:P52713; -.
DR EPD; P52713; -.
DR PaxDb; P52713; -.
DR PeptideAtlas; P52713; -.
DR EnsemblMetazoa; F13D12.4a.1; F13D12.4a.1; WBGene00000114.
DR GeneID; 174800; -.
DR KEGG; cel:CELE_F13D12.4; -.
DR UCSC; F13D12.4a.2; c. elegans.
DR CTD; 174800; -.
DR WormBase; F13D12.4a; CE02183; WBGene00000114; alh-8.
DR eggNOG; KOG2449; Eukaryota.
DR HOGENOM; CLU_005391_1_10_1; -.
DR InParanoid; P52713; -.
DR OMA; HGKRAQC; -.
DR OrthoDB; 608999at2759; -.
DR PhylomeDB; P52713; -.
DR Reactome; R-CEL-70895; Branched-chain amino acid catabolism.
DR PRO; PR:P52713; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00000114; Expressed in larva and 4 other tissues.
DR ExpressionAtlas; P52713; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; HDA:WormBase.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; ISS:UniProtKB.
DR GO; GO:0018478; F:malonate-semialdehyde dehydrogenase (acetylating) activity; ISS:UniProtKB.
DR GO; GO:0102662; F:malonate-semialdehyde dehydrogenase (acetylating, NAD+) activity; IEA:RHEA.
DR GO; GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (acylating) activity; ISS:UniProtKB.
DR GO; GO:0006210; P:thymine catabolic process; IBA:GO_Central.
DR GO; GO:0019859; P:thymine metabolic process; ISS:UniProtKB.
DR GO; GO:0006574; P:valine catabolic process; IBA:GO_Central.
DR GO; GO:0006573; P:valine metabolic process; ISS:UniProtKB.
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 3: Inferred from homology;
KW Mitochondrion; NAD; Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 23..523
FT /note="Probable methylmalonate-semialdehyde dehydrogenase
FT [acylating], mitochondrial"
FT /id="PRO_0000007191"
FT ACT_SITE 307
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 199..203
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 251..256
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 407
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
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
