MMSA_DROPS
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 03-AUG-2022, entry version 86.
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 ORFNames=GA14712;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1] {ECO:0000312|EMBL:EAL31846.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
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., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., 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: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
CC -!- FUNCTION: Plays a role in valine and pyrimidine metabolism. Binds fatty
CC acyl-CoA (By similarity). {ECO:0000250|UniProtKB:Q02252}.
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 Evidence={ECO:0000250|UniProtKB:Q02252};
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 Evidence={ECO:0000250|UniProtKB:Q02252};
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 Evidence={ECO:0000250|UniProtKB:Q02252};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q02252}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q02252}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL31846.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH379064; EAL31846.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001354791.1; XM_001354755.2.
DR AlphaFoldDB; Q29HB2; -.
DR SMR; Q29HB2; -.
DR STRING; 7237.FBpp0282492; -.
DR EnsemblMetazoa; FBtr0284054; FBpp0282492; FBgn0074739.
DR GeneID; 4815188; -.
DR KEGG; dpo:Dpse_GA14712; -.
DR eggNOG; KOG2449; Eukaryota.
DR HOGENOM; CLU_005391_1_10_1; -.
DR InParanoid; Q29HB2; -.
DR OMA; HGKRAQC; -.
DR PhylomeDB; Q29HB2; -.
DR Proteomes; UP000001819; Chromosome X.
DR Bgee; FBgn0074739; Expressed in female reproductive system and 3 other tissues.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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:0019859; P:thymine metabolic process; ISS:UniProtKB.
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..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..520
FT /note="Probable methylmalonate-semialdehyde dehydrogenase
FT [acylating], mitochondrial"
FT /id="PRO_0000312824"
FT ACT_SITE 303
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q02252,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 195..199
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 247..252
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 403
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
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
