MMSA_AEDAE
ID MMSA_AEDAE Reviewed; 521 AA.
AC Q17M80;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=AAEL001134;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1] {ECO:0000312|EMBL:EAT47764.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
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}.
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DR EMBL; CH477208; EAT47764.1; -; Genomic_DNA.
DR RefSeq; XP_001652386.1; XM_001652336.1.
DR AlphaFoldDB; Q17M80; -.
DR SMR; Q17M80; -.
DR STRING; 7159.AAEL001134-PA; -.
DR GeneID; 5568558; -.
DR KEGG; aag:5568558; -.
DR VEuPathDB; VectorBase:AAEL001134; -.
DR eggNOG; KOG2449; Eukaryota.
DR HOGENOM; CLU_005391_1_10_1; -.
DR InParanoid; Q17M80; -.
DR OMA; HGKRAQC; -.
DR OrthoDB; 608999at2759; -.
DR PhylomeDB; Q17M80; -.
DR Proteomes; UP000008820; Chromosome 3.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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 ?..521
FT /note="Probable methylmalonate-semialdehyde dehydrogenase
FT [acylating], mitochondrial"
FT /id="PRO_0000312823"
FT ACT_SITE 304
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q02252,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 196..200
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 248..253
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 404
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
SQ SEQUENCE 521 AA; 56572 MW; 9FC4A9E85D5F39A7 CRC64;
MALVRLLGVE CRNALQRSYS TASVPTTKMF IDGKFVDSKT TEWIDLHDPA TNKVVTRVPK
CTQDEMESAV ESSKKAFKTW SQTSILGRQQ VMFKLQHLIR NNMSELAKNI TKEQGKTLVD
AEGDVLRGLQ VVEHCCSITS LQMGETVPNI AKDMDTYSYT LPLGVTAGIC PFNFPAMIPL
WMFPVAITCG NTSIIKPSER VPGATMMLME LLNEAGCPPG VVNVIHGAHD AVNFICDNPT
IKAVSFVGSD QAGKYIYERA GRNGKRVQSN MGAKNHGVIM ADANKENTLN QLAGAAFGAA
GQRCMALSTA VFVGEAKQWI PDLVERARKL KVNAGHVPGT DVGPVISPQS KQRINELVES
GVKEGAKLVL DGRSIKVENF ENGNFVGPTI LTDVSTNMKC YTEEIFGPVL VCLTVDTVDE
AVEMINNNPY GNGTAIFTTN GATARKFVNE IDVGQVGVNV PIPVPLPMFS FTGSRGSFMG
DCHFYGKQGV KFYTQTKTVT QLWREGDVSH TKAAVAMPTM K
