ID   I3IWX8_ORENI            Unreviewed;       501 AA.
AC   I3IWX8;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=methylmalonate-semialdehyde dehydrogenase (CoA acylating) {ECO:0000256|ARBA:ARBA00013048};
DE            EC=1.2.1.27 {ECO:0000256|ARBA:ARBA00013048};
GN   Name=ALDH6A1 {ECO:0000313|Ensembl:ENSONIP00000001118.2};
OS   Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000001118.2, ECO:0000313|Proteomes:UP000005207};
RN   [1] {ECO:0000313|Proteomes:UP000005207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Broad Institute Genome Assembly Team;
RG   Broad Institute Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSONIP00000001118.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00036429};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20805;
CC         Evidence={ECO:0000256|ARBA:ARBA00036429};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxopropanoate + CoA + H2O + NAD(+) = acetyl-CoA + H(+) +
CC         hydrogencarbonate + NADH; Xref=Rhea:RHEA:76615, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:33190,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.27;
CC         Evidence={ECO:0000256|ARBA:ARBA00036793};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76616;
CC         Evidence={ECO:0000256|ARBA:ARBA00036793};
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   AlphaFoldDB; I3IWX8; -.
DR   STRING; 8128.ENSONIP00000001119; -.
DR   Ensembl; ENSONIT00000001117.2; ENSONIP00000001118.2; ENSONIG00000000884.2.
DR   eggNOG; KOG2449; Eukaryota.
DR   GeneTree; ENSGT00940000156110; -.
DR   HOGENOM; CLU_005391_1_10_1; -.
DR   TreeFam; TF105651; -.
DR   Proteomes; UP000005207; Linkage group LG15.
DR   GO; GO:0018478; F:malonate-semialdehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity; IEA:UniProtKB-EC.
DR   CDD; cd07085; ALDH_F6_MMSDH; 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   NCBIfam; TIGR01722; MMSDH; 1.
DR   PANTHER; PTHR43866; MALONATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43866:SF3; METHYLMALONATE-SEMIALDEHYDE DEHYDROGENASE [ACYLATING], MITOCHONDRIAL; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000005207}.
FT   DOMAIN          19..478
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
SQ   SEQUENCE   501 AA;  54356 MW;  1A1B35BEF162AEED CRC64;
     MCYSSSSVPT TKLFIDGKFV ESNTSEWLDI HNPATNEVVG RVPKATQEEM LAAVDSCSRA
     FRSWSETSIL SRQQIFLRYQ QLIKDNIIAY LGTLLLADFL NPFLAHSSEV VEHACSITSL
     MLGETLPSIT KDMDTYTYRL PIGVCAGIAP FNFPAMIPLW MFPIGMVCGN TYLMKPSERV
     PGCTMLLAKM LQDAGAPDGT LNIIHGQHAA VNFICDHPAI KAISFVGSNQ AGEYIYERGS
     KNGKRVQSNM GAKNHGVVMP DANKENTINQ LVGAAFGAAG QRCMALSTAI FVGESREWLP
     ELVQRSKSLR VNSGDQPGAD VGPLITPEAK ARVESLIQSG VDEGAKLLLD GRNVKVKGYE
     NGNFVGPTIL AGVKANMKCY KEEIFGPVLI VLEADSLDEA ISLINRNPYG NGTAIFTTNG
     ATARKYTHEV DVGQIGVNVP IPVPLPMFSF TGSRGSFRGD TNFYGKQGIQ FYTQIKTVTS
     QWKAEDATLT SPAVTMPTMG R
//