ID I3N6F6_ICTTR Unreviewed; 533 AA.
AC I3N6F6;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 67.
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:ENSSTOP00000019952.1};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000019952.1, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000019952.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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};
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DR EMBL; AGTP01020488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01020489; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005321285.1; XM_005321228.2.
DR AlphaFoldDB; I3N6F6; -.
DR STRING; 43179.ENSSTOP00000019952; -.
DR Ensembl; ENSSTOT00000029919.2; ENSSTOP00000019952.1; ENSSTOG00000028534.2.
DR GeneID; 101977987; -.
DR CTD; 4329; -.
DR eggNOG; KOG2449; Eukaryota.
DR GeneTree; ENSGT00940000156110; -.
DR HOGENOM; CLU_005391_1_10_1; -.
DR InParanoid; I3N6F6; -.
DR OMA; HGKRAQC; -.
DR OrthoDB; 275238at2759; -.
DR TreeFam; TF105651; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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 GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
DR GO; GO:0006210; P:thymine catabolic process; IEA:Ensembl.
DR GO; GO:0006574; P:valine catabolic process; IEA:Ensembl.
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:UP000005215}.
FT DOMAIN 46..510
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 533 AA; 57829 MW; C6AD6AD72AE989C6 CRC64;
MAAVVAAATV RSRILQVSSK VHSTWYPASS FSSSVPTVKL FIDGKFVESK SDKWIDIHNP
ATNEVISRVP QSTKAEMDAA VASCKRAFPA WADTSVLSRQ QVLLRYQQLI KENLKEIAKL
ITLEQGKTLA DAEGDVFRGL QVVEHACSVT SLMLGETMPS ITKDMDLYSY RLPLGVCAGI
APFNFPAMIP LWMFPMAMVC GNTFLMKPSE RVPGATMLLA KLLQDSGAPD GTLNIIHGQH
EAVNFICDHP DIKAISFVGS NQAGEYIFER GSRHGKRVQA NMGAKNHGVV MPDANKENTL
NQLVGAAFGA AGQRCMALST AILVGEAKKW LPELVERAKK LRVNAGDQPG ADLGPLITPQ
AKERVCNLID SGTKEGASIL LDGRKIKVKG YENGNFVGPT IISNVKPNMT CYKEEIFGPV
LVVLETETLD EAIKIVNDNP YGNGTAIFTT NGATARKYSH LVDVGQVGVN VPIPVPLPMF
SFTGSRSSFR GDTNFYGKQG IQFYTQLKTI TSQWKEEDAT LSSPAVVMPT MGR
//