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Database: UniProt
Entry: I3N6F6_ICTTR
LinkDB: I3N6F6_ICTTR
Original site: I3N6F6_ICTTR 
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
//
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