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Database: UniProt
Entry: F1N7K8_BOVIN
LinkDB: F1N7K8_BOVIN
Original site: F1N7K8_BOVIN 
ID   F1N7K8_BOVIN            Unreviewed;       521 AA.
AC   F1N7K8;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 2.
DT   24-JAN-2024, entry version 84.
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:ENSBTAP00000024584.4,
GN   ECO:0000313|VGNC:VGNC:25817};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000024584.4, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000024584.4, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000024584.4,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000024584.4}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000024584.4};
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   AlphaFoldDB; F1N7K8; -.
DR   Ensembl; ENSBTAT00000024584.4; ENSBTAP00000024584.4; ENSBTAG00000018469.4.
DR   VEuPathDB; HostDB:ENSBTAG00000018469; -.
DR   VGNC; VGNC:25817; ALDH6A1.
DR   GeneTree; ENSGT00940000156110; -.
DR   HOGENOM; CLU_005391_1_10_1; -.
DR   TreeFam; TF105651; -.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000018469; Expressed in adult mammalian kidney and 109 other cell types or tissues.
DR   ExpressionAtlas; F1N7K8; baseline and differential.
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:UP000009136}.
FT   DOMAIN          30..498
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
SQ   SEQUENCE   521 AA;  56792 MW;  11078902A6DC5F25 CRC64;
     SSKVNSSWQP ASSFSSSSVP TVKLFIDGKF IESKSDKWID IHNPATNEVI GRVPESTKAE
     MDAAVSSCKR TFPAWADTSI LSRQQVLLRY QQLIKENLKE IARLITLEQG KTLADAEGDV
     FRGLQVVEHA CSVTSLMLGE TMPSITKDMD LYSYRLPLGV CAGIAPFNFP AMIPLWMFPM
     AMVCGNTFLM KPSERVPGAT MLLAKLFQDS GAPDGTLNII HGQHEAVNFI CDHPDIKAIS
     FVGSNQAGEY IFERGSRHGK RVQANMGAKN HGVVMPDANK ENTLNQLVGA AFGAAGQRCM
     ALSTAILLVE RQSCLFLPLP LFVLDSLSFR FIFRDQPGAD LGPLITPQAK ERVCNLIDSG
     TKEGASILLD GRSIKVKGYE NGNFVGPTII SNVKPNMTCY KEEIFGPVLV VLETDTLDEA
     IKIVNDNPYG NGTAIFTTNG ATARKYSHLV DVGQVGVNVP IPVPLPMFSF TGSRASFRGD
     TNFYGKQGIQ FYTQLKTITS QWKEEDASLS SPAVVMPTMG R
//
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