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
//