AL3B1_BOVIN
ID AL3B1_BOVIN Reviewed; 468 AA.
AC Q1JPA0; A6QLG7;
DT 14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Aldehyde dehydrogenase family 3 member B1;
DE EC=1.2.1.28 {ECO:0000250|UniProtKB:P43353};
DE EC=1.2.1.5 {ECO:0000250|UniProtKB:P43353};
DE EC=1.2.1.7 {ECO:0000250|UniProtKB:P43353};
DE Flags: Precursor;
GN Name=ALDH3B1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Oxidizes medium and long chain saturated and unsaturated
CC aldehydes. Metabolizes also benzaldehyde. Low activity towards
CC acetaldehyde and 3,4-dihydroxyphenylacetaldehyde. May not metabolize
CC short chain aldehydes. Can use both NADP(+) and NAD(+) as electron
CC acceptor. May have a protective role against the cytotoxicity induced
CC by lipid peroxidation. {ECO:0000250|UniProtKB:P43353}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NADP(+) = a carboxylate + 2 H(+) + NADPH;
CC Xref=Rhea:RHEA:11888, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.2.1.5;
CC Evidence={ECO:0000250|UniProtKB:P43353};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.5;
CC Evidence={ECO:0000250|UniProtKB:P43353};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + hexadecanoate + NADH = H2O + hexadecanal + NAD(+);
CC Xref=Rhea:RHEA:33739, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17600, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P43353};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + octanal = 2 H(+) + NADH + octanoate;
CC Xref=Rhea:RHEA:44100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17935, ChEBI:CHEBI:25646, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P43353};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADP(+) + octanal = 2 H(+) + NADPH + octanoate;
CC Xref=Rhea:RHEA:59904, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17935, ChEBI:CHEBI:25646, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; Evidence={ECO:0000250|UniProtKB:P43353};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzaldehyde + H2O + NADP(+) = benzoate + 2 H(+) + NADPH;
CC Xref=Rhea:RHEA:21660, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16150, ChEBI:CHEBI:17169, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.2.1.7;
CC Evidence={ECO:0000250|UniProtKB:P43353};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzaldehyde + H2O + NAD(+) = benzoate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:11840, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16150, ChEBI:CHEBI:17169, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.28;
CC Evidence={ECO:0000250|UniProtKB:P43353};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexanal + NADP(+) = 2 H(+) + hexanoate + NADPH;
CC Xref=Rhea:RHEA:59908, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17120, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:88528; Evidence={ECO:0000250|UniProtKB:P43353};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-hydroxynon-2-enal + H2O + NADP(+) = (E)-4-hydroxynon-2-
CC enoate + 2 H(+) + NADPH; Xref=Rhea:RHEA:59912, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58968, ChEBI:CHEBI:142920;
CC Evidence={ECO:0000250|UniProtKB:P43353};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-octenal + H2O + NADP(+) = (2E)-octenoate + 2 H(+) +
CC NADPH; Xref=Rhea:RHEA:59916, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:61748,
CC ChEBI:CHEBI:143526; Evidence={ECO:0000250|UniProtKB:P43353};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-octenal + H2O + NAD(+) = (2E)-octenoate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:59920, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:61748,
CC ChEBI:CHEBI:143526; Evidence={ECO:0000250|UniProtKB:P43353};
CC -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol:
CC step 2/2.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}. Note=Primarily in the plasma membrane as well as in some
CC punctate structures in the cytoplasm. {ECO:0000250}.
CC -!- PTM: Dually lipidated in the C-terminus; prenylation occurs prior to,
CC and is a prerequisite for palmitoylation. It is also required for
CC activity towards long-chain substrates. {ECO:0000250|UniProtKB:Q80VQ0}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; BT025453; ABF57409.1; -; mRNA.
DR EMBL; BT026328; ABG81484.1; -; mRNA.
DR EMBL; BC147958; AAI47959.1; -; mRNA.
DR RefSeq; NP_001068986.1; NM_001075518.1.
DR RefSeq; XP_005227117.2; XM_005227060.3.
DR RefSeq; XP_005227118.1; XM_005227061.3.
DR RefSeq; XP_005227119.1; XM_005227062.3.
DR AlphaFoldDB; Q1JPA0; -.
DR SMR; Q1JPA0; -.
DR STRING; 9913.ENSBTAP00000042081; -.
DR PaxDb; Q1JPA0; -.
DR PeptideAtlas; Q1JPA0; -.
DR Ensembl; ENSBTAT00000015995; ENSBTAP00000015995; ENSBTAG00000013093.
DR Ensembl; ENSBTAT00000017408; ENSBTAP00000017408; ENSBTAG00000013093.
DR Ensembl; ENSBTAT00000044598; ENSBTAP00000042081; ENSBTAG00000013093.
DR Ensembl; ENSBTAT00000076578; ENSBTAP00000069355; ENSBTAG00000013093.
DR GeneID; 511469; -.
DR KEGG; bta:511469; -.
DR CTD; 221; -.
DR VEuPathDB; HostDB:ENSBTAG00000013093; -.
DR VGNC; VGNC:56255; ALDH3B1.
DR eggNOG; KOG2456; Eukaryota.
DR GeneTree; ENSGT00940000155904; -.
DR HOGENOM; CLU_005391_3_0_1; -.
DR InParanoid; Q1JPA0; -.
DR OMA; AWMKDQK; -.
DR OrthoDB; 646662at2759; -.
DR TreeFam; TF314264; -.
DR Reactome; R-BTA-1660661; Sphingolipid de novo biosynthesis.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR UniPathway; UPA00780; UER00768.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000013093; Expressed in uterine cervix and 102 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0018479; F:benzaldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0018477; F:benzaldehyde dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IBA:GO_Central.
DR GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR PANTHER; PTHR43570; PTHR43570; 1.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036492; ALDH; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell membrane; Lipid metabolism; Lipoprotein; Membrane;
KW Methylation; NAD; Oxidoreductase; Palmitate; Prenylation;
KW Reference proteome.
FT CHAIN 1..465
FT /note="Aldehyde dehydrogenase family 3 member B1"
FT /id="PRO_0000259960"
FT PROPEP 466..468
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000424192"
FT ACT_SITE 210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 244
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT BINDING 188..193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P43353"
FT MOD_RES 465
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 463
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P43353"
FT LIPID 465
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P43353"
FT CONFLICT 27
FT /note="D -> A (in Ref. 2; AAI47959)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="I -> T (in Ref. 2; AAI47959)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 468 AA; 51800 MW; 7D14AF7895810ED8 CRC64;
MDPFADTLQR LREAFVSGRT RPAEFRDAQL KGLSRFLREN KQLLQEALAQ DLHKSAFEAE
VSEISISQNE INLALRNLRT WMKDEKVSKN LATQLDSAFI RKEPFGLVLI LSPWNYPLNL
SLGPLVGALA AGNCVVLKPS EISKNTEKVL AEVLPRYLDQ SCFAVVLGGP QETGRLLEHK
FDYIFFTGNP QVGKIVMTAA AKHLTPVTLE LGGKNPCYVD DNCDPQTVAN RVAFFRCFNA
GQTCVAPDYV LCSPEMQAQL VPALQSAITR FYGDDPQSSP NLGRIISQKH FQRLRGLLSC
GRVVIGGQSD ECDLYIAPTV LVDVQETDPV MQEEIFGPIL PIVNVRSLGQ AIDFINRREK
PLALYAFSNS SQVVKRVLAQ TSSGGFCGND GFMHLTLASL PFGGVGSSGM GNYHGKFSFD
TFSHHRACLL RRPGLEKIYA IRYPPHTPRN LRVLLMAMET RSCSCTLL
