AL3B1_RAT
ID AL3B1_RAT Reviewed; 468 AA.
AC Q5XI42;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway; TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; BC083850; AAH83850.1; -; mRNA.
DR RefSeq; NP_001006999.1; NM_001006998.1.
DR RefSeq; XP_006230849.1; XM_006230787.3.
DR RefSeq; XP_008758356.1; XM_008760134.1.
DR AlphaFoldDB; Q5XI42; -.
DR SMR; Q5XI42; -.
DR BioGRID; 259282; 1.
DR STRING; 10116.ENSRNOP00000023789; -.
DR PhosphoSitePlus; Q5XI42; -.
DR PaxDb; Q5XI42; -.
DR Ensembl; ENSRNOT00000023789; ENSRNOP00000023789; ENSRNOG00000017512.
DR GeneID; 309147; -.
DR KEGG; rno:309147; -.
DR UCSC; RGD:1359546; rat.
DR CTD; 221; -.
DR RGD; 1359546; Aldh3b1.
DR eggNOG; KOG2456; Eukaryota.
DR GeneTree; ENSGT00940000162915; -.
DR HOGENOM; CLU_005391_3_1_1; -.
DR InParanoid; Q5XI42; -.
DR OrthoDB; 646662at2759; -.
DR PhylomeDB; Q5XI42; -.
DR TreeFam; TF314264; -.
DR Reactome; R-RNO-1660661; Sphingolipid de novo biosynthesis.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR UniPathway; UPA00780; UER00768.
DR PRO; PR:Q5XI42; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000017512; Expressed in ovary and 19 other tissues.
DR ExpressionAtlas; Q5XI42; baseline and differential.
DR Genevisible; Q5XI42; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; ISO:RGD.
DR GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; ISO:RGD.
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:0046185; P:aldehyde catabolic process; ISO:RGD.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:RGD.
DR GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; ISO:RGD.
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; IPR016160; Ald_DH_CS_CYS.
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; PS00070; ALDEHYDE_DEHYDR_CYS; 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_0000056483"
FT PROPEP 466..468
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000424195"
FT ACT_SITE 210
FT /evidence="ECO:0000250"
FT ACT_SITE 244
FT /evidence="ECO:0000250"
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 462
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q80VQ0"
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"
SQ SEQUENCE 468 AA; 52147 MW; 47AA217F9DC48935 CRC64;
MDSFEDKLQQ LREAFNAGRT RSAEFRAAQL QGLSHFLRDN KQQLQEALAQ DLHKSAFESE
VSEIAISQAE VDLALRNLRS WMKDEKVSKN LATQLDSAFI RKEPFGLVLI IVPWNYPLNL
TLVPLVGAIA AGNCVVLKPS EISKATEKIL AEVLPRYLDQ SCFAVVLGGP QETGQLLEHR
FDYIFFTGNT YVGKIVMAAA AKHLTPITLE LGGKNPCYVD DNCDPQTVAN RVAWFRYFNA
GQTCVAPDYV LCSQEMQERL VPALQNAITR FYGDNPQTSP NLGRIINQKH FERLQGLLGC
GRVAIGGQSD EGERYIAPTV LVDVQETEPV MQEEIFGPIL PLVTVTNLDE AIEFINRREK
PLALYAFSKR SQVIKQVLAR TSSGGFCGND GFMHMTLSSL PFGGVGTSGM GRYHGKFSFD
TFSNQRACLL RSPGMEKIND LRYPPYTSRN LRVLLVAMEK RCCSCTLL
