AL1B1_BOVIN
ID AL1B1_BOVIN Reviewed; 511 AA.
AC P52476;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Aldehyde dehydrogenase X, mitochondrial;
DE EC=1.2.1.3;
DE AltName: Full=ALDH class 2;
DE AltName: Full=ALDHX;
DE AltName: Full=Aldehyde dehydrogenase family 1 member B1;
DE Flags: Precursor; Fragment;
GN Name=ALDH1B1; Synonyms=ALDH1B2, ALDH5, ALDHX;
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 GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 284-409.
RC TISSUE=Cornea;
RX PubMed=8493893; DOI=10.1007/978-1-4615-2904-0_17;
RA Algar E.M., Cheung B., Hayes J., Holmes R.S., Beacham I.R.;
RT "Bovine corneal aldehyde dehydrogenases: evidence for multiple gene
RT products (ALDH3 and ALDHX).";
RL Adv. Exp. Med. Biol. 328:153-157(1993).
CC -!- FUNCTION: ALDHs play a major role in the detoxification of alcohol-
CC derived acetaldehyde. They are involved in the metabolism of
CC corticosteroids, biogenic amines, neurotransmitters, and lipid
CC peroxidation. In the cornea, this enzyme may help in the absorption of
CC the damaging UV-B, as well as in the detoxification of the UV-induced
CC peroxidic aldehydes.
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=1.2.1.3;
CC -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol:
CC step 2/2.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AAFC03050684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S61045; AAB26659.1; -; mRNA.
DR PIR; I46935; I46935.
DR AlphaFoldDB; P52476; -.
DR SMR; P52476; -.
DR STRING; 9913.ENSBTAP00000027172; -.
DR PaxDb; P52476; -.
DR PRIDE; P52476; -.
DR eggNOG; KOG2450; Eukaryota.
DR HOGENOM; CLU_005391_0_0_1; -.
DR InParanoid; P52476; -.
DR UniPathway; UPA00780; UER00768.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
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; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Mitochondrion; NAD; Oxidoreductase; Reference proteome;
KW Transit peptide.
FT TRANSIT <1..11
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 12..511
FT /note="Aldehyde dehydrogenase X, mitochondrial"
FT /id="PRO_0000056477"
FT ACT_SITE 279
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 313
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 256..261
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 180
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 45
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 46
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 46
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 75
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 377
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 377
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 393
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 393
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 420
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 420
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 423
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT CONFLICT 308
FT /note="N -> S (in Ref. 2; AAB26659)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 511 AA; 56770 MW; D032C6E84D9799B3 CRC64;
PRLFALHHSA TQYFSAAALP SPIPNPDIPD NQLFISNKWH DAVSKKTFPT VSPATGEVIG
HVAEGDWADV DLAAKAARAA FRLGSPWRWM DALKRGWLLN HLADLVERDC VYLASLESLD
NGKPFQESYV LDLDEVIKVY RYFAGWADKW HGKTIPMDGE HFCFTRHEPV GVCCQIIPWN
FPLVMQSWKL ALALAMGNTV VTKVAEQTPF SALYLASLIK EVGLPPGLVN IVTGYGPTAG
AAIAHHMDIG KVAFTGSTKV GHLIQKAAGN SSLKRVTLEL GGKSLSIVLA DADMDHAVEQ
RQEALFFNMG QCCCPGSWTF IEESIYDEFL ERTVEKAKQR RVGNPFDLDT QQGPQVDRER
FERILGYIQL GQKEGAKLLC GGEHFRQQCF FIKPTVFGGV QDDMRIAREE IFGPVQPLFK
FKKIEEVIER ADNTRYGLAA AVFTQDLDKA MYFTQALQTG TVWVNTYNVV TCHTPLGGFK
EPGNGRELGE DGLKAYTEVK TVTIKVPQKN S
