AL1B1_RAT
ID AL1B1_RAT Reviewed; 519 AA.
AC Q66HF8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Aldehyde dehydrogenase X, mitochondrial;
DE EC=1.2.1.3;
DE AltName: Full=Aldehyde dehydrogenase family 1 member B1;
DE Flags: Precursor;
GN Name=Aldh1b1; Synonyms=Aldhx;
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 TISSUE=Kidney;
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).
RN [2]
RP PROTEIN SEQUENCE OF 55-75; 162-174; 327-340 AND 444-453, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
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 (By similarity). {ECO:0000250}.
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; BC081884; AAH81884.1; -; mRNA.
DR RefSeq; NP_001011975.1; NM_001011975.1.
DR AlphaFoldDB; Q66HF8; -.
DR SMR; Q66HF8; -.
DR STRING; 10116.ENSRNOP00000015282; -.
DR iPTMnet; Q66HF8; -.
DR PhosphoSitePlus; Q66HF8; -.
DR jPOST; Q66HF8; -.
DR PaxDb; Q66HF8; -.
DR PRIDE; Q66HF8; -.
DR GeneID; 298079; -.
DR KEGG; rno:298079; -.
DR UCSC; RGD:1306737; rat.
DR CTD; 219; -.
DR RGD; 1306737; Aldh1b1.
DR eggNOG; KOG2450; Eukaryota.
DR InParanoid; Q66HF8; -.
DR OrthoDB; 153834at2759; -.
DR PhylomeDB; Q66HF8; -.
DR Reactome; R-RNO-71384; Ethanol oxidation.
DR UniPathway; UPA00780; UER00768.
DR PRO; PR:Q66HF8; -.
DR Proteomes; UP000002494; 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; 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 Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..19
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 20..519
FT /note="Aldehyde dehydrogenase X, mitochondrial"
FT /id="PRO_0000271413"
FT ACT_SITE 287
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 321
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 264..269
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 188
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 53
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 54
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 54
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 366
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 366
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 385
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 385
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 401
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 401
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 428
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 428
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 431
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
SQ SEQUENCE 519 AA; 57625 MW; 6D25E0E806F8EA50 CRC64;
MLNARFLVPR LLCLQGRTTS YSTAAALPNP IPNPEIRYNQ LFINNEWHDA VSKKTFPTVN
PTTGEVIGHV AEGDRADVDL AVRAAREAFR LGSPWRRMDA SERGRLLNRL ADLVERDRVY
LASLETLDNG KPFQESYVLD LDEVIKVYRY LAGWADKWHG KTIPMDGEHF CFTRHEPVGV
CGQIIPWNFP LVMQGWKLAP ALATGNTVVM KVAEQTPLSA LYLASLIKEA GFPPGVVNII
TGYGPTAGAA IAQHMDVDKV AFTGSTEVGH LIQKAAGDSN LKRVTLELGG KSPSIVLADA
DMDHAVDQCH EALFFNMGQC CCAGSRTFVE ESIYHEFLER TVEKAKKRKV GNPFELDTQQ
GPQVDKEQFE KILGYIRLGQ KEGAKLLCGG ERFGERGFFI KPTVFGNVQD DMRIAREEIF
GPVQPLFKFK KIEEVIQRAN NTRYGLAAAV FTRDLDKALY FSQALQAGTV WVNTYNIVTC
HTPFGGFKES GNGRELGEDG LKAYTEVKTV TIKVSEKNS
