AL1B1_PONAB
ID AL1B1_PONAB Reviewed; 517 AA.
AC Q5R6B5;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR860576; CAH92701.1; -; mRNA.
DR RefSeq; NP_001127576.1; NM_001134104.1.
DR AlphaFoldDB; Q5R6B5; -.
DR SMR; Q5R6B5; -.
DR STRING; 9601.ENSPPYP00000021352; -.
DR GeneID; 100174654; -.
DR KEGG; pon:100174654; -.
DR CTD; 219; -.
DR eggNOG; KOG2450; Eukaryota.
DR InParanoid; Q5R6B5; -.
DR OrthoDB; 153834at2759; -.
DR UniPathway; UPA00780; UER00768.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
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 2: Evidence at transcript level;
KW Acetylation; Mitochondrion; NAD; Oxidoreductase; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..17
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 18..517
FT /note="Aldehyde dehydrogenase X, mitochondrial"
FT /id="PRO_0000271412"
FT ACT_SITE 285
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 319
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 262..267
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 186
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 51
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 52
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 52
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 81
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 364
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 364
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 383
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 383
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 399
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 399
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 414
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 414
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 426
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 426
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
FT MOD_RES 429
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZS1"
SQ SEQUENCE 517 AA; 57261 MW; 105F47E5840D4229 CRC64;
MLRFLAPRLL SLQGRTARYS SAAALPSPIL NPDIPYNQLF INNEWQDAVS KKTFPTVNPT
TGEVIGHVAE GDRADVDRAV KAAREAFRLG SPWRRMDASE RGRLLNCLAD LVERDRVYLA
SLETLDNGKP FQESYALDLD EVIKVYRYFA GWADKWHGKT IPMDGQHFCF TRHEPIGVCG
QIIPWNFPLV MQGWKLAPAL ATGNTVVMKV AEQTPLSALY LASLIKEAGF PPGVVNIITG
YGPTAGAAIA QHMDVDKVAF TGSTEVGHLI QKAAGDSNLK RVTLELGGKS PSIVLADADM
EHAVEQCHEA LFFNMGQCCC AGSRTFVEES IYNEFLERTV EKAKQRKVGN PFELDTQQGP
QVDKEQFERV LGYIQLGQKE GAKLLCGGER FGERGFFIKP TVFGGVQDDM RIAKEEIFGP
VQPLFKFKKM EEVIERANTT RYGLAAAVFT RDLDKAMYFT QALQAGTVWV NTYNIVTCHT
PFGGFKESGN GRELGEDGLK AYTEVKTVTI KVPQKNS
