AL1A7_RAT
ID AL1A7_RAT Reviewed; 501 AA.
AC P13601;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Aldehyde dehydrogenase, cytosolic 1;
DE EC=1.2.1.3 {ECO:0000269|PubMed:10998257};
DE AltName: Full=ALDH class 1;
DE AltName: Full=ALDH-E1;
DE AltName: Full=ALHDII;
DE AltName: Full=Aldehyde dehydrogenase family 1 member A7;
DE AltName: Full=Aldehyde dehydrogenase phenobarbital-inducible;
GN Name=Aldh1a7;
GN Synonyms=Aldh-pb {ECO:0000303|PubMed:10998257}, Aldh1, Aldh1a4;
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 [MRNA].
RX PubMed=2753900; DOI=10.1016/s0021-9258(18)51595-7;
RA Dunn T.J., Koleske A.J., Lindahl R., Pitot H.C.;
RT "Phenobarbital-inducible aldehyde dehydrogenase in the rat. cDNA sequence
RT and regulation of the mRNA by phenobarbital in responsive rats.";
RL J. Biol. Chem. 264:13057-13065(1989).
RN [2]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, TISSUE SPECIFICITY, AND
RP CATALYTIC ACTIVITY.
RX PubMed=10998257; DOI=10.1021/bi001120m;
RA Kathmann E.C., Naylor S., Lipsky J.J.;
RT "Rat liver constitutive and phenobarbital-inducible cytosolic aldehyde
RT dehydrogenases are highly homologous proteins that function as distinct
RT isozymes.";
RL Biochemistry 39:11170-11176(2000).
CC -!- FUNCTION: Can oxidize benzaldehyde, propionaldehyde and acetaldehyde.
CC No detectable activity with retinal. {ECO:0000269|PubMed:10998257}.
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 Evidence={ECO:0000269|PubMed:10998257};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16186;
CC Evidence={ECO:0000269|PubMed:10998257};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.4 mM for acetaldehyde {ECO:0000269|PubMed:10998257};
CC KM=1.6 mM for propionaldehyde {ECO:0000269|PubMed:10998257};
CC KM=4.7 uM for benzaldehyde {ECO:0000269|PubMed:10998257};
CC Note=The highest catalytic efficiency is observed with benzaldehyde
CC as substrate. No activity with retinal.;
CC -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol:
CC step 2/2. {ECO:0000305|PubMed:10998257}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10998257}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Very low levels in lung and liver.
CC {ECO:0000269|PubMed:10998257}.
CC -!- INDUCTION: By phenobarbital.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; M23995; AAA40718.1; -; mRNA.
DR PIR; A32616; A32616.
DR RefSeq; NP_058968.14; NM_017272.15.
DR AlphaFoldDB; P13601; -.
DR SMR; P13601; -.
DR IntAct; P13601; 3.
DR BindingDB; P13601; -.
DR ChEMBL; CHEMBL5354; -.
DR iPTMnet; P13601; -.
DR PhosphoSitePlus; P13601; -.
DR jPOST; P13601; -.
DR PRIDE; P13601; -.
DR UCSC; RGD:620252; rat.
DR RGD; 620252; Aldh1a7.
DR InParanoid; P13601; -.
DR PhylomeDB; P13601; -.
DR SABIO-RK; P13601; -.
DR UniPathway; UPA00780; UER00768.
DR PRO; PR:P13601; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; NAS:RGD.
DR GO; GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; IDA:RGD.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IDA:RGD.
DR GO; GO:0018479; F:benzaldehyde dehydrogenase (NAD+) activity; IDA:RGD.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0051287; F:NAD binding; ISS:CAFA.
DR GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0035106; P:operant conditioning; IEP: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 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; Cytoplasm; NAD; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT CHAIN 2..501
FT /note="Aldehyde dehydrogenase, cytosolic 1"
FT /id="PRO_0000056426"
FT ACT_SITE 269
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 303
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 246..251
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 170
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 91
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 128
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 252
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 353
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 367
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 410
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 419
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 435
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT MOD_RES 495
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00352"
SQ SEQUENCE 501 AA; 54560 MW; E6806A1AF736AF1F CRC64;
MSSPAQPAVP APLANLKIQH TKIFINNEWH NSLNGKKFPV INPATEEVIC HVEEGDKADV
DKAVKAARQA FQIGSPWRTM DASERGCLLN KLADLMERDR VLLATMESMN AGKIFTHAYL
LDTEVSIKAL KYFAGWADKI HGQTIPSDGD VFTYTRREPI GVCGQIIPWN GPLILFIWKI
GAALSCGNTV IVKPAEQTPL TALYMASLIK EAGFPPGVVN VVPGYGSTAG AAISSHMDID
KVSFTGSTEV GKLIKEAAGK SNLKRVTLEL GGKSPCIVFA DADLDSAVEF AHQGVFFHQG
QICVAASRLF VEESIYDEFV RRSVERAKKY VLGNPLDSGI SQGPQIDKEQ HAKILDLIES
GKKEGAKLEC GGGRWGNKGF FVQPTVFSNV TDEMRIAKEE IFGPVQQIMK FKSIDEVIKR
ANNTPYGLAA GVFTKDLDRA ITVSSALQAG TVWVNCYLTL SVQCPFGGFK MSGNGREMGE
QGVYEYTELK TVAMKISQKN S
