ID H3AUS8_LATCH Unreviewed; 524 AA.
AC H3AUS8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Aldehyde dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00040706};
DE EC=1.2.1.3 {ECO:0000256|ARBA:ARBA00024226};
DE AltName: Full=ALDH class 2 {ECO:0000256|ARBA:ARBA00041743};
DE AltName: Full=ALDH-E2 {ECO:0000256|ARBA:ARBA00042494};
GN Name=ALDH2 {ECO:0000313|Ensembl:ENSLACP00000013399.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000013399.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000013399.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Required for clearance of cellular formaldehyde, a cytotoxic
CC and carcinogenic metabolite that induces DNA damage.
CC {ECO:0000256|ARBA:ARBA00037438}.
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:0000256|ARBA:ARBA00024149};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
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DR EMBL; AFYH01073451; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01073452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01073453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01073454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01073455; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3AUS8; -.
DR STRING; 7897.ENSLACP00000013399; -.
DR Ensembl; ENSLACT00000013495.1; ENSLACP00000013399.1; ENSLACG00000011798.1.
DR eggNOG; KOG2450; Eukaryota.
DR GeneTree; ENSGT00940000156240; -.
DR HOGENOM; CLU_005391_0_1_1; -.
DR InParanoid; H3AUS8; -.
DR OMA; HGIGYYP; -.
DR TreeFam; TF300455; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000011798; Expressed in muscle tissue and 6 other cell types or tissues.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd07141; ALDH_F1AB_F2_RALDH1; 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 PANTHER; PTHR11699:SF233; ALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672}.
FT DOMAIN 51..515
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 291
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 524 AA; 57355 MW; 810BAE796BC1C566 CRC64;
MLRLALGNLS KLSRFSSPVS LNRFSAAAAA IPTPNPQQEV YFNKIFINNE WHDAVSKKTL
PSINPATGEV ICQVAEGDKA DVDKAVKAAR NAFKLGSPWR RMDASERGVL LNRLADLIER
DRTYLATLEA LDNGKPYAVA YAVDLNMVVK CLRYYAGWAD KCHGKTIPMD GDFFCYTRHE
PVGVCGQIIP WNFPLLMQAW KLGPALATGN VIVMKVAEQT PLTALYVANL IKEAGFPPGV
VNIIPGFGPT AGAAIASHMD VDKVAFTGST EVGHLIQKAA GGSNLKRITL ELGGKSPNII
MSDADMDYAV EQAHFALFFN QGQCCCAGSR TYVQDSIYDE FLERSVERAK ARVVGNPFDL
NTEQGPQIDE EQFQKILGYI STGKREGAKL LCGGGVAADR GYFILFFFFF NLHKGQKVQI
VSLIFGPVMQ VLKFKSIEEV IERANDTQYG LAAAVFTRDL DKANYVSQGL RAGTVWINCY
DVFGAQSPFG GYKTSGNGRE LGEYGLEAYT EVKTVTIKVP QKNS
//
