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Database: UniProt
Entry: L9KUJ3_TUPCH
LinkDB: L9KUJ3_TUPCH
Original site: L9KUJ3_TUPCH 
ID   L9KUJ3_TUPCH            Unreviewed;       512 AA.
AC   L9KUJ3;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
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   ORFNames=TREES_T100016955 {ECO:0000313|EMBL:ELW66580.1};
OS   Tupaia chinensis (Chinese tree shrew).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX   NCBI_TaxID=246437 {ECO:0000313|EMBL:ELW66580.1, ECO:0000313|Proteomes:UP000011518};
RN   [1] {ECO:0000313|Proteomes:UP000011518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhang G., Fan Y., Yao Y., Huang Z.;
RT   "Genome of the Chinese tree shrew, a rising model animal genetically
RT   related to primates.";
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000011518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23385571; DOI=10.1038/ncomms2416;
RA   Fan Y., Huang Z.Y., Cao C.C., Chen C.S., Chen Y.X., Fan D.D., He J.,
RA   Hou H.L., Hu L., Hu X.T., Jiang X.T., Lai R., Lang Y.S., Liang B.,
RA   Liao S.G., Mu D., Ma Y.Y., Niu Y.Y., Sun X.Q., Xia J.Q., Xiao J.,
RA   Xiong Z.Q., Xu L., Yang L., Zhang Y., Zhao W., Zhao X.D., Zheng Y.T.,
RA   Zhou J.M., Zhu Y.B., Zhang G.J., Wang J., Yao Y.G.;
RT   "Genome of the Chinese tree shrew.";
RL   Nat. Commun. 4:1426-1426(2013).
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; KB320648; ELW66580.1; -; Genomic_DNA.
DR   AlphaFoldDB; L9KUJ3; -.
DR   STRING; 246437.L9KUJ3; -.
DR   eggNOG; KOG2450; Eukaryota.
DR   InParanoid; L9KUJ3; -.
DR   Proteomes; UP000011518; Unassembled WGS sequence.
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:UP000011518}.
FT   DOMAIN          40..503
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        280
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   512 AA;  55480 MW;  2D4C9570583A6147 CRC64;
     MRPDVLAFTL PMALAPADGG SSTLTVAICE AALIFIDNEW HDAISKKTFP TVNPSTGEVI
     CQVAAGDKED VDKAVKAARA AFQLGSPWRR MDASDRGRLL YRLADLIERD RTYLAALETL
     DNGKPYVISY LVDLDMVLKC LRYYAGWADK YHGKTIPIDG DFFSYTRHEP VGVCGQIIPW
     NFPLLMQAWK LGPALATGNV VVMKVAEQTP LTALYVANLI KEAGFPPGVV NIVPGFGPTA
     GAAIASHDDV DKVAFTGSTE VGHLIQIAAG KSNLKRVTLE LGGKSPNIIM SDADMAWAVE
     QAHFALFFNQ GQCCCAGSRT YVQEDVYAEF VERSVARAKS RVVGNPFDSQ TEQGPQVDET
     QFKKILGYIQ SGKQEGAKLL CGGGPAADRG YFIQPTVFGD VQDGMTIAKE EIFGPVMQIL
     KFKTIEEVVG RANNSKYGLA AAVFTKDLDK ANYLSQALQA GTVWVNCYDV FGAQSPFGGY
     KMSGSGRELG EYGLQAYTEV KTVTVKVPQK NS
//
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