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Database: UniProt/SWISS-PROT
Entry: ALDH2_PONAB
LinkDB: ALDH2_PONAB
Original site: ALDH2_PONAB 
ID   ALDH2_PONAB             Reviewed;         517 AA.
AC   Q5RF00;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   05-DEC-2018, entry version 70.
DE   RecName: Full=Aldehyde dehydrogenase, mitochondrial;
DE            EC=1.2.1.3;
DE   AltName: Full=ALDH class 2;
DE   AltName: Full=ALDH-E2;
DE   Flags: Precursor;
GN   Name=ALDH2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Is capable of converting retinaldehyde to retinoic acid.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) +
CC         NADH; Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.3;
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
DR   EMBL; CR857362; CAH89657.1; -; mRNA.
DR   RefSeq; NP_001124747.1; NM_001131275.1.
DR   UniGene; Pab.6233; -.
DR   ProteinModelPortal; Q5RF00; -.
DR   SMR; Q5RF00; -.
DR   STRING; 9601.ENSPPYP00000005665; -.
DR   PRIDE; Q5RF00; -.
DR   GeneID; 100171596; -.
DR   KEGG; pon:100171596; -.
DR   CTD; 217; -.
DR   eggNOG; KOG2450; Eukaryota.
DR   eggNOG; COG1012; LUCA.
DR   HOVERGEN; HBG000097; -.
DR   InParanoid; Q5RF00; -.
DR   KO; K00128; -.
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   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; Complete proteome; Mitochondrion; NAD; Oxidoreductase;
KW   Reference proteome; Transit peptide.
FT   TRANSIT       1     17       Mitochondrion. {ECO:0000250}.
FT   CHAIN        18    517       Aldehyde dehydrogenase, mitochondrial.
FT                                /FTId=PRO_0000312493.
FT   NP_BIND     262    267       NAD. {ECO:0000250}.
FT   ACT_SITE    285    285       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10007, ECO:0000255|PROSITE-
FT                                ProRule:PRU10008}.
FT   ACT_SITE    319    319       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10007, ECO:0000255|PROSITE-
FT                                ProRule:PRU10008}.
FT   SITE        186    186       Transition state stabilizer.
FT                                {ECO:0000250|UniProtKB:P20000}.
FT   MOD_RES      52     52       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES      73     73       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES      78     78       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     159    159       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     368    368       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     383    383       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     426    426       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     428    428       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     451    451       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
SQ   SEQUENCE   517 AA;  56380 MW;  E8F74D4CFA27220E CRC64;
     MLRAAARFGP RLGRRLLSAA ATQAVPAPNQ QPEVFCNQIF INNEWHDAVS RKTFPTVNPS
     TGEVICQVAE GDKEDVDKAV KAARAAFQLG SPWRRMDASH RGRLLNRLAD LIERDRTYLA
     ALETLDNGKP YVISYLVDLD MVLKCLRYYA GWADKYHGKT IPIDGDFFSY TRHEPVGVCG
     QIIPWNFPLL MQAWKLGPAL ATGNVVVMKV AEQTPLTALY VANLIKEAGF PPGVVNIVPG
     FGPTAGAAIA SHEDVDKVAF TGSTEIGRVI QVAAGSSNLK RVTLELGGKS PNIIMSDADM
     DWAVEQAHFA LFFNQGQCCC AGSRTFVQED IYDEFVERSV ARAKSRVVGN PFDSKTEQGP
     QVDETQFKKI LGYINTGKQE GAKLLCGGGI AADRGYFIQP TVFGDVQDGM TIAKEEIFGP
     VMQILKFKTI EEVVGRANNS TYGLAAAVFT KDLDKANYLS QALQAGTVWV NCYNVFGAQS
     PFGGYKMSGS GRELGEYGLQ AYTEVKTVTV KVPQKNS
//
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