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Database: UniProt/SWISS-PROT
Entry: AL7A1_BOVIN
LinkDB: AL7A1_BOVIN
Original site: AL7A1_BOVIN 
ID   AL7A1_BOVIN             Reviewed;         539 AA.
AC   Q2KJC9;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 4.
DT   18-JUL-2018, entry version 79.
DE   RecName: Full=Alpha-aminoadipic semialdehyde dehydrogenase;
DE            Short=Alpha-AASA dehydrogenase;
DE            EC=1.2.1.31;
DE   AltName: Full=Aldehyde dehydrogenase family 7 member A1;
DE            EC=1.2.1.3;
DE   AltName: Full=Antiquitin-1;
DE   AltName: Full=Betaine aldehyde dehydrogenase;
DE            EC=1.2.1.8;
DE   AltName: Full=Delta1-piperideine-6-carboxylate dehydrogenase;
DE            Short=P6c dehydrogenase;
DE   Flags: Precursor;
GN   Name=ALDH7A1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Heart ventricle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Multifunctional enzyme mediating important protective
CC       effects. Metabolizes betaine aldehyde to betaine, an important
CC       cellular osmolyte and methyl donor. Protects cells from oxidative
CC       stress by metabolizing a number of lipid peroxidation-derived
CC       aldehydes. Involved in lysine catabolism (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: (S)-2-amino-6-oxohexanoate + NAD(P)(+) + H(2)O
CC       = L-2-aminoadipate + NAD(P)H.
CC   -!- CATALYTIC ACTIVITY: Betaine aldehyde + NAD(+) + H(2)O = betaine +
CC       NADH.
CC   -!- CATALYTIC ACTIVITY: An aldehyde + NAD(+) + H(2)O = a carboxylate +
CC       NADH.
CC   -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis
CC       via choline pathway; betaine from betaine aldehyde: step 1/1.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P49419}.
CC       Cytoplasm, cytosol {ECO:0000250|UniProtKB:P49419}. Mitochondrion
CC       {ECO:0000250|UniProtKB:P49419}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI05407.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; BC105406; AAI05407.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001039434.2; NM_001045969.2.
DR   UniGene; Bt.22086; -.
DR   ProteinModelPortal; Q2KJC9; -.
DR   SMR; Q2KJC9; -.
DR   IntAct; Q2KJC9; 2.
DR   STRING; 9913.ENSBTAP00000048297; -.
DR   PaxDb; Q2KJC9; -.
DR   PeptideAtlas; Q2KJC9; -.
DR   PRIDE; Q2KJC9; -.
DR   GeneID; 507477; -.
DR   KEGG; bta:507477; -.
DR   CTD; 501; -.
DR   eggNOG; KOG2453; Eukaryota.
DR   eggNOG; COG1012; LUCA.
DR   HOGENOM; HOG000271511; -.
DR   HOVERGEN; HBG050485; -.
DR   InParanoid; Q2KJC9; -.
DR   KO; K14085; -.
DR   UniPathway; UPA00529; UER00386.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004043; F:L-aminoadipate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 2.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
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; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Complete proteome; Cytoplasm; Mitochondrion; NAD;
KW   Nucleus; Oxidoreductase; Reference proteome; Transit peptide.
FT   TRANSIT       1     26       Mitochondrion. {ECO:0000255}.
FT   CHAIN        27    539       Alpha-aminoadipic semialdehyde
FT                                dehydrogenase.
FT                                /FTId=PRO_0000244567.
FT   NP_BIND     274    279       NAD. {ECO:0000250}.
FT   ACT_SITE    296    296       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10007}.
FT   ACT_SITE    330    330       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10007}.
FT   SITE        195    195       Transition state stabilizer.
FT                                {ECO:0000250}.
FT   MOD_RES      94     94       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q9DBF1}.
FT   MOD_RES      94     94       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q9DBF1}.
FT   MOD_RES     462    462       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9DBF1}.
FT   MOD_RES     500    500       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9DBF1}.
FT   MOD_RES     537    537       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q9DBF1}.
SQ   SEQUENCE   539 AA;  58582 MW;  3052D80937989DB4 CRC64;
     MWRVPGLLCV RVARKSKFSG SWNRPAAFMS TLLINQPQYA WLKELGLREE NDGVYNGSWG
     GRGEVITTYC PANNEPIARV RQASMADYEE TVEKAREAWS IWADVPAPKR GEVVRQIGDA
     LREKIQVLGS LVSLEMGKIL VEGVGEVQEY VDVCDYAVGL SRMIGGPILP SERPGHALIE
     QWNPVGLVGI ITAFNFPVAV YGWNNAIAMI CGNACLWKGA PTTSLISVAV TKIIAKVLED
     NKLPGAICSL TCGGADIGTA MAKDERVDLL SFTGSTQVGK QVALMVQERF GRSLLELGGN
     NAIIAFEDAD LSLVVPSALF AAVGTAGQRC TTARRLFLHE SIHDEVVNRL KKAYAQIRVG
     NPWDSNVLYG PLHTKQAVSM FLGAVEEAKK EGGTVVYGGK VMDRPGNYVE PTIVTGLDHD
     ASIVHTETFA PILYVFKFKN EDEVFAWNNE VKQGLSSSIF TKDMGRIFRW LGPKGSDCGI
     VNVNIPTSGA EIGGAFGGEK HTGGGRESGS DAWKQYMRRS TCTINYSKDL PLAQGIKFQ
//
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