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Alpha-aminoadipic semialdehyde dehydrogenase (Alpha-AASA dehydrogenase) (EC 1.2.1.31) (Aldehyde dehydrogenase family 7 member A1) (EC 1.2.1.3) (Antiquitin-1) (Betaine aldehyde dehydrogenase) (EC 1.2.1.8) (Delta1-piperideine-6-carboxylate dehydrogenase) (P6c dehydrogenase)

 AL7A1_BOVIN             Reviewed;         539 AA.
Q2KJC9;
27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
20-APR-2010, sequence version 4.
28-FEB-2018, entry version 78.
RecName: Full=Alpha-aminoadipic semialdehyde dehydrogenase;
Short=Alpha-AASA dehydrogenase;
EC=1.2.1.31;
AltName: Full=Aldehyde dehydrogenase family 7 member A1;
EC=1.2.1.3;
AltName: Full=Antiquitin-1;
AltName: Full=Betaine aldehyde dehydrogenase;
EC=1.2.1.8;
AltName: Full=Delta1-piperideine-6-carboxylate dehydrogenase;
Short=P6c dehydrogenase;
Flags: Precursor;
Name=ALDH7A1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Heart ventricle;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Multifunctional enzyme mediating important protective
effects. Metabolizes betaine aldehyde to betaine, an important
cellular osmolyte and methyl donor. Protects cells from oxidative
stress by metabolizing a number of lipid peroxidation-derived
aldehydes. Involved in lysine catabolism (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: (S)-2-amino-6-oxohexanoate + NAD(P)(+) + H(2)O
= L-2-aminoadipate + NAD(P)H.
-!- CATALYTIC ACTIVITY: Betaine aldehyde + NAD(+) + H(2)O = betaine +
NADH.
-!- CATALYTIC ACTIVITY: An aldehyde + NAD(+) + H(2)O = a carboxylate +
NADH.
-!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis
via choline pathway; betaine from betaine aldehyde: step 1/1.
-!- SUBUNIT: Homotetramer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P49419}.
Cytoplasm, cytosol {ECO:0000250|UniProtKB:P49419}. Mitochondrion
{ECO:0000250|UniProtKB:P49419}.
-!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAI05407.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; BC105406; AAI05407.1; ALT_INIT; mRNA.
RefSeq; NP_001039434.2; NM_001045969.2.
UniGene; Bt.22086; -.
ProteinModelPortal; Q2KJC9; -.
SMR; Q2KJC9; -.
IntAct; Q2KJC9; 2.
STRING; 9913.ENSBTAP00000048297; -.
PaxDb; Q2KJC9; -.
PeptideAtlas; Q2KJC9; -.
PRIDE; Q2KJC9; -.
GeneID; 507477; -.
KEGG; bta:507477; -.
CTD; 501; -.
eggNOG; KOG2453; Eukaryota.
eggNOG; COG1012; LUCA.
HOGENOM; HOG000271511; -.
HOVERGEN; HBG050485; -.
InParanoid; Q2KJC9; -.
KO; K14085; -.
UniPathway; UPA00529; UER00386.
Proteomes; UP000009136; Unplaced.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0004043; F:L-aminoadipate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniPathway.
Gene3D; 3.40.309.10; -; 1.
Gene3D; 3.40.605.10; -; 2.
InterPro; IPR016161; Ald_DH/histidinol_DH.
InterPro; IPR016163; Ald_DH_C.
InterPro; IPR029510; Ald_DH_CS_GLU.
InterPro; IPR016162; Ald_DH_N.
InterPro; IPR015590; Aldehyde_DH_dom.
Pfam; PF00171; Aldedh; 1.
SUPFAM; SSF53720; SSF53720; 1.
PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
2: Evidence at transcript level;
Acetylation; Complete proteome; Cytoplasm; Mitochondrion; NAD;
Nucleus; Oxidoreductase; Reference proteome; Transit peptide.
TRANSIT 1 26 Mitochondrion. {ECO:0000255}.
CHAIN 27 539 Alpha-aminoadipic semialdehyde
dehydrogenase.
/FTId=PRO_0000244567.
NP_BIND 274 279 NAD. {ECO:0000250}.
ACT_SITE 296 296 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10007}.
ACT_SITE 330 330 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU10007}.
SITE 195 195 Transition state stabilizer.
{ECO:0000250}.
MOD_RES 94 94 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q9DBF1}.
MOD_RES 94 94 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q9DBF1}.
MOD_RES 462 462 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9DBF1}.
MOD_RES 500 500 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9DBF1}.
MOD_RES 537 537 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9DBF1}.
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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