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 03-AUG-2022, entry version 91.
DE RecName: Full=Alpha-aminoadipic semialdehyde dehydrogenase;
DE Short=Alpha-AASA dehydrogenase;
DE EC=1.2.1.31 {ECO:0000250|UniProtKB:P49419};
DE AltName: Full=Aldehyde dehydrogenase family 7 member A1;
DE EC=1.2.1.3 {ECO:0000250|UniProtKB:P49419};
DE AltName: Full=Antiquitin-1;
DE AltName: Full=Betaine aldehyde dehydrogenase;
DE EC=1.2.1.8 {ECO:0000250|UniProtKB:P49419};
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; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC 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 cellular
CC osmolyte and methyl donor. Protects cells from oxidative stress by
CC metabolizing a number of lipid peroxidation-derived aldehydes. Involved
CC in lysine catabolism. {ECO:0000250|UniProtKB:P49419}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + nonanal = 2 H(+) + NADH + nonanoate;
CC Xref=Rhea:RHEA:69759, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32361, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:84268; Evidence={ECO:0000250|UniProtKB:P49419};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69760;
CC Evidence={ECO:0000250|UniProtKB:P49419};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2-amino-6-oxohexanoate + H2O + NAD(+) = 2 H(+) + L-2-
CC aminoadipate + NADH; Xref=Rhea:RHEA:12308, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58321, ChEBI:CHEBI:58672; EC=1.2.1.31;
CC Evidence={ECO:0000250|UniProtKB:P49419};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12309;
CC Evidence={ECO:0000250|UniProtKB:P49419};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15710, ChEBI:CHEBI:17750, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.8;
CC Evidence={ECO:0000250|UniProtKB:P49419};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15306;
CC Evidence={ECO:0000250|UniProtKB:P49419};
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:0000250|UniProtKB:P49419};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16186;
CC Evidence={ECO:0000250|UniProtKB:P49419};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexanal + NAD(+) = 2 H(+) + hexanoate + NADH;
CC Xref=Rhea:RHEA:67276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17120, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:88528; Evidence={ECO:0000250|UniProtKB:P49419};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67277;
CC Evidence={ECO:0000250|UniProtKB:P49419};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + octanal = 2 H(+) + NADH + octanoate;
CC Xref=Rhea:RHEA:44100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17935, ChEBI:CHEBI:25646, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P49419};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44101;
CC Evidence={ECO:0000250|UniProtKB:P49419};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-non-2-enal + H2O + NAD(+) = (E)-non-2-enoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:69767, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:142592,
CC ChEBI:CHEBI:143908; Evidence={ECO:0000250|UniProtKB:P49419};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69768;
CC Evidence={ECO:0000250|UniProtKB:P49419};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-hydroxynon-2-enal + H2O + NAD(+) = (E)-4-hydroxynon-2-
CC enoate + 2 H(+) + NADH; Xref=Rhea:RHEA:67248, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58968, ChEBI:CHEBI:142920;
CC Evidence={ECO:0000250|UniProtKB:P49419};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67249;
CC Evidence={ECO:0000250|UniProtKB:P49419};
CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC choline pathway; betaine from betaine aldehyde: step 1/1.
CC {ECO:0000250|UniProtKB:P49419}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P49419}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P49419}. Nucleus {ECO:0000250|UniProtKB:P49419}.
CC Mitochondrion {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; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC105406; AAI05407.1; ALT_INIT; mRNA.
DR RefSeq; NP_001039434.2; NM_001045969.2.
DR AlphaFoldDB; 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 InParanoid; Q2KJC9; -.
DR OrthoDB; 692580at2759; -.
DR UniPathway; UPA00529; UER00386.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
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; -; 1.
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 InterPro; IPR044638; ALDH7A1-like.
DR PANTHER; PTHR43521; PTHR43521; 1.
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; Cytoplasm; Mitochondrion; NAD; Nucleus; Oxidoreductase;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..539
FT /note="Alpha-aminoadipic semialdehyde dehydrogenase"
FT /id="PRO_0000244567"
FT ACT_SITE 296
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 330
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT BINDING 192..194
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P49419"
FT BINDING 218
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P49419"
FT BINDING 258..259
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P49419"
FT BINDING 274..279
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 274..275
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P49419"
FT BINDING 296..297
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P49419"
FT BINDING 331
FT /ligand="(S)-2-amino-6-oxohexanoate"
FT /ligand_id="ChEBI:CHEBI:58321"
FT /evidence="ECO:0000250|UniProtKB:P49419"
FT BINDING 427
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P49419"
FT BINDING 489
FT /ligand="(S)-2-amino-6-oxohexanoate"
FT /ligand_id="ChEBI:CHEBI:58321"
FT /evidence="ECO:0000250|UniProtKB:P49419"
FT BINDING 490
FT /ligand="(S)-2-amino-6-oxohexanoate"
FT /ligand_id="ChEBI:CHEBI:58321"
FT /evidence="ECO:0000250|UniProtKB:P49419"
FT SITE 195
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 94
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBF1"
FT MOD_RES 94
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBF1"
FT MOD_RES 462
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBF1"
FT MOD_RES 500
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBF1"
FT MOD_RES 537
FT /note="N6-succinyllysine"
FT /evidence="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
