ID Q6S9W9_GOSHI Unreviewed; 503 AA.
AC Q6S9W9;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=aminobutyraldehyde dehydrogenase {ECO:0000256|ARBA:ARBA00039138};
DE EC=1.2.1.19 {ECO:0000256|ARBA:ARBA00039138};
OS Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=3635 {ECO:0000313|EMBL:AAR23816.2};
RN [1] {ECO:0000313|EMBL:AAR23816.2}
RP NUCLEOTIDE SEQUENCE.
RA Shan D., Yang Y., Wu C., Zhang Y., Xue H., Zhang M., Gao Z.;
RT "Betaine-aldehyde dehydrogenase (BADH).";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-aminopropanal + H2O + NAD(+) = beta-alanine + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:30695, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57966,
CC ChEBI:CHEBI:58374; Evidence={ECO:0000256|ARBA:ARBA00036519};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30696;
CC Evidence={ECO:0000256|ARBA:ARBA00036519};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:19105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58264,
CC ChEBI:CHEBI:59888; EC=1.2.1.19;
CC Evidence={ECO:0000256|ARBA:ARBA00036645};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19106;
CC Evidence={ECO:0000256|ARBA:ARBA00036645};
CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC choline pathway; betaine from betaine aldehyde: step 1/1.
CC {ECO:0000256|ARBA:ARBA00037921}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR EMBL; AY461804; AAR23816.2; -; mRNA.
DR RefSeq; NP_001314194.1; NM_001327265.1.
DR AlphaFoldDB; Q6S9W9; -.
DR GeneID; 107926694; -.
DR KEGG; ghi:107926694; -.
DR OrthoDB; 3078548at2759; -.
DR GO; GO:0019145; F:aminobutyraldehyde dehydrogenase activity; IEA:UniProt.
DR GO; GO:0110095; P:cellular detoxification of aldehyde; IEA:UniProt.
DR CDD; cd07110; ALDH_F10_BADH; 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; PTHR43860; BETAINE ALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43860:SF2; BETAINE 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 2: Evidence at transcript level;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW Sodium {ECO:0000256|ARBA:ARBA00023053}.
FT DOMAIN 23..485
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 260
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 503 AA; 54722 MW; 96CDAE7CC92A3836 CRC64;
MAVQVPSRQL FIDGEWREPI LKERLPTINP ATEEIIGNIP AATAEDVELA VAAARRALSR
NKGKDWATAP GAVRAKYLRA IAAKVTERKT ELAKLEAIDC GKPLDEAVWD IEDVAGCFEY
YADLAEGLDA RQKAPVSLPM ETFKSYVLKE PIGVVGLITP WNYPLLMATW KVAPSLAAGC
AAILKPSELA SITCLELAKV VKGSRLPPGV LNILAGLGPE AGAPLASHPD VDKIAFTGSS
ATGSKIMAAA AQMVKPVSLE LGGKSPIIVF EDVDLDKAAE WTAFGCFWTN GQICSATSRL
IVHENIAREF LDRLVKWTKN IKISDPFEEG CRLGPVVSGG QYEKVLKFIS TAKSEGATIL
SGGVRPEHLK KGFFVEPTII TDVTTSMQIW REEVFGPVLC VKTFRTEEEA LELANDTHYG
LGAAVISNDL ERCDRVSKNL QAGIVWVNCS QPCFCQAPWG GNKRSGFGRE LGEWGLDNYL
SVKQVTQYVS DEPWGWYRSP SKL
//
