ID G8EWJ4_9ROSA Unreviewed; 503 AA.
AC G8EWJ4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=aminobutyraldehyde dehydrogenase {ECO:0000256|ARBA:ARBA00039138};
DE EC=1.2.1.19 {ECO:0000256|ARBA:ARBA00039138};
OS Pyrus betulifolia.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Pyrus.
OX NCBI_TaxID=436086 {ECO:0000313|EMBL:AER10509.1};
RN [1] {ECO:0000313|EMBL:AER10509.1}
RP NUCLEOTIDE SEQUENCE.
RA Li H., Cong Y., Chang Y.H., Lin J.;
RT "Molecular cloning and transcription response of choline monooxygenase,
RT phosphoethanolamine N-methyltransferase and betaine-aldehyde dehydrogenase
RT genes to abiotic stresses in birch-leaf pear (Pyrus betulaefolia Bunge.).";
RL Submitted (MAY-2011) 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; JF968601; AER10508.1; -; mRNA.
DR EMBL; JF968602; AER10509.1; -; Genomic_DNA.
DR AlphaFoldDB; G8EWJ4; -.
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 16..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; 54595 MW; A5C76889DE2B8175 CRC64;
MAIQIPSRLL FIDGEWREPV LKKRIPIINP ATEEIIGVIP AATAEDVELA VEAARRALSR
NKGRDWASAP GAVRAKYLRA IAAKIGERKP EIAKLEAIDC GKPLDEAAWD IDDVSGCFEY
YAELAEGLDA QQKAPISLPM EQFKSHVLKE PIGVVGLITP WNYPLLMATW KVAPALAAGC
AAILKPSELA SVTCLELADV CREVGLPPGV LNILTGLGHE AGAPLASHPH VDKIAFTGST
MTGSKIMTAA APLVKPVSLE LGGKSPIVVF DDVDIDKAAE WTAFGCFWTN GQICSATSRL
ILHEDIATEF LDRLVKWCKN IKIADPLEEG CRLGPVVSGG QYEKILKSIE TAKSEGARVL
SGGARPEHLK KGFFIEPTII TDVTTSMQIW REEVFGPVLC VKTFSSEDEA LELANDTHYG
LGAAVISKDL ERCDRFSKGL QAGIVWINCS QPCFCQAPWG GNKRSGFGRE LGKWGLDNYL
TVKQVTEYVS DDPWGWYASP SKL
//
