ID A0A444Z2N9_ARAHY Unreviewed; 503 AA.
AC A0A444Z2N9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=aminobutyraldehyde dehydrogenase {ECO:0000256|ARBA:ARBA00039138};
DE EC=1.2.1.19 {ECO:0000256|ARBA:ARBA00039138};
GN ORFNames=Ahy_B05g076147 {ECO:0000313|EMBL:RYR08453.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR08453.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYR08453.1, ECO:0000313|Proteomes:UP000289738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC TISSUE=Leaves {ECO:0000313|EMBL:RYR08453.1};
RA Chen X.;
RT "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT genome evolution and oil improvement.";
RL Submitted (JAN-2019) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RYR08453.1}.
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DR EMBL; SDMP01000015; RYR08453.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A444Z2N9; -.
DR STRING; 3818.A0A444Z2N9; -.
DR Proteomes; UP000289738; Chromosome b05.
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:SF9; NAD-DEPENDENT ALDEHYDE DEHYDROGENASE FAMILY PROTEIN; 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 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000289738};
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; 54470 MW; BF3D2D4CF0D67A31 CRC64;
MAISTPRREL FIDGEWKAPL LNNRIPIINP STELIIGDIP AATKEDVELA VDAARRALSR
NKGKDWSTAS GSLRATYLRA IAAKITEKKD ELAKLEATDN GKPLDEAAAD MDDVIGCFSY
YAELAEGLDA KQKAHVSLPM ENFKSYVIKE PIGVVALITP WNYPLLMAAW KVGAALAAGC
TAVLKPSELA SVTCLELAEI CKEVGLPAGV LNVITGLGTE AGAPLASHPD VDKISFTGSS
ATGSKIMQAA ALQVKPVSLE LGGKSPIIVF DDVDIDKVAE WTMLGCFFTN GQICSATSRL
IVHENIATKF LNRLVEWAKN IKVSDPLEDG CKLGAIVSEA QYQKVLKFIS TAKSEGATIL
TGGSRPENLK KGYFVEPTII TDVSTSMQIW REEVFGPVLC AKTFSSEEEA IELANDTHYG
LGSAVMSNDP ERCERISKAV QAGIVWINCS QPTFIQAPWG GIKRSGFGRE LGEWGLDNFL
SVKQVTKYIS DEQWGWYKCP SKM
//
