ID A0A0L9T6L5_PHAAN Unreviewed; 493 AA.
AC A0A0L9T6L5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN ORFNames=LR48_Vigan238s007800 {ECO:0000313|EMBL:KOM26245.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM26245.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492}.
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DR EMBL; KQ258309; KOM26245.1; -; Genomic_DNA.
DR RefSeq; XP_017406242.1; XM_017550753.1.
DR AlphaFoldDB; A0A0L9T6L5; -.
DR STRING; 3914.A0A0L9T6L5; -.
DR EnsemblPlants; KOM26245; KOM26245; LR48_Vigan238s007800.
DR GeneID; 108319579; -.
DR Gramene; KOM26245; KOM26245; LR48_Vigan238s007800.
DR KEGG; var:108319579; -.
DR OMA; DAFSHTR; -.
DR OrthoDB; 1205055at2759; -.
DR Proteomes; UP000053144; Unassembled WGS sequence.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR PANTHER; PTHR43570; ALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43570:SF30; ALDEHYDE DEHYDROGENASE; 1.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036492; ALDH; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR036492};
KW Reference proteome {ECO:0000313|Proteomes:UP000053144}.
FT DOMAIN 14..439
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 213
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
FT ACT_SITE 251
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ SEQUENCE 493 AA; 55405 MW; 2D8DD86C41E30FC4 CRC64;
MEIMSSFDRD LNDMREYYES GKTKQASWRE SQLKSLRCFL MEKQQHIMEA LMQDLGKHQL
EAFRDEIGTL IKTLNLALKS LKAWMSGKKA ELPQVALLTS AEIVSEPLGL VLIISSWNFP
FGLSLEPLIG AIAAGNVAIL KPSELSPASS SLLASSLTSY LDNKAIKVIQ GGPQETQQLL
EQRWDKIFFT GSARVGRIVM SAAVKNLTPV TLELGGKCPA VVDSLSSSWD IEATVKRIVV
GKFGTCAGQA CIAIDYVLVE NKYCSKLVEL MKVWIKKMFG ENPQRSKTIT RIVNKHHFSR
LNNLLADKMV KESVVYGGSV DEENLFIEPT ILVDPPLDAA IMSEEIFGPL LPIITVEKIE
DSIRFIRSRP KPLALYVFTK NKTLERRMIS ETSSGSLTFN DAILQYAADS LPFGGVGESG
FGMYHGKFSF DTFSHQKAIV RRSFLTDFWF RYPPWTLNKL QLLEECYNYD YLGMFLVMLG
LKRSSKRLFA NHM
//
