ID E4ZT61_LEPMJ Unreviewed; 501 AA.
AC E4ZT61;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Similar to aldehyde dehydrogenase {ECO:0000313|EMBL:CBX94492.1};
GN ORFNames=LEMA_P119830.1 {ECO:0000313|EMBL:CBX94492.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
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DR EMBL; FP929123; CBX94492.1; -; Genomic_DNA.
DR RefSeq; XP_003837936.1; XM_003837888.1.
DR AlphaFoldDB; E4ZT61; -.
DR STRING; 985895.E4ZT61; -.
DR EnsemblFungi; CBX94492; CBX94492; LEMA_P119830.1.
DR GeneID; 13291083; -.
DR eggNOG; KOG2450; Eukaryota.
DR HOGENOM; CLU_005391_0_1_1; -.
DR InParanoid; E4ZT61; -.
DR OMA; KCAKAMR; -.
DR OrthoDB; 216092at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd07144; ALDH_ALD2-YMR170C; 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 PANTHER; PTHR43720; 2-AMINOMUCONIC SEMIALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43720:SF2; 2-AMINOMUCONIC SEMIALDEHYDE DEHYDROGENASE; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 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:UP000002668}.
FT DOMAIN 28..493
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 266
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 501 AA; 54356 MW; 50A2FDF2B793F9E3 CRC64;
MSDLFVELTA PNGRKYSQPR GLFINNEFVK SKSGETITSI NPSDESEIVS VYAAGPEDVD
DAVAAARKAF KNPDWRDMDT NARADLLYRF AQLIDENKET LATIETWDNG KPYSVALNDD
LGEVVGTIKY YAGWANKIHG QVIDTGPAKL AYTLREPLGV CGQIIPWNFP LAMAAWKLGP
ALCTGNTIVM KAAEQTPLSI LYLASLVKEA GFPPGVVNII NGEGRKAGAA LAQHLDVDKI
AFTGSTATGK EIMKMAAVNM KNITLETGGK SPLVIFDDAD LDQAVKWTHV GIMYNQGQVC
TATSRVLVQE GIYEKFIESF KQHVKTTSIV GDPFQDDTFQ GPQVTKAQFD RVLGFIEAGK
SEGATLVAGG EAHKNAGGKG FFIAPTIFTD VKDHMKIYRE EVFGPFVVIS SFKTEEEAIE
RANDTTYGLG AAVFTENITK AHRVARRIEA GMVWINSSND SDIRVPFGGV KQSGIGRELG
EAGLEAYTNK KAIHVNLGTK L
//
