ID   A0A072PEB6_9EURO        Unreviewed;       351 AA.
AC   A0A072PEB6;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:KEF58439.1};
GN   ORFNames=A1O9_06365 {ECO:0000313|EMBL:KEF58439.1};
OS   Exophiala aquamarina CBS 119918.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF58439.1, ECO:0000313|Proteomes:UP000027920};
RN   [1] {ECO:0000313|EMBL:KEF58439.1, ECO:0000313|Proteomes:UP000027920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF58439.1,
RC   ECO:0000313|Proteomes:UP000027920};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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:KEF58439.1}.
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DR   EMBL; AMGV01000004; KEF58439.1; -; Genomic_DNA.
DR   RefSeq; XP_013261029.1; XM_013405575.1.
DR   AlphaFoldDB; A0A072PEB6; -.
DR   STRING; 1182545.A0A072PEB6; -.
DR   GeneID; 25281282; -.
DR   VEuPathDB; FungiDB:A1O9_06365; -.
DR   HOGENOM; CLU_049966_1_0_1; -.
DR   OrthoDB; 6339at2759; -.
DR   Proteomes; UP000027920; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
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:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR005676; Asp_semi-ald_DH_pep-lack.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR   NCBIfam; TIGR00978; asd_EA; 1.
DR   PANTHER; PTHR46718; ASPARTATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR46718:SF1; ASPARTATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR   Pfam; PF01118; Semialdhyde_dh; 1.
DR   Pfam; PF02774; Semialdhyde_dhC; 1.
DR   PIRSF; PIRSF000148; ASA_dh; 1.
DR   SMART; SM00859; Semialdhyde_dh; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027920}.
FT   DOMAIN          3..122
FT                   /note="Semialdehyde dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00859"
FT   ACT_SITE        142
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
FT   ACT_SITE        239
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
SQ   SEQUENCE   351 AA;  37756 MW;  67D739B9B010E842 CRC64;
     MDSGSVGQRF ILLLADHPLL HLQAVGASSR SAGKLYKDAV RWKQARPMSE QLANLEVREC
     KASNFPDVDL VFSGLDSDVA GDVEMEFLKA EIPVFSNAKN YRRDPVVPLV VPTVNISHLG
     LIPHQRKHFG LKKGFLVCNS NCAVIGIVIP FAALQVKFGP VEDVEVFTEQ AVSGAGYPGV
     SSMDIMDNVI PYIAGEEDKL ETEAQKILGA MNSDATAFEE QSGLTVGATC TRVGVTDGHM
     AFVSLRFKQR PPPSADQVKQ AMREYVAEAQ KLGCPSAPEK AIVVFDEPDR PQPRLDRDIS
     GGYAVSVGRV REAAKGSHFD IRFAALSHNT VIGAAGSSIL NAEAAIIQGL L
//