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Database: UniProt
Entry: A0A3S1BE12_ELYCH
LinkDB: A0A3S1BE12_ELYCH
Original site: A0A3S1BE12_ELYCH 
ID   A0A3S1BE12_ELYCH        Unreviewed;       278 AA.
AC   A0A3S1BE12;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Aspartate dehydrogenase domain-containing protein {ECO:0000256|ARBA:ARBA00020169};
GN   ORFNames=EGW08_013601 {ECO:0000313|EMBL:RUS78631.1};
OS   Elysia chlorotica (Eastern emerald elysia) (Sea slug).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Sacoglossa; Placobranchoidea;
OC   Plakobranchidae; Elysia.
OX   NCBI_TaxID=188477 {ECO:0000313|EMBL:RUS78631.1, ECO:0000313|Proteomes:UP000271974};
RN   [1] {ECO:0000313|EMBL:RUS78631.1, ECO:0000313|Proteomes:UP000271974}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC2010 {ECO:0000313|EMBL:RUS78631.1};
RC   TISSUE=Whole organism of an adult {ECO:0000313|EMBL:RUS78631.1};
RA   Cai H., Li Q., Fang X., Li J., Curtis N.E., Altenburger A., Shibata T.,
RA   Feng M., Maeda T., Schwartz J.A., Shigenobu S., Lundholm N., Nishiyama T.,
RA   Yang H., Hasebe M., Li S., Pierce S.K., Wang J.;
RT   "A draft genome assembly of the solar-powered sea slug Elysia chlorotica.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the L-aspartate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00008331}.
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:RUS78631.1}.
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DR   EMBL; RQTK01000498; RUS78631.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S1BE12; -.
DR   STRING; 188477.A0A3S1BE12; -.
DR   Proteomes; UP000271974; Unassembled WGS sequence.
DR   GO; GO:0033735; F:aspartate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR   InterPro; IPR002811; Asp_DH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR31873:SF6; ASPARTATE DEHYDROGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR31873; L-ASPARTATE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF01958; Asp_DH_C; 1.
DR   Pfam; PF03447; NAD_binding_3; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000271974}.
FT   DOMAIN          12..116
FT                   /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03447"
FT   DOMAIN          167..257
FT                   /note="Aspartate dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF01958"
SQ   SEQUENCE   278 AA;  30118 MW;  22D894C3A9ECA2CE CRC64;
     MSEVSRRVGI VGFGHLGQYL VEEIEKRNDV ELAFVWNRTP EALMGKVSDS LILKDLSNFK
     ERGADLIVEV AHPSISQQYG PSFLAHADYM VGSPTALADP ELESSLRSAA TSHGLYIPSG
     AFWGGDDIKK MADRGTLQAL KVTMKKHPTC FKLSGELEVL NKTVKDKAVI LYDDKVRGLC
     HVAPNNVNTM AAAALAAHNL GFDKVQGTLV SDPSLRDWHI VEVEVWGPGN MLEDKAFHCK
     TVRRNPATFG AVTGSATYAS FLSSMLGAHS KGPGVHLC
//
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