ID   A0A3B4UY21_SERDU        Unreviewed;       278 AA.
AC   A0A3B4UY21;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Aspartate dehydrogenase domain-containing protein {ECO:0000256|ARBA:ARBA00020169};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000023376.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000023376.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the L-aspartate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00008331}.
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DR   AlphaFoldDB; A0A3B4UY21; -.
DR   STRING; 41447.ENSSDUP00000023376; -.
DR   Ensembl; ENSSDUT00000023811.1; ENSSDUP00000023376.1; ENSSDUG00000016990.1.
DR   GeneTree; ENSGT00390000004452; -.
DR   OMA; HIVEVDV; -.
DR   OrthoDB; 2879851at2759; -.
DR   Proteomes; UP000261420; Unplaced.
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; IPR011182; L-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   PIRSF; PIRSF005227; Asp_dh_NAD_syn; 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;
FT   DOMAIN          14..125
FT                   /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03447"
FT   DOMAIN          173..257
FT                   /note="Aspartate dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF01958"
SQ   SEQUENCE   278 AA;  29994 MW;  E230B625E302FD89 CRC64;
     MATSSSSLRI GVVGYGHLGQ YLVKRILQDG AALGFTLAFV WNRNSDKLKG LVPDELILGD
     LSSFADRRCD VIVEVCHPQI VKEFGLHFLS QSHFMVGSPS ALSDADLNKR LRQAAQQYGR
     TLYVPSGALW GGQDIQRLND SGALKALFIR MSKHPSCFRL TGDILSHWTE GEGRRVLFRG
     SVAELCPLAP NNVNTMAAAA VAAGTLGFTG VQGEIVSDTA LSDYHVVEVE VTGPDGFSVH
     TVRRNPARLG AVTGSATYNS FWNSLLVCKG HGGRVYLC
//