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Database: UniProt
Entry: A0A090MYD4_STRRB
LinkDB: A0A090MYD4_STRRB
Original site: A0A090MYD4_STRRB 
ID   A0A090MYD4_STRRB        Unreviewed;       267 AA.
AC   A0A090MYD4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Aspartate dehydrogenase domain-containing protein {ECO:0000256|ARBA:ARBA00020169};
GN   ORFNames=SRAE_2000165400 {ECO:0000313|EMBL:CEF66989.1,
GN   ECO:0000313|WBParaSite:SRAE_2000165400.1,
GN   ECO:0000313|WormBase:SRAE_2000165400};
OS   Strongyloides ratti (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF66989.1};
RN   [1] {ECO:0000313|EMBL:CEF66989.1, ECO:0000313|Proteomes:UP000035682}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC   ECO:0000313|WBParaSite:SRAE_2000165400.1}, and ED321 Heterogonic
RC   {ECO:0000313|EMBL:CEF66989.1};
RA   Martin A.A.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:SRAE_2000165400.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (DEC-2020) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the L-aspartate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00008331}.
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DR   EMBL; LN609529; CEF66989.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A090MYD4; -.
DR   STRING; 34506.A0A090MYD4; -.
DR   EnsemblMetazoa; SRAE_2000165400.1; SRAE_2000165400.1; WBGene00261860.
DR   WBParaSite; SRAE_2000165400.1; SRAE_2000165400.1; WBGene00261860.
DR   WormBase; SRAE_2000165400; SRP06507; WBGene00261860; -.
DR   OMA; HIVEVDV; -.
DR   OrthoDB; 2879851at2759; -.
DR   Proteomes; UP000035682; Chromosome X.
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:UP000035682}.
FT   DOMAIN          7..111
FT                   /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03447"
FT   DOMAIN          164..246
FT                   /note="Aspartate dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF01958"
SQ   SEQUENCE   267 AA;  29679 MW;  D1A532C28B69DCB2 CRC64;
     MKIGIIGFGH LGQFLKNQLD EDNDYEVIKI WNRTPDVDNN ILPLNDITKD NLKDIDLVVE
     VAHPDITKMY AKIILSECNL FIGSPTALSD QETYNLVEDL GKKYNRSIFV PTGALWAAED
     IMKMAELGQL KKLSISMIKH PSSFKVFGDL KKLCDEAMET STLKVLYSGP VRHLCKLAPN
     NVNTMAGAAI AAKNLGFDNV EANLIADPEM LEWHIVELDV TGEDGFNVKI RRKNPAKPGA
     VTGNATYFSF LASIHRCKYK PSGIHIC
//
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