ID A0A1U7R095_MESAU Unreviewed; 287 AA.
AC A0A1U7R095;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Aspartate dehydrogenase domain-containing protein {ECO:0000256|ARBA:ARBA00020169};
GN Name=Aspdh {ECO:0000313|RefSeq:XP_005084839.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_005084839.1};
RN [1] {ECO:0000313|RefSeq:XP_005084839.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the L-aspartate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008331}.
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DR RefSeq; XP_005084839.1; XM_005084782.3.
DR AlphaFoldDB; A0A1U7R095; -.
DR GeneID; 101836570; -.
DR KEGG; maua:101836570; -.
DR CTD; 554235; -.
DR eggNOG; ENOG502QVGC; Eukaryota.
DR OrthoDB; 2879851at2759; -.
DR Proteomes; UP000189706; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000189706}.
FT DOMAIN 17..127
FT /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF03447"
FT DOMAIN 176..265
FT /note="Aspartate dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01958"
SQ SEQUENCE 287 AA; 30320 MW; 77C01E842676439A CRC64;
MATSIVPRVP QKVGVVGYGR LGQSLVSRLL AQGSELGLEL VFVWNRDPGR MAGSVPPALQ
LQDLTALEDR HPDLVVEVAH PNIIHESGAQ ILRHANLLVG SPSALADQTT EQQLMEASNC
WGHTVFVARG ALWGTEDIRR LDLAGGLQSL RVTMATHPDG FRLEGSLAAA HISGPRTVLY
EGPVRGLCPL APRNSNTMAA AALAAPSLGF DRVVGVLVAD LSLRDMHVVD VELKGPPGPT
GHSFAVHTHR ENPAQPGAVT GSATVTAFWL SLLGCCQLPS KPGIHLC
//
