ID   F1RH12_PIG              Unreviewed;       376 AA.
AC   F1RH12;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 2.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Aspartate dehydrogenase domain-containing protein {ECO:0000256|ARBA:ARBA00020169};
GN   Name=ASPDH {ECO:0000313|Ensembl:ENSSSCP00000023660.2};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000023660.2, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000023660.2, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000023660.2,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSSCP00000023660.2}
RP   IDENTIFICATION.
RG   Ensembl;
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   AlphaFoldDB; F1RH12; -.
DR   PaxDb; 9823-ENSSSCP00000023660; -.
DR   PeptideAtlas; F1RH12; -.
DR   Ensembl; ENSSSCT00000022461.4; ENSSSCP00000023660.2; ENSSSCG00000054855.1.
DR   eggNOG; ENOG502QVGC; Eukaryota.
DR   GeneTree; ENSGT00390000004452; -.
DR   HOGENOM; CLU_063528_0_0_1; -.
DR   TreeFam; TF315092; -.
DR   Proteomes; UP000008227; Chromosome 6.
DR   Bgee; ENSSSCG00000003217; Expressed in longissimus lumborum muscle and 45 other cell types or tissues.
DR   ExpressionAtlas; F1RH12; baseline and differential.
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   1: Evidence at protein level;
KW   Proteomics identification {ECO:0007829|PeptideAtlas:F1RH12};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227}.
FT   DOMAIN          106..216
FT                   /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03447"
FT   DOMAIN          265..354
FT                   /note="Aspartate dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF01958"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   376 AA;  40038 MW;  E4DD45DB1E08312F CRC64;
     MGRVRGAGRG DKLRAPEPQT IVPSAPPDSH PTPTRHTHTP TSGPLLEEGG RFRRGSRVKC
     PKISCCPNLQ WGWAVGSEPP VELSPLTITP KGMALDQVPR KVGIVGYGRL GQSLVSHLLT
     QGPELGLELV FVWNRDPGRM AGSVPPSLQL QNLAALGERH PDLVVEVAHP KIIHESGAEI
     LRYAHLLVGS PSALAEQATE QRLLEASHRW GHAVFVARGA LWGTDDITRL DKAGGLQSLR
     VTMATHPDGF RLEGPLATAH STGPRTVLYE GPVRGLCPFA PRNSNTMAAA ALAAPSLGFD
     RVIGVLVADF SLKDMHVVDV ELSGPPGPTG RSFAVHTHRE NPAEPGAVTG SATVTAFWRS
     LLGCCQLPSK PGIHFC
//