ID   R7GFJ5_9CLOT            Unreviewed;       258 AA.
AC   R7GFJ5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Predicted dinucleotide-utilizing enzyme {ECO:0000313|EMBL:CDE25598.1};
GN   ORFNames=BN598_00220 {ECO:0000313|EMBL:CDE25598.1};
OS   Clostridium sp. CAG:307.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262795 {ECO:0000313|EMBL:CDE25598.1, ECO:0000313|Proteomes:UP000018128};
RN   [1] {ECO:0000313|EMBL:CDE25598.1, ECO:0000313|Proteomes:UP000018128}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:307 {ECO:0000313|Proteomes:UP000018128};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDE25598.1}.
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DR   EMBL; CBIO010000065; CDE25598.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7GFJ5; -.
DR   Proteomes; UP000018128; 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:UP000018128}.
FT   DOMAIN          8..120
FT                   /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03447"
FT   DOMAIN          165..238
FT                   /note="Aspartate dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF01958"
SQ   SEQUENCE   258 AA;  27999 MW;  697DAB929ABD7CDF CRC64;
     MKRIGLYGCG HLNKIVVSCY KKGLLEGYEI VGCYSKTKEN REAMALNLGI KPCDSYEEML
     ERNLDFVVEA TNPAATKLIL ERTIEKGINV VLLSIGALSD ETYYEMIKNK CIASNAKIYL
     ASGAISGFEV LMTARLMGLT SASLTNTKGA RALAKTSLYD PKMEKEDMTA FKGSAYEAIK
     NLPTGINVGV ATALATRGVH NTIITIQTKP DFIGDSQCID IECGDEIKAH LDVYSKSSDI
     AGYSVVALLK NLNSPIVF
//