ID A0A1G1KFC4_9BACT Unreviewed; 216 AA.
AC A0A1G1KFC4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Aspartate dehydrogenase {ECO:0000313|EMBL:OGW91560.1};
GN ORFNames=A3D28_04795 {ECO:0000313|EMBL:OGW91560.1};
OS Omnitrophica bacterium RIFCSPHIGHO2_02_FULL_63_14.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1801824 {ECO:0000313|EMBL:OGW91560.1, ECO:0000313|Proteomes:UP000179358};
RN [1] {ECO:0000313|EMBL:OGW91560.1, ECO:0000313|Proteomes:UP000179358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGW91560.1}.
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DR EMBL; MHFJ01000033; OGW91560.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1KFC4; -.
DR Proteomes; UP000179358; 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;
FT DOMAIN 5..66
FT /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF03447"
FT DOMAIN 115..202
FT /note="Aspartate dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01958"
SQ SEQUENCE 216 AA; 23662 MW; F98911DCE143DDCE CRC64;
MLEPDELIKK CDLVIEAASA QAAYEIARKA LSQGKDVMVM SVGGLIGREK EVFRLAKTHR
CCLYLPSGGV VGLDGLKAAG IGKIQRVTLT TRKPPQGFMD APYVLRRRIR LQHLKQEKLL
FEGSAARAVK GFPKNINVSA TLSLAGLGAK RTRVRIIANP LMLLNVHELY VQGDFGSFYT
RTENFPAPHN PKTSQLAILS AVATLDRILR NVKIGT
//
