ID A0A0M0BWR9_9ARCH Unreviewed; 234 AA.
AC A0A0M0BWR9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KON32820.1};
GN ORFNames=AC479_06505 {ECO:0000313|EMBL:KON32820.1};
OS miscellaneous Crenarchaeota group-6 archaeon AD8-1.
OC Archaea; Candidatus Bathyarchaeota; Candidatus Bathyarchaeia.
OX NCBI_TaxID=1685126 {ECO:0000313|EMBL:KON32820.1, ECO:0000313|Proteomes:UP000037259};
RN [1] {ECO:0000313|EMBL:KON32820.1, ECO:0000313|Proteomes:UP000037259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD8-1 {ECO:0000313|EMBL:KON32820.1};
RA Lazar C.S., Baker B.J., Seitz K.W., Hyde A.S., Dick G.J., Hinrichs K.-U.,
RA Teske A.P.;
RT "New insights into the roles of widespread benthic archaea in carbon and
RT nitrogen cycling.";
RL Submitted (JUN-2015) 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:KON32820.1}.
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DR EMBL; LFWW01000041; KON32820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M0BWR9; -.
DR STRING; 1685126.AC479_06505; -.
DR PATRIC; fig|1685126.3.peg.1777; -.
DR Proteomes; UP000037259; 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; 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; 2.
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 13..109
FT /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF03447"
FT DOMAIN 141..224
FT /note="Aspartate dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01958"
SQ SEQUENCE 234 AA; 25638 MW; B99A631BA81F6E2C CRC64;
MSEKKTVKVG IIGCGAIGTL IAQAIEKKIV KCEELILYDY IQKKAKDLKN SIDFPVTIAE
NLNKMLNLKP TIIVEAASQK AVKDYIKPIT SKGIKLIVMS SGALIGSNYQ TERIYVPSGA
IGGLDAISSA ALTKISKVVL TTIFEGNAEK AATQFPRSMN VASTLSFIVK PAKVHVRLIS
DPTIKRNTHE IKVEWQYGEM YFCFSNDPHP ENPKTSALAA WSAIQLLKTL IKNQ
//
