GenomeNet

Database: UniProt
Entry: A0A0F5K3F8_9BURK
LinkDB: A0A0F5K3F8_9BURK
Original site: A0A0F5K3F8_9BURK 
ID   A0A0F5K3F8_9BURK        Unreviewed;       283 AA.
AC   A0A0F5K3F8;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KKB64424.1};
GN   ORFNames=WM40_05775 {ECO:0000313|EMBL:KKB64424.1};
OS   Robbsia andropogonis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Robbsia.
OX   NCBI_TaxID=28092 {ECO:0000313|EMBL:KKB64424.1, ECO:0000313|Proteomes:UP000033618};
RN   [1] {ECO:0000313|EMBL:KKB64424.1, ECO:0000313|Proteomes:UP000033618}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICMP2807 {ECO:0000313|EMBL:KKB64424.1,
RC   ECO:0000313|Proteomes:UP000033618};
RA   Lopes-Santos L., Castro D.B., Ottoboni L.M., Park D., Weirc B.S.,
RA   Destefano S.A.;
RT   "Draft Genome Sequence of Burkholderia andropogonis type strain ICMP2807,
RT   isolated from Sorghum bicolor.";
RL   Submitted (MAR-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:KKB64424.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LAQU01000004; KKB64424.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F5K3F8; -.
DR   STRING; 28092.WM40_05775; -.
DR   PATRIC; fig|28092.6.peg.1375; -.
DR   Proteomes; UP000033618; 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; 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:UP000033618}.
FT   DOMAIN          14..129
FT                   /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03447"
FT   DOMAIN          186..268
FT                   /note="Aspartate dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF01958"
SQ   SEQUENCE   283 AA;  29589 MW;  6666486D09A9BE2B CRC64;
     MGVARPPLRV GLAGFGAVGQ DLARRLLRGD LPGAVLSAVC ANRLDAARER LDALDDVAGA
     GKTVPAMRLD AMLDKVDIVC ECATAESFPA IARAVVSAGK TMITVSVAGL PNTPDLMDLA
     LRHGGRIRVA SGGLPGLDAV RAVKEDGIDT IRLKTTFRPE SLAHEPFVRG LGFDFGSVPA
     ASVPNTKVFA GTAREAAAAF PRHFNVAIAL SLCGVGFDKT DVEVWVDGAV EGAVQEIDVK
     AYAADLTLIS RNRPSRNPRT SRIVAPSVMA ALRNFVDILQ VGS
//
DBGET integrated database retrieval system