GenomeNet

Database: UniProt
Entry: A0A2A4M078_9BACT
LinkDB: A0A2A4M078_9BACT
Original site: A0A2A4M078_9BACT 
ID   A0A2A4M078_9BACT        Unreviewed;       247 AA.
AC   A0A2A4M078;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding domain-containing protein {ECO:0000259|Pfam:PF02826};
GN   ORFNames=COC21_06530 {ECO:0000313|EMBL:PCH53310.1};
OS   Verrucomicrobiales bacterium.
OC   Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales.
OX   NCBI_TaxID=2026801 {ECO:0000313|EMBL:PCH53310.1, ECO:0000313|Proteomes:UP000219702};
RN   [1] {ECO:0000313|Proteomes:UP000219702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT   "A dynamic microbial community with high functional redundancy inhabits the
RT   cold, oxic subseafloor aquifer.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854}.
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:PCH53310.1}.
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; NVQP01000133; PCH53310.1; -; Genomic_DNA.
DR   Proteomes; UP000219702; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:UniProt.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR   PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          9..195
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
FT   UNSURE          211
FT                   /note="E or Q"
FT                   /evidence="ECO:0000313|EMBL:PCH53310.1"
SQ   SEQUENCE   247 AA;  26897 MW;  106CFC1FD9CC09AD CRC64;
     MDEVADQAIG MLIACNRRFL RVERGLKESL EPWDCRAVEP VPRLAGATLG IVGLGRIGQA
     TAQRAKAMRM RVIAHDPYLR PGIEKVFGVE XVXXXELLET SDAVSLHVPL TDETRQMIDA
     DALGRMKPSA ILVNTARGAV VDTAALAAAL REGKIAGAGV DVLPAEPARA DEPLIQLWRD
     ADESNVNLIL MPHTAFYSVE GLLEMRTKAA EEIVRAXRGX KLINCVNAQW LPEEMRDRVL
     VGTPPTV
//
DBGET integrated database retrieval system