ID F6AU72_DELSC Unreviewed; 338 AA.
AC F6AU72;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Glyoxylate reductase {ECO:0000313|EMBL:AEF90269.1};
DE EC=1.1.1.26 {ECO:0000313|EMBL:AEF90269.1};
GN OrderedLocusNames=DelCs14_3273 {ECO:0000313|EMBL:AEF90269.1};
OS Delftia sp. (strain Cs1-4).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=742013 {ECO:0000313|EMBL:AEF90269.1, ECO:0000313|Proteomes:UP000009225};
RN [1] {ECO:0000313|Proteomes:UP000009225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cs1-4 {ECO:0000313|Proteomes:UP000009225};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Bradfield C., Sheety A., Cheng S.,
RA Chain P., Denef V., Hickey W., Woyke T.;
RT "Complete sequence of Delftia sp. Cs1-4.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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; CP002735; AEF90269.1; -; Genomic_DNA.
DR RefSeq; WP_013802619.1; NC_015563.1.
DR AlphaFoldDB; F6AU72; -.
DR KEGG; del:DelCs14_3273; -.
DR HOGENOM; CLU_019796_1_3_4; -.
DR OMA; KHGAWQQ; -.
DR Proteomes; UP000009225; Chromosome.
DR GO; GO:0047964; F:glyoxylate reductase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd12169; PGDH_like_1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
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; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719,
KW ECO:0000313|EMBL:AEF90269.1}.
FT DOMAIN 39..323
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 111..296
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 338 AA; 36801 MW; 2886F0A17328D453 CRC64;
MNIIILDDYQ DAVRKLDCAR LLEPFNAKVF TNTVKGVGQL SVRLRDADII VLTRERTQIS
RQLLEKLPRL KLIAQTGKAG AHIDVQACTD QGVAIAEGVG SPIAPAELTW SLIMAATRRL
PQYIANLKHG AWQQSGFKAA SMPANFGLGS VLHGRTLGIW GYGRIGRLVA HYGHAFGMQV
LVWGSESSRQ KAQADGFAAA ESREAFFTES DVLSMHLRLH EATRGIVTAQ DLARMKPTAL
FVNTSRAELV EADALLGALN RGRPGLAAVD VFESEPILQG HALLRLENCI CTPHIGYVEQ
DSYELYFRAA FDNVVNFVAG QPSNILNPEV FSGPARAG
//