ID A0A258P8Y7_9BURK Unreviewed; 328 AA.
AC A0A258P8Y7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=D-glycerate dehydrogenase {ECO:0000313|EMBL:OYY38992.1};
GN ORFNames=B7Y60_01545 {ECO:0000313|EMBL:OYY38992.1};
OS Polaromonas sp. 35-63-35.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=1970418 {ECO:0000313|EMBL:OYY38992.1, ECO:0000313|Proteomes:UP000216365};
RN [1] {ECO:0000313|EMBL:OYY38992.1, ECO:0000313|Proteomes:UP000216365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35-63-35 {ECO:0000313|EMBL:OYY38992.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-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 ECO:0000256|RuleBase:RU003719}.
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:OYY38992.1}.
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DR EMBL; NCFQ01000002; OYY38992.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A258P8Y7; -.
DR Proteomes; UP000216365; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd05301; GDH; 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; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 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.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 6..321
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 110..289
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 328 AA; 35161 MW; 550879A437C1AE03 CRC64;
MSKPNILVAR AVFPEVITHL QQHFEVHANQ ADETWSKAEL IEKLRGMDGA FTTGGDRIDA
EVLAACPTLK ICANMAVGYN NFDIDAMTAA GVLATNAPDV LTETTADFGF ALLMATARRI
TESEHYLRAG KWSKWSYDMF AGSDIHGSTL GVLGMGRIGQ GIARRGAHGF GMKVIYHNRS
RLDAALEAEC KASYVSKEEL LRTADHVVLV LPYSPASHHT IGAAELALMK PTATLVNIAR
GGIVDDAALA AALRDRRIAA AGLDVFEGEP QVHPDLLTVP NVVLTPHIAS ATVPTRMAMA
MLAADNLIGF FKEKRPLTPL NPAVLAAK
//
