ID A0A1G3CSN8_9BURK Unreviewed; 337 AA.
AC A0A1G3CSN8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=D-glycerate dehydrogenase {ECO:0000313|EMBL:OHC10476.1};
GN ORFNames=A2X74_01140 {ECO:0000313|EMBL:OHC10476.1};
OS Polynucleobacter sp. GWA2_45_21.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=1801989 {ECO:0000313|EMBL:OHC10476.1, ECO:0000313|Proteomes:UP000176957};
RN [1] {ECO:0000313|EMBL:OHC10476.1, ECO:0000313|Proteomes:UP000176957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OHC10476.1}.
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DR EMBL; MHZG01000001; OHC10476.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G3CSN8; -.
DR STRING; 1801989.A2X74_01140; -.
DR Proteomes; UP000176957; 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 16..331
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 120..299
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 337 AA; 35841 MW; B89C91B1E56E734C CRC64;
MNTPANHSTT SSKPKILVAR AIFPEALAKL EESYEVISNQ PDKVMTPEEL KKALSEVEGA
LVAGSERIDA TALSGAKNLK VVANISVGYN NFDVPAITAA GVMATNTPDV LTDTTADFGF
ALLMATARRI TESEHWVRAG KWGQWSIVTN PLGMDLHHST LGIIGMGRIG QGIAKRALGF
GMKVIYHNRK PLSEADEKAC GATYVSKEEL LRTADHVVLV LPYTAQNHHT IGAAEIAMMK
PSATLVNIAR GGIVDDAALA QALQSGKIFA AGLDVFEGEP QVHPELLKCS NIVLAPHIAS
ATEKTRRAMV DLAVQNLRAA LDGKKPPSLI NAEVLSA
//
