ID   A0A2A4S923_9CHLR        Unreviewed;       363 AA.
AC   A0A2A4S923;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Glycerate dehydrogenase {ECO:0000313|EMBL:PCI17561.1};
GN   ORFNames=COB68_09510 {ECO:0000313|EMBL:PCI17561.1};
OS   SAR202 cluster bacterium.
OC   Bacteria; Chloroflexota; SAR202 cluster.
OX   NCBI_TaxID=2030829 {ECO:0000313|EMBL:PCI17561.1, ECO:0000313|Proteomes:UP000217661};
RN   [1] {ECO:0000313|Proteomes:UP000217661}
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       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:PCI17561.1}.
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DR   EMBL; NVSQ01000030; PCI17561.1; -; Genomic_DNA.
DR   Proteomes; UP000217661; 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   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd12172; PGDH_like_2; 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; 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.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719}.
FT   DOMAIN          63..354
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          155..327
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   363 AA;  39439 MW;  D994F1CB8983380D CRC64;
     MKSVTWPDAA PRFTRNKALT PRIIPLILRR GVRPMSNNKP FALLVVPDDE PPVLSGTPYE
     DRARALAENV EWHFDRPLDN DETVARMQNA EAVINIRSSV QFTREVLAAC PALKILSVWG
     TGVDHVDLTA AEELGITVSN TPAYGAPYVS EHALTLALAV SRQIVINDQH IRSGGWTRGF
     INELYGKTLG VVGTGAIGRR MIQLGKGIGM RVVAWTVHPS PERAAEYDVE FLSLDDLLRQ
     SDVVSLHVAL TEITRGLIGR AQFDLMKDTA ILVNTSRGLA VDEDAXIDAL ENGRIAGAAL
     DVFQAEPLAP GHRLTQLENV VLSPHAGGMA YNGTMRGLEM SVENLESFAA GSPIYVVAQG
     SRR
//