ID   K8FB18_9CHLO            Unreviewed;       392 AA.
AC   K8FB18;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CCO18808.1};
GN   OrderedLocusNames=Bathy12g02420 {ECO:0000313|EMBL:CCO18808.1};
OS   Bathycoccus prasinos.
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Bathycoccaceae; Bathycoccus.
OX   NCBI_TaxID=41875 {ECO:0000313|EMBL:CCO18808.1, ECO:0000313|Proteomes:UP000198341};
RN   [1] {ECO:0000313|EMBL:CCO18808.1, ECO:0000313|Proteomes:UP000198341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC 1105 {ECO:0000313|EMBL:CCO18808.1,
RC   ECO:0000313|Proteomes:UP000198341};
RA   Genoscope - CEA;
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; FO082267; CCO18808.1; -; Genomic_DNA.
DR   RefSeq; XP_007509693.1; XM_007509631.1.
DR   AlphaFoldDB; K8FB18; -.
DR   STRING; 41875.K8FB18; -.
DR   GeneID; 19012457; -.
DR   KEGG; bpg:Bathy12g02420; -.
DR   eggNOG; KOG0069; Eukaryota.
DR   OrthoDB; 6392at2759; -.
DR   Proteomes; UP000198341; Chromosome_12.
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   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; PTHR42938:SF25; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR42938; FORMATE DEHYDROGENASE 1; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000198341}.
FT   DOMAIN          59..382
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          155..228
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
FT   DOMAIN          258..355
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   392 AA;  42881 MW;  B53F84467455A445 CRC64;
     MKTTDDNDDE DNDETNTSEN NIIVRVLFCG EEFIGGFEAT KRYTEASSSS SSSSSDGVTV
     KVQNCPRERV KDMIQEYDVL VPLMTRFDET VINSAAGNGS GDRGKKLSKC KLILQFGVGL
     EGVAIDLATK AGIKVGRIRS DSNPNATSTA EMGVFLTLAA LKKVNECQIS VENKVLGSPM
     GESLFGATVL FVGWGRVAKA QAKMFKFGFQ CKIYALRRKR ERKGEEDDED DNELLDGLYE
     GDISDVDLVG NFPSGRNNIV VIACTCTPEN RKMVNKTFLD SLKFGEERVP GIVVNVARGA
     LVDERAMREA CENGMVLYYA TDVCYDEPVD VGGDLLSLGE NGKRASNIFV TPHVGGVTVN
     SYERMGKIVA EYARKIVKEK RIESDECVSI VN
//