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Database: UniProt
Entry: A0A1I0EWQ9_9BACT
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Original site: A0A1I0EWQ9_9BACT 
ID   A0A1I0EWQ9_9BACT        Unreviewed;       322 AA.
AC   A0A1I0EWQ9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:SET49106.1};
GN   ORFNames=SAMN04487998_2002 {ECO:0000313|EMBL:SET49106.1};
OS   Hymenobacter actinosclerus.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=82805 {ECO:0000313|EMBL:SET49106.1, ECO:0000313|Proteomes:UP000198697};
RN   [1] {ECO:0000313|Proteomes:UP000198697}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15310 {ECO:0000313|Proteomes:UP000198697};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FOHS01000002; SET49106.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0EWQ9; -.
DR   STRING; 82805.SAMN04487998_2002; -.
DR   OrthoDB; 1522997at2; -.
DR   Proteomes; UP000198697; 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   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   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198697}.
FT   DOMAIN          5..311
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          108..289
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   322 AA;  34863 MW;  460A82D74DF728A1 CRC64;
     MSLCLVIDEM HPSLPEYLEP LGLTLHYRPD LTAAEVPAAL AAHPYEGLVV RSKLRITREL
     LAYGPHLRYV CRAGAGVDNI DEAALAEAGV TLLNAPEGNR DAVGEYAVGL LLALFRHLPR
     ADAEVRAGHW RREANRGEEI GGKTIGLLGY GHMGRAFARR LSAFGCTVLA HDHDPACPPD
     DYATLVPLAE LRARAEVLSL HIPYAKANHH FVNEDFLAGF PNAIWLLNTA RGEVLDHAAL
     VSGLRTGQIR GAALDVLENE KLTGLTPEQQ ARFDYLRTAA NVVLSPHIGG WTFQSYERIN
     AVLARKLAAF LGVGEAGEQG VG
//
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