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Database: UniProt
Entry: A0A1I0DGG3_9FIRM
LinkDB: A0A1I0DGG3_9FIRM
Original site: A0A1I0DGG3_9FIRM 
ID   A0A1I0DGG3_9FIRM        Unreviewed;       313 AA.
AC   A0A1I0DGG3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:SET31182.1};
GN   ORFNames=SAMN04487771_101217 {ECO:0000313|EMBL:SET31182.1};
OS   [Clostridium] aminophilum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1526 {ECO:0000313|EMBL:SET31182.1, ECO:0000313|Proteomes:UP000199820};
RN   [1] {ECO:0000313|EMBL:SET31182.1, ECO:0000313|Proteomes:UP000199820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH1P1 {ECO:0000313|EMBL:SET31182.1,
RC   ECO:0000313|Proteomes:UP000199820};
RA   de Groot N.N.;
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; FOIL01000012; SET31182.1; -; Genomic_DNA.
DR   RefSeq; WP_074649098.1; NZ_FOIL01000012.1.
DR   AlphaFoldDB; A0A1I0DGG3; -.
DR   STRING; 1526.SAMN02910262_00222; -.
DR   eggNOG; COG0111; Bacteria.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000199820; 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:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR   GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR   CDD; cd05303; PGDH_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; IPR029753; D-isomer_DH_CS.
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.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 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:UP000199820}.
FT   DOMAIN          4..310
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          106..288
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   313 AA;  34309 MW;  BBF450DA2A3341CA CRC64;
     MKCLIIDRVH ALIGEELSKY MQVDTKILPT QEELAAIIPD YDVLIMRVDP KIDKTILDAA
     KNLKVIGVCS VGLNHIDMDA AKANNITVYN APGMNANAVA ELTISKLLDI SRHVVAAHID
     VTKNHEWDKY KFVGCELRGK TLGIMGFGRI GRRVGELARA FKMDVVAYDP FLKPEDFEKE
     HAKGVTVEEM LKVADYVTIH VPLTKDTKDL FNKDSIAKMK DGAVVLNMSR GGICNEADMY
     EALKSGKLGG YGADVMENEL AGGGLTGNDT FVSPLFDCDN FLVTPHLGAQ SVDASYDIGV
     MITGKIKEFL NLK
//
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