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Database: UniProt
Entry: A0A1I5F0Q5_9FIRM
LinkDB: A0A1I5F0Q5_9FIRM
Original site: A0A1I5F0Q5_9FIRM 
ID   A0A1I5F0Q5_9FIRM        Unreviewed;       313 AA.
AC   A0A1I5F0Q5;
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:SFO16911.1};
GN   ORFNames=SAMN04489757_11195 {ECO:0000313|EMBL:SFO16911.1};
OS   Anaerocolumna aminovalerica.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Anaerocolumna.
OX   NCBI_TaxID=1527 {ECO:0000313|EMBL:SFO16911.1, ECO:0000313|Proteomes:UP000198806};
RN   [1] {ECO:0000313|EMBL:SFO16911.1, ECO:0000313|Proteomes:UP000198806}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1283 {ECO:0000313|EMBL:SFO16911.1,
RC   ECO:0000313|Proteomes:UP000198806};
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|RuleBase:RU003719}.
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DR   EMBL; FOWD01000011; SFO16911.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5F0Q5; -.
DR   STRING; 1527.SAMN04489757_11195; -.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000198806; 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; cd12161; GDH_like_1; 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; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198806}.
FT   DOMAIN          21..311
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          112..283
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   313 AA;  33961 MW;  95A35C622A9F5B91 CRC64;
     MKLVIIEPIG VEKERLLSLA AEALGDKIEI TYYDTKVTDT ETLIERGKDA DIIAVSNLPL
     NEDVINGCKN LKLLSVAFTG VDHIAMETCK KNGVMVCNCA GYSTAAVADL VFGMIITLYR
     NIIPCNKVTR EEGTKDGLIG FELEGKKFGV IGTGTIGMRV ANIARAFGCE VYAYSRTQKE
     VQGITYVDLD TLLSTCDIVS IHTPLNESTK GLIHGEKLAL MKKNAILINT ARGPIVDSKA
     LADALNSGKI AGAGIDVFEK EPPIEKDHPL FHTPNTVVAP HIGFATKEAL VKRAVIVFDN
     VVKWMENKPQ NVM
//
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