ID A0A1I3QSA8_9SPHI Unreviewed; 315 AA.
AC A0A1I3QSA8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:SFJ36409.1};
GN ORFNames=SAMN05444682_10986 {ECO:0000313|EMBL:SFJ36409.1};
OS Parapedobacter indicus.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Parapedobacter.
OX NCBI_TaxID=1477437 {ECO:0000313|EMBL:SFJ36409.1, ECO:0000313|Proteomes:UP000198670};
RN [1] {ECO:0000313|EMBL:SFJ36409.1, ECO:0000313|Proteomes:UP000198670}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RK1 {ECO:0000313|EMBL:SFJ36409.1,
RC ECO:0000313|Proteomes:UP000198670};
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; FOQO01000009; SFJ36409.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3QSA8; -.
DR STRING; 1477437.SAMN05444682_10986; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000198670; 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; 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; 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:UP000198670}.
FT DOMAIN 7..314
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 106..291
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 315 AA; 33396 MW; A10556813BBE61EB CRC64;
MKILANDGID PLGKQLLEDA GFSVDTTHIP QEELAERLQA YDAITVRSAT KIRAALIDAC
PNLKLIGRGG VGMDNIDVDY ARSKGIAVVN TPAASSLSVA ELVFAHLLGG VRFLYDSQRK
MPVEGATNFG GLKKAYAKGV ELRGKTLGVI GFGRIGRETA KVGLGLGMDV IVSDLFEAPK
SLPLVLSGGI TVDIPIQQVE IADLLERADF ISLHVPFIDK PIIGAAEFAQ VKPGVGIVNA
SRGGVIDELA LLEALNSGKV AFAGLDVFDN EPTPRTELLT HPKVSLTPHI GAATNEAQER
IGEELANLII EHLKK
//