ID A0A1I4CT19_9PROT Unreviewed; 326 AA.
AC A0A1I4CT19;
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:SFK84045.1};
GN ORFNames=SAMN02745775_108157 {ECO:0000313|EMBL:SFK84045.1};
OS Falsiroseomonas stagni DSM 19981.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Falsiroseomonas.
OX NCBI_TaxID=1123062 {ECO:0000313|EMBL:SFK84045.1, ECO:0000313|Proteomes:UP000199473};
RN [1] {ECO:0000313|EMBL:SFK84045.1, ECO:0000313|Proteomes:UP000199473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19981 {ECO:0000313|EMBL:SFK84045.1,
RC ECO:0000313|Proteomes:UP000199473};
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; FOSQ01000008; SFK84045.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4CT19; -.
DR STRING; 1123062.SAMN02745775_108157; -.
DR OrthoDB; 9793626at2; -.
DR Proteomes; UP000199473; 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; cd12173; PGDH_4; 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; 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; 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:UP000199473}.
FT DOMAIN 6..315
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 106..285
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 326 AA; 34598 MW; 982A029996CDD3BE CRC64;
MPHVICVRPI HEAAIEKMRS TEGVTVEILM DISPESLARN LPRADALIVR TIRIDRPFLA
HCTNLRLLAR HGVGYDAVDV PALTERGIPL TITPEANAVS VAEHALMLML ACARQLSGYD
SNLRQAKPVW GGQANLPTFD LAGKTVLVVG FGRIGTRVAK LCAAFGMKVL VRDPNIGKGS
IRGLGFTPVD DVMEAAAEAD IVTIHCPSDA STRHMVNAPF LARMKKGAVF INTARGTLVD
EAALDAALRA GHLGAAGIDV FHDEPVETAI PLLTAPNLIF TPHVAASTAE GLARMAMDAA
EACLACFDGT LDPDIVVNKE VLAGRN
//
