ID A0A024JRU6_9MYCO Unreviewed; 318 AA.
AC A0A024JRU6;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:CDO86565.1};
GN Name=serA3 {ECO:0000313|EMBL:CDO86565.1};
GN ORFNames=BN973_00909 {ECO:0000313|EMBL:CDO86565.1};
OS Mycobacterium triplex.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium simiae complex.
OX NCBI_TaxID=47839 {ECO:0000313|EMBL:CDO86565.1};
RN [1] {ECO:0000313|EMBL:CDO86565.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO86565.1};
RX PubMed=24874681; DOI=10.1128/genomeA.00499-14;
RA Sassi M., Croce O., Robert C., Raoult D., Drancourt M.;
RT "Draft Genome Sequence of Mycobacterium triplex DSM 44626.";
RL Genome Announc. Announc.2:e00499-e00414(2014).
RN [2] {ECO:0000313|EMBL:CDO86565.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO86565.1};
RA Urmite Genomes U.;
RL Submitted (APR-2014) 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; HG964446; CDO86565.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024JRU6; -.
DR STRING; 47839.BN973_00909; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_3_11; -.
DR OrthoDB; 117809at2; -.
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; cd12175; 2-Hacid_dh_11; 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; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 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; PS00670; D_2_HYDROXYACID_DH_2; 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}.
FT DOMAIN 27..313
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 109..280
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 318 AA; 34196 MW; 93D893A832EC0B74 CRC64;
MALRVLAHFV PGKRVLDFLA AEADWLDIRW CAADDDDGFY RELPDAEVIW HVLRPLSGAD
LKRGERLRLV HKLGAGVNTI DVATATDRGI AVANMPGANA PSVAEGTVLL MLAALRRLPQ
LDHATRQGRG WPLDPELGET VRDIGSCTVG LVGYGNIAKR VAAVVGAMGA TVLHTSTRDD
GRPGWLPLPE LLAASDIVSL HLPLTAQTHH LLNRDAIASM KPTAVLVNTS RGAIVDEDAL
VGALRDGRLA AAGLDVFEAE PTAADNPLFD LDNVVLTPHV TWYTADTMRR YLVEAVSNCR
RLRDGEPLAN VVNLPTGY
//
