ID A0A1H8YDG7_9PROT Unreviewed; 332 AA.
AC A0A1H8YDG7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:SEP50189.1};
GN ORFNames=SAMN02990966_07562 {ECO:0000313|EMBL:SEP50189.1};
OS Rhodospirillales bacterium URHD0017.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales.
OX NCBI_TaxID=1380357 {ECO:0000313|EMBL:SEP50189.1, ECO:0000313|Proteomes:UP000198826};
RN [1] {ECO:0000313|EMBL:SEP50189.1, ECO:0000313|Proteomes:UP000198826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=URHD0017 {ECO:0000313|EMBL:SEP50189.1,
RC ECO:0000313|Proteomes:UP000198826};
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; FODP01000034; SEP50189.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8YDG7; -.
DR STRING; 1380357.SAMN02990966_07562; -.
DR OrthoDB; 9793626at2; -.
DR Proteomes; UP000198826; 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:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd12169; PGDH_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; 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}.
FT DOMAIN 19..324
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 119..293
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 332 AA; 35940 MW; 8EBFC5ADE4335020 CRC64;
MPQTCKLALL DDYQKVALKM ADWDRLRKRG VEITVFHEPF SSVEDAAKKL APFDVLGLLR
ERTAFPRALI EKLPNLKFMV LTGARASSLD DKAATDRGIP ISNTPGGGSN ASTAELSWAL
LMMCARDLAK GERLMRSGGW HDGIEQMVVL EGKRLGVIGL GRLGSRVAGY AKAFGMDVVA
WSQNLTEEKA AKGGAKLVTK DELLKTSDFV SIHLVLSDRT RGLLGAADLA KMKKSAILVN
TSRGPIVDEA ALLAALKNGT IAHAGLDVYD KEPVAPGHPF TKLENVTLIP HLGYVVEDSY
RHFYAGTIED VEAWLDGKPI NVINPEALKK AA
//
