ID A0A1W2B589_9BURK Unreviewed; 323 AA.
AC A0A1W2B589;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:SMC68004.1};
GN ORFNames=SAMN06296008_11177 {ECO:0000313|EMBL:SMC68004.1};
OS Polynucleobacter kasalickyi.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=1938817 {ECO:0000313|EMBL:SMC68004.1, ECO:0000313|Proteomes:UP000192708};
RN [1] {ECO:0000313|EMBL:SMC68004.1, ECO:0000313|Proteomes:UP000192708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VK13 {ECO:0000313|EMBL:SMC68004.1,
RC ECO:0000313|Proteomes:UP000192708};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; FWXJ01000011; SMC68004.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W2B589; -.
DR STRING; 1938817.SAMN06296008_11177; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000192708; 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; 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; 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:UP000192708}.
FT DOMAIN 20..313
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 111..286
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 323 AA; 36068 MW; 2D3E05189FDF3476 CRC64;
MNIVIADDYQ NCVKDLNCYA TLSEHQVQVY VEPVQHRDEL IDRLKDADIL VIIRERISID
EELLRQLPKL RLISLVGRHS KTIDYAACTK YGVAVTHGIS SSPEAPAELT LALMLAVRRN
VVLEATRMKE GKFPITLSHR LAGSTLSIYG LGVIGQIVAK AAQAMGMQIL VWGREASLNK
AKELGYEIAQ SKADLFTRAD VLSLHLRYNK DTANSVSYAD LSLMKPTALF INTARAELVE
EGALEKALRQ GQPGFAGVDV YENEPILDGN HPFLSMENVV CMPHLGWADI DTFELYFGEA
FEQVVRYLNK ESLRLINPEV ILR
//
