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Database: UniProt
Entry: A0A0C1DMU8_9SPHI
LinkDB: A0A0C1DMU8_9SPHI
Original site: A0A0C1DMU8_9SPHI 
ID   A0A0C1DMU8_9SPHI        Unreviewed;       308 AA.
AC   A0A0C1DMU8;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Phosphoglycerate dehydrogenase {ECO:0000313|EMBL:KIA95360.1};
GN   ORFNames=OC25_05795 {ECO:0000313|EMBL:KIA95360.1};
OS   Pedobacter kyungheensis.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1069985 {ECO:0000313|EMBL:KIA95360.1, ECO:0000313|Proteomes:UP000031246};
RN   [1] {ECO:0000313|EMBL:KIA95360.1, ECO:0000313|Proteomes:UP000031246}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KACC 16221 {ECO:0000313|EMBL:KIA95360.1,
RC   ECO:0000313|Proteomes:UP000031246};
RA   Anderson B.M., Newman J.D.;
RT   "Pedobacter Kyungheensis.";
RL   Submitted (OCT-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KIA95360.1}.
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DR   EMBL; JSYN01000005; KIA95360.1; -; Genomic_DNA.
DR   RefSeq; WP_039472773.1; NZ_JSYN01000005.1.
DR   AlphaFoldDB; A0A0C1DMU8; -.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000031246; 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:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR   GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
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; PS00670; D_2_HYDROXYACID_DH_2; 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          4..106
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          107..285
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   308 AA;  34545 MW;  D7DB00F1F7EB9AE5 CRC64;
     MKKILIVDDL HPAFKEQAIA MGYEVDDEPQ ITRQQTLGKI KDYTGIAVRT KFKIDAEIFA
     AAPHLKFVAR AGAGLDNIDD KIAFERNIEL INAPEGNCDA VGEHATGLLL SLMNNFRRAD
     IEIRNGLWDR EGNRGYELKG KKVGIIGYGF MGQSFAKKLA GFEVDVMAYD KYKTGFSDAF
     AREVSMEEIV KHSDVLSLHI PLTAETKLMV DDEYFFHFKK PIFFINTARG EIVKIDAVLN
     AIKAGKILGA GLDVLQTEKF PALGEQPWYN ELKNNDKVIL TPHVGGWTFD SYRKISEVLA
     EKLSVLHF
//
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