ID A0A133Q6J7_9BACT Unreviewed; 305 AA.
AC A0A133Q6J7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=D-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:KXA38494.1};
GN ORFNames=HMPREF3226_01586 {ECO:0000313|EMBL:KXA38494.1};
OS Prevotella corporis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=28128 {ECO:0000313|EMBL:KXA38494.1, ECO:0000313|Proteomes:UP000070533};
RN [1] {ECO:0000313|Proteomes:UP000070533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJR7716 {ECO:0000313|Proteomes:UP000070533};
RA Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-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}.
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:KXA38494.1}.
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DR EMBL; LRQG01000113; KXA38494.1; -; Genomic_DNA.
DR RefSeq; WP_060940801.1; NZ_KQ957260.1.
DR AlphaFoldDB; A0A133Q6J7; -.
DR STRING; 28128.HMPREF3226_01586; -.
DR PATRIC; fig|28128.5.peg.1626; -.
DR eggNOG; COG1052; Bacteria.
DR OrthoDB; 9777288at2; -.
DR Proteomes; UP000070533; 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; 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.
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:UP000070533}.
FT DOMAIN 26..304
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 123..248
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 305 AA; 32803 MW; 12CB75D5A4D41A37 CRC64;
MKVLIATEKP FAAAAVNGIR KEIEGAGHEL ILLEKYTEKA QLLDAVKDVD AMIIRSDKAD
AEVLAAAKNL KVIVRAGAGY DNIDLAAATE HNVVAENTPG QNSNAVAELV LGLLVYGVRN
FYNGKSGSEL KGKKLGILAF GNVGRNVARI AKGFGMEVYA FDAFCPKDVI EAAGVKAVDN
QDALFETCDI VSLHIPATPE TKQSINYALV NKMHKGGILI NTARKEVINE AELIKLMGER
EDLKFITDIK PDADADFAKF EGRYFSTPKK MGAQTAEANI NAGIAAAKQI NAFFATGDKK
FQVNK
//
