ID F3PYQ7_9BACE Unreviewed; 306 AA.
AC F3PYQ7;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=D-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:EGF49327.1};
GN ORFNames=HMPREF9446_03963 {ECO:0000313|EMBL:EGF49327.1};
OS Bacteroides fluxus YIT 12057.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=763034 {ECO:0000313|EMBL:EGF49327.1, ECO:0000313|Proteomes:UP000003416};
RN [1] {ECO:0000313|EMBL:EGF49327.1, ECO:0000313|Proteomes:UP000003416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 12057 {ECO:0000313|EMBL:EGF49327.1,
RC ECO:0000313|Proteomes:UP000003416};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2011) 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:EGF49327.1}.
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DR EMBL; AFBN01000115; EGF49327.1; -; Genomic_DNA.
DR RefSeq; WP_009127129.1; NZ_GL882697.1.
DR AlphaFoldDB; F3PYQ7; -.
DR STRING; 763034.HMPREF9446_03963; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_3_10; -.
DR Proteomes; UP000003416; 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; 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:UP000003416}.
FT DOMAIN 21..305
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 123..250
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 306 AA; 32953 MW; 62291E13A3D106B5 CRC64;
MKVLVATDKP FAKVAVDGIR KEIEAAGYEL VLLEKYGEKA KLLEAVKDAN AIIIRSDIID
AEVLDAAKDL KIVVRAGAGY DNVDLEAATA HNVCVMNTPG QNSNAVAELA FGLMVMAVRN
MYNGTSGTEL MGKKLGIHAY GNVGRNVARI AKGFGMEIYA FDAFCPKEVI EKDGVKAVGS
AEELYSICNV VSLHIPATAE TKNSINHALV NRLPKGGLLV NTARKEVINE AELIQLMEER
ADLKYMTDIM PAAHETFAAK FAGRYFSTPK KMGAQTAEAN INAGIAAAKQ IVGFLKDGCE
KFRVNK
//
