ID Q5LE11_BACFN Unreviewed; 318 AA.
AC Q5LE11;
DT 21-JUN-2005, integrated into UniProtKB/TrEMBL.
DT 21-JUN-2005, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE SubName: Full=Glycerate dehydrogenase {ECO:0000313|EMBL:CAH07642.1};
DE EC=1.1.1.29 {ECO:0000313|EMBL:CAH07642.1};
GN ORFNames=BF9343_1861 {ECO:0000313|EMBL:CAH07642.1};
OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS / NCTC 9343 / Onslow).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=272559 {ECO:0000313|EMBL:CAH07642.1, ECO:0000313|Proteomes:UP000006731};
RN [1] {ECO:0000313|EMBL:CAH07642.1, ECO:0000313|Proteomes:UP000006731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 /
RC Onslow {ECO:0000313|Proteomes:UP000006731};
RX PubMed=15746427; DOI=10.1126/science.1107008;
RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA Barrell B.G., Parkhill J.;
RT "Extensive DNA inversions in the B. fragilis genome control variable gene
RT expression.";
RL Science 307:1463-1465(2005).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CR626927; CAH07642.1; -; Genomic_DNA.
DR RefSeq; WP_005786931.1; NZ_UFTH01000001.1.
DR PaxDb; 272559-BF9343_1861; -.
DR KEGG; bfs:BF9343_1861; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_3_10; -.
DR BioCyc; BFRA272559:G1GHZ-2015-MONOMER; -.
DR Proteomes; UP000006731; Chromosome.
DR GO; GO:0008465; F:glycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd12162; 2-Hacid_dh_4; 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; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 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.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000006731}.
FT DOMAIN 21..317
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 107..286
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 318 AA; 35345 MW; 4D149F26D60D8155 CRC64;
MKIVVLDGYA ANPGDLNWDE LRTLGECEIY DRTAPDEVLE RSKDAEAILT NKVVITAEHM
ASLPNLKYIG VIATGYNIID VAAAKERGIT VTNIPAYSTP SVGQMVFAHI LNITQRVQHY
ADEVREGRWT QSQDFCYWDT PLIELLGKKI GLIGLGQTGY NTARIAIGFG MKVWAYTSKS
RLQLPPEIRK AELDQIFREC DIVSLHCPLT ESTRDLVNTR RLELMKPNAI LINTSRGPLV
NEHDLAEALN NYKIYAAGLD VLSTEPPRAD NPLLTARNCF ITPHIAWATS AARERLMAIL
VDNLKAYIGG KPVNNVAK
//
