ID F3PH77_9BACE Unreviewed; 333 AA.
AC F3PH77;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=D-lactate dehydrogenase {ECO:0000313|EMBL:EGF53092.1};
GN ORFNames=HMPREF9445_01424 {ECO:0000313|EMBL:EGF53092.1};
OS Bacteroides clarus YIT 12056.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=762984 {ECO:0000313|EMBL:EGF53092.1, ECO:0000313|Proteomes:UP000010321};
RN [1] {ECO:0000313|EMBL:EGF53092.1, ECO:0000313|Proteomes:UP000010321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 12056 {ECO:0000313|EMBL:EGF53092.1,
RC ECO:0000313|Proteomes:UP000010321};
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:EGF53092.1}.
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DR EMBL; AFBM01000010; EGF53092.1; -; Genomic_DNA.
DR RefSeq; WP_009121577.1; NZ_GL882585.1.
DR AlphaFoldDB; F3PH77; -.
DR STRING; 762984.SAMN05444376_1148; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_1_10; -.
DR OrthoDB; 9777288at2; -.
DR Proteomes; UP000010321; 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; cd12183; LDH_like_2; 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; PTHR43026; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR PANTHER; PTHR43026:SF1; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 6..332
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 112..300
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 333 AA; 37474 MW; 3A84B6B55E709ECC CRC64;
MAYTIAFFGS KPYDEASFNE KNSEYGFELR YYKGHLNLNN VILTQGVDAV CIFVNDTADA
EVIRQMAANG VKLLALRCAG YNNVDLKAAA ENGITVVRVP AYSPYAVAEY TVALMLSLNR
KIPRATWRTR DGNFSLHGLL GFDMYGKTAG IIGTGKIAKK LITILRGFGM NILAYDLYPD
YNFAREHQVV YTTLDELYHN SDIISLHCPL TEQTKYLIND YSISKMKDGV MIINTGRGQL
IHTNALIEGL KNKRIGSAGL DVYEEESEYF YEDQSDKIID DDTLARLLSF NNVIVTSHQA
FFTREALANI ASTTLMNIKD FMEHKKLENE VKL
//
