ID B1R3R7_CLOPF Unreviewed; 332 AA.
AC B1R3R7;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Putative D-lactate dehydrogenase {ECO:0000313|EMBL:EDT25030.1};
GN ORFNames=AC1_0601 {ECO:0000313|EMBL:EDT25030.1};
OS Clostridium perfringens B str. ATCC 3626.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=451754 {ECO:0000313|EMBL:EDT25030.1, ECO:0000313|Proteomes:UP000004342};
RN [1] {ECO:0000313|EMBL:EDT25030.1, ECO:0000313|Proteomes:UP000004342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B str. ATCC 3626 {ECO:0000313|Proteomes:UP000004342};
RA Paulsen I., Sebastian Y.;
RT "Annotation of Clostridium perfringens B str. ATCC 3626.";
RL Submitted (JUL-2007) 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:EDT25030.1}.
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DR EMBL; ABDV01000002; EDT25030.1; -; Genomic_DNA.
DR RefSeq; WP_003455390.1; NZ_ABDV01000002.1.
DR AlphaFoldDB; B1R3R7; -.
DR Proteomes; UP000004342; 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; cd12184; HGDH_like; 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; IPR029752; D-isomer_DH_CS1.
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; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 6..331
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 332 AA; 36937 MW; 503E35FB4B5E26F7 CRC64;
MIKLVCYGVR ETEVPYFHKL NEEFGYDLTL VEKNLNHENV EEAIGAEAIM VRGNCMADRQ
NLELLKSKGL KYVLTRTVGF DHVDLEAAKD LGLQVARVPG YSPNAIGELA VSLAMMLLRH
TAYTTNRTSN KNFVVDGFMF SKEIRNCTVG ILGAGRIGLT TAKLFKGLGA KVVAYDVFQS
DAAKEIVEFM PLDEVLKVSD VISVHMPYIK GQNYHMINEE FISKMKNDAI IINTARGELQ
DIEAIVKALE EGRLGGFGAD VLEGESAVFF KNLEGQKLEN ESYEKLISLY PRALVTPHMG
SYTDEALRNM IGISYENLKE YLEGNTCKNA IA
//
