ID   DLD_ANAHA               Reviewed;         475 AA.
AC   D4MUV9;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=D-lactate dehydrogenase {ECO:0000303|PubMed:34555022};
DE            EC=1.1.99.6 {ECO:0000269|PubMed:34555022};
GN   ORFNames=CL2_23160 {ECO:0000312|EMBL:CBL39175.1};
OS   Anaerostipes hadrus.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Anaerostipes.
OX   NCBI_TaxID=649756;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSC/2;
RG   metaHIT consortium;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Clostridiales sp. SSC/2.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=34555022; DOI=10.1371/journal.pcbi.1009446;
RA   Rembeza E., Engqvist M.K.M.;
RT   "Experimental and computational investigation of enzyme functional
RT   annotations uncovers misannotation in the EC 1.1.3.15 enzyme class.";
RL   PLoS Comput. Biol. 17:e1009446-e1009446(2021).
CC   -!- FUNCTION: Catalyzes the dehydrogenation of (R)-lactate (D-lactate) to
CC       pyruvate. Active in vitro with the artificial electron acceptor 2,6-
CC       dichlorophenolindophenol (DCPIP), but not with NAD, NADP, or cytochrome
CC       c. Also displays a very low oxidase activity in vitro on D-lactate and
CC       L-lactate with O2 as the electron acceptor, but this activity is most
CC       likely not physiological. {ECO:0000269|PubMed:34555022}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-lactate + A = AH2 + pyruvate; Xref=Rhea:RHEA:15089,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15361, ChEBI:CHEBI:16004,
CC         ChEBI:CHEBI:17499; EC=1.1.99.6;
CC         Evidence={ECO:0000269|PubMed:34555022};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:O29853};
CC       Note=Binds 1 FAD non-covalently per subunit.
CC       {ECO:0000250|UniProtKB:O29853};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:O29853};
CC       Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000250|UniProtKB:O29853};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.40 mM for (R)-lactate (at pH 7.4 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:34555022};
CC         Note=kcat is 5.2 sec(-1) with DCPIP as electron acceptor (at pH 7.4
CC         and 25 degrees Celsius). {ECO:0000269|PubMed:34555022};
CC   -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC       4 family. {ECO:0000305}.
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DR   EMBL; FP929061; CBL39175.1; -; Genomic_DNA.
DR   STRING; 649756.ERS852387_00121; -.
DR   EnsemblBacteria; CBL39175; CBL39175; CL2_23160.
DR   KEGG; bprl:CL2_23160; -.
DR   PATRIC; fig|245018.3.peg.2604; -.
DR   OMA; MLLMEFH; -.
DR   Proteomes; UP000008960; Chromosome.
DR   GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047809; F:D-2-hydroxy-acid dehydrogenase activity; IEA:RHEA.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 1.10.45.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR004113; FAD-linked_oxidase_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF55103; SSF55103; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Oxidoreductase; Reference proteome; Zinc.
FT   CHAIN           1..475
FT                   /note="D-lactate dehydrogenase"
FT                   /id="PRO_0000454851"
FT   DOMAIN          43..222
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
SQ   SEQUENCE   475 AA;  51601 MW;  1E6894B50DE245AE CRC64;
     MSEYQYNKVT PEMIEKFKEI APKRVLVGDE INEDFTHDEM AIYGKARPEV LVEATSTEEV
     AAVVKLCNEN KIPVTPSGAR TGLVGGAVSI GGGVMISLTK MNKILGYDKE NFVVKIQSGV
     LLNDLAQDAE KQGLLYPPDP GEKFATVGGN VATNAGGMRA VKYGCTRDYV RAMTVVLPTG
     EIVKLGATVS KTSSGYSLLN LMIGSEGTLG IITELTLKVI PAPKSVISLI IPYENLEDCI
     ATVPQFFMHH LAPQALEFME KEVVMDTEKF LGKQVYPKEL EGTEIGAYLL ATFDGNSEEQ
     LEDIIEQASE VVLEAGAIDV LVADTPALKK DAWAVRGALL EAIEADTVLL DECDVVVPTN
     KIAEFLTYTK SLEAEADFRV KSFGHAGDGN LHIYTCSNDM EEGEFKKQVA VFMDKVYAKA
     TEFGGMISGE HGIGHGKMDY LAESLGPVQM RIMEGVKEVF DPNMILNPGK ICYKL