LCTD_ACEWD
ID LCTD_ACEWD Reviewed; 466 AA.
AC H6LBS1;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Lactate dehydrogenase (NAD(+),ferredoxin) subunit LctD {ECO:0000305};
DE EC=1.3.1.110 {ECO:0000269|PubMed:24762045};
GN Name=lctD {ECO:0000303|PubMed:24762045};
GN Synonyms=glcD {ECO:0000312|EMBL:AFA47664.1};
GN OrderedLocusNames=Awo_c08730 {ECO:0000312|EMBL:AFA47664.1};
OS Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655
OS / WB1).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Eubacteriaceae;
OC Acetobacterium.
OX NCBI_TaxID=931626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1;
RA Poehlein A., Schmidt S., Kaster A.-K., Goenrich M., Vollmers J.,
RA Thuermer A., Gottschalk G., Thauer R.K., Daniel R., Mueller V.;
RT "Complete genome sequence of Acetobacterium woodii.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1;
RX PubMed=24762045; DOI=10.1111/1462-2920.12493;
RA Weghoff M.C., Bertsch J., Mueller V.;
RT "A novel mode of lactate metabolism in strictly anaerobic bacteria.";
RL Environ. Microbiol. 17:670-677(2015).
CC -!- FUNCTION: The lactate dehydrogenase-Etf complex catalyzes the oxidation
CC of lactate to pyruvate. It uses flavin-based electron confurcation to
CC drive endergonic lactate oxidation with NAD(+) as oxidant at the
CC expense of simultaneous exergonic electron flow from reduced ferredoxin
CC to NAD(+). {ECO:0000269|PubMed:24762045}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=lactate + 2 NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = 2 NADH
CC + 2 oxidized [2Fe-2S]-[ferredoxin] + pyruvate; Xref=Rhea:RHEA:46964,
CC Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:24996, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.110;
CC Evidence={ECO:0000269|PubMed:24762045};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:O29853};
CC -!- ACTIVITY REGULATION: Activity is stimulated by divalent cations.
CC Highest stimulation is observed with Ca(2+).
CC {ECO:0000269|PubMed:24762045}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.6 mM for D-lactate {ECO:0000269|PubMed:24762045};
CC KM=112 mM for L-lactate {ECO:0000269|PubMed:24762045};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:24762045};
CC Temperature dependence:
CC Optimum temperature is between 20 and 30 degrees Celsius.
CC {ECO:0000269|PubMed:24762045};
CC -!- SUBUNIT: Part of the stable heterotrimeric lactate dehydrogenase-Etf
CC complex, which is formed by the lactate dehydrogenase LctD and the
CC electron-transferring flavoprotein (Etf) alpha (LctC) and beta (LctB)
CC subunits. {ECO:0000269|PubMed:24762045}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24762045}.
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000305}.
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DR EMBL; CP002987; AFA47664.1; -; Genomic_DNA.
DR RefSeq; WP_014355267.1; NC_016894.1.
DR STRING; 931626.Awo_c08730; -.
DR EnsemblBacteria; AFA47664; AFA47664; Awo_c08730.
DR KEGG; awo:Awo_c08730; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_9_2_9; -.
DR OMA; TPRTCGE; -.
DR OrthoDB; 1188552at2; -.
DR BioCyc; MetaCyc:MON-21372; -.
DR BRENDA; 1.3.1.110; 52.
DR Proteomes; UP000007177; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008720; F:D-lactate dehydrogenase activity; IEA:UniProtKB-EC.
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 Cytoplasm; FAD; Flavoprotein; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..466
FT /note="Lactate dehydrogenase (NAD(+),ferredoxin) subunit
FT LctD"
FT /id="PRO_0000453363"
FT DOMAIN 41..219
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
SQ SEQUENCE 466 AA; 51142 MW; 8297A5BAA0872D45 CRC64;
MNYKKVEASD IAAIKELIPA ERVFVGTEIG EDFSHDELGS IHSYPEVLIK VTSTEEVSKI
MKYAYEHNIP VVVRGSGTGL VGACVPLFGG IMLETTLMNN ILELDTENLT VTVEPGVLLM
ELSKFVEEND LFYPPDPGEK SATIAGNIST NAGGMRAVKY GVTRDYVRGL TVVLANGEII
ELGGKIVKNS SGYSLKDLVI GSEGTLCVIT KAILKLLPLP KMTLSLLIPF ENISDAAGIV
PKIIKSKAIP TAIEFMERQT ILFAEDFLGK KFPDSSSNAY ILLTFDGNTK EQVEAEYETV
ANLCLAEGAK DVYIVDTVER KDSVWSARGA FLEAIKASTT EMDECDVVVP RNRIAEFIEF
THDLAKEMDV RIPSFGHAGD GNLHIYVCRD ELCQADWEAK LAEAMDRMYA KALTFEGLVS
GEHGIGYAKR KYLLNDFGTE HLALMAGIKQ TFDPKNLLNP KKVCQM
