LCTC_ACEWD
ID LCTC_ACEWD Reviewed; 418 AA.
AC H6LBB1;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Lactate dehydrogenase (NAD(+),ferredoxin) subunit LctC {ECO:0000305};
DE EC=1.3.1.110 {ECO:0000269|PubMed:24762045};
DE AltName: Full=Electron transfer flavoprotein large subunit {ECO:0000250|UniProtKB:H6LGM8};
DE AltName: Full=Electron transfer flavoprotein subunit alpha {ECO:0000250|UniProtKB:H6LGM8};
DE Short=EtfA {ECO:0000305};
DE AltName: Full=Lactate dehydrogenase-Etf complex subunit LctC {ECO:0000305};
GN Name=lctC {ECO:0000303|PubMed:24762045};
GN Synonyms=etfA {ECO:0000312|EMBL:AFA47663.1};
GN OrderedLocusNames=Awo_c08720 {ECO:0000312|EMBL:AFA47663.1};
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(+). The electron transfer flavoprotein (Etf) mediates the
CC electron transfer between the different donors and acceptors.
CC {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:P13804};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P13804};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:H6LGM8};
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=31 uM for ferredoxin {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 ETF alpha-subunit/FixB family.
CC {ECO:0000305}.
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DR EMBL; CP002987; AFA47663.1; -; Genomic_DNA.
DR RefSeq; WP_014355266.1; NC_016894.1.
DR SMR; H6LBB1; -.
DR STRING; 931626.Awo_c08720; -.
DR EnsemblBacteria; AFA47663; AFA47663; Awo_c08720.
DR KEGG; awo:Awo_c08720; -.
DR eggNOG; COG1145; Bacteria.
DR eggNOG; COG2025; Bacteria.
DR HOGENOM; CLU_034178_1_1_9; -.
DR OMA; DMKENTD; -.
DR OrthoDB; 1400253at2; -.
DR BioCyc; MetaCyc:MON-21371; -.
DR BRENDA; 1.3.1.110; 52.
DR Proteomes; UP000007177; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01715; ETF_alpha; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR014730; ETF_a/b_N.
DR InterPro; IPR001308; ETF_a/FixB.
DR InterPro; IPR033947; ETF_alpha_N.
DR InterPro; IPR014731; ETF_asu_C.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR43153; PTHR43153; 1.
DR Pfam; PF01012; ETF; 1.
DR Pfam; PF00766; ETF_alpha; 1.
DR SMART; SM00893; ETF; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cytoplasm; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..418
FT /note="Lactate dehydrogenase (NAD(+),ferredoxin) subunit
FT LctC"
FT /id="PRO_0000453361"
FT BINDING 285
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P13804"
FT BINDING 325..328
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P13804"
FT BINDING 343..348
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P13804"
FT BINDING 362
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P13804"
FT BINDING 380..381
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P13804"
SQ SEQUENCE 418 AA; 46170 MW; 0E113BEDDE4C9EC5 CRC64;
MAGIKIIKEN VDRETFEALA EICPFDAFSY ENDKLEVTAA CKMCKMCLKK GPEGVLILEE
DEKVAIDKSL YRGITVYVDH IEGQIHPVTF ELIGKARELA AVIGHPVYAL LMGTNITEKA
DELLKYGVDK VFVYDKPELK HFVIEPYANV LEDFIEKVKP SSILVGATNV GRSLAPRVAA
RYRTGLTADC TILEMKENTD LVQIRPAFGG NIMAQIVTEN TRPQFCTVRY KVFTAPERVN
EPWGDVEMMD IEKAKLVSAI EVMEVIKKEK GIDLSEAETI VAVGRGVKCE KDLDMIHEFA
EKIGATVACT RPGIEAGWFD ARLQIGLSGR TVKPKLIIAL GISGAVQFAA GMQNSEYIIA
INSDPKAPIF NIAHCGMVGD LYEILPELLT MIEGPENNKD TETISIPEAI ETPERMVV
