LCTB_ACEWD
ID LCTB_ACEWD Reviewed; 264 AA.
AC H6LBB0;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Lactate dehydrogenase (NAD(+),ferredoxin) subunit LctB {ECO:0000305};
DE EC=1.3.1.110 {ECO:0000269|PubMed:24762045};
DE AltName: Full=Electron transfer flavoprotein small subunit {ECO:0000250|UniProtKB:H6LGM7};
DE AltName: Full=Electron transfer flavoprotein subunit beta {ECO:0000250|UniProtKB:H6LGM7};
DE Short=EtfB {ECO:0000305};
DE AltName: Full=Lactate dehydrogenase-Etf complex subunit LctB {ECO:0000305};
GN Name=lctB {ECO:0000303|PubMed:24762045};
GN Synonyms=etfB {ECO:0000312|EMBL:AFA47662.1};
GN OrderedLocusNames=Awo_c08710 {ECO:0000312|EMBL:AFA47662.1};
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:H6LGM7};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:H6LGM7};
CC -!- COFACTOR:
CC Name=AMP; Xref=ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:H6LGM7};
CC Note=Binds 1 AMP per subunit. {ECO:0000250|UniProtKB:H6LGM7};
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=430 uM for NAD(+) {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 beta-subunit/FixA family. {ECO:0000305}.
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DR EMBL; CP002987; AFA47662.1; -; Genomic_DNA.
DR RefSeq; WP_014355265.1; NC_016894.1.
DR SMR; H6LBB0; -.
DR STRING; 931626.Awo_c08710; -.
DR EnsemblBacteria; AFA47662; AFA47662; Awo_c08710.
DR KEGG; awo:Awo_c08710; -.
DR eggNOG; COG2086; Bacteria.
DR HOGENOM; CLU_060196_2_1_9; -.
DR OMA; GIDSKMN; -.
DR OrthoDB; 1027643at2; -.
DR BioCyc; MetaCyc:MON-21370; -.
DR BRENDA; 1.3.1.110; 52.
DR Proteomes; UP000007177; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR CDD; cd01714; ETF_beta; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR014730; ETF_a/b_N.
DR InterPro; IPR012255; ETF_b.
DR InterPro; IPR033948; ETF_beta_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR21294; PTHR21294; 1.
DR Pfam; PF01012; ETF; 1.
DR PIRSF; PIRSF000090; Beta-ETF; 1.
DR SMART; SM00893; ETF; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; FAD; Flavoprotein; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..264
FT /note="Lactate dehydrogenase (NAD(+),ferredoxin) subunit
FT LctB"
FT /id="PRO_0000453362"
SQ SEQUENCE 264 AA; 29069 MW; 7340B3B5503BE6D5 CRC64;
MKILVCIKQV PGTSNVEVDP ETGVLIRDGV ESKLNPYDLF GLETAFRLKE QLGGTITTLS
MGPMQSKEVL MESFYMGADE GCLLSDRKFG GADVVATSYT LAQGTKRLGD FDLIICGKQT
TDGDTAQVGP EMAEFLGIPH VTNVIKILAA DEKGLTLQMN MEESLEIQRV PYPCLITVDK
DIYTPRLPSY KRKLDISKNP EIKILTLKDM YDTNEKKYGL SGSPTQVERI FPPESNVEKT
SFEGDGKVLA KALLGILTEK KYLG
