TFRA_METTM
ID TFRA_METTM Reviewed; 547 AA.
AC D9PU00; O53141;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Fumarate reductase (CoM/CoB) subunit A {ECO:0000305};
DE EC=1.3.4.1 {ECO:0000269|PubMed:9578488};
DE AltName: Full=Thiol:fumarate reductase subunit A {ECO:0000303|PubMed:9578488};
GN Name=tfrA {ECO:0000303|PubMed:9578488};
GN OrderedLocusNames=MTBMA_c00880 {ECO:0000312|EMBL:ADL57698.1};
OS Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=79929 {ECO:0000312|EMBL:ADL57698.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19 AND 368-380,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg
RC {ECO:0000269|PubMed:9578488};
RX PubMed=9578488; DOI=10.1046/j.1432-1327.1998.2530292.x;
RA Heim S., Kunkel A., Thauer R.K., Hedderich R.;
RT "Thiol:fumarate reductase (Tfr) from Methanobacterium thermoautotrophicum--
RT identification of the catalytic sites for fumarate reduction and thiol
RT oxidation.";
RL Eur. J. Biochem. 253:292-299(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg
RC {ECO:0000312|EMBL:ADL57698.1};
RX PubMed=20802048; DOI=10.1128/jb.00844-10;
RA Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA Gottschalk G., Thauer R.K.;
RT "Complete genome sequence of Methanothermobacter marburgensis, a
RT methanoarchaeon model organism.";
RL J. Bacteriol. 192:5850-5851(2010).
RN [3]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=2499256; DOI=10.1128/aem.55.4.856-861.1989;
RA Khandekar S.S., Eirich L.D.;
RT "Purification and characterization of an anabolic fumarate reductase from
RT Methanobacterium thermoautotrophicum.";
RL Appl. Environ. Microbiol. 55:856-861(1989).
CC -!- FUNCTION: Catalyzes the reduction of fumarate with reduced coenzyme M
CC (CoM-S-H) and coenzyme B (CoB-S-H). In vitro, is able to reduces
CC fumarate with reduced benzyl viologen, oxidize CoM-S-H and CoB-S-H to
CC CoM-S-S-CoB with methylene blue, and reduce CoM-S-S-CoB with reduced
CC benzyl viologen. The enzyme has specificity for the two thiol compounds
CC as the CoB--CoM heterodisulfide reductase. The enzyme is very sensitive
CC to oxygen. {ECO:0000269|PubMed:9578488}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=coenzyme B + coenzyme M + fumarate = coenzyme M-coenzyme B
CC heterodisulfide + succinate; Xref=Rhea:RHEA:40235, ChEBI:CHEBI:29806,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:58319, ChEBI:CHEBI:58411,
CC ChEBI:CHEBI:58596; EC=1.3.4.1; Evidence={ECO:0000269|PubMed:9578488};
CC -!- COFACTOR:
CC Name=an oxidized flavin; Xref=ChEBI:CHEBI:60531;
CC Evidence={ECO:0000269|PubMed:9578488};
CC Note=Binds 1 flavin covalently per subunit.
CC {ECO:0000269|PubMed:9578488};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 mM for fumarate {ECO:0000269|PubMed:2499256};
CC pH dependence:
CC Optimum pH is7.0. {ECO:0000269|PubMed:2499256};
CC Temperature dependence:
CC Optimum temperature is 75 degrees Celsius.
CC {ECO:0000269|PubMed:2499256};
CC -!- SUBUNIT: Subunit A of the heterodimeric fumarate reductase of
CC methanogenic Archaea, composed of subunits A (TfrA) and B (TfrB).
CC {ECO:0000269|PubMed:9578488}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000303|PubMed:2499256}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC {ECO:0000305}.
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DR EMBL; AJ000941; CAA04398.1; -; Genomic_DNA.
DR EMBL; CP001710; ADL57698.1; -; Genomic_DNA.
DR RefSeq; WP_013294927.1; NC_014408.1.
DR AlphaFoldDB; D9PU00; -.
DR SMR; D9PU00; -.
DR STRING; 79929.MTBMA_c00880; -.
DR EnsemblBacteria; ADL57698; ADL57698; MTBMA_c00880.
DR GeneID; 9703793; -.
DR KEGG; mmg:MTBMA_c00880; -.
DR PATRIC; fig|79929.8.peg.86; -.
DR HOGENOM; CLU_014312_8_1_2; -.
DR OMA; PTAHHFM; -.
DR OrthoDB; 8547at2157; -.
DR Proteomes; UP000000345; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IDA:UniProtKB.
DR GO; GO:0006106; P:fumarate metabolic process; IDA:UniProtKB.
DR Gene3D; 3.50.50.60; -; 1.
DR Gene3D; 3.90.700.10; -; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR InterPro; IPR030664; SdhA/FrdA/AprA.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR PANTHER; PTHR11632; PTHR11632; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
DR SUPFAM; SSF46977; SSF46977; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF56425; SSF56425; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Flavoprotein; Oxidoreductase.
FT CHAIN 1..547
FT /note="Fumarate reductase (CoM/CoB) subunit A"
FT /id="PRO_0000430753"
FT CONFLICT 6
FT /note="Y -> D (in Ref. 1; CAA04398)"
FT CONFLICT 128
FT /note="R -> E (in Ref. 1; CAA04398)"
FT CONFLICT 256
FT /note="R -> K (in Ref. 1; CAA04398)"
FT CONFLICT 313..320
FT /note="PDEVIEEK -> LMRYRGE (in Ref. 1; CAA04398)"
FT CONFLICT 339..343
FT /note="PMEVA -> QWRL (in Ref. 1; CAA04398)"
FT CONFLICT 360
FT /note="R -> T (in Ref. 1; CAA04398)"
FT CONFLICT 367
FT /note="F -> Y (in Ref. 1; CAA04398)"
SQ SEQUENCE 547 AA; 60229 MW; 67728F3B60EC56EF CRC64;
MESELYECDV LIIGSGGAGC RAAIEVSEHK LTPIIVSKGL SFKSGCTGMA EGGYNAAFAC
VDPEDSPDVH FEDTMRGGGF INDPRLVRIL VDEAPDRLRD LEEYGALFDR QESGLLDQRP
FGGQTYRRTC YHGDRTGHEM ITALKEEVIR RDIETIDEVM ITSLLVEDGS VLGAMGVSIM
NSEPVAFRAS STILASGGAG HIYPVTSNTM QKGGDGFAIA WKAGADLIDM EQVQFHPTGM
VYPESRRGVL VTEAVRGEGG ILLNSEGERF MGRYDPRGEL ATRDVVARAI YTEIMEGRGT
ENGGVYLDVS HLPDEVIEEK LETMLLQFLD VGVDIRSEPM EVAPTAHHFM GGVRIDEWGR
TNLKNLFAAG EVSGGVHGAN RLGGNALADT QVFGRRAGIS AAKNAMSSSR RHVRSLIEEE
EQRIKDMVRD GSIRPAEIRD ELHEAMWSDV AIVRSRRSLE SAMSRISTLM DKLGDLDVPE
TGGFNSNLLE ALELENMLIT ASLVTRSALI REESRGSHYR EDFPETRPEW KRSILLNRKM
EPQFIGR
