TFRB_METTM
ID TFRB_METTM Reviewed; 489 AA.
AC D9PUX5; O53142;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Fumarate reductase (CoM/CoB) subunit B {ECO:0000305};
DE EC=1.3.4.1 {ECO:0000269|PubMed:9578488};
DE AltName: Full=Thiol:fumarate reductase subunit B {ECO:0000303|PubMed:9578488};
GN Name=tfrB {ECO:0000303|PubMed:9578488};
GN OrderedLocusNames=MTBMA_c04210 {ECO:0000312|EMBL:ADL58022.1};
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:ADL58022.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20 AND 398-412,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
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:ADL58022.1};
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=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:9578488};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000269|PubMed:9578488};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:9578488};
CC Note=Binds 2 [4Fe-4S] clusters 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 B 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}.
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DR EMBL; AJ000942; CAA04399.1; -; Genomic_DNA.
DR EMBL; CP001710; ADL58022.1; -; Genomic_DNA.
DR RefSeq; WP_013295248.1; NC_014408.1.
DR AlphaFoldDB; D9PUX5; -.
DR SMR; D9PUX5; -.
DR STRING; 79929.MTBMA_c04210; -.
DR EnsemblBacteria; ADL58022; ADL58022; MTBMA_c04210.
DR GeneID; 9704127; -.
DR KEGG; mmg:MTBMA_c04210; -.
DR PATRIC; fig|79929.8.peg.410; -.
DR HOGENOM; CLU_023081_2_0_2; -.
DR OMA; VYQDACH; -.
DR OrthoDB; 21885at2157; -.
DR Proteomes; UP000000345; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
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:0051536; F:iron-sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 1.10.1060.10; -; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR004017; Cys_rich_dom.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR004489; Succ_DH/fum_Rdtase_Fe-S.
DR InterPro; IPR025192; Succ_DH/fum_Rdtase_N.
DR Pfam; PF02754; CCG; 2.
DR Pfam; PF13085; Fer2_3; 1.
DR Pfam; PF13183; Fer4_8; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR TIGRFAMs; TIGR00384; dhsB; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 2Fe-2S; 4Fe-4S; Cytoplasm; Direct protein sequencing; Iron; Iron-sulfur;
KW Metal-binding; Oxidoreductase; Repeat.
FT CHAIN 1..489
FT /note="Fumarate reductase (CoM/CoB) subunit B"
FT /id="PRO_0000430754"
FT DOMAIN 2..89
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 124..158
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 178..209
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 53
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 58
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 61
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 73
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 136
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 139
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 142
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 146
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 189
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 192
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 195
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 199
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT CONFLICT 445
FT /note="L -> V (in Ref. 1; CAA04399)"
FT CONFLICT 467
FT /note="K -> M (in Ref. 1; CAA04399)"
FT CONFLICT 487..489
FT /note="SDD -> ND (in Ref. 1; CAA04399)"
SQ SEQUENCE 489 AA; 54086 MW; D0233F4348F83FF7 CRC64;
MINVKVLRFE PGVDEKPHLE SYDIPSKEKM KVLDALQLIN KMYNANIAFR SSCRAGQCGS
CAVKMNGEVV LACRAEVEDG AVIEPVDLPV IKDLMVDRSE IEDKVRAMGL YLQSEARGIQ
RIKPEDYQDT KKLRGCIECF SCISSCPVIK ESTEYAGPYF MRYISKFAFD PRDEAERAAG
GVEEGLYCCT TCGKCAEVCP KELNVPGDAI EKLRAMACRE GAGPLDAHRK IKKLISETGR
SVDHIGKGFI ESVGQNPGSR IGFFTGCLVD YRMPDVGMAL LRVLREHGFE VDVPDGQVCC
GSPMIRTGQL DIVEDLVERN RRALEGYDTI ITVCAGCGAT LKKDYPRYGV ELNVLDISEF
LADRIDDIKM KPVNMRVTYH DPCHLLRGQG VKLEPRKILN SIPGLEFVEM EKQGQCCGSG
GGVKSGKPEI AESLGKKKAE MIRKLNVDAV ITICPFCQLH IKDSLEKEGL GDVKVMNILE
LLDMAYSDD
