FRDB_MYCTU
ID FRDB_MYCTU Reviewed; 247 AA.
AC P9WN89; L0T766; Q10761;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Fumarate reductase iron-sulfur subunit;
DE EC=1.3.5.4;
DE AltName: Full=Quinol-fumarate reductase iron-sulfur subunit;
DE Short=QFR iron-sulfur subunit;
GN Name=frdB; OrderedLocusNames=Rv1553; ORFNames=MTCY48.12c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + succinate = a quinol + fumarate;
CC Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.4;
CC Evidence={ECO:0000250|UniProtKB:P0AC47};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a menaquinone + succinate = a menaquinol + fumarate;
CC Xref=Rhea:RHEA:27834, Rhea:RHEA-COMP:9537, Rhea:RHEA-COMP:9539,
CC ChEBI:CHEBI:16374, ChEBI:CHEBI:18151, ChEBI:CHEBI:29806,
CC ChEBI:CHEBI:30031; EC=1.3.5.4;
CC Evidence={ECO:0000250|UniProtKB:P0AC47};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000250|UniProtKB:P0AC47};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250|UniProtKB:P0AC47};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000250|UniProtKB:P0AC47};
CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250|UniProtKB:P0AC47};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P0AC47};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P0AC47};
CC -!- SUBUNIT: Fumarate dehydrogenase forms part of an enzyme complex
CC containing four subunits: a flavoprotein, an iron-sulfur, and two
CC hydrophobic anchor proteins. {ECO:0000250|UniProtKB:P0AC47}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P0AC47};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P0AC47}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:P0AC47}.
CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase
CC iron-sulfur protein family. {ECO:0000305}.
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DR EMBL; AL123456; CCP44317.1; -; Genomic_DNA.
DR PIR; F70762; F70762.
DR RefSeq; NP_216069.1; NC_000962.3.
DR RefSeq; WP_003407767.1; NZ_NVQJ01000004.1.
DR AlphaFoldDB; P9WN89; -.
DR SMR; P9WN89; -.
DR STRING; 83332.Rv1553; -.
DR PaxDb; P9WN89; -.
DR DNASU; 886378; -.
DR GeneID; 886378; -.
DR KEGG; mtu:Rv1553; -.
DR TubercuList; Rv1553; -.
DR eggNOG; COG0479; Bacteria.
DR OMA; AFASDCR; -.
DR PhylomeDB; P9WN89; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0045284; C:plasma membrane fumarate reductase complex; IBA:GO_Central.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051538; F:3 iron, 4 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:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1060.10; -; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR004489; Succ_DH/fum_Rdtase_Fe-S.
DR InterPro; IPR025192; Succ_DH/fum_Rdtase_N.
DR Pfam; PF13085; Fer2_3; 1.
DR Pfam; PF13183; Fer4_8; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR TIGRFAMs; TIGR00384; dhsB; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3Fe-4S; 4Fe-4S; Cell membrane; Electron transport; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Oxidoreductase; Reference proteome;
KW Transport; Tricarboxylic acid cycle.
FT CHAIN 1..247
FT /note="Fumarate reductase iron-sulfur subunit"
FT /id="PRO_0000158705"
FT DOMAIN 14..94
FT /note="2Fe-2S ferredoxin-type"
FT DOMAIN 140..169
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 12
FT /ligand="a menaquinone"
FT /ligand_id="ChEBI:CHEBI:16374"
FT /evidence="ECO:0000250|UniProtKB:P0AC47"
FT BINDING 56
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P0AC47"
FT BINDING 61
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P0AC47"
FT BINDING 76
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P0AC47"
FT BINDING 149
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P0AC47"
FT BINDING 152
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P0AC47"
FT BINDING 155
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P0AC47"
FT BINDING 159
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:P0AC47"
FT BINDING 205
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:P0AC47"
FT BINDING 211
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:P0AC47"
FT BINDING 215
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P0AC47"
FT BINDING 226..229
FT /ligand="a menaquinone"
FT /ligand_id="ChEBI:CHEBI:16374"
FT /evidence="ECO:0000250|UniProtKB:P0AC47"
SQ SEQUENCE 247 AA; 27234 MW; 15863DCCB2C82B0B CRC64;
MMDRIVMEVS RYRPEIESAP TFQAYEVPLT REWAVLDGLT YIKDHLDGTL SFRWSCRMGI
CGSSGMTING DPKLACATFL ADYLPGPVRV EPMRNFPVIR DLVVDISDFM AKLPSVKPWL
VRHDEPPVED GEYRQTPAEL DAFKQFSMCI NCMLCYSACP VYALDPDFLG PAAIALGQRY
NLDSRDQGAA DRRDVLAAAD GAWACTLVGE CSTACPKGVD PAGAIQRYKL TAATHALKKL
LFPWGGG
