ID A0A4Y7RJM6_9FIRM Unreviewed; 249 AA.
AC A0A4Y7RJM6;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Fumarate reductase iron-sulfur subunit {ECO:0000313|EMBL:TEB09198.1};
DE EC=1.3.5.1 {ECO:0000313|EMBL:TEB09198.1};
GN Name=frdB_1 {ECO:0000313|EMBL:TEB09198.1};
GN ORFNames=Pmgp_03331 {ECO:0000313|EMBL:TEB09198.1};
OS Pelotomaculum propionicicum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Pelotomaculum.
OX NCBI_TaxID=258475 {ECO:0000313|EMBL:TEB09198.1, ECO:0000313|Proteomes:UP000297597};
RN [1] {ECO:0000313|EMBL:TEB09198.1, ECO:0000313|Proteomes:UP000297597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGP {ECO:0000313|EMBL:TEB09198.1,
RC ECO:0000313|Proteomes:UP000297597};
RX PubMed=30126076; DOI=.1111/1462-2920.14388;
RA Hidalgo-Ahumada C.A.P., Nobu M.K., Narihiro T., Tamaki H., Liu W.T.,
RA Kamagata Y., Stams A.J.M., Imachi H., Sousa D.Z.;
RT "Novel energy conservation strategies and behaviour of Pelotomaculum
RT schinkii driving syntrophic propionate catabolism.";
RL Environ. Microbiol. 20:4503-4511(2018).
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000256|ARBA:ARBA00001927};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase
CC iron-sulfur protein family. {ECO:0000256|ARBA:ARBA00009433}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TEB09198.1}.
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DR EMBL; QFFZ01000056; TEB09198.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Y7RJM6; -.
DR OrthoDB; 9804391at2; -.
DR Proteomes; UP000297597; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 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:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
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 NCBIfam; TIGR00384; dhsB; 1.
DR PANTHER; PTHR11921:SF36; FUMARATE REDUCTASE IRON-SULFUR SUBUNIT; 1.
DR PANTHER; PTHR11921; SUCCINATE DEHYDROGENASE IRON-SULFUR PROTEIN; 1.
DR Pfam; PF13085; Fer2_3; 1.
DR Pfam; PF13183; Fer4_8; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00022714};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00022714};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:TEB09198.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000297597}.
FT DOMAIN 141..170
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 249 AA; 28095 MW; F75DBC40DE482A00 CRC64;
MGRQLTISCF RYNPNIPGDK PRMQDYKLEE YEGMTLFVAL NEIREKLDPT LMFDFVCRAA
ICGSCAMLIN GRPRLACKTM TRTLPSRFTV MPLPVFKLIG DLSVDTGTWF RNLQIRTESW
IHTNKKFDFN ALEVRMENKT AEAIYEPERC IECGCCVAAC VTANIREDFL GATGINRVAR
FILDPRDERS NAEYFEVVGN EDGAFGCVGI MACADLCPME IPLQENLAFV RRKMAAAGLK
LQFPGVKIS
//