ID A0A0P9CHK5_9BACL Unreviewed; 246 AA.
AC A0A0P9CHK5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Fumarate reductase {ECO:0000313|EMBL:KPV45231.1};
GN Name=frdB {ECO:0000313|EMBL:KPV45231.1};
GN ORFNames=AN477_02160 {ECO:0000313|EMBL:KPV45231.1};
OS Alicyclobacillus ferrooxydans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=471514 {ECO:0000313|EMBL:KPV45231.1, ECO:0000313|Proteomes:UP000050482};
RN [1] {ECO:0000313|EMBL:KPV45231.1, ECO:0000313|Proteomes:UP000050482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC-34 {ECO:0000313|EMBL:KPV45231.1,
RC ECO:0000313|Proteomes:UP000050482};
RA Hemp J.;
RT "Draft genome sequence of Alicyclobacillus ferrooxydans DSM 22381.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:KPV45231.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LJCO01000011; KPV45231.1; -; Genomic_DNA.
DR RefSeq; WP_054967555.1; NZ_LJCO01000011.1.
DR AlphaFoldDB; A0A0P9CHK5; -.
DR STRING; 471514.AN477_02160; -.
DR PATRIC; fig|471514.4.peg.2762; -.
DR OrthoDB; 9804391at2; -.
DR Proteomes; UP000050482; 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: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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000050482}.
FT DOMAIN 142..171
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 246 AA; 27547 MW; 88BBBAF14433891D CRC64;
MASRELTFRI LRYNPETPDV KPHLQDFHLN EEPGMTLFIV LNRLREEQDP SLRFDFVCRA
SICGSCGMLI NGKPNLACKT LTKALPDVTT LMPLPVFKLL GDLSVDTGVW FRDVSLRTES
WVHTDEVFDP DAAEEKMDNE LAKEIYEAER CIECGCCIGG CATANIKPSF IGAAGINRVA
RFMMDPRDKR TEQEYFEVVA SEDGVFGCVG LMACDDNCPV GVPLRSQLAY VRRKMAVAGW
HMGRGR
//
