ID Q97W78_SACS2 Unreviewed; 316 AA.
AC Q97W78;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=Fumarate reductase iron-sulfur subunit {ECO:0000256|ARBA:ARBA00017261};
DE AltName: Full=Quinol-fumarate reductase iron-sulfur subunit {ECO:0000256|ARBA:ARBA00029732};
GN Name=sdhB {ECO:0000313|EMBL:AAK42510.1};
GN OrderedLocusNames=SSO2357 {ECO:0000313|EMBL:AAK42510.1};
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057 {ECO:0000313|EMBL:AAK42510.1, ECO:0000313|Proteomes:UP000001974};
RN [1] {ECO:0000313|Proteomes:UP000001974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2
RC {ECO:0000313|Proteomes:UP000001974};
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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=1.3.5.1;
CC Evidence={ECO:0000256|ARBA:ARBA00034412};
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=1.3.5.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000030};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004287};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004287};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004287}.
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DR EMBL; AE006641; AAK42510.1; -; Genomic_DNA.
DR PIR; G90406; G90406.
DR RefSeq; WP_009989494.1; NC_002754.1.
DR AlphaFoldDB; Q97W78; -.
DR STRING; 273057.SSO2357; -.
DR PaxDb; 273057-SSO2357; -.
DR EnsemblBacteria; AAK42510; AAK42510; SSO2357.
DR GeneID; 72910938; -.
DR KEGG; sso:SSO2357; -.
DR PATRIC; fig|273057.12.peg.2444; -.
DR eggNOG; arCOG00962; Archaea.
DR HOGENOM; CLU_044838_3_1_2; -.
DR InParanoid; Q97W78; -.
DR PhylomeDB; Q97W78; -.
DR BRENDA; 1.3.5.1; 6163.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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 NCBIfam; TIGR00384; dhsB; 1.
DR PANTHER; PTHR43551; FUMARATE REDUCTASE IRON-SULFUR SUBUNIT; 1.
DR PANTHER; PTHR43551:SF2; FUMARATE REDUCTASE IRON-SULFUR SUBUNIT; 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; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001974}.
FT DOMAIN 146..175
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 199..229
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 316 AA; 36792 MW; ABEAAC2D7EB2A2AE CRC64;
MTQSQEEEVI LKVKRFNPEK GYWWAEYKLK VDRFTQFTEA LRRIKSEQDP TLSYRASCHM
AVCGSCGMKI NGEPRLACKT LVLDVVKKYN NNVITIEPMD YFKPIKDLIV DWDEFYERMF
KIKPRLYQAK EVLEGKAEHR LKPEDQRELW KFAQCIWCGL CVSACPAVVI DQQFLGPAAH
AKGYRFLADP RDTITEERMK ILIDSSWRCT YCYQCFNVCP RDIEPVTAIK KTRSFTKTYK
DKSEIAERGE KHVEAIHESI LKTGKLAEAP VYLKTYGVLQ SLVDLVYMSK TGKLKYALVQ
ERPVQNINEI KKIIGE
//
