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Database: UniProt
Entry: N6VIL1_BARVB
LinkDB: N6VIL1_BARVB
Original site: N6VIL1_BARVB 
ID   N6VIL1_BARVB            Unreviewed;       259 AA.
AC   N6VIL1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Succinate dehydrogenase iron-sulfur subunit {ECO:0000256|ARBA:ARBA00022131, ECO:0000256|RuleBase:RU361237};
DE            EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792, ECO:0000256|RuleBase:RU361237};
GN   Name=sdhB {ECO:0000313|EMBL:ENN93046.1};
GN   ORFNames=BVtw_17010 {ECO:0000313|EMBL:ENN93046.1};
OS   Bartonella vinsonii subsp. berkhoffii str. Tweed.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=1094502 {ECO:0000313|EMBL:ENN93046.1, ECO:0000313|Proteomes:UP000014011};
RN   [1] {ECO:0000313|EMBL:ENN93046.1, ECO:0000313|Proteomes:UP000014011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tweed {ECO:0000313|EMBL:ENN93046.1};
RX   PubMed=23555299; DOI=10.1371/journal.pgen.1003393;
RA   Guy L., Nystedt B., Toft C., Zaremba-Niedzwiedzka K., Berglund E.C.,
RA   Granberg F., Naslund K., Eriksson A.S., Andersson S.G.;
RT   "A gene transfer agent and a dynamic repertoire of secretion systems hold
RT   the keys to the explosive radiation of the emerging pathogen Bartonella.";
RL   PLoS Genet. 9:E1003393-E1003393(2013).
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|RuleBase:RU361237};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|RuleBase:RU361237};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000256|RuleBase:RU361237};
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000256|RuleBase:RU361237};
CC       Note=Binds 1 [3Fe-4S] cluster. {ECO:0000256|RuleBase:RU361237};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|RuleBase:RU361237};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|RuleBase:RU361237};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate
CC       from succinate (bacterial route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004894}.
CC   -!- SUBUNIT: Part of an enzyme complex containing four subunits: a
CC       flavoprotein, an iron-sulfur, cytochrome b-556, and a hydrophobic
CC       anchor protein. {ECO:0000256|ARBA:ARBA00011294}.
CC   -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase
CC       iron-sulfur protein family. {ECO:0000256|ARBA:ARBA00009433,
CC       ECO:0000256|RuleBase:RU361237}.
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:ENN93046.1}.
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DR   EMBL; AGWD01000027; ENN93046.1; -; Genomic_DNA.
DR   RefSeq; WP_010705863.1; NZ_KB915638.1.
DR   AlphaFoldDB; N6VIL1; -.
DR   PATRIC; fig|1094502.3.peg.2132; -.
DR   HOGENOM; CLU_044838_0_2_5; -.
DR   UniPathway; UPA00223; UER01005.
DR   Proteomes; UP000014011; Unassembled WGS sequence.
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:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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; 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; 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:SF29; SUCCINATE DEHYDROGENASE [UBIQUINONE] IRON-SULFUR SUBUNIT, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11921; SUCCINATE DEHYDROGENASE IRON-SULFUR PROTEIN; 1.
DR   Pfam; PF13085; Fer2_3; 1.
DR   Pfam; PF13534; Fer4_17; 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; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|RuleBase:RU361237};
KW   3Fe-4S {ECO:0000256|ARBA:ARBA00023291, ECO:0000256|RuleBase:RU361237};
KW   4Fe-4S {ECO:0000256|RuleBase:RU361237};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU361237};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU361237};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361237};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          31..119
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          160..190
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   259 AA;  29772 MW;  6BA81BB1A31CAB2A CRC64;
     MVQIKLPKNS QVKTGKVWPK PEGATRLTEF HVYRWSPDDE ENPHLDTYYV DRSACGPMIL
     DGLLFIKNHI DPTLTLRRSC REGICGSCAM NIDGTNTLAC TKGMDDVKHP IKVYPLPSMP
     VVKDLVPDLK RFYAQHRVIE PWLQTVSPEP AKEWLQSHSD RQKIDGLYEC ILCACCQTSC
     PSYWWNGDRY LGPAILLQAY RWIADSRDEM CGERLDNLED PFRLYRCHTI MNCTQTCPKG
     LNPAKAIAEI KKLMVERRL
//
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