ID B2I7Z5_XYLF2 Unreviewed; 261 AA.
AC B2I7Z5;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 84.
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 OrderedLocusNames=XfasM23_0345 {ECO:0000313|EMBL:ACB91793.1};
OS Xylella fastidiosa (strain M23).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=405441 {ECO:0000313|EMBL:ACB91793.1, ECO:0000313|Proteomes:UP000001698};
RN [1] {ECO:0000313|EMBL:ACB91793.1, ECO:0000313|Proteomes:UP000001698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M23 {ECO:0000313|EMBL:ACB91793.1,
RC ECO:0000313|Proteomes:UP000001698};
RX PubMed=20601474; DOI=10.1128/JB.00651-10;
RA Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT causing almond leaf scorch disease in California.";
RL J. Bacteriol. 192:4534-4534(2010).
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 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.
CC {ECO:0000256|ARBA:ARBA00005163}.
CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase
CC iron-sulfur protein family. {ECO:0000256|ARBA:ARBA00009433,
CC ECO:0000256|RuleBase:RU361237}.
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DR EMBL; CP001011; ACB91793.1; -; Genomic_DNA.
DR RefSeq; WP_004089282.1; NC_010577.1.
DR AlphaFoldDB; B2I7Z5; -.
DR GeneID; 58015904; -.
DR KEGG; xfn:XfasM23_0345; -.
DR HOGENOM; CLU_044838_0_2_6; -.
DR Proteomes; UP000001698; Chromosome.
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-KW.
DR CDD; cd00207; fer2; 1.
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 ECO:0000313|EMBL:ACB91793.1};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 30..120
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 162..192
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 261 AA; 29587 MW; 91701E59C5FEBA53 CRC64;
MAEFTLPKNS KIGKGTHFPA KSGTKNARTF KVYRWNPDDD ANPRTDTYEI DLDTCGPMVL
DALIKIKNEI DPTLTFRRSC REGICGSCAM NIDGTNTLAC TKAISACTIS EIPIYPLPHM
NVIKDLIPDL THFYAQYASI KPWIRTQTPP PPDRERLQSP VDRKKLDGLY ECILCACCST
SCPSYWWNGD RYLGPAILLQ AYRWIIDSRD EDTGARLDDL EDPFKLYRCH TIMNCTRTCP
KGLNPAQAIA EIKKLMMLRR A
//
