ID A0A424SA87_9PROT Unreviewed; 258 AA. AC A0A424SA87; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 12-AUG-2020, entry version 6. 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 ORFNames=CBD13_002920 {ECO:0000313|EMBL:RPH00654.1}; OS Candidatus Pelagibacter sp. TMED153. OC Bacteria; Proteobacteria; Alphaproteobacteria; Pelagibacterales; OC Pelagibacteraceae; Candidatus Pelagibacter; OC unclassified Candidatus Pelagibacter. OX NCBI_TaxID=1986803 {ECO:0000313|EMBL:RPH00654.1, ECO:0000313|Proteomes:UP000195484}; RN [1] {ECO:0000313|EMBL:RPH00654.1, ECO:0000313|Proteomes:UP000195484} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TMED153 {ECO:0000313|EMBL:RPH00654.1}; RX PubMed=28713657; DOI=10.7717/peerj.3558; RA Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.; RT "290 metagenome-assembled genomes from the Mediterranean Sea: a resource RT for marine microbiology."; RL PeerJ 5:e3558-e3558(2017). 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:49601; 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:RPH00654.1}. 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; NHHC02000043; RPH00654.1; -; Genomic_DNA. DR UniPathway; UPA00223; UER01005. DR Proteomes; UP000195484; 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: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:InterPro. DR Gene3D; 1.10.1060.10; -; 1. DR Gene3D; 3.10.20.30; -; 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 Pfam; PF13085; Fer2_3; 1. DR SUPFAM; SSF46548; SSF46548; 1. DR SUPFAM; SSF54292; SSF54292; 1. DR TIGRFAMs; TIGR00384; dhsB; 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|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 Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}. FT DOMAIN 28..119 FT /note="2Fe-2S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51085" FT DOMAIN 161..191 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51379" SQ SEQUENCE 258 AA; 29342 MW; C80ED6C52F3CF0D4 CRC64; MVQFNLPQNS KIEVGKQYKD ETNSENLKKV NVYRWDPSNG QNPRVDTFEV DMDNCGPKVL DILFKIKNEI DPSLTFRRSC AHGVCGSCAM NIDGVNTLAC IKSHTDINGD LNIYPLPHLK VVKDLIGDLS TLYKQYESIK PWLQTEQTGK EKEELRQSQK DREKLDGYYE CILCACCSTA CPSYWWNGDK YLGPAVLLQA YRWINDSRDG DKKERLKKVA DELKLYRCHT IMNCTNSCPK GLNPAKAIGS IKKMLATS //