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Entry: A0A0C5WI89_9GAMM
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ID   A0A0C5WI89_9GAMM        Unreviewed;       246 AA.
AC   A0A0C5WI89;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Succinate dehydrogenase iron-sulfur subunit {ECO:0000256|RuleBase:RU361237};
DE            EC=1.3.5.1 {ECO:0000256|RuleBase:RU361237};
GN   ORFNames=H744_2c0076 {ECO:0000313|EMBL:AJR06838.1};
OS   Photobacterium gaetbulicola Gung47.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=658445 {ECO:0000313|EMBL:AJR06838.1, ECO:0000313|Proteomes:UP000032303};
RN   [1] {ECO:0000313|EMBL:AJR06838.1, ECO:0000313|Proteomes:UP000032303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gung47 {ECO:0000313|EMBL:AJR06838.1,
RC   ECO:0000313|Proteomes:UP000032303};
RA   Kim Y.-O.;
RT   "Complete genome sequence of the lipase-producing bacterium Photobacterium
RT   gaetbulicola Gung47.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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         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   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004515}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004515}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004515}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
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; CP005974; AJR06838.1; -; Genomic_DNA.
DR   RefSeq; WP_039458938.1; NZ_CP005974.1.
DR   AlphaFoldDB; A0A0C5WI89; -.
DR   STRING; 658445.H744_2c0076; -.
DR   KEGG; pgb:H744_2c0076; -.
DR   PATRIC; fig|658445.3.peg.1969; -.
DR   HOGENOM; CLU_044838_3_2_6; -.
DR   OrthoDB; 9804391at2; -.
DR   Proteomes; UP000032303; Chromosome 2.
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:RHEA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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; PF13237; Fer4_10; 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|RuleBase:RU361237};
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU361237};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU361237};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU361237};
KW   Membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361237};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032303}.
FT   DOMAIN          7..97
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          139..169
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   246 AA;  27491 MW;  89011AF93CBC4375 CRC64;
     MSDNRIQKVE ILRYDPAKDA EPYFEMFEVP FNETMSVLDA LGYIKDNLDK DLAYRWSCRM
     AICGSCGMMV NKVPKLACKT FLRDYPNGLK IEALSNFAIE KDLVVDMTPF IERLEAIKPY
     IIGNDRKPED GPNNQTPEQM AKYKQFAGCI NCGLCYAACP QFGLNPEFIG PAALTLAHRY
     NLDSRDNGSD ERMKLINGEN GAWGCTFVGY CSEVCPKSVD PAAAVNQGKV ESSKDFVIAM
     MKPQEA
//
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