ID L8MAA2_9CYAN Unreviewed; 242 AA.
AC L8MAA2;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Fumarate reductase iron-sulfur subunit {ECO:0000256|RuleBase:RU361237};
DE EC=1.3.5.1 {ECO:0000256|RuleBase:RU361237};
GN ORFNames=Xen7305DRAFT_00050440 {ECO:0000313|EMBL:ELS05301.1};
OS Xenococcus sp. PCC 7305.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Xenococcaceae;
OC Xenococcus.
OX NCBI_TaxID=102125 {ECO:0000313|EMBL:ELS05301.1, ECO:0000313|Proteomes:UP000011203};
RN [1] {ECO:0000313|EMBL:ELS05301.1, ECO:0000313|Proteomes:UP000011203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7305 {ECO:0000313|EMBL:ELS05301.1,
RC ECO:0000313|Proteomes:UP000011203};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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|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 -!- 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:ELS05301.1}.
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DR EMBL; ALVZ01000065; ELS05301.1; -; Genomic_DNA.
DR RefSeq; WP_006507605.1; NZ_ALVZ01000065.1.
DR AlphaFoldDB; L8MAA2; -.
DR STRING; 102125.Xen7305DRAFT_00050440; -.
DR PATRIC; fig|102125.3.peg.354; -.
DR eggNOG; COG0479; Bacteria.
DR OrthoDB; 9804391at2; -.
DR Proteomes; UP000011203; 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:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
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:SF41; 4FE-4S FERREDOXIN IRON-SULFUR BINDING DOMAIN PROTEIN; 1.
DR PANTHER; PTHR11921; SUCCINATE DEHYDROGENASE IRON-SULFUR PROTEIN; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000011203};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 18..103
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 150..179
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 242 AA; 26131 MW; 9470351706DBE7F4 CRC64;
MKLKLKIWRQ ANPKSPGKFV EYSVSDLDPD MSFLEMLDVL NEQLIKTNQT PIEFDNDCRE
GICGSCGMVI NGIAHGSQKQ TAACQLHLRS LKDGETVVIE PWRAKAFPVI KDLVVDRSSF
DRIISAGGYI SVNAGSAPDA NSLPVAKENS DRAFAYAACI GCGACVAACP NASASLFTAA
KIAHLSLLPQ GAPERKLRVA KMTQQMSQEG FGDCSNHGEC EAVCPKGISI DAIATMRREY
MK
//
