ID A0A4P8YG21_9ENTR Unreviewed; 244 AA.
AC A0A4P8YG21;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Succinate dehydrogenase iron-sulfur subunit {ECO:0000256|RuleBase:RU361237};
DE EC=1.3.5.1 {ECO:0000256|RuleBase:RU361237};
GN ORFNames=FEM41_07780 {ECO:0000313|EMBL:QCT19559.1};
OS Jejubacter calystegiae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Jejubacter.
OX NCBI_TaxID=2579935 {ECO:0000313|EMBL:QCT19559.1, ECO:0000313|Proteomes:UP000302163};
RN [1] {ECO:0000313|EMBL:QCT19559.1, ECO:0000313|Proteomes:UP000302163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSNA2 {ECO:0000313|EMBL:QCT19559.1,
RC ECO:0000313|Proteomes:UP000302163};
RA Jiang L., Jeong J.C., Kim C.Y., Kim D.H., Kim S.W., Lee j.;
RT "Complete genome sequence of Izhakiella calystegiae KSNA2, an endophyte
RT isolated from beach morning glory (Calystegia soldanella).";
RL Submitted (MAY-2019) 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; CP040428; QCT19559.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4P8YG21; -.
DR KEGG; izh:FEM41_07780; -.
DR OrthoDB; 9804391at2; -.
DR Proteomes; UP000302163; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:InterPro.
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:UP000302163}.
FT DOMAIN 7..97
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 140..169
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 244 AA; 27297 MW; 315CDA8949D498D6 CRC64;
MAEMKQMKIE VVRYNPETDD TPHSAWYEIP WDEQTSLLDA LGYIKDNLAP DLSYRWSCRM
AICGSCGMMV NGVPKLACKT FMREYTGGMK VEALANFPIE RDLVVDMTHF IESLEAIKPY
IIGNARTPDQ GPNRQTPAQM AKYHQFSGCI NCGLCYAACP QFGLNPEFIG PAAITLAHRY
NLDSRDNGRK ERMPQLNGQN GVWSCTFVGF CSEVCPKHVD PAAAIQQGKV ESSKDFLIAT
LKPR
//
