ID A0A0M4H685_9ACTO Unreviewed; 251 AA.
AC A0A0M4H685;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN ORFNames=AM609_10670 {ECO:0000313|EMBL:ALC99815.1};
OS Actinomyces sp. oral taxon 414.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=712122 {ECO:0000313|EMBL:ALC99815.1, ECO:0000313|Proteomes:UP000061022};
RN [1] {ECO:0000313|Proteomes:UP000061022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0588 {ECO:0000313|Proteomes:UP000061022};
RA Holder M.E., Ajami N.J., Petrosino J.F.;
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000256|ARBA:ARBA00001927};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase
CC iron-sulfur protein family. {ECO:0000256|ARBA:ARBA00009433}.
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DR EMBL; CP012590; ALC99815.1; -; Genomic_DNA.
DR RefSeq; WP_053587251.1; NZ_CP012590.1.
DR AlphaFoldDB; A0A0M4H685; -.
DR STRING; 712122.AM609_10670; -.
DR KEGG; acq:AM609_10670; -.
DR PATRIC; fig|712122.3.peg.2420; -.
DR OrthoDB; 9804391at2; -.
DR Proteomes; UP000061022; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
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 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; 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; IPR025192; Succ_DH/fum_Rdtase_N.
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; PF12838; Fer4_7; 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; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 150..179
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 251 AA; 26909 MW; E7496372A113069A CRC64;
MRVELEIWRQ DGPRARGFFE SHVVEDAEPQ MSLLELLDRL NDQIIESGGE PVVFESDCRE
GVCGACGFLV NGVPHGPLDT TPACRQHLRA FPGVTHFRLE PWRSAAFPVI RDLAVDRTAL
DELIRAGGTV DVAAGTAPDA DDVAQGHLQA ERALDFAACI GCGACVAACP NGAAALFAGA
KLAHLSLMPQ GRHERGRRAR AMTRALDEFF GPCSVYGECV PACPAGIPIE AIARLNREVL
RAGLRGSTRD D
//
