ID F9PIC3_9ACTO Unreviewed; 256 AA.
AC F9PIC3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Succinate dehydrogenase/fumarate reductase iron-sulfur subunit {ECO:0000313|EMBL:EGV14367.1};
DE EC=1.3.99.1 {ECO:0000313|EMBL:EGV14367.1};
GN ORFNames=HMPREF9058_1676 {ECO:0000313|EMBL:EGV14367.1};
OS Actinomyces sp. oral taxon 175 str. F0384.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=944560 {ECO:0000313|EMBL:EGV14367.1, ECO:0000313|Proteomes:UP000004281};
RN [1] {ECO:0000313|EMBL:EGV14367.1, ECO:0000313|Proteomes:UP000004281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0384 {ECO:0000313|EMBL:EGV14367.1,
RC ECO:0000313|Proteomes:UP000004281};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000256|ARBA:ARBA00001927};
CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase
CC iron-sulfur protein family. {ECO:0000256|ARBA:ARBA00009433}.
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:EGV14367.1}.
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; AFUR01000001; EGV14367.1; -; Genomic_DNA.
DR RefSeq; WP_003785183.1; NZ_AFUR01000001.1.
DR AlphaFoldDB; F9PIC3; -.
DR GeneID; 64257412; -.
DR eggNOG; COG0479; Bacteria.
DR Proteomes; UP000004281; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
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; 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; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:EGV14367.1}.
FT DOMAIN 155..185
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 256 AA; 27584 MW; 43256723ECD7BAF9 CRC64;
MNIKLKIWRQ KNKDSKGHFE EYAMSGIEEH MSFLEVLDLL NEQLFAEGKE PVAFDSDCRE
GICGQCGVVI NGQAHGPIRS TTCQLHMRHL AEDPSFKDGS TITIEPWRST GFPVLRDLIV
DRSALDRIVQ AGGYISVNTG GAPEAHSVPV QKEKADAAFE AAACIGCGAC VAACPNASAM
LFTGAKISHL GLLPQGQPER LARVVSMLNQ HDAEGFGGCT NIGECAAVCP KSVPLEVISR
LNRDLGHALW KGQHAH
//