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Database: UniProt
Entry: A0A519KE61_FLASP
LinkDB: A0A519KE61_FLASP
Original site: A0A519KE61_FLASP 
ID   A0A519KE61_FLASP        Unreviewed;       247 AA.
AC   A0A519KE61;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Succinate dehydrogenase/fumarate reductase iron-sulfur subunit {ECO:0000313|EMBL:RZJ35276.1};
GN   ORFNames=EOO51_06475 {ECO:0000313|EMBL:RZJ35276.1};
OS   Flavobacterium sp.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=239 {ECO:0000313|EMBL:RZJ35276.1, ECO:0000313|Proteomes:UP000316154};
RN   [1] {ECO:0000313|EMBL:RZJ35276.1, ECO:0000313|Proteomes:UP000316154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PMG_266 {ECO:0000313|EMBL:RZJ35276.1};
RX   PubMed=30498029; DOI=.1073/pnas.1812668115;
RA   Crombie A.T., Larke-Mejia N.L., Emery H., Dawson R., Pratscher J.,
RA   Murphy G.P., McGenity T.J., Murrell J.C.;
RT   "Poplar phyllosphere harbors disparate isoprene-degrading bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 115:13081-13086(2018).
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:RZJ35276.1}.
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DR   EMBL; SEBT01000010; RZJ35276.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A519KE61; -.
DR   Proteomes; UP000316154; 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   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; 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; PS51379; 4FE4S_FER_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000316154}.
FT   DOMAIN          151..181
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   247 AA;  26928 MW;  19A955D4A4CF3D17 CRC64;
     MKLTLKIWRQ KNAADKGKIV DYPIDGISPD MSFLEMLDVL NEQLINSGQD PVAFDHDCRE
     GICGMCSLFI NGEAHGPDRG VTTCQLHMRM FKDGDTIFIE PFRAKAFPVI KDLIVDRSSF
     ERIQQAGGFI SVGTSGNTID ANTIPINKHD ADTAFDSATC ISCGACVASC KNASAMLFVS
     AKVSQFALLP QGQVEAAERV LNMVAQMDHE GFGNCTNTGA CEVECPKGIS LENIARMNRE
     YLKASFK
//
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