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Database: UniProt
Entry: D5BCT0_ZUNPS
LinkDB: D5BCT0_ZUNPS
Original site: D5BCT0_ZUNPS 
ID   D5BCT0_ZUNPS            Unreviewed;       230 AA.
AC   D5BCT0;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Succinate dehydrogenase {ECO:0000313|EMBL:ADF50593.1};
GN   OrderedLocusNames=ZPR_0232 {ECO:0000313|EMBL:ADF50593.1};
OS   Zunongwangia profunda (strain DSM 18752 / CCTCC AB 206139 / SM-A87) (Wangia
OS   profunda).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Zunongwangia.
OX   NCBI_TaxID=655815 {ECO:0000313|EMBL:ADF50593.1, ECO:0000313|Proteomes:UP000001654};
RN   [1] {ECO:0000313|EMBL:ADF50593.1, ECO:0000313|Proteomes:UP000001654}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18752 / CCTCC AB 206139 / SM-A87
RC   {ECO:0000313|Proteomes:UP000001654};
RX   PubMed=20398413; DOI=10.1186/1471-2164-11-247;
RA   Qin Q.L., Zhang X.Y., Wang X.M., Liu G.M., Chen X.L., Xie B.B., Dang H.Y.,
RA   Zhou B.C., Yu J., Zhang Y.Z.;
RT   "The complete genome of Zunongwangia profunda SM-A87 reveals its adaptation
RT   to the deep-sea environment and ecological role in sedimentary organic
RT   nitrogen degradation.";
RL   BMC Genomics 11:247-247(2010).
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}.
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DR   EMBL; CP001650; ADF50593.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5BCT0; -.
DR   STRING; 655815.ZPR_0232; -.
DR   KEGG; zpr:ZPR_0232; -.
DR   eggNOG; COG0479; Bacteria.
DR   HOGENOM; CLU_044838_3_3_10; -.
DR   Proteomes; UP000001654; Chromosome.
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; IPR001041; 2Fe-2S_ferredoxin-type.
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; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   3: Inferred from homology;
FT   DOMAIN          1..85
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          133..163
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   230 AA;  24731 MW;  26737DD557FBCA8D CRC64;
     MVSYPIDGIE GDMSFLEMLD VLNEELVAKG EDPVEFDHDC REGICGACSL QINGEPHGPD
     KLITTCQLHM RSFKDGDTIV IEPFRANAFP VVKDLIVDRS SFDRIQQAGG YVSINTSGNT
     IDANSIPVNK HDADDSFAAA TCIGCGACVA ACKNASAMLF TSAKVSQYAL LPQGQVEATD
     RVMNMVRQMD AEGFGNCTNT GACEIECPKG ISLENIARMN REYLSASTKG
//
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