ID   A0A1U7GQD9_9BACT        Unreviewed;       253 AA.
AC   A0A1U7GQD9;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Succinate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BGO49_06455 {ECO:0000313|EMBL:OJW24675.1};
OS   Planctomycetales bacterium 71-10.
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales.
OX   NCBI_TaxID=1895807 {ECO:0000313|EMBL:OJW24675.1, ECO:0000313|Proteomes:UP000185848};
RN   [1] {ECO:0000313|EMBL:OJW24675.1, ECO:0000313|Proteomes:UP000185848}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=71-10 {ECO:0000313|EMBL:OJW24675.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:OJW24675.1}.
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DR   EMBL; MKTT01000036; OJW24675.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1U7GQD9; -.
DR   STRING; 1895807.BGO49_06455; -.
DR   Proteomes; UP000185848; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   CDD; cd03498; SQR_TypeB_2_TM; 1.
DR   Gene3D; 1.20.1300.10; Fumarate reductase/succinate dehydrogenase, transmembrane subunit; 1.
DR   InterPro; IPR011138; Cytochrome_b-558.
DR   InterPro; IPR034804; SQR/QFR_C/D.
DR   InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR   NCBIfam; TIGR02046; sdhC_b558_fam; 1.
DR   Pfam; PF01127; Sdh_cyt; 1.
DR   SUPFAM; SSF81343; Fumarate reductase respiratory complex transmembrane subunits; 1.
PE   4: Predicted;
KW   Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        51..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        96..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        137..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        186..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          215..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   253 AA;  26626 MW;  7E85C9ED4A91854F CRC64;
     MTSSIGLKLI MALTGVALSL FVLGHMLGNL QAFQGAEALN DYAKLLRKEP ALLWAVRAGL
     LTMVGLHIYA FLALAKKNAA ARPQAYRKRV WRESSYASRS MKITGPLLLA FIIFHILHLT
     TGTVHPSFDA HDVYHNVVTG LGGLVGLIYV LAMAMLALHL WHGVWSMLLT LGLPEGRYGS
     TGRAGATIFT ALVTIGFAVV PLLVMAGVIG PEDAAPPPAA TSDAALAPPR PAEPEPATAA
     PKAAEPAAPA EAK
//