ID   DHSU_CHLTI              Reviewed;          48 AA.
AC   P20161;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Sulfide dehydrogenase [flavocytochrome c] flavoprotein chain;
DE            EC=1.8.2.3;
DE   AltName: Full=FCSD;
DE   AltName: Full=Flavocytochrome c flavoprotein subunit;
DE            Short=FC;
DE   Flags: Fragment;
OS   Chlorobaculum thiosulfatiphilum (Chlorobium limicola f.sp.
OS   thiosulfatophilum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX   NCBI_TaxID=115852;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=DSM 249 / 6230 / Tassajara;
RX   PubMed=2161842; DOI=10.1016/s0021-9258(19)38741-1;
RA   van Beeumen J., van Bun S., Meyer T.E., Bartsch R.G., Cusanovich M.A.;
RT   "Complete amino acid sequence of the cytochrome subunit and amino-terminal
RT   sequence of the flavin subunit of flavocytochrome c (sulfide dehydrogenase)
RT   from Chlorobium thiosulfatophilum.";
RL   J. Biol. Chem. 265:9793-9799(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 40-46.
RX   PubMed=196652; DOI=10.1016/0005-2744(77)90074-2;
RA   Kenney W.C., McIntire W., Yamanaka T.;
RT   "Structure of the covalently bound flavin of Chlorobium cytochrome.";
RL   Biochim. Biophys. Acta 483:467-474(1977).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Fe(III)-[cytochrome c] + hydrogen sulfide = 2 Fe(II)-
CC         [cytochrome c] + H(+) + sulfur; Xref=Rhea:RHEA:30223, Rhea:RHEA-
CC         COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:26833, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC         ChEBI:CHEBI:29919; EC=1.8.2.3;
CC   -!- SUBUNIT: Dimer of one cytochrome and one flavoprotein.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
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DR   AlphaFoldDB; P20161; -.
DR   SMR; P20161; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0070225; F:sulfide dehydrogenase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase; Periplasm.
FT   CHAIN           1..>48
FT                   /note="Sulfide dehydrogenase [flavocytochrome c]
FT                   flavoprotein chain"
FT                   /id="PRO_0000079894"
FT   BINDING         40..46
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   NON_TER         48
SQ   SEQUENCE   48 AA;  4927 MW;  C1706B50F4B308BC CRC64;
     GTKRVVVVGG GFGGASTAKY LRKLDPSISV TLVEPKTAFV TCPFSNAV