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Database: UniProt
Entry: B1Y6J8_LEPCP
LinkDB: B1Y6J8_LEPCP
Original site: B1Y6J8_LEPCP 
ID   B1Y6J8_LEPCP            Unreviewed;       433 AA.
AC   B1Y6J8;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Flavocytochrome c sulphide dehydrogenase flavin-binding {ECO:0000313|EMBL:ACB36026.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Lcho_3772 {ECO:0000313|EMBL:ACB36026.1};
OS   Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS   discophora (strain SP-6)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Leptothrix.
OX   NCBI_TaxID=395495 {ECO:0000313|EMBL:ACB36026.1, ECO:0000313|Proteomes:UP000001693};
RN   [1] {ECO:0000313|EMBL:ACB36026.1, ECO:0000313|Proteomes:UP000001693}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51168 / LMG 8142 / SP-6
RC   {ECO:0000313|Proteomes:UP000001693};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT   "Complete sequence of Leptothrix cholodnii SP-6.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001013; ACB36026.1; -; Genomic_DNA.
DR   RefSeq; WP_012348773.1; NC_010524.1.
DR   AlphaFoldDB; B1Y6J8; -.
DR   STRING; 395495.Lcho_3772; -.
DR   KEGG; lch:Lcho_3772; -.
DR   eggNOG; COG0446; Bacteria.
DR   HOGENOM; CLU_030742_0_0_4; -.
DR   OrthoDB; 9802771at2; -.
DR   Proteomes; UP000001693; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 3.90.760.10; Flavocytochrome c sulphide dehydrogenase, flavin-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR049386; FCSD_central.
DR   InterPro; IPR015323; FlavoCytC_S_DH_flav-bd.
DR   InterPro; IPR037092; FlavoCytC_S_DH_flav-bd_sf.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR43755; -; 1.
DR   PANTHER; PTHR43755:SF1; POSSIBLE DEHYDROGENASE_REDUCTASE; 1.
DR   Pfam; PF09242; FCSD-flav_bind; 1.
DR   Pfam; PF21706; FCSD_central; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001693}.
FT   DOMAIN          41..145
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          174..288
FT                   /note="Sulfide dehydrogenase [flavocytochrome c]
FT                   flavoprotein chain central"
FT                   /evidence="ECO:0000259|Pfam:PF21706"
FT   DOMAIN          366..432
FT                   /note="Flavocytochrome c sulphide dehydrogenase flavin-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF09242"
SQ   SEQUENCE   433 AA;  46214 MW;  D02E7D33D7E58211 CRC64;
     MNKHTQQRRL LLQGLIAGGA IGSLGLSGCA SLGGTSASRA KVLVIGGGYG GATAAKYVRM
     LSDYSIDVMM VEPNREFVSC PVSNLVLGGQ RTMADITNPY TGLSKTHGVR IVHDRVASID
     ATKKVATLAS GGTVSYDKLV LSPGIDMMWD QTAGLQAAHA AGQVLHAWKA GPETVALRRQ
     LEAMRDGGVY AITIPEAPYR CPPGPYERAS VIAAYFKKAK PKSKILILDG NPDVTSKGPL
     FKKAWKELYG DMIEYRPQHK AVAVDGASNT VKFEIQDDVK ADVLNVLPVM RAGSLAVQTG
     LANANGRWCH VNFLNFESTA AKDIHVIGDA IQVAQGMPKS GHMANSHAKV TAAAIVAELQ
     GLEINPHPLL TNVCMSFVDD THVIHVASVH EYQAPKKSFF TIGGSGGVSD VRSDLEGRYA
     DAWARNIWAD VLM
//
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