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
//