ID A0A0S8DWC3_9GAMM Unreviewed; 428 AA.
AC A0A0S8DWC3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Cytochrome C {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMJ69_02000 {ECO:0000313|EMBL:KPK40517.1};
OS Gammaproteobacteria bacterium SG8_47.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1703406 {ECO:0000313|EMBL:KPK40517.1, ECO:0000313|Proteomes:UP000054199};
RN [1] {ECO:0000313|EMBL:KPK40517.1, ECO:0000313|Proteomes:UP000054199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_47 {ECO:0000313|EMBL:KPK40517.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK40517.1}.
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DR EMBL; LJTV01000012; KPK40517.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8DWC3; -.
DR STRING; 1703406.AMJ69_02000; -.
DR PATRIC; fig|1703406.3.peg.80; -.
DR Proteomes; UP000054199; Unassembled WGS sequence.
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 InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
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; PS51318; TAT; 1.
PE 4: Predicted;
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..428
FT /note="Cytochrome C"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006644660"
FT DOMAIN 36..150
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 167..283
FT /note="Sulfide dehydrogenase [flavocytochrome c]
FT flavoprotein chain central"
FT /evidence="ECO:0000259|Pfam:PF21706"
FT DOMAIN 358..427
FT /note="Flavocytochrome c sulphide dehydrogenase flavin-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF09242"
SQ SEQUENCE 428 AA; 46056 MW; F2F6CC49B014CDDD CRC64;
MSRFTRRDFL KFTGAASALG VVGHPFNAFA AGAAGRVVVI GGGFGGATVA KYLHRINPAI
HVTLIEPNAE FVTCPFSNLV VAGMRDLASI SHGYERLRDK YAVNVIHEAA TSVDPVAKKV
VLASGKFVPY DRLVMSPGIR MLWGEIEGYD EAAAEKMPHA WKAGPQTLNL RRQLEAMPDG
GTVIIAPPAN PYRCPPGPYE RASLIAHYLK QNKPKSKILI LDAKDKFSKQ PLFEQGWNKL
YPGMIEWVKG TKGGRVVRVD TSSNTVYNEI GDAFKADVIN LIPPQAAAEI TQAAGVADST
GWCPVNQVTF ESLMQKDVHV IGDSSIAGAM PKSGYAASSE GKVAATAIAT HFAGLEMPEP
SYVNTCYSLM APDYGISVAA VYRMTDDGIT KVEGSGGDSP LLATEGQRRM EAVYATGWYD
SVTSDMFW
//
