ID   O33435_PARDE            Unreviewed;       236 AA.
AC   O33435; O07820;
DT   01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 2.
DT   13-SEP-2023, entry version 80.
DE   SubName: Full=Cytochrome {ECO:0000313|EMBL:CAA55828.2};
GN   Name=soxE {ECO:0000313|EMBL:CAA55828.2};
OS   Paracoccus denitrificans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=266 {ECO:0000313|EMBL:CAA55828.2};
RN   [1] {ECO:0000313|EMBL:CAA55828.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GB17 {ECO:0000313|EMBL:CAA55828.2};
RX   PubMed=7928987;
RA   Wodara C., Kostka S., Egert M., Kelly D.P., Friedrich C.;
RT   "Identification and sequence analysis of the soxB gene essential for sulfur
RT   oxidation of Paracoccus denitrificans GB17.";
RL   J. Bacteriol. 176:6188-6191(1994).
RN   [2] {ECO:0000313|EMBL:CAA55828.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GB17 {ECO:0000313|EMBL:CAA55828.2};
RX   PubMed=9260941;
RA   Wodara C., Bardischewsky F., Friedrich C.G.;
RT   "Cloning and characterization of sulfite dehydrogenase, two c-type
RT   cytochromes, and a flavoprotein of Paracoccus denitrificans GB17: essential
RT   role of sulfite dehydrogenase in lithotrophic sulfur oxidation.";
RL   J. Bacteriol. 179:5014-5023(1997).
RN   [3] {ECO:0000313|EMBL:CAA55828.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GB17 {ECO:0000313|EMBL:CAA55828.2};
RA   Friedrich C.;
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X79242; CAA55828.2; -; Genomic_DNA.
DR   PIR; T46967; T46967.
DR   AlphaFoldDB; O33435; -.
DR   BioCyc; MetaCyc:SOXEDENIT-MONOMER; -.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 2.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; CYTOCHROME C; 1.
DR   PANTHER; PTHR11961:SF12; CYTOCHROME C-RELATED; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome c; 2.
DR   PROSITE; PS51007; CYTC; 1.
PE   4: Predicted;
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00433}; Signal {ECO:0000256|SAM:SignalP};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..236
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004158093"
FT   DOMAIN          27..131
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
SQ   SEQUENCE   236 AA;  25927 MW;  E46A10C85C00AB00 CRC64;
     MRQRKLLSAL FTVAAAGATP AAAEEIGDTV HGAVLFRKEC AICHRIGQDA RNAVGPRLNG
     VFGRRAAALA DFNYSRAMKR KGNDGLTWTL ETLDAYIENP KALVTGTRMS YRGLADPQAR
     ADLMAYMRDH SDRPQDIPEA EPTARRNAPV LSEEVLALRG DPEFGAYLSA EWTTCHQRDG
     SDQGIPSIAG WPQEDFVVAM HAYKQKLRPH PVMQMMAGRL SEEEIAALAA FFATLE
//