ID O07819_PARDE Unreviewed; 384 AA.
AC O07819;
DT 01-JUL-1997, integrated into UniProtKB/TrEMBL.
DT 01-JUL-1997, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=Cytochrome {ECO:0000313|EMBL:CAA55825.1};
GN Name=soxD {ECO:0000313|EMBL:CAA55825.1};
OS Paracoccus denitrificans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=266 {ECO:0000313|EMBL:CAA55825.1};
RN [1] {ECO:0000313|EMBL:CAA55825.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GB17 {ECO:0000313|EMBL:CAA55825.1};
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:CAA55825.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GB17 {ECO:0000313|EMBL:CAA55825.1};
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:CAA55825.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GB17 {ECO:0000313|EMBL:CAA55825.1};
RA Johansson A.;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0007829|PDB:2XTS}
RP X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 25-229 IN COMPLEX WITH HEME, AND
RP DISULFIDE BONDS.
RX PubMed=21147779; DOI=10.1074/jbc.M110.193631;
RA Zander U., Faust A., Klink B.U., de Sanctis D., Panjikar S., Quentmeier A.,
RA Bardischewsky F., Friedrich C.G., Scheidig A.J.;
RT "Structural basis for the oxidation of protein-bound sulfur by the sulfur
RT cycle molybdohemo-enzyme sulfane dehydrogenase SoxCD.";
RL J. Biol. Chem. 286:8349-8360(2011).
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DR EMBL; X79242; CAA55825.1; -; Genomic_DNA.
DR PIR; T46966; T46966.
DR PDB; 2XTS; X-ray; 1.33 A; B/D=25-229.
DR PDBsum; 2XTS; -.
DR AlphaFoldDB; O07819; -.
DR SMR; O07819; -.
DR BioCyc; MetaCyc:MONOMER-12240; -.
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; 1.
DR Pfam; PF00034; Cytochrom_C; 2.
DR PRINTS; PR00604; CYTCHRMECIAB.
DR SUPFAM; SSF46626; Cytochrome c; 2.
DR PROSITE; PS51007; CYTC; 2.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:2XTS}; Calcium {ECO:0007829|PDB:2XTS};
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..384
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004157781"
FT DOMAIN 57..145
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 280..383
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT REGION 206..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 36
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:2XTS"
FT BINDING 70
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_note="covalent"
FT /evidence="ECO:0007829|PDB:2XTS"
FT BINDING 74
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /ligand_part_note="axial binding residue"
FT /evidence="ECO:0007829|PDB:2XTS"
FT BINDING 107
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /evidence="ECO:0007829|PDB:2XTS"
FT BINDING 121
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /ligand_part_note="axial binding residue"
FT /evidence="ECO:0007829|PDB:2XTS"
FT BINDING 128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:2XTS"
FT BINDING 214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0007829|PDB:2XTS"
FT DISULFID 188..192
FT /evidence="ECO:0007829|PDB:2XTS"
SQ SEQUENCE 384 AA; 39985 MW; 9926A674C859CEF5 CRC64;
MSKSLELFLG SVLAASVLAG PAMADKLGLG REALPEEISA WDTAVLPDGQ GLRPGSGDVA
TGDALFADNC ASCHGDFAEG LDSWPVLAGG DGSLTDPRPV KTIGSYWPYL STVYDYVHRS
MPFGSAQTLS VDDTYAITAF LLYSNGLVED DFVLTHENFT QVVLPNAEGF YPDDRDQTEY
PLFSKEPCMT DCAVGVEITK RAVDLNVTPE DPDGRPAGSM PDLGAAAAPA EPAEPVEKKA
EAAPAEAPAP AAAPEVVVKA AAMAPEAPAP AGAATAADPT LLAEGEKVFK KCAACHKVGD
DAKNGTGPLL NGIVGRAAGD IEGFKYSKPL LAMASEGLVW DDASLHAFLE NPKGFMKGTK
MSFAGLKKED ERAAVIAYLA TFAK
//