NIRC_PARDP
ID NIRC_PARDP Reviewed; 103 AA.
AC Q51702; A1B4Y2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Cytochrome c55X;
DE Flags: Precursor;
GN Name=nirC; OrderedLocusNames=Pden_2489;
OS Paracoccus denitrificans (strain Pd 1222).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=318586;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7747927; DOI=10.1007/bf00871635;
RA de Boer A.P.N., Reijnders W.N.M., Kuenen J.G., Stouthamer A.H.,
RA van Spanning R.J.M.;
RT "Isolation, sequencing and mutational analysis of a gene cluster involved
RT in nitrite reduction in Paracoccus denitrificans.";
RL Antonie Van Leeuwenhoek 66:111-127(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Monoheme c-type cytochrome.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Binds 1 heme c group covalently per subunit.
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DR EMBL; U05002; AAA93120.1; -; Genomic_DNA.
DR EMBL; CP000489; ABL70576.1; -; Genomic_DNA.
DR RefSeq; WP_011748769.1; NC_008686.1.
DR AlphaFoldDB; Q51702; -.
DR SMR; Q51702; -.
DR STRING; 318586.Pden_2489; -.
DR PRIDE; Q51702; -.
DR EnsemblBacteria; ABL70576; ABL70576; Pden_2489.
DR KEGG; pde:Pden_2489; -.
DR eggNOG; COG2010; Bacteria.
DR HOGENOM; CLU_159748_0_0_5; -.
DR OMA; DCGACHG; -.
DR Proteomes; UP000000361; Chromosome 1.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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; -; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR SUPFAM; SSF46626; SSF46626; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 3: Inferred from homology;
KW Electron transport; Heme; Iron; Metal-binding; Periplasm;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..103
FT /note="Cytochrome c55X"
FT /id="PRO_0000006571"
FT BINDING 36
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 39
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 40
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
SQ SEQUENCE 103 AA; 10992 MW; 99ED7C1B3F0E2004 CRC64;
MARLALLLVL LAGTAVAGPP DAARQDELRH LVRQDCGSCH GLRMTGGLGR PITAAALAGR
DVEDLSDVIL DGMPGTAMPG WRPLLTEDDA RWIADYLLKT ETE