CY1_PARDE
ID CY1_PARDE Reviewed; 450 AA.
AC P13627;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Cytochrome c1;
DE Flags: Precursor;
GN Name=petC;
OS Paracoccus denitrificans.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=266;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2820981; DOI=10.1016/s0021-9258(19)76497-7;
RA Kurowski B., Ludwig B.;
RT "The genes of the Paracoccus denitrificans bc1 complex. Nucleotide sequence
RT and homologies between bacterial and mitochondrial subunits.";
RL J. Biol. Chem. 262:13805-13811(1987).
CC -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase complex
CC (complex III or cytochrome b-c1 complex), which is a respiratory chain
CC that generates an electrochemical potential coupled to ATP synthesis.
CC c1 functions as an electron donor to cytochrome c.
CC -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b,
CC cytochrome c1 and the Rieske protein.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- PTM: Binds 1 heme c group covalently per subunit.
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DR EMBL; M17522; AAA25573.1; -; Genomic_DNA.
DR EMBL; X05799; CAA29245.1; -; Genomic_DNA.
DR PIR; C29413; C29413.
DR RefSeq; WP_011748591.1; NZ_FOYK01000005.1.
DR PDB; 2YIU; X-ray; 2.70 A; B/E=25-38, B/E=202-450.
DR PDBsum; 2YIU; -.
DR AlphaFoldDB; P13627; -.
DR SMR; P13627; -.
DR TCDB; 3.D.3.1.1; the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
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 InterPro; IPR002326; Cyt_c1.
DR PANTHER; PTHR10266; PTHR10266; 1.
DR Pfam; PF02167; Cytochrom_C1; 1.
DR PRINTS; PR00603; CYTOCHROMEC1.
DR SUPFAM; SSF46626; SSF46626; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Respiratory chain; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..21
FT CHAIN 22..450
FT /note="Cytochrome c1"
FT /id="PRO_0000006560"
FT TRANSMEM 421..435
FT /note="Helical; Note=Anchors to the membrane"
FT /evidence="ECO:0000255"
FT REGION 24..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..76
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..106
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..190
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 245
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 248
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 249
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 BINDING 373
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"
FT HELIX 231..243
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 256..260
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 269..276
FT /evidence="ECO:0007829|PDB:2YIU"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:2YIU"
FT STRAND 284..291
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 337..345
FT /evidence="ECO:0007829|PDB:2YIU"
FT STRAND 361..373
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 392..407
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 411..440
FT /evidence="ECO:0007829|PDB:2YIU"
FT TURN 441..443
FT /evidence="ECO:0007829|PDB:2YIU"
SQ SEQUENCE 450 AA; 46875 MW; C1EA8B6E48FE7603 CRC64;
MTLRNASLTA VAALTVALAG GAVAQDASTA PGTTAPAGSS YHTNEAAPAA ADTAPAAEAA
DEPAAEEAEA GEAEVTEEPA ATETPAEEPA ADEPAATEEP DAEAEPAAEE AQATTEEAPA
EEPAAEEPAA EEPAEEPAAD APAEEAAAEE APAEPEAAAE EPAAEEPEAT EEEAPAEEAA
AEEAPAEEVV EDEAAADHGD AAAQEAGDSH AAAHIEDISF SFEGPFGKFD QHQLQRGLQV
YTEVCSACHG LRYVPLRTLA DEGGPQLPED QVRAYAANFD ITDPETEEDR PRVPTDHFPT
VSGEGMGPDL SLMAKARAGF HGPYGTGLSQ LFNGIGGPEY IHAVLTGYDG EEKEEAGAVL
YHNAAFAGNW IQMAAPLSDD QVTYEDGTPA TVDQMATDVA AFLMWTAEPK MMDRKQVGFV
SVIFLIVLAA LLYLTNKKLW QPIKHPRKPE
