CYC_ASPNG
ID CYC_ASPNG Reviewed; 111 AA.
AC P56205;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Cytochrome c;
GN Name=cycA;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=2544196; DOI=10.1007/bf01024941;
RA Chin C.C.Q., Niehaus W.G., Wold F.;
RT "Amino acid sequence of cytochrome c from Aspergillus niger.";
RL J. Protein Chem. 8:165-171(1989).
CC -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC c heme group can accept an electron from the heme group of the
CC cytochrome c1 subunit of cytochrome reductase. Cytochrome c then
CC transfers this electron to the cytochrome oxidase complex, the final
CC protein carrier in the mitochondrial electron-transport chain.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC associated with the inner membrane.
CC -!- PTM: Binds 1 heme c group covalently per subunit.
CC -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC November 2006;
CC URL="https://web.expasy.org/spotlight/back_issues/076";
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DR PIR; A61490; A61490.
DR AlphaFoldDB; P56205; -.
DR SMR; P56205; -.
DR STRING; 5061.CADANGAP00001644; -.
DR VEuPathDB; FungiDB:An02g01830; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1144442; -.
DR VEuPathDB; FungiDB:ATCC64974_60490; -.
DR VEuPathDB; FungiDB:M747DRAFT_291904; -.
DR eggNOG; KOG3453; Eukaryota.
DR GO; GO:0005758; C:mitochondrial intermembrane space; 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; IPR002327; Cyt_c_1A/1B.
DR PANTHER; PTHR11961; PTHR11961; 1.
DR Pfam; PF00034; Cytochrom_C; 1.
DR PRINTS; PR00604; CYTCHRMECIAB.
DR SUPFAM; SSF46626; SSF46626; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW Methylation; Mitochondrion; Respiratory chain; Transport.
FT CHAIN 1..111
FT /note="Cytochrome c"
FT /id="PRO_0000108317"
FT BINDING 22
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 25
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 26
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 88
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 MOD_RES 80
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 111 AA; 11954 MW; 1F49BA817E205EB1 CRC64;
GKDASFAPGD SAKGAKLFQT RCAQCHTVEA GGPHKVGPNL HGLFGRKTGQ SEGYAYTDAN
KQAGVTWDEN TLFSYLENPK KFIPGTKMAF GGLKKGKERN DLITYLKEST A