CY1_KLULA
ID CY1_KLULA Reviewed; 292 AA.
AC Q00988;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Cytochrome c1, heme protein, mitochondrial;
DE EC=7.1.1.8;
DE AltName: Full=Complex III subunit 4;
DE AltName: Full=Complex III subunit IV;
DE AltName: Full=Cytochrome b-c1 complex subunit 4;
DE AltName: Full=Ubiquinol-cytochrome-c reductase complex cytochrome c1 subunit;
DE Short=Cytochrome c-1;
DE Flags: Precursor;
GN Name=CYT1; OrderedLocusNames=KLLA0F16555g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC MYA-539 / JBD100;
RX PubMed=8660461; DOI=10.1007/s002940050113;
RA Gbelska Y., Horvathova K., van der Aart Q.J.M., Zonneveld B.,
RA Steensma H.Y., Subik J.;
RT "Isolation and molecular analysis of the gene for cytochrome c1 from
RT Kluyveromyces lactis.";
RL Curr. Genet. 30:145-150(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a
CC multisubunit transmembrane complex that is part of the mitochondrial
CC electron transport chain which drives oxidative phosphorylation. The
CC respiratory chain contains 3 multisubunit complexes succinate
CC dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase
CC (complex IV, CIV), that cooperate to transfer electrons derived from
CC NADH and succinate to molecular oxygen, creating an electrochemical
CC gradient over the inner membrane that drives transmembrane transport
CC and the ATP synthase. The cytochrome b-c1 complex catalyzes electron
CC transfer from ubiquinol to cytochrome c, linking this redox reaction to
CC translocation of protons across the mitochondrial inner membrane, with
CC protons being carried across the membrane as hydrogens on the quinol.
CC In the process called Q cycle, 2 protons are consumed from the matrix,
CC 4 protons are released into the intermembrane space and 2 electrons are
CC passed to cytochrome c. Cytochrome c1 is a catalytic core subunit
CC containing a c-type heme. It transfers electrons from the [2Fe-2S]
CC iron-sulfur cluster of the Rieske protein to cytochrome c.
CC {ECO:0000250|UniProtKB:P07143}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2
CC Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:132124; EC=7.1.1.8;
CC Evidence={ECO:0000250|UniProtKB:P07143};
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000250|UniProtKB:P07143};
CC Note=Binds 1 heme c group covalently per subunit.
CC {ECO:0000250|UniProtKB:P07143};
CC -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme
CC composed of 3 respiratory subunits cytochrome b, cytochrome c1 and
CC Rieske protein, 2 core protein subunits, and additional low-molecular
CC weight protein subunits. The complex exists as an obligatory dimer and
CC forms supercomplexes (SCs) in the inner mitochondrial membrane with
CC cytochrome c oxidase (complex IV, CIV). {ECO:0000250|UniProtKB:P07143}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P07143}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P07143}.
CC -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
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DR EMBL; X95899; CAA65144.1; -; Genomic_DNA.
DR EMBL; CR382126; CAG98532.1; -; Genomic_DNA.
DR PIR; S72323; S72323.
DR RefSeq; XP_455824.1; XM_455824.1.
DR AlphaFoldDB; Q00988; -.
DR SMR; Q00988; -.
DR STRING; 28985.XP_455824.1; -.
DR EnsemblFungi; CAG98532; CAG98532; KLLA0_F16555g.
DR GeneID; 2895671; -.
DR KEGG; kla:KLLA0_F16555g; -.
DR eggNOG; KOG3052; Eukaryota.
DR HOGENOM; CLU_040334_1_1_1; -.
DR InParanoid; Q00988; -.
DR OMA; VWVKKFK; -.
DR Proteomes; UP000000598; Chromosome F.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IEA:EnsemblFungi.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:EnsemblFungi.
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 InterPro; IPR021157; Cyt_c1_TM_anchor_C.
DR PANTHER; PTHR10266; PTHR10266; 1.
DR Pfam; PF02167; Cytochrom_C1; 1.
DR PRINTS; PR00603; CYTOCHROMEC1.
DR SUPFAM; SSF46626; SSF46626; 1.
DR SUPFAM; SSF81496; SSF81496; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 3: Inferred from homology;
KW Electron transport; Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW Transit peptide; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 47..292
FT /note="Cytochrome c1, heme protein, mitochondrial"
FT /id="PRO_0000006565"
FT TOPO_DOM 47..253
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P07143"
FT TRANSMEM 254..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..292
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P07143"
FT DOMAIN 73..226
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT REGION 117..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 86
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07143"
FT BINDING 89
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07143"
FT BINDING 90
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:0000250|UniProtKB:P07143"
FT BINDING 210
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:0000250|UniProtKB:P07143"
SQ SEQUENCE 292 AA; 31947 MW; 07F909B81B1C1C72 CRC64;
MFRSFSTAAK QAVKGTYVQR AIVGGAAVVG IGASTMLYAD SLTADAMTAA EHGLHAPGYG
WSHNGPLETF DHSSIRRGYQ VYREVCAACH SLDRVAWRTM VGVSHTNAEV RAMAEEFEYD
DEPDDQGNPK KRPGKLADYV PGPYPNEQAA RAANQGALPP DLSLIVKARH GGPDYIFALL
TGYPEEPPAG VVLPPGANYN PYFPGGSIAM GRVLFDDLVE YEDGTPATTS QMAKDVTTFL
HWCSEPEHDE RKRLGLKAMI VLSSLYLLSV WVKKFKWASI KSRKIVFNPP KK
