CCHL_YEAST
ID CCHL_YEAST Reviewed; 269 AA.
AC P06182; D6VPH7;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Holocytochrome-c synthase {ECO:0000305|PubMed:3034577};
DE EC=4.4.1.17 {ECO:0000269|PubMed:3034577};
DE AltName: Full=Cytochrome c heme lyase {ECO:0000305|PubMed:3034577};
DE Short=CCHL;
GN Name=CYC3; OrderedLocusNames=YAL039C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=B-7034;
RX PubMed=3034577; DOI=10.1002/j.1460-2075.1987.tb04744.x;
RA Dumont M.E., Ernst J.F., Hampsey D.M., Sherman F.;
RT "Identification and sequence of the gene encoding cytochrome c heme lyase
RT in the yeast Saccharomyces cerevisiae.";
RL EMBO J. 6:235-241(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=22984289; DOI=10.1074/mcp.m112.021105;
RA Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J.,
RA Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.;
RT "Intermembrane space proteome of yeast mitochondria.";
RL Mol. Cell. Proteomics 11:1840-1852(2012).
CC -!- FUNCTION: Lyase that catalyzes the covalent linking of the heme group
CC to the cytochrome C apoprotein to produce the mature functional
CC cytochrome. {ECO:0000269|PubMed:3034577}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=holo-[cytochrome c] = apo-[cytochrome c] + heme b;
CC Xref=Rhea:RHEA:22648, Rhea:RHEA-COMP:10725, Rhea:RHEA-COMP:10726,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:60344, ChEBI:CHEBI:83739; EC=4.4.1.17;
CC Evidence={ECO:0000269|PubMed:3034577};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22649;
CC Evidence={ECO:0000305|PubMed:3034577};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q00873}. Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:22984289}.
CC -!- MISCELLANEOUS: Present with 3870 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cytochrome c-type heme lyase family.
CC {ECO:0000305}.
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DR EMBL; X04776; CAA28470.1; -; Genomic_DNA.
DR EMBL; U12980; AAC04992.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06947.1; -; Genomic_DNA.
DR PIR; A26162; A26162.
DR RefSeq; NP_009361.1; NM_001178184.1.
DR AlphaFoldDB; P06182; -.
DR BioGRID; 31726; 105.
DR IntAct; P06182; 13.
DR STRING; 4932.YAL039C; -.
DR iPTMnet; P06182; -.
DR MaxQB; P06182; -.
DR PaxDb; P06182; -.
DR PRIDE; P06182; -.
DR EnsemblFungi; YAL039C_mRNA; YAL039C; YAL039C.
DR GeneID; 851192; -.
DR KEGG; sce:YAL039C; -.
DR SGD; S000000037; CYC3.
DR VEuPathDB; FungiDB:YAL039C; -.
DR eggNOG; KOG3996; Eukaryota.
DR GeneTree; ENSGT00390000004175; -.
DR HOGENOM; CLU_048602_0_1_1; -.
DR InParanoid; P06182; -.
DR OMA; EGAWDEI; -.
DR BioCyc; YEAST:YAL039C-MON; -.
DR BRENDA; 4.4.1.17; 984.
DR PRO; PR:P06182; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P06182; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0004408; F:holocytochrome-c synthase activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0018063; P:cytochrome c-heme linkage; IDA:SGD.
DR InterPro; IPR000511; Holocyt_c/c1_synthase.
DR PANTHER; PTHR12743; PTHR12743; 1.
DR Pfam; PF01265; Cyto_heme_lyase; 1.
DR PROSITE; PS00821; CYTO_HEME_LYASE_1; 1.
DR PROSITE; PS00822; CYTO_HEME_LYASE_2; 1.
PE 1: Evidence at protein level;
KW Heme; Iron; Lyase; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat.
FT CHAIN 1..269
FT /note="Holocytochrome-c synthase"
FT /id="PRO_0000121718"
FT REPEAT 25..30
FT /note="HRM 1"
FT REPEAT 41..46
FT /note="HRM 2"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 269 AA; 30081 MW; A672A48BBFD848AF CRC64;
MGWFWADQKT TGKDIGGAAV SSMSGCPVMH ESSSSSPPSS ECPVMQGDND RINPLNNMPE
LAASKQPGQK MDLPVDRTIS SIPKSPDSNE FWEYPSPQQM YNAMVRKGKI GGSGEVAEDA
VESMVQVHNF LNEGCWQEVL EWEKPHTDES HVQPKLLKFM GKPGVLSPRA RWMHLCGLLF
PSHFSQELPF DRHDWIVLRG ERKAEQQPPT FKEVRYVLDF YGGPDDENGM PTFHVDVRPA
LDSLDNAKDR MTRFLDRMIS GPSSSSSAP
