CCHL_CANAW
ID CCHL_CANAW Reviewed; 264 AA.
AC P53700; C4YR04;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Holocytochrome-c synthase {ECO:0000305|PubMed:9786186};
DE EC=4.4.1.17 {ECO:0000305|PubMed:9786186};
DE AltName: Full=Cytochrome c heme lyase {ECO:0000305|PubMed:9786186};
DE Short=CCHL;
GN Name=CYC3; ORFNames=CAWG_04502;
OS Candida albicans (strain WO-1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294748;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=WO-1;
RX PubMed=9786186; DOI=10.1046/j.1365-2958.1998.01039.x;
RA Cervera A.M., Gozalbo D., McCreath K.J., Gow N.A., Martinez J.P.,
RA Casanova M.;
RT "Molecular cloning and characterization of a Candida albicans gene coding
RT for cytochrome c haem lyase and a cell wall-related protein.";
RL Mol. Microbiol. 30:67-81(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- FUNCTION: Lyase that probably catalyzes the covalent linking of the
CC heme group to the cytochrome C apoprotein to produce the mature
CC functional cytochrome. {ECO:0000269|PubMed:9786186}.
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:0000305|PubMed:9786186};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22650;
CC Evidence={ECO:0000305|PubMed:9786186};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:9786186}.
CC -!- SIMILARITY: Belongs to the cytochrome c-type heme lyase family.
CC {ECO:0000305}.
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DR EMBL; U62148; AAB04135.1; -; Genomic_DNA.
DR EMBL; CM000311; EEQ46157.1; -; Genomic_DNA.
DR AlphaFoldDB; P53700; -.
DR STRING; 5476.P53700; -.
DR EnsemblFungi; EEQ46157; EEQ46157; CAWG_04502.
DR VEuPathDB; FungiDB:CAWG_04502; -.
DR HOGENOM; CLU_048602_0_1_1; -.
DR OMA; EGAWDEI; -.
DR BRENDA; 4.4.1.17; 1096.
DR Proteomes; UP000001429; Chromosome 5.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004408; F:holocytochrome-c synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; Repeat.
FT CHAIN 1..264
FT /note="Holocytochrome-c synthase"
FT /id="PRO_0000121717"
FT REPEAT 25..30
FT /note="HRM 1"
FT REPEAT 39..44
FT /note="HRM 2"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 114
FT /note="G -> V (in Ref. 1; AAB04135)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="T -> A (in Ref. 1; AAB04135)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 264 AA; 30170 MW; 89923AB2FC3A97A6 CRC64;
MGWFWADKPS QDTVKATSSF TTPSACPIDH SKLASSSPTC PVKLNNDNDE VLNPLNNMPM
AISSERAPGQ RIKLSTERTI STIPRGESED QGLWEYPSPQ QMLNAMLSKG KGDGVPEDAV
ESMVEVHNFL NEGAWQQILT WEDQYTQQTK VEPRLKKFTG RPHDLSPKAR MYLWLGQLFP
ETFNTIPPFD RHDWTVLRSC GRNQGWKEVR YVIDYYGAPD DEETGMPAFM LDTRPALDNL
TNARDRFTHW AYPLWKKAMG EVRD
