CYT2_YEAST
ID CYT2_YEAST Reviewed; 224 AA.
AC Q00873; D6VXK1;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Holocytochrome-c1 synthase {ECO:0000305|PubMed:1499554};
DE EC=4.4.1.17 {ECO:0000269|PubMed:1499554};
DE AltName: Full=Cytochrome c1 heme lyase {ECO:0000305|PubMed:1499554};
DE Short=CC1HL {ECO:0000303|PubMed:1499554};
GN Name=CYT2 {ECO:0000303|PubMed:1499554}; OrderedLocusNames=YKL087C;
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, CATALYTIC ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 204510 / AB320;
RX PubMed=1499554; DOI=10.1111/j.1432-1033.1992.tb17146.x;
RA Zollner A., Roedel G., Haid A.;
RT "Molecular cloning and characterization of the Saccharomyces cerevisiae
RT CYT2 gene encoding cytochrome-c1-heme lyase.";
RL Eur. J. Biochem. 207:1093-1100(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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).
CC -!- FUNCTION: Lyase that catalyzes the covalent linking of the heme group
CC to the cytochrome C1 apoprotein to produce the mature functional
CC cytochrome. {ECO:0000269|PubMed:1499554}.
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:1499554};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22649;
CC Evidence={ECO:0000305|PubMed:1499554};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:1499554}. Note=Partially exposed to the
CC intermembrane space. {ECO:0000305|PubMed:1499554}.
CC -!- SIMILARITY: Belongs to the cytochrome c-type heme lyase family.
CC {ECO:0000305}.
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DR EMBL; X67017; CAA47407.1; -; Genomic_DNA.
DR EMBL; Z28087; CAA81925.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09071.1; -; Genomic_DNA.
DR PIR; S24365; S24365.
DR RefSeq; NP_012836.1; NM_001179653.1.
DR AlphaFoldDB; Q00873; -.
DR BioGRID; 34046; 204.
DR DIP; DIP-2118N; -.
DR STRING; 4932.YKL087C; -.
DR iPTMnet; Q00873; -.
DR MaxQB; Q00873; -.
DR PaxDb; Q00873; -.
DR PRIDE; Q00873; -.
DR DNASU; 853775; -.
DR EnsemblFungi; YKL087C_mRNA; YKL087C; YKL087C.
DR GeneID; 853775; -.
DR KEGG; sce:YKL087C; -.
DR SGD; S000001570; CYT2.
DR VEuPathDB; FungiDB:YKL087C; -.
DR eggNOG; KOG3996; Eukaryota.
DR GeneTree; ENSGT00390000004175; -.
DR HOGENOM; CLU_048602_1_2_1; -.
DR InParanoid; Q00873; -.
DR OMA; VNERVWN; -.
DR BioCyc; YEAST:YKL087C-MON; -.
DR BRENDA; 4.4.1.B1; 984.
DR PRO; PR:Q00873; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; Q00873; 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; IMP:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0018063; P:cytochrome c-heme linkage; IMP: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.
FT CHAIN 1..224
FT /note="Holocytochrome-c1 synthase"
FT /id="PRO_0000121719"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 224 AA; 26076 MW; F2AE1A2B4A5D55A6 CRC64;
MMSSDQQGKC PVDEETKKLW LREHGNEAHP GATAPGNQLE CSANPQDNDK TPEYHTTVDL
SQSREVSTIP RTNSDRNWIY PSEKQFYEAM MKKNWDPNSD DMKVVVPLHN SINERVWNYI
KSWEDKQGGE ACGGIKLTNF KGDSKKLTPR AWFRSRILHL AKPFDRHDWQ IDRCGKTVDY
VIDFYSTDLN DANSQQQPLI YLDVRPKLNS FEGFRLRFWK SLGF
