YE42_SCHPO
ID YE42_SCHPO Reviewed; 216 AA.
AC O13962;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Putative holocytochrome-c1 synthase {ECO:0000250|UniProtKB:Q00873};
DE EC=4.4.1.17 {ECO:0000250|UniProtKB:Q00873};
DE AltName: Full=Cytochrome c1 heme lyase {ECO:0000250|UniProtKB:Q00873};
DE Short=CC1HL {ECO:0000250|UniProtKB:Q00873};
GN ORFNames=SPAC24C9.02c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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:0000250|UniProtKB:Q00873}.
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:0000250|UniProtKB:Q00873};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22650;
CC Evidence={ECO:0000250|UniProtKB:Q00873};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q00873}.
CC -!- SIMILARITY: Belongs to the cytochrome c-type heme lyase family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB11259.1; -; Genomic_DNA.
DR PIR; T38343; T38343.
DR RefSeq; NP_594026.1; NM_001019451.2.
DR AlphaFoldDB; O13962; -.
DR STRING; 4896.SPAC24C9.02c.1; -.
DR MaxQB; O13962; -.
DR PaxDb; O13962; -.
DR EnsemblFungi; SPAC24C9.02c.1; SPAC24C9.02c.1:pep; SPAC24C9.02c.
DR GeneID; 2541462; -.
DR KEGG; spo:SPAC24C9.02c; -.
DR PomBase; SPAC24C9.02c; -.
DR VEuPathDB; FungiDB:SPAC24C9.02c; -.
DR eggNOG; KOG3996; Eukaryota.
DR HOGENOM; CLU_048602_1_2_1; -.
DR InParanoid; O13962; -.
DR OMA; VNERVWN; -.
DR PhylomeDB; O13962; -.
DR PRO; PR:O13962; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004408; F:holocytochrome-c synthase activity; ISO:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1903607; P:cytochrome c biosynthetic process; IC:PomBase.
DR GO; GO:0018063; P:cytochrome c-heme linkage; IBA:GO_Central.
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 3: Inferred from homology;
KW Heme; Iron; Lyase; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome.
FT CHAIN 1..216
FT /note="Putative holocytochrome-c1 synthase"
FT /id="PRO_0000121720"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 216 AA; 25161 MW; DE0D4D56C16491A8 CRC64;
MQPEQLNQEE ESKCPVPPEV RDAWLKSHGG KKPSEVHDTP HPTMLPTERE ISTIPKVVTE
SDSGKEEKWI YPSQQMFFDA MKRKNWNPHP EDMKTIVPIH NAVNERAWQD ILQWEQGWGS
EKCGGPKLER FDGNVKKLTP KARILNLLGY NKPFDRHDWL VNRCGRKVAY VIDFYNGPTV
NGTPSIYLDV RPKLSVHGAW MRVYRWTNEH FSQNSK
