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HEM6_SCHPO
ID   HEM6_SCHPO              Reviewed;         312 AA.
AC   Q9UTE2;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Probable oxygen-dependent coproporphyrinogen-III oxidase;
DE            Short=COX;
DE            Short=Coprogen oxidase;
DE            Short=Coproporphyrinogenase;
DE            EC=1.3.3.3;
GN   Name=hem13; ORFNames=SPAC222.11;
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: Involved in the heme biosynthesis. Catalyzes the aerobic
CC       oxidative decarboxylation of propionate groups of rings A and B of
CC       coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-
CC       IX (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=coproporphyrinogen III + 2 H(+) + O2 = 2 CO2 + 2 H2O +
CC         protoporphyrinogen IX; Xref=Rhea:RHEA:18257, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57307, ChEBI:CHEBI:57309; EC=1.3.3.3;
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (O2
CC       route): step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the aerobic coproporphyrinogen-III oxidase
CC       family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB60703.1; -; Genomic_DNA.
DR   PIR; T50152; T50152.
DR   RefSeq; NP_593150.1; NM_001018547.2.
DR   AlphaFoldDB; Q9UTE2; -.
DR   SMR; Q9UTE2; -.
DR   BioGRID; 278422; 4.
DR   IntAct; Q9UTE2; 1.
DR   STRING; 4896.SPAC222.11.1; -.
DR   iPTMnet; Q9UTE2; -.
DR   MaxQB; Q9UTE2; -.
DR   PaxDb; Q9UTE2; -.
DR   EnsemblFungi; SPAC222.11.1; SPAC222.11.1:pep; SPAC222.11.
DR   GeneID; 2541934; -.
DR   KEGG; spo:SPAC222.11; -.
DR   PomBase; SPAC222.11; hem13.
DR   VEuPathDB; FungiDB:SPAC222.11; -.
DR   eggNOG; KOG1518; Eukaryota.
DR   HOGENOM; CLU_026169_0_0_1; -.
DR   InParanoid; Q9UTE2; -.
DR   OMA; HDKGTLF; -.
DR   PhylomeDB; Q9UTE2; -.
DR   Reactome; R-SPO-189451; Heme biosynthesis.
DR   UniPathway; UPA00251; UER00322.
DR   PRO; PR:Q9UTE2; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0004109; F:coproporphyrinogen oxidase activity; ISO:PomBase.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IMP:PomBase.
DR   Gene3D; 3.40.1500.10; -; 1.
DR   InterPro; IPR001260; Coprogen_oxidase_aer.
DR   InterPro; IPR036406; Coprogen_oxidase_aer_sf.
DR   InterPro; IPR018375; Coprogen_oxidase_CS.
DR   PANTHER; PTHR10755; PTHR10755; 1.
DR   Pfam; PF01218; Coprogen_oxidas; 1.
DR   PIRSF; PIRSF000166; Coproporphyri_ox; 1.
DR   PRINTS; PR00073; COPRGNOXDASE.
DR   SUPFAM; SSF102886; SSF102886; 1.
DR   PROSITE; PS01021; COPROGEN_OXIDASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Heme biosynthesis; Oxidoreductase; Porphyrin biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..312
FT                   /note="Probable oxygen-dependent coproporphyrinogen-III
FT                   oxidase"
FT                   /id="PRO_0000109877"
FT   REGION          53..62
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000250"
FT   REGION          252..288
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        118
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         120..122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         271..276
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            187
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   312 AA;  36244 MW;  33C785A534977583 CRC64;
     MSDITVEPIG KQMEKLILDV QQEIVAGLEA VDGQKFFQDK WTKGEGGYGI SCVIQDGNVF
     EKGGVNTSIV QGKLNQDAVQ RMRANHEGID RTAKELPFFA AGISMVIHPR NPMAPTTHLN
     YRYFELVNSD GKKIWWFGGG ADLTPSILFE EDGKHFHKLH KEACDRHDPT FYPRFKKWAD
     EYFLIKHRKE TRGIGGIFFD DLSEKDPQEL FAFVKDCAHT FLPAYVPIME KRKNMEFTED
     DKEFQLIRRG YYAEFNVMYD RGTWFGLQAP EPRVESILMT LPLHASWRYK YEPKQERHKA
     LLKVTHTPIE WC
 
 
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