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HEM6_DROME
ID   HEM6_DROME              Reviewed;         390 AA.
AC   Q9V3D2;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Oxygen-dependent coproporphyrinogen-III oxidase;
DE            Short=COX;
DE            Short=Coprogen oxidase;
DE            Short=Coproporphyrinogenase;
DE            EC=1.3.3.3;
GN   Name=Coprox; ORFNames=CG3433;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Ovary;
RX   PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA   Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA   Harvey D.A.;
RT   "A Drosophila complementary DNA resource.";
RL   Science 287:2222-2224(2000).
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   -!- SIMILARITY: Belongs to the aerobic coproporphyrinogen-III oxidase
CC       family. {ECO:0000305}.
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DR   EMBL; AE014134; AAF52469.1; -; Genomic_DNA.
DR   EMBL; AF160897; AAD46837.1; -; mRNA.
DR   RefSeq; NP_001285697.1; NM_001298768.1.
DR   RefSeq; NP_524777.1; NM_080038.4.
DR   AlphaFoldDB; Q9V3D2; -.
DR   SMR; Q9V3D2; -.
DR   BioGRID; 69213; 7.
DR   DIP; DIP-23030N; -.
DR   IntAct; Q9V3D2; 8.
DR   STRING; 7227.FBpp0078980; -.
DR   PaxDb; Q9V3D2; -.
DR   PRIDE; Q9V3D2; -.
DR   DNASU; 44701; -.
DR   EnsemblMetazoa; FBtr0079352; FBpp0078980; FBgn0021944.
DR   EnsemblMetazoa; FBtr0346584; FBpp0312175; FBgn0021944.
DR   GeneID; 44701; -.
DR   KEGG; dme:Dmel_CG3433; -.
DR   CTD; 44701; -.
DR   FlyBase; FBgn0021944; Coprox.
DR   VEuPathDB; VectorBase:FBgn0021944; -.
DR   eggNOG; KOG1518; Eukaryota.
DR   HOGENOM; CLU_026169_0_1_1; -.
DR   InParanoid; Q9V3D2; -.
DR   OMA; HDKGTLF; -.
DR   OrthoDB; 1080991at2759; -.
DR   PhylomeDB; Q9V3D2; -.
DR   Reactome; R-DME-189451; Heme biosynthesis.
DR   UniPathway; UPA00251; UER00322.
DR   BioGRID-ORCS; 44701; 0 hits in 1 CRISPR screen.
DR   ChiTaRS; Coprox; fly.
DR   GenomeRNAi; 44701; -.
DR   PRO; PR:Q9V3D2; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0021944; Expressed in adult midgut (Drosophila) and 29 other tissues.
DR   ExpressionAtlas; Q9V3D2; baseline and differential.
DR   Genevisible; Q9V3D2; DM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; ISS:FlyBase.
DR   GO; GO:0004109; F:coproporphyrinogen oxidase activity; ISS:FlyBase.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0006783; P:heme biosynthetic process; ISS:FlyBase.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Heme biosynthesis; Oxidoreductase; Porphyrin biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..390
FT                   /note="Oxygen-dependent coproporphyrinogen-III oxidase"
FT                   /id="PRO_0000109875"
FT   REGION          131..140
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000250"
FT   REGION          329..365
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        195
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         197..199
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         348..353
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            264
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   390 AA;  44420 MW;  E63FBA5583530863 CRC64;
     MNALRHTISL VSLGTFQLVR RTRGPHARGF LLGTGLGLAS FSAVTYAHSA EAVDPKVNGV
     QMNTSRFMAE PITDSKALLG DKENMRHRME ILIMEIQAEF CRALEAEENC GQKFKVDRWE
     RPEGGGGITC VLQDGDVFEK AGVNISVVTG SLPPAAVQQM RARGKNLKEG ASLPFFASGV
     SAVIHPRNPH VPTIHFNYRY FEVETAKGEK QWWFGGGTDL TPYYLCEKDA SHFHQTLKSA
     CDEHDPTYYP RFKKWCDDYF RIKHRNESRG IGGIFFDDID SPNQEAAFNF VSSCARAVIP
     SYVPLVRKHK NREYGNNERQ WQLLRRGRYV EFNLIYDRGT KFGLYTPGAR YESILMSLPL
     HARWEYMHEP KSQSEEGKLM KVLKNPKDWV
 
 
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