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Q9V3D2 (HEM6_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Coproporphyrinogen-III oxidase
Short name=COX
Short name=Coprogen oxidase
Short name=Coproporphyrinogenase
EC=1.3.3.3
Gene names
Name:Coprox
ORF Names:CG3433
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length390 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Key enzyme in heme biosynthesis. Catalyzes the oxidative decarboxylation of propionic acid side chains of rings A and B of coproporphyrinogen III By similarity.

Catalytic activity

Coproporphyrinogen-III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O.

Pathway

Porphyrin metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (O2 route): step 1/1.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the aerobic coproporphyrinogen-III oxidase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

dlP15330-21EBI-153438,EBI-198400

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 390390Coproporphyrinogen-III oxidase
PRO_0000109875

Regions

Region131 – 14010Important for dimerization By similarity
Region197 – 1993Substrate binding By similarity
Region329 – 36537Important for dimerization By similarity
Region348 – 3536Substrate binding By similarity

Sites

Active site1951Proton donor By similarity
Binding site1811Substrate By similarity
Site2641Important for dimerization By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9V3D2 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: E63FBA5583530863

FASTA39044,420
        10         20         30         40         50         60 
MNALRHTISL VSLGTFQLVR RTRGPHARGF LLGTGLGLAS FSAVTYAHSA EAVDPKVNGV 

        70         80         90        100        110        120 
QMNTSRFMAE PITDSKALLG DKENMRHRME ILIMEIQAEF CRALEAEENC GQKFKVDRWE 

       130        140        150        160        170        180 
RPEGGGGITC VLQDGDVFEK AGVNISVVTG SLPPAAVQQM RARGKNLKEG ASLPFFASGV 

       190        200        210        220        230        240 
SAVIHPRNPH VPTIHFNYRY FEVETAKGEK QWWFGGGTDL TPYYLCEKDA SHFHQTLKSA 

       250        260        270        280        290        300 
CDEHDPTYYP RFKKWCDDYF RIKHRNESRG IGGIFFDDID SPNQEAAFNF VSSCARAVIP 

       310        320        330        340        350        360 
SYVPLVRKHK NREYGNNERQ WQLLRRGRYV EFNLIYDRGT KFGLYTPGAR YESILMSLPL 

       370        380        390 
HARWEYMHEP KSQSEEGKLM KVLKNPKDWV

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[2]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[3]"A Drosophila complementary DNA resource."
Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M., Harvey D.A.
Science 287:2222-2224(2000) [PubMed: 10731138] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Ovary.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE014134 Genomic DNA. Translation: AAF52469.1.
AF160897 mRNA. Translation: AAD46837.1.
RefSeqNP_524777.1. NM_080038.2.
UniGeneDm.1822.

3D structure databases

ProteinModelPortalQ9V3D2.
SMRQ9V3D2. Positions 65-390.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-23030N.
IntActQ9V3D2. 1 interaction.
MINTMINT-1024659.
STRINGQ9V3D2.

Proteomic databases

PRIDEQ9V3D2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0079352; FBpp0078980; FBgn0021944.
GeneID44701.
KEGGdme:Dmel_CG3433.
NMPDRfig|7227.3.peg.1171.

Organism-specific databases

CTD44701.
FlyBaseFBgn0021944. Coprox.

Phylogenomic databases

eggNOGinNOG04066.
GeneTreeEMGT00050000017297.
InParanoidQ9V3D2.
OMAVFKPWCD.
OrthoDBEOG4BRV25.
PhylomeDBQ9V3D2.

Gene expression databases

ArrayExpressQ9V3D2.
BgeeQ9V3D2.
GermOnlineCG3433. Drosophila melanogaster.

Family and domain databases

InterProIPR001260. Coprogen_oxidase_aer.
IPR018375. Coprogen_oxidase_CS.
[Graphical view]
Gene3DG3DSA:3.40.1500.10. Coprogen_oxidas. 1 hit.
KOK00228.
PANTHERPTHR10755. Coprogen_oxidas. 1 hit.
PfamPF01218. Coprogen_oxidas. 1 hit.
[Graphical view]
PIRSFPIRSF000166. Coproporphyri_ox. 1 hit.
PRINTSPR00073. COPRGNOXDASE.
SUPFAMSSF102886. Coprogen_oxidas. 1 hit.
PROSITEPS01021. COPROGEN_OXIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio837551.

Entry information

Entry nameHEM6_DROME
AccessionPrimary (citable) accession number: Q9V3D2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 2000
Last modified: January 25, 2012
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents