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P95651 (HEMN_RHOS5) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Oxygen-independent coproporphyrinogen-III oxidase

Short name=CPO
EC=1.3.99.22
Alternative name(s):
Coproporphyrinogen III dehydrogenase
Short name=CPDH
Gene names
Name:hemN
Ordered Locus Names:Rsph17025_0977
OrganismRhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) [Complete proteome] [HAMAP]
Taxonomic identifier349102 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Protein attributes

Sequence length452 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in the heme and chlorophyll biosynthesis. Catalyzes the anaerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX By similarity.

Catalytic activity

Coproporphyrinogen-III + 2 S-adenosyl-L-methionine = protoporphyrinogen-IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine.

Cofactor

Binds 1 4Fe-4S cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity.

Pathway

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

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the anaerobic coproporphyrinogen-III oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 452452Oxygen-independent coproporphyrinogen-III oxidase
PRO_0000109949

Regions

Region112 – 1132S-adenosyl-L-methionine 2 binding By similarity

Sites

Metal binding601Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding641Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding671Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Binding site541S-adenosyl-L-methionine 1 By similarity
Binding site661S-adenosyl-L-methionine 2; via carbonyl oxygen By similarity
Binding site1111S-adenosyl-L-methionine 1; via amide nitrogen and carbonyl oxygen By similarity
Binding site1441S-adenosyl-L-methionine 1 By similarity
Binding site1711S-adenosyl-L-methionine 2 By similarity
Binding site1831S-adenosyl-L-methionine 2 By similarity
Binding site2081S-adenosyl-L-methionine 2 By similarity

Experimental info

Sequence conflict221S → C in AAB38508. Ref.1
Sequence conflict701R → P in AAB38508. Ref.1
Sequence conflict197 – 1982LR → CA in AAB38508. Ref.1
Sequence conflict3021S → T in AAB38508. Ref.1
Sequence conflict3061R → G in AAB38508. Ref.1
Sequence conflict3561G → A in AAB38508. Ref.1
Sequence conflict4021I → L in AAB38508. Ref.1
Sequence conflict4431T → S in AAB38508. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P95651 [UniParc].

Last modified October 23, 2007. Version 2.
Checksum: 814AFC17EE710CDA

FASTA45249,947
        10         20         30         40         50         60 
MTNIALLQSL GLFDARVPRY TSYPAAPVFS GAVGADFQAQ AIEALDPAVP ISVYIHVPFC 

        70         80         90        100        110        120 
ERLCWFCACR TQGTQTLAPV EAYVGTLLQE LELVKKHLPA GVKAGRLHWG GGTPTILSPE 

       130        140        150        160        170        180 
LIHKLAQAIK AVIPFAEDYE FSVEIDPMMV DEPKIRALSE EGMNRASIGI QDFTDIVQSA 

       190        200        210        220        230        240 
IGREQPFENT RACVETLRRY GVHSLNTDLV YGLPHQNRES LAATIDKVLQ LGPDRVAIFG 

       250        260        270        280        290        300 
YAHVPWMAKR QKLIDENVLP NDMERHELAN LAAKMFTEGG FERIGIDHFA RPDDSMAVAA 

       310        320        330        340        350        360 
RSGKLRRNFQ GYTDDTCPTL LGIGASSISK FEQGYLQNTA ATAAYIKAIE EGRLPGYRGH 

       370        380        390        400        410        420 
RMTDEDYLHG RAIEMIMCEF RLDLPALRAR FGEAAETMVP RITEAAAKFA PFITVDEAGS 

       430        440        450 
MSIEAEGRAL TRMIARVFDA YETPEARYSQ AS 

« Hide

References

« Hide 'large scale' references
[1]Shi J., Bartnikas T.B., Shapleigh J.P.
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of chromosome of Rhodobacter sphaeroides ATCC 17025."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Richardson P., Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17025 / ATH 2.4.3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U80081 Genomic DNA. Translation: AAB38508.1.
CP000661 Genomic DNA. Translation: ABP69878.1.
PIRT10882.
RefSeqYP_001167183.1. NC_009428.1.

3D structure databases

ProteinModelPortalP95651.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349102.Rsph17025_0977.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP69878; ABP69878; Rsph17025_0977.
GeneID5083193.
KEGGrsq:Rsph17025_0977.
PATRIC23160133. VBIRhoSph94549_1000.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0635.
HOGENOMHOG000257214.
KOK02495.
OMARAIEMIM.
OrthoDBEOG683S9D.

Enzyme and pathway databases

BioCycRSPH349102:GHE1-2305-MONOMER.
UniPathwayUPA00251; UER00323.

Family and domain databases

Gene3D3.80.30.20. 1 hit.
InterProIPR004558. Coprogen_oxidase_HemN.
IPR006638. Elp3/MiaB/NifB.
IPR007197. rSAM.
IPR023404. rSAM_horseshoe.
[Graphical view]
PfamPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFPIRSF000167. HemN. 1 hit.
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00538. hemN. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHEMN_RHOS5
AccessionPrimary (citable) accession number: P95651
Secondary accession number(s): A4WR64
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: October 23, 2007
Last modified: May 14, 2014
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways