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Entry version 117 (26 Feb 2020)
Sequence version 2 (23 Oct 2007)
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Protein

Oxygen-independent coproporphyrinogen III oxidase

Gene

hemN

Organism
Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3)
Status
Reviewed-Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Protein inferred from homologyi <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protoporphyrin-IX biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes protoporphyrinogen-IX from coproporphyrinogen-III (AdoMet route).
Proteins known to be involved in this subpathway in this organism are:
  1. Oxygen-independent coproporphyrinogen III oxidase (hemN), Coproporphyrinogen-III oxidase (Rsph17025_0531)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes protoporphyrinogen-IX from coproporphyrinogen-III (AdoMet route), the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei54S-adenosyl-L-methionine 1By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi60Iron-sulfur (4Fe-4S-S-AdoMet)By similarity1
Metal bindingi64Iron-sulfur (4Fe-4S-S-AdoMet)By similarity1
Binding sitei66S-adenosyl-L-methionine 2; via carbonyl oxygenBy similarity1
Metal bindingi67Iron-sulfur (4Fe-4S-S-AdoMet)By similarity1
Binding sitei111S-adenosyl-L-methionine 1; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei144S-adenosyl-L-methionine 1By similarity1
Binding sitei171S-adenosyl-L-methionine 2By similarity1
Binding sitei183S-adenosyl-L-methionine 2By similarity1
Binding sitei208S-adenosyl-L-methionine 2By similarity1
Binding sitei242S-adenosyl-L-methionine 2; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei328S-adenosyl-L-methionine 1; via amide nitrogen and carbonyl oxygenBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
Biological processPorphyrin biosynthesis
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
RSPH349102:G1G8M-1002-MONOMER

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00251;UER00323

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Oxygen-independent coproporphyrinogen III oxidase (EC:1.3.98.3By similarity)
Short name:
CPO
Alternative name(s):
Coproporphyrinogen III dehydrogenase
Short name:
CPDH
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:hemN
Ordered Locus Names:Rsph17025_0977
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri349102 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000234 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001099491 – 452Oxygen-independent coproporphyrinogen III oxidaseAdd BLAST452

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P95651

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

By similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
349102.Rsph17025_0977

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P95651

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni112 – 113S-adenosyl-L-methionine 2 bindingBy similarity2

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105D4P Bacteria
COG0635 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_027579_3_0_5

KEGG Orthology (KO)

More...
KOi
K02495

Identification of Orthologs from Complete Genome Data

More...
OMAi
IFGYAHV

Database of Orthologous Groups

More...
OrthoDBi
1130951at2

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.80.30.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004558 Coprogen_oxidase_HemN
IPR034505 Coproporphyrinogen-III_oxidase
IPR006638 Elp3/MiaB/NifB
IPR007197 rSAM
IPR023404 rSAM_horseshoe

The PANTHER Classification System

More...
PANTHERi
PTHR13932 PTHR13932, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF04055 Radical_SAM, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000167 HemN, 1 hit

Structure-Function Linkage Database

More...
SFLDi
SFLDS00029 Radical_SAM, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00729 Elp3, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00538 hemN, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P95651-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTNIALLQSL GLFDARVPRY TSYPAAPVFS GAVGADFQAQ AIEALDPAVP
60 70 80 90 100
ISVYIHVPFC ERLCWFCACR TQGTQTLAPV EAYVGTLLQE LELVKKHLPA
110 120 130 140 150
GVKAGRLHWG GGTPTILSPE LIHKLAQAIK AVIPFAEDYE FSVEIDPMMV
160 170 180 190 200
DEPKIRALSE EGMNRASIGI QDFTDIVQSA IGREQPFENT RACVETLRRY
210 220 230 240 250
GVHSLNTDLV YGLPHQNRES LAATIDKVLQ LGPDRVAIFG YAHVPWMAKR
260 270 280 290 300
QKLIDENVLP NDMERHELAN LAAKMFTEGG FERIGIDHFA RPDDSMAVAA
310 320 330 340 350
RSGKLRRNFQ GYTDDTCPTL LGIGASSISK FEQGYLQNTA ATAAYIKAIE
360 370 380 390 400
EGRLPGYRGH RMTDEDYLHG RAIEMIMCEF RLDLPALRAR FGEAAETMVP
410 420 430 440 450
RITEAAAKFA PFITVDEAGS MSIEAEGRAL TRMIARVFDA YETPEARYSQ

AS
Length:452
Mass (Da):49,947
Last modified:October 23, 2007 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i814AFC17EE710CDA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti22S → C in AAB38508 (Ref. 1) Curated1
Sequence conflicti70R → P in AAB38508 (Ref. 1) Curated1
Sequence conflicti197 – 198LR → CA in AAB38508 (Ref. 1) Curated2
Sequence conflicti302S → T in AAB38508 (Ref. 1) Curated1
Sequence conflicti306R → G in AAB38508 (Ref. 1) Curated1
Sequence conflicti356G → A in AAB38508 (Ref. 1) Curated1
Sequence conflicti402I → L in AAB38508 (Ref. 1) Curated1
Sequence conflicti443T → S in AAB38508 (Ref. 1) Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U80081 Genomic DNA Translation: AAB38508.1
CP000661 Genomic DNA Translation: ABP69878.1

Protein sequence database of the Protein Information Resource

More...
PIRi
T10882

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
ABP69878; ABP69878; Rsph17025_0977

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rsq:Rsph17025_0977

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U80081 Genomic DNA Translation: AAB38508.1
CP000661 Genomic DNA Translation: ABP69878.1
PIRiT10882

3D structure databases

SMRiP95651
ModBaseiSearch...

Protein-protein interaction databases

STRINGi349102.Rsph17025_0977

Proteomic databases

PRIDEiP95651

Genome annotation databases

EnsemblBacteriaiABP69878; ABP69878; Rsph17025_0977
KEGGirsq:Rsph17025_0977

Phylogenomic databases

eggNOGiENOG4105D4P Bacteria
COG0635 LUCA
HOGENOMiCLU_027579_3_0_5
KOiK02495
OMAiIFGYAHV
OrthoDBi1130951at2

Enzyme and pathway databases

UniPathwayiUPA00251;UER00323
BioCyciRSPH349102:G1G8M-1002-MONOMER

Family and domain databases

Gene3Di3.80.30.20, 1 hit
InterProiView protein in InterPro
IPR004558 Coprogen_oxidase_HemN
IPR034505 Coproporphyrinogen-III_oxidase
IPR006638 Elp3/MiaB/NifB
IPR007197 rSAM
IPR023404 rSAM_horseshoe
PANTHERiPTHR13932 PTHR13932, 1 hit
PfamiView protein in Pfam
PF04055 Radical_SAM, 1 hit
PIRSFiPIRSF000167 HemN, 1 hit
SFLDiSFLDS00029 Radical_SAM, 1 hit
SMARTiView protein in SMART
SM00729 Elp3, 1 hit
TIGRFAMsiTIGR00538 hemN, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHEMN_RHOS5
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P95651
Secondary accession number(s): A4WR64
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: October 23, 2007
Last modified: February 26, 2020
This is version 117 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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