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Entry version 167 (11 Dec 2019)
Sequence version 4 (01 Nov 1997)
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Protein

Oxygen-independent coproporphyrinogen III oxidase

Gene

hemN

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 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>
-Experimental evidence at protein leveli <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 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. It can use NAD or NADP, but NAD is preferred.2 Publications

Miscellaneous

The structure carries two S-adenosyl-L-methionine binding sites with only one binding to the iron-sulfur cluster.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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] cluster2 PublicationsNote: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by EDTA.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'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. Coproporphyrinogen-III oxidase (hemN), Oxygen-independent coproporphyrinogen III oxidase (hemN), Coproporphyrinogen-III oxidase (hemN), Coproporphyrinogen-III oxidase (hemN)
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_section">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 sitei56S-adenosyl-L-methionine 1Combined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi62Iron-sulfur (4Fe-4S-S-AdoMet)Combined sources1 Publication1
Metal bindingi66Iron-sulfur (4Fe-4S-S-AdoMet)Combined sources1 Publication1
Metal bindingi69Iron-sulfur (4Fe-4S-S-AdoMet)Combined sources1 Publication1
Binding sitei112S-adenosyl-L-methionine 1; via amide nitrogen and carbonyl oxygenCombined sources1 Publication1
Binding sitei145S-adenosyl-L-methionine 1Combined sources1 Publication1
Binding sitei172S-adenosyl-L-methionine 2Combined sources1 Publication1
Binding sitei184S-adenosyl-L-methionine 2Combined sources1 Publication1
Binding sitei209S-adenosyl-L-methionine 2Combined sources1 Publication1
Binding sitei243S-adenosyl-L-methionine 2; via amide nitrogen and carbonyl oxygenCombined sources1 Publication1
Binding sitei329S-adenosyl-L-methionine 1; via amide nitrogen and carbonyl oxygenCombined sources1 Publication1

<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
EcoCyc:HEMN-MONOMER
ECOL316407:JW3838-MONOMER
MetaCyc:HEMN-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.3.99.22 2026

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_and_taxonomy_section">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:1.3.98.31 Publication)
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_and_taxonomy_section">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
Synonyms:yihJ
Ordered Locus Names:b3867, JW3838
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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
  • UP000000625 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 provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi56Y → A or L: Loss of activity. 2 Publications1
Mutagenesisi56Y → F: Decreases activity by 50%. 2 Publications1
Mutagenesisi58H → L: Results in loss of iron-sulfur cluster and activity. 1 Publication1
Mutagenesisi62C → S: Results in loss of iron-sulfur cluster and activity. 1 Publication1
Mutagenesisi66C → S: Results in loss of iron-sulfur cluster and activity. 1 Publication1
Mutagenesisi68F → L: No effect. 1 Publication1
Mutagenesisi69C → S: Results in loss of iron-sulfur cluster and activity. 1 Publication1
Mutagenesisi71C → S: No effect on iron-sulfur cluster, but results in activity loss. 1 Publication1
Mutagenesisi111G → V: Loss of activity and much less iron-sulfur cluster formed; when associated with V-113. 1 Publication1
Mutagenesisi113G → V: Loss of activity and much less iron-sulfur cluster formed; when associated with V-111. 1 Publication1
Mutagenesisi145E → A or I: Loss of activity. Iron content reduced by about 80%. 1 Publication1
Mutagenesisi310F → A or L: Loss of activity. Iron content reduced by about 50%. Can cleave up to one molecule of S-adenosyl-L-methionine (in vitro). 1 Publication1
Mutagenesisi311Q → A: Loss of activity. No change in iron content. Can cleave up to one molecule of S-adenosyl-L-methionine (in vitro). 1 Publication1
Mutagenesisi329I → A: Loss of activity. No change in iron content. Can cleave up to one molecule of S-adenosyl-L-methionine (in vitro). 1 Publication1

<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_00001099411 – 457Oxygen-independent coproporphyrinogen III oxidaseAdd BLAST457

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P32131

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P32131

PRoteomics IDEntifications database

More...
PRIDEi
P32131

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4262627, 13 interactors
852659, 2 interactors

Database of interacting proteins

More...
DIPi
DIP-9887N

Protein interaction database and analysis system

More...
IntActi
P32131, 7 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b3867

<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

Secondary structure

1457
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P32131

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P32131

<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>Regioni68 – 70S-adenosyl-L-methionine 2 bindingCombined sources1 Publication3
Regioni113 – 114S-adenosyl-L-methionine 2 bindingCombined sources1 Publication2

<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
HOG000257214

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P32131

KEGG Orthology (KO)

More...
KOi
K02495

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P32131

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
IPR010723 HemN_C
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
PF06969 HemN_C, 1 hit
PF04055 Radical_SAM, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000167 HemN, 1 hit

Structure-Function Linkage Database

More...
SFLDi
SFLDF00277 oxygen-independent_coproporphy, 1 hit
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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

P32131-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSVQQIDWDL ALIQKYNYSG PRYTSYPTAL EFSEDFGEQA FLQAVARYPE
60 70 80 90 100
RPLSLYVHIP FCHKLCYFCG CNKIVTRQQH KADQYLDALE QEIVHRAPLF
110 120 130 140 150
AGRHVSQLHW GGGTPTYLNK AQISRLMKLL RENFQFNADA EISIEVDPRE
160 170 180 190 200
IELDVLDHLR AEGFNRLSMG VQDFNKEVQR LVNREQDEEF IFALLNHARE
210 220 230 240 250
IGFTSTNIDL IYGLPKQTPE SFAFTLKRVA ELNPDRLSVF NYAHLPTIFA
260 270 280 290 300
AQRKIKDADL PSPQQKLDIL QETIAFLTQS GYQFIGMDHF ARPDDELAVA
310 320 330 340 350
QREGVLHRNF QGYTTQGDTD LLGMGVSAIS MIGDCYAQNQ KELKQYYQQV
360 370 380 390 400
DEQGNALWRG IALTRDDCIR RDVIKSLICN FRLDYAPIEK QWDLHFADYF
410 420 430 440 450
AEDLKLLAPL AKDGLVDVDE KGIQVTAKGR LLIRNICMCF DTYLRQKARM

QQFSRVI
Length:457
Mass (Da):52,729
Last modified:November 1, 1997 - v4
<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:i047EBB65D9B8F133
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAB03001 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

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 conflicti232L → V in CAA57578 (PubMed:7768836).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D16509 Genomic DNA Translation: BAA03961.1
X82073 Genomic DNA Translation: CAA57578.1
L19201 Genomic DNA Translation: AAB03001.1 Different initiation.
U00096 Genomic DNA Translation: AAC76864.2
AP009048 Genomic DNA Translation: BAE77442.1

NCBI Reference Sequences

More...
RefSeqi
NP_418303.2, NC_000913.3
WP_000116090.1, NZ_STEB01000017.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC76864; AAC76864; b3867
BAE77442; BAE77442; BAE77442

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
948362

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW3838
eco:b3867

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.2845

<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
D16509 Genomic DNA Translation: BAA03961.1
X82073 Genomic DNA Translation: CAA57578.1
L19201 Genomic DNA Translation: AAB03001.1 Different initiation.
U00096 Genomic DNA Translation: AAC76864.2
AP009048 Genomic DNA Translation: BAE77442.1
RefSeqiNP_418303.2, NC_000913.3
WP_000116090.1, NZ_STEB01000017.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OLTX-ray2.07A1-457[»]
SMRiP32131
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi4262627, 13 interactors
852659, 2 interactors
DIPiDIP-9887N
IntActiP32131, 7 interactors
STRINGi511145.b3867

Proteomic databases

jPOSTiP32131
PaxDbiP32131
PRIDEiP32131

Genome annotation databases

EnsemblBacteriaiAAC76864; AAC76864; b3867
BAE77442; BAE77442; BAE77442
GeneIDi948362
KEGGiecj:JW3838
eco:b3867
PATRICifig|1411691.4.peg.2845

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB1782

Phylogenomic databases

eggNOGiENOG4105D4P Bacteria
COG0635 LUCA
HOGENOMiHOG000257214
InParanoidiP32131
KOiK02495
PhylomeDBiP32131

Enzyme and pathway databases

UniPathwayiUPA00251;UER00323
BioCyciEcoCyc:HEMN-MONOMER
ECOL316407:JW3838-MONOMER
MetaCyc:HEMN-MONOMER
BRENDAi1.3.99.22 2026

Miscellaneous databases

EvolutionaryTraceiP32131

Protein Ontology

More...
PROi
PR:P32131

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
IPR010723 HemN_C
IPR007197 rSAM
IPR023404 rSAM_horseshoe
PANTHERiPTHR13932 PTHR13932, 1 hit
PfamiView protein in Pfam
PF06969 HemN_C, 1 hit
PF04055 Radical_SAM, 1 hit
PIRSFiPIRSF000167 HemN, 1 hit
SFLDiSFLDF00277 oxygen-independent_coproporphy, 1 hit
SFLDS00029 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_ECOLI
<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: P32131
Secondary accession number(s): P76772, Q2M8G4
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: November 1, 1997
Last modified: December 11, 2019
This is version 167 of the entry and version 4 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

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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