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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-Protein inferred from homologyi

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

Catalytic activityi

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

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

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 (Rsph17025_0531), Oxygen-independent 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
Binding sitei54S-adenosyl-L-methionine 1By similarity1
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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

UniPathwayiUPA00251; UER00323.

Names & Taxonomyi

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
Gene namesi
Name:hemN
Ordered Locus Names:Rsph17025_0977
OrganismiRhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3)
Taxonomic identifieri349102 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
Proteomesi
  • UP000000234 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001099491 – 452Oxygen-independent coproporphyrinogen III oxidaseAdd BLAST452

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi349102.Rsph17025_0977.

Structurei

3D structure databases

ProteinModelPortaliP95651.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni112 – 113S-adenosyl-L-methionine 2 bindingBy similarity2

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105D4P. Bacteria.
COG0635. LUCA.
HOGENOMiHOG000257214.
KOiK02495.
OMAiCERLCWF.
OrthoDBiPOG091H019R.

Family and domain databases

Gene3Di3.80.30.20. 1 hit.
InterProiIPR004558. Coprogen_oxidase_HemN.
IPR006638. Elp3/MiaB/NifB.
IPR007197. rSAM.
IPR023404. rSAM_horseshoe.
[Graphical view]
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF000167. HemN. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00538. hemN. 1 hit.

Sequencei

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
Checksum:i814AFC17EE710CDA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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:
EMBLi
GenBanki
DDBJi
Links Updated
U80081 Genomic DNA. Translation: AAB38508.1.
CP000661 Genomic DNA. Translation: ABP69878.1.
PIRiT10882.
RefSeqiWP_011908017.1. NC_009428.1.

Genome annotation databases

EnsemblBacteriaiABP69878; ABP69878; Rsph17025_0977.
KEGGirsq:Rsph17025_0977.
PATRICi23160133. VBIRhoSph94549_1000.

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.
RefSeqiWP_011908017.1. NC_009428.1.

3D structure databases

ProteinModelPortaliP95651.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi349102.Rsph17025_0977.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABP69878; ABP69878; Rsph17025_0977.
KEGGirsq:Rsph17025_0977.
PATRICi23160133. VBIRhoSph94549_1000.

Phylogenomic databases

eggNOGiENOG4105D4P. Bacteria.
COG0635. LUCA.
HOGENOMiHOG000257214.
KOiK02495.
OMAiCERLCWF.
OrthoDBiPOG091H019R.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00323.

Family and domain databases

Gene3Di3.80.30.20. 1 hit.
InterProiIPR004558. Coprogen_oxidase_HemN.
IPR006638. Elp3/MiaB/NifB.
IPR007197. rSAM.
IPR023404. rSAM_horseshoe.
[Graphical view]
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF000167. HemN. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00538. hemN. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHEMN_RHOS5
AccessioniPrimary (citable) accession number: P95651
Secondary accession number(s): A4WR64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: October 23, 2007
Last modified: November 2, 2016
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.