Oxygen-independent coproporphyrinogen-III oxidase

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P0A1E2 (HEMN_SALTI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Oxygen-independent coproporphyrinogen-III oxidase
Short name=Coprogen oxidase
Short name=Coproporphyrinogenase
EC=1.3.99.22

Gene names

Name:	hemN
Ordered Locus Names:	STY3877, t3617

Organism

Salmonella typhi [Complete proteome] [HAMAP]

Taxonomic identifier

90370 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length	457 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Anaerobic transformation of coproporphyrinogen-III into 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 metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (AdoMet route): step 1/1.
Subunit structure	Monomer.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the anaerobic coproporphyrinogen-III oxidase family.

Ontologies

Keywords
Biological process	Porphyrin biosynthesis
Cellular component	Cytoplasm
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding S-adenosyl-L-methionine
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	porphyrin-containing compound biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW coproporphyrinogen dehydrogenase activity Inferred from electronic annotation. Source: EC coproporphyrinogen oxidase activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 457

457

Oxygen-independent coproporphyrinogen-III oxidase

PRO_0000109951

Regions

Region

113 – 114

S-adenosyl-L-methionine 2 binding By similarity

Sites

Metal binding

Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

Metal binding

Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

Metal binding

Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

Binding site

S-adenosyl-L-methionine 1 By similarity

Binding site

S-adenosyl-L-methionine 2; via carbonyl oxygen By similarity

Binding site

112

S-adenosyl-L-methionine 1; via amide nitrogen and carbonyl oxygen By similarity

Binding site

145

S-adenosyl-L-methionine 1 By similarity

Binding site

172

S-adenosyl-L-methionine 2 By similarity

Binding site

184

S-adenosyl-L-methionine 2 By similarity

Binding site

209

S-adenosyl-L-methionine 2 By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P0A1E2 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: 5667B4FE76204DAB
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FASTA

457

52,828

        10         20         30         40         50         60 
MSEQQIDWDL ALIQKYNYSG PRYTSYPTAL EFSEDFEDAA FLQAVARYPE RPLSLYVHIP 

        70         80         90        100        110        120 
FCHKLCYFCG CNKIVTRQQH KADQYLDALE QEIRHRAPLF ADRHVSQLHW GGGTPTYLNK 

       130        140        150        160        170        180 
AQISRLMTLL RENFHFNTDA EISIEVDPRE IELDVLDHLR AEGFNRLSMG VQDFNKEVQR 

       190        200        210        220        230        240 
LVNREQDEEF IFALLNHARD IGFTSTNIDL IYGLPKQTPE SFAFTLKRVT ELNPDRLSVF 

       250        260        270        280        290        300 
NYAHLPTLFA AQRKIKDADL PSAQQKLDIL QETIVSLTQA GYQFIGMDHF ARPDDELAVA 

       310        320        330        340        350        360 
QREGVLHRNF QGYTTQGDTD LLGMGVSAIS MIGDGYMQNQ KELKRYYQQV DERGNALWRG 

       370        380        390        400        410        420 
ITLTRDDCIR RDVIKALICN FRLDFNAVEQ QWGLHFAEYF AEDLQLLSPL AKDGLVDISE 

       430        440        450 
KGIQVTAKGR LLIRNICMCF DAYLRQKARM QQFSRVI

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References

[1]

"Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18."
Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., Davis P.

Barrell B.G.
Nature 413:848-852(2001) [PubMed: 11677608] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CT18.

[2]

"Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18."
Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.
J. Bacteriol. 185:2330-2337(2003) [PubMed: 12644504] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700931 / Ty2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL627280 Genomic DNA. Translation: CAD03096.1. AE014613 Genomic DNA. Translation: AAO71118.1.
RefSeq	NP_458045.1. NC_003198.1. NP_807258.1. NC_004631.1.
3D structure databases
ProteinModelPortal	P0A1E2.
SMR	P0A1E2. Positions 4-444.
ModBase	Search...
Proteomic databases
PRIDE	P0A1E2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1068278. 1250123.
GenomeReviews	Gene locus t3617 in contig AE014613_GR. Gene locus STY3877 in contig AL513382_GR.
KEGG	stt:t3617. sty:STY3877.
PATRIC	18545923. VBISalEnt120419_3955.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG285973.
OMA	TPTFFSP.
ProtClustDB	PRK09249.
Enzyme and pathway databases
BioCyc	SENT209261:T3617-MONOMER. SENT220341:STY3877-MONOMER.
Family and domain databases
InterPro	IPR004558. Coprogen_oxidase_HemN. IPR006638. Elp3/MiaB/NifB. IPR010723. HemN_C. IPR007197. rSAM. IPR023404. rSAM_horseshoe. [Graphical view]
Gene3D	G3DSA:3.80.30.20. G3DSA:3.80.30.20. 1 hit.
KO	K02495.
Pfam	PF06969. HemN_C. 1 hit. PF04055. Radical_SAM. 1 hit. [Graphical view]
SMART	SM00729. Elp3. 1 hit. [Graphical view]
TIGRFAMs	TIGR00538. HemN. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HEMN_SALTI

Accession

Primary (citable) accession number: P0A1E2
Secondary accession number(s): P37129

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	March 1, 2005
Last modified:	January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents