Oxygen-independent coproporphyrinogen-III oxidase

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Reviewed, UniProtKB/Swiss-Prot O31381 (HEMN_BRAJA)

Last modified November 3, 2009. Version 59. History...

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

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

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

Gene names

Name:	hemN
Ordered Locus Names:	bll7086

Organism

Bradyrhizobium japonicum [Complete proteome] [HAMAP]

Taxonomic identifier

375 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Bradyrhizobium

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Protein attributes

Sequence length	450 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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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.

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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	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW porphyrin 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 iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 450

450

Oxygen-independent coproporphyrinogen-III oxidase

PRO_0000109940

Regions

Region

109 – 110

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

108

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

Binding site

141

S-adenosyl-L-methionine 1 By similarity

Binding site

168

S-adenosyl-L-methionine 2 By similarity

Binding site

180

S-adenosyl-L-methionine 2 By similarity

Binding site

205

S-adenosyl-L-methionine 2 By similarity

Experimental info

Sequence conflict

307

Q → H in CAA05507. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

O31381-1 [UniParc].

Last modified February 28, 2003. Version 2.
Checksum: EEAC485931754EE9
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FASTA

450

49,327

        10         20         30         40         50         60 
MRADLAVSYG EERLPRYTSY PTAPHFSPVI DAGTYARWLS ELPAGASASL YLHVPFCREM 

        70         80         90        100        110        120 
CWYCGCHTQI VRRDDLIAAY QRTLRSEIAL VAETIGRRIK VEHIHFGGGT PTIMAPEAFA 

       130        140        150        160        170        180 
ELMAAMRQAF FVLPSAEIAV EIDPRTLTAD MVEAMRLSGV NRASLGVQSF DPIVQRAINR 

       190        200        210        220        230        240 
IQSFEQTAAV VDMLRHAGIA GINFDLIYGL PHQTVASCLD TVRRSLLLAP DRFSVFGYAH 

       250        260        270        280        290        300 
VPDFKKHQRM INQGALPDGP ARHDQACAIA NALKEAGYVQ IGLDHFARPD DSMAVAFEER 

       310        320        330        340        350        360 
TLRRNFQGYT TDQGEVLLGF GASAIGHLPQ GYVQNEVQIG AYAQSIGASR LATAKGYGLT 

       370        380        390        400        410        420 
DDDRLRADII ERIMCEFSAD LGDICARHGA EPEAMLKSAS RLKPLISDGV VRLDGDRLAV 

       430        440        450 
ANDSRFLVRS VAAAFDAHLD PGKQLHSRAV

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"One of two hemN genes in Bradyrhizobium japonicum is functional during anaerobic growth and in symbiosis." Fischer H.-M., Velasco L., Delgado M.J., Bedmar E.J., Schaeren S., Zingg D., Goettfert M., Hennecke H. J. Bacteriol. 183:1300-1311(2001) [PubMed: 11157943] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: USDA 110.
[2]	"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110." Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S. DNA Res. 9:189-197(2002) [PubMed: 12597275] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: USDA 110.

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Cross-references

Sequence databases
	AJ002517 Genomic DNA. Translation: CAA05507.1. BA000040 Genomic DNA. Translation: BAC52351.1.
RefSeq	NP_773726.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1047805.
GenomeReviews	Gene locus bll7086 in contig BA000040_GR.
KEGG	bja:bll7086.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	O31381.
OMA	HVPFCRE.
Enzyme and pathway databases
BioCyc	BJAP224911:BLL7086-MON.
BRENDA	1.3.99.22. 280.
Family and domain databases
InterPro	IPR006638. Elp3/MiaB/NifB. IPR004558. HemN. IPR010723. HemN_C. IPR007197. Radical_SAM. [Graphical view]
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...

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Entry information

Entry name

HEMN_BRAJA

Accession

Primary (citable) accession number: O31381

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	February 28, 2003
Last modified:	November 3, 2009
This is version 59 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents