Oxygen-independent coproporphyrinogen-III oxidase - Ralstonia eutropha (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)

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Reviewed, UniProtKB/Swiss-Prot O34162 (HEMN_RALEH)

Last modified June 16, 2009. Version 60. 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:	H16_A3615

Organism

Ralstonia eutropha (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)) [Complete proteome] [HAMAP]

Taxonomic identifier

381666 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

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Protein attributes

Sequence length	494 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.
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 – 494

494

Oxygen-independent coproporphyrinogen-III oxidase

PRO_0000109937

Regions

Region

127 – 128

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

126

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

Binding site

159

S-adenosyl-L-methionine 1 By similarity

Binding site

186

S-adenosyl-L-methionine 2 By similarity

Binding site

198

S-adenosyl-L-methionine 2 By similarity

Binding site

223

S-adenosyl-L-methionine 2 By similarity

Experimental info

Sequence conflict

63 – 65

Missing in AAB66374. Ref.1

Sequence conflict

480 – 481

QP → HA in AAB66374. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

O34162-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: CEDE1267B17A069F
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FASTA

494

54,499

        10         20         30         40         50         60 
MIPSAITSPA PDRRALSDFR ALAGRIDGNG PRYTSYPTAD RFHNGPDLSL YHDALAACRA 

        70         80         90        100        110        120 
DAPAPLSLYL HIPFCENICY YCGCNKIITR DHGRSARYVN YLGREMALVA DRLGPRRQVL 

       130        140        150        160        170        180 
QSHWGGGTPT FLDPGEMRRV MALLHEHFEL AAEGEHSIEI DPRRVDHARM ALLAELGFNR 

       190        200        210        220        230        240 
VSLGVQDFDP EVQQAIHRIQ PFEETRAVVD AARTLGFRSV SLDLIYGLPH QTAARFGRTI 

       250        260        270        280        290        300 
DQVLALRPDR LSVYSYAHLP HVFKPQRRID ENALPPAGEK LDILVSTIER LSAEGYVYIG 

       310        320        330        340        350        360 
MDHFALPDDD LAVAQREGRL QRNFQGYSTH AGYDQVGLGI SAIGAIAGRY VQNARTLDEY 

       370        380        390        400        410        420 
YGALDHGRLP LARGVAMSAD DHLRREIIGA LMCNGVLDIP ALEARHGIRF GTAFAPELAD 

       430        440        450        460        470        480 
LAALGADGLV QCAPDRITVT PLGRLLVRRV AMVFDRYLRE DAARPASTGA QAVAANDGAQ 

       490 
PVRFVPRARY SRVV

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Alcaligenes eutrophus hemN gene encoding the oxygen-independent coproporphyrinogen III oxidase, is required for heme biosynthesis during anaerobic growth." Lieb C., Siddiqui R.A., Hippler B., Jahn D., Friedrich B. Arch. Microbiol. 169:52-60(1998) [PubMed: 9396835] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16." Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B. Nat. Biotechnol. 24:1257-1262(2006) [PubMed: 16964242] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases
	U94742 Genomic DNA. Translation: AAB66374.1. AM260479 Genomic DNA. Translation: CAJ94672.1. Different initiation.
RefSeq	YP_728040.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4247051.
GenomeReviews	Gene locus H16_A3615 in contig AM260479_GR.
KEGG	reh:H16_A3615.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	O34162.
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_RALEH

Accession

Primary (citable) accession number: O34162
Secondary accession number(s): Q0K5P9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 60 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

Family and domain databases

Entry information

Relevant documents