Coproporphyrinogen-III oxidase, anaerobic 1 - Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)

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Reviewed, UniProtKB/Swiss-Prot P33770 (HEMF_RHOS4)

Last modified June 16, 2009. Version 66. History...

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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:
    Coproporphyrinogen-III oxidase, anaerobic 1
      Short name=Coproporphyrinogenase
      Short name=Coprogen oxidase
    EC=1.3.99.22

Gene names

Name:	hemN
Ordered Locus Names:	RHOS4_19250
ORF Names:	RSP_0317

Organism

Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158) [Complete proteome] [HAMAP]

Taxonomic identifier

272943 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

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Protein attributes

Sequence length	452 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. Dedicated to bacteriochlorophyll biosynthesis.
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.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the anaerobic coproporphyrinogen-III oxidase family.

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Ontologies

Keywords
Biological process	Bacteriochlorophyll biosynthesis Chlorophyll biosynthesis 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	bacteriochlorophyll biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction 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 – 452

452

Coproporphyrinogen-III oxidase, anaerobic 1

PRO_0000109948

Regions

Region

112 – 113

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

111

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

Binding site

144

S-adenosyl-L-methionine 1 By similarity

Binding site

171

S-adenosyl-L-methionine 2 By similarity

Binding site

183

S-adenosyl-L-methionine 2 By similarity

Binding site

208

S-adenosyl-L-methionine 2 By similarity

Experimental info

Sequence conflict

195 – 197

ETL → QSV in AAB24393. Ref.1

Sequence conflict

383

D → E in AAB24393. Ref.1

Sequence conflict

400 – 409

PRIAEAAEKF → LAHRRSGREV in AAB24393. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P33770-1 [UniParc].

Last modified January 24, 2006. Version 3.
Checksum: 36E1430A36C0D6C9
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FASTA

452

50,054

        10         20         30         40         50         60 
MTNIALLQSL GLFDARVPRY TSYPAAPVFS GAVGADFQAQ AIEALDPAVP ISVYVHVPFC 

        70         80         90        100        110        120 
ERLCWFCACR TQGTQTLAPV EAYVGTLLQE LELVKQHLPA GVKAGRLHWG GGTPTILSPE 

       130        140        150        160        170        180 
LIHKLAQAIK AVIPFAEDYE FSVEIDPMMV DEPKIRALSE EGMNRASIGI QDFTDIVQNA 

       190        200        210        220        230        240 
IGREQPFENT KACVETLRRY GVHSLNTDLV YGLPHQNRES LAATIDKVLS LRPDRVAIFG 

       250        260        270        280        290        300 
YAHVPWMAKR QKLIDETVLP PDIERHELAN LAARLFTEGG FERIGIDHFA LPDDSMAVAA 

       310        320        330        340        350        360 
RSRKLRRNFQ GYTDDTCPTL LGIGASSISK FEQGYLQNTA ATAAYIKSIE EGRLPGYRGH 

       370        380        390        400        410        420 
RMTEEDYLHG RAIEMIMCDF FLDLPALRAR FGEPAETMVP RIAEAAEKFT PFVTVDADGS 

       430        440        450 
MSIAKEGRAL ARMIARLFDA YETPEARYSQ AS

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A putative anaerobic coproporphyrinogen III oxidase in Rhodobacter sphaeroides. I. Molecular cloning, transposon mutagenesis and sequence analysis of the gene." Coomber S.A., Jones R.M., Jordan P.M., Hunter C.N. Mol. Microbiol. 6:3159-3169(1992) [PubMed: 1333567] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases
	S50573 Genomic DNA. Translation: AAB24393.1. Different initiation. CP000143 Genomic DNA. Translation: ABA79493.1.
PIR	S28440.
RefSeq	YP_353394.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3719077.
GenomeReviews	Gene locus RHOS4_19250 in contig CP000143_GR.
KEGG	rsp:RSP_0317.
NMPDR	fig\|272943.3.peg.1725.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P33770.
OMA	P33770. AFGMTSI.
Enzyme and pathway databases
BioCyc	RSPH272943:RSP_0317-MON.
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

HEMF_RHOS4

Accession

Primary (citable) accession number: P33770
Secondary accession number(s): Q3J141

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	January 24, 2006
Last modified:	June 16, 2009
This is version 66 of the entry and version 3 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