Coproporphyrinogen-III oxidase, anaerobic 2 - Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P51008 (HEMZ_RHOS4)

Last modified June 16, 2009. Version 58. History...

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

Documents (2) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

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

Hide | Top

Names and origin

Protein names

Recommended name:
    Coproporphyrinogen-III oxidase, anaerobic 2
      Short name=Coproporphyrinogenase
      Short name=Coprogen oxidase
    EC=1.3.99.22

Gene names

Name:	hemZ
Ordered Locus Names:	RHOS4_23070
ORF Names:	RSP_0699

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

Hide | Top

Protein attributes

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

Hide | Top

General annotation (Comments)

Function	Anaerobic transformation of coproporphyrinogen-III into protoporphyrinogen-IX. Dedicated to bacteriochlorophyll biosynthesis 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.
Subcellular location	Cytoplasm Potential.
Sequence similarities	Belongs to the anaerobic coproporphyrinogen-III oxidase family.

Hide | Top

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...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 450

450

Coproporphyrinogen-III oxidase, anaerobic 2

PRO_0000109950

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

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P51008-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: CD391AB6F80BBA3E
Show »

FASTA

450

49,103

        10         20         30         40         50         60 
MAAVSHLAKL GLFDARVPRY TSYPTAPNFG VGVTENLHAD WISSIPAGGS ISLYLHVPFC 

        70         80         90        100        110        120 
RRLCWFCACR TQGTSSDAPV RAYAAALKSE LALLRARLAP GVRLARMHWG GGTPTLLPPT 

       130        140        150        160        170        180 
LIHELALAIR DAVPSDAETD FSVEIDPTEI DAARLDALFE AGMTRVSIGV QDFDPLIQQS 

       190        200        210        220        230        240 
IGREQSFELT QRLTEDLRHR GLMGLDADIL YGLPHQTAPG VADSVQKLLS LSPDRVAVLG 

       250        260        270        280        290        300 
YAHVPAVSRR QLMIPTASIP GPEERLDLFE TARTLILWDG YQQVGLDHFA RAGDPLAHAH 

       310        320        330        340        350        360 
ACGRLCRSFQ GYTDDRAEVL IGLGASAISR FPQGFTQNAP STSDHLRAIR SGRFSTARGH 

       370        380        390        400        410        420 
VLSDEDRLRG RMIEQLLCEF RISRAQILAR FAVAPERLET LFRTCAAAFP GVVEITGHGL 

       430        440        450 
EILEEGRPLA RIVARSFDRY DASGKPQGAI

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Aerobic and anaerobic regulation in Rhodobacter sphaeroides 2.4.1: the role of the fnrL gene." Zeilstra-Ryalls J.H., Kaplan S. J. Bacteriol. 177:6422-6431(1995) [PubMed: 7592416] [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].

Hide | Top

Cross-references

Sequence databases
	Z49746 Genomic DNA. Translation: CAA89819.1. CP000143 Genomic DNA. Translation: ABA79875.1.
RefSeq	YP_353776.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3718177.
GenomeReviews	Gene locus RHOS4_23070 in contig CP000143_GR.
KEGG	rsp:RSP_0699.
NMPDR	fig\|272943.3.peg.3048.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P51008.
OMA	P51008. ISRFPQG.
Enzyme and pathway databases
BioCyc	RSPH272943:RSP_0699-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...

Hide | Top

Entry information

Entry name

HEMZ_RHOS4

Accession

Primary (citable) accession number: P51008
Secondary accession number(s): Q3J009

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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

Hide | Top

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

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