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Reviewed, UniProtKB/Swiss-Prot P74132 (HEMN_SYNY3)

Last modified June 16, 2009. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

Names and origin

Protein namesRecommended 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: sll1876
OrganismSynechocystis sp. (strain PCC 6803) [Complete proteome] [HAMAP]
Taxonomic identifier1148 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaChroococcalesSynechocystis

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 466466Oxygen-independent coproporphyrinogen-III oxidase
PRO_0000109954

Regions

Region118 – 1192S-adenosyl-L-methionine 2 binding By similarity

Sites

Metal binding661Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding701Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding731Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Binding site601S-adenosyl-L-methionine 1 By similarity
Binding site721S-adenosyl-L-methionine 2; via carbonyl oxygen By similarity
Binding site1171S-adenosyl-L-methionine 1; via amide nitrogen and carbonyl oxygen By similarity
Binding site1501S-adenosyl-L-methionine 1 By similarity
Binding site1771S-adenosyl-L-methionine 2 By similarity
Binding site1891S-adenosyl-L-methionine 2 By similarity
Binding site2141S-adenosyl-L-methionine 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
P74132-1 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: D49735A905A5C572

FASTA46653,161
        10         20         30         40         50         60 
MTTTFPTVEF SAELLNKYNQ GIPRYTSYPP ATELNKEFDP SDFQTAINLG NYKKTPLSLY 

        70         80         90        100        110        120 
CHIPFCAKAC YFCGCNTIIT QHKPAVDPYL KAVAKQIALV APLVDQQRPV QQLHWGGGTP 

       130        140        150        160        170        180 
NYLTLEQAEF LFNTITDAFP LAENAEISIE INPCYVDKDY IFALRQLGFN RISFGIQDFN 

       190        200        210        220        230        240 
SQVQQAVNRI QPEAMLFQVM DWIRQANFDS VNVDLIYGLP HQNLATFRET LRKTAQLNPD 

       250        260        270        280        290        300 
RIAVFNFAYV PWLKPVQKKM PESALPPAEE KLKIMQATIA DLTEQGYVFI GMDHFAKPDD 

       310        320        330        340        350        360 
ELAIAQRRGE LHRNFQGYTT QPESDLLGFG ITSISMLQDV YAQNHKTLKA FYNALDREVM 

       370        380        390        400        410        420 
PIEKGFKLSQ DDLIRRTVIK ELMCQFKLSA QELESKYNLG FDCDFNDYFA KELSALDVLE 

       430        440        450        460 
ADGLLRRLGD GLEVTPRGRI LIRNIAAVFD TYLQNKSKQQ MFSRAI 

« Hide

References

[1]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. expand/collapse author list , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

BA000022 Genomic DNA. Translation: BAA18218.1.
PIRS75657.
RefSeqNP_441538.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID955014.
GenomeReviewsGene locus sll1876 in contig BA000022_GR.
KEGGsyn:sll1876.
NMPDRfig|1148.1.peg.1639.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP74132.
OMAP74132. HVPFCES.

Enzyme and pathway databases

BioCycSSP1148:SLL1876-MON.

Family and domain databases

InterProIPR006638. Elp3/MiaB/NifB.
IPR004558. HemN.
IPR010723. HemN_C.
IPR007197. Radical_SAM.
[Graphical view]
PfamPF06969. HemN_C. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00538. hemN. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHEMN_SYNY3
AccessionPrimary (citable) accession number: P74132
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 1, 1997
Last modified: June 16, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

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