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UniProtKB/Swiss-Prot entry P32131

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HEMN_ECOLI
Primary accession number P32131
Secondary accession numbers P76772 Q2M8G4
Integrated into Swiss-Prot on October 1, 1993
Sequence was last modified on November 1, 1997 (Sequence version 4)
Annotations were last modified on    July 22, 2008 (Entry version 80)
Name and origin of the protein
Protein name Oxygen-independent coproporphyrinogen III oxidase
Synonyms Coproporphyrinogenase
Coprogen oxidase
EC 1.3.99.22
Gene name
Name: hemN
Synonyms: yihJ
OrderedLocusNames: b3867, JW3838
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
Wachi M., Hamano-Takaku F., Nagano K., Kobayashi M., Yukawa H., Nagai K.;
"Sequence of the downstream flanking region of the glnALG genes of Escherichia coli.";
Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=7768836 [NCBI, ExPASy, EBI, Israel, Japan]
Troup B., Hungerer C., Jahn D.;
"Cloning and characterization of the Escherichia coli hemN gene encoding the oxygen-independent coproporphyrinogen III oxidase.";
J. Bacteriol. 177:3326-3331(1995).
[3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1093/nar/21.15.3391; PubMed=8346018 [NCBI, ExPASy, EBI, Israel, Japan]
Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
"Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes.";
Nucleic Acids Res. 21:3391-3398(1993).
[4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
 CHARACTERIZATION, AND MUTAGENESIS OF TYR-56; HIS-58; CYS-62; CYS-66; PHE-68; CYS-69; CYS-71; GLY-111 AND GLY-113.
DOI=10.1074/jbc.M205247200; PubMed=12114526 [NCBI, ExPASy, EBI, Israel, Japan]
Layer G., Verfuerth K., Mahlitz E., Jahn D.;
"Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli.";
J. Biol. Chem. 277:34136-34142(2002).
[7]
 FUNCTIONAL FEATURES, AND MUTAGENESIS OF TYR-56; GLU-145; PHE-310; GLN-311 AND ILE-329.
DOI=10.1074/jbc.M501275200; PubMed=15967800 [NCBI, ExPASy, EBI, Israel, Japan]
Layer G., Grage K., Teschner T., Schuenemann V., Breckau D., Masoumi A., Jahn M., Heathcote P., Trautwein A.X., Jahn D.;
"Radical S-adenosylmethionine enzyme coproporphyrinogen III oxidase HemN: functional features of the [4Fe-4S] cluster and the two bound S-adenosyl-L-methionines.";
J. Biol. Chem. 280:29038-29046(2005).
[8]
 X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS), AND CATALYTIC MECHANISM.
DOI=10.1093/emboj/cdg598; PubMed=14633981 [NCBI, ExPASy, EBI, Israel, Japan]
Layer G., Moser J., Heinz D.W., Jahn D., Schubert W.-D.;
"Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of Radical SAM enzymes.";
EMBO J. 22:6214-6224(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D16509; BAA03961.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X82073; CAA57578.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L19201; AAB03001.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76864.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77442.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq AP_003941.1; -.
NP_418303.2; -.
3D structure databases
PDB
1OLT; X-ray; 2.07 A; A=1-457.[ExPASy / RCSB / EBI]
PDBsum 1OLT; -.
ModBase P32131.
Protein-protein interaction databases
IntAct P32131; -.
Enzyme and pathway databases
BioCyc EcoCyc:HEMN-MON; -.
Organism-specific databases
EchoBASE EB1782; -.
EcoGene EG11836; hemN.
Ontologies
GO
GO:0051989; Molecular function: coproporphyrinogen dehydrogenase activity (inferred from electronic annotation from EC).
QuickGo view.
Family and domain databases
InterPro IPR006638; Elp3/MiaB/NifB.
IPR004558; HemN.
IPR010723; HemN_C.
IPR007197; Radical_SAM.
Graphical view of domain structure.
Pfam PF06969; HemN_C; 1.
PF04055; Radical_SAM; 1.
Pfam graphical view of domain structure.
SMART SM00729; Elp3; 1.
SMART graphical view of domain structure.
TIGRFAMs TIGR00538; hemN; 1.
BLOCKS P32131.
Genome annotation databases
GeneID 948362; -.
GenomeReviews U00096_GR; b3867.
AP009048_GR; JW3838.
KEGG ecj:JW3838; -.
eco:b3867; -.
Phylogenomic databases
HOGENOM P32131; -.
Genome annotation databases
CMR P32131; b3867.
Other
ProtoNet P32131.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; 4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Oxidoreductase; Porphyrin biosynthesis; S-adenosyl-L-methionine.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   457  457     Oxygen-independent coproporphyrinogen III oxidase. PRO_0000109941
REGION   113   114  2     S-adenosyl-L-methionine 2 binding. 
METAL   62    62        Iron-sulfur (4Fe-4S-S-AdoMet). 
METAL   66    66        Iron-sulfur (4Fe-4S-S-AdoMet). 
METAL   69    69        Iron-sulfur (4Fe-4S-S-AdoMet). 
BINDING   56    56        S-adenosyl-L-methionine 1. 
BINDING   68    68        S-adenosyl-L-methionine 2; via carbonyl oxygen. 
BINDING   112   112        S-adenosyl-L-methionine 1; via amide nitrogen and carbonyl oxygen. 
BINDING   145   145        S-adenosyl-L-methionine 1. 
BINDING   172   172        S-adenosyl-L-methionine 2. 
BINDING   184   184        S-adenosyl-L-methionine 2. 
BINDING   209   209        S-adenosyl-L-methionine 2. 
MUTAGEN   56    56        Y->A,L: Loss of activity. 
MUTAGEN   56    56        Y->F: Decreases activity by 50%. 
MUTAGEN   58    58        H->L: Results in loss of iron-sulfur cluster and activity. 
MUTAGEN   62    62        C->S: Results in loss of iron-sulfur cluster and activity. 
MUTAGEN   66    66        C->S: Results in loss of iron-sulfur cluster and activity. 
MUTAGEN   68    68        F->L: No effect. 
MUTAGEN   69    69        C->S: Results in loss of iron-sulfur cluster and activity. 
MUTAGEN   71    71        C->S: No effect on iron-sulfur cluster, but results in activity loss. 
MUTAGEN   111   111        G->V: Loss of activity and much less iron-sulfur cluster formed; when associated with V-113. 
MUTAGEN   113   113        G->V: Loss of activity and much less iron-sulfur cluster formed; when associated with V-111. 
MUTAGEN   145   145        E->A,I: Loss of activity. Iron content reduced by about 80%. 
MUTAGEN   310   310        F->A,L: Loss of activity. Iron content reduced by about 50%. Can cleave up to one molecule of S-adenosyl-L-methionine (in vitro). 
MUTAGEN   311   311        Q->A: Loss of activity. No change in iron content. Can cleave up to one molecule of S-adenosyl-L-methionine (in vitro). 
MUTAGEN   329   329        I->A: Loss of activity. No change in iron content. Can cleave up to one molecule of S-adenosyl-L-methionine (in vitro). 
CONFLICT   232   232        L -> V (in Ref. 2; CAA57578). 
TURN   10    12  3      
STRAND   25    27  3      
HELIX   29    31  3      
HELIX   38    45  8      
STRAND   53    59  7      
STRAND   61    64  4      
HELIX   80    96  17      
HELIX   97   100  4      
STRAND   105   113  9      
HELIX   115   117  3      
HELIX   120   133  14      
STRAND   136   146  11      
STRAND   148   150  3      
HELIX   154   161  8      
STRAND   166   172  7      
HELIX   176   182  7      
HELIX   188   200  13      
STRAND   207   213  7      
HELIX   219   232  14      
STRAND   235   241  7      
TURN   246   248  3      
HELIX   250   254  5      
HELIX   257   259  3      
HELIX   263   279  17      
STRAND   283   286  4      
STRAND   289   291  3      
HELIX   296   303  8      
STRAND   313   315  3      
STRAND   320   325  6      
STRAND   329   332  4      
STRAND   335   339  5      
HELIX   343   353  11      
STRAND   357   362  6      
HELIX   365   380  16      
STRAND   381   384  4      
HELIX   385   391  7      
HELIX   396   399  4      
HELIX   401   412  12      
STRAND   415   418  4      
STRAND   420   425  6      
TURN   427   429  3      
HELIX   430   432  3      
HELIX   433   438  6      
Sequence information
Length: 457 AA [This is the length of the unprocessed precursor] Molecular weight: 52729 Da [This is the MW of the unprocessed precursor] CRC64: 047EBB65D9B8F133 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSVQQIDWDL ALIQKYNYSG PRYTSYPTAL EFSEDFGEQA FLQAVARYPE RPLSLYVHIP 

        70         80         90        100        110        120 
FCHKLCYFCG CNKIVTRQQH KADQYLDALE QEIVHRAPLF AGRHVSQLHW GGGTPTYLNK 

       130        140        150        160        170        180 
AQISRLMKLL RENFQFNADA EISIEVDPRE IELDVLDHLR AEGFNRLSMG VQDFNKEVQR 

       190        200        210        220        230        240 
LVNREQDEEF IFALLNHARE IGFTSTNIDL IYGLPKQTPE SFAFTLKRVA ELNPDRLSVF 

       250        260        270        280        290        300 
NYAHLPTIFA AQRKIKDADL PSPQQKLDIL QETIAFLTQS GYQFIGMDHF ARPDDELAVA 

       310        320        330        340        350        360 
QREGVLHRNF QGYTTQGDTD LLGMGVSAIS MIGDCYAQNQ KELKQYYQQV DEQGNALWRG 

       370        380        390        400        410        420 
IALTRDDCIR RDVIKSLICN FRLDYAPIEK QWDLHFADYF AEDLKLLAPL AKDGLVDVDE 

       430        440        450 
KGIQVTAKGR LLIRNICMCF DTYLRQKARM QQFSRVI
P32131 in FASTA format

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