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UniProtKB/Swiss-Prot entry P0A1E2

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

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Entry information
Entry name HEMN_SALTI
Primary accession number P0A1E2
Secondary accession number P37129
Integrated into Swiss-Prot on March 1, 2005
Sequence was last modified on March 1, 2005 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 24)
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
OrderedLocusNames: STY3877, t3617
From
Salmonella typhi [TaxID: 601] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Salmonella.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CT18;
DOI=10.1038/35101607; PubMed=11677608 [NCBI, ExPASy, EBI, Israel, Japan]
Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.;
"Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18.";
Nature 413:848-852(2001).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700931 / Ty2;
DOI=10.1128/JB.185.7.2330-2337.2003; PubMed=12644504 [NCBI, ExPASy, EBI, Israel, Japan]
Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.;
"Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18.";
J. Bacteriol. 185:2330-2337(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
AL627280; CAD03096.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014613; AAO71118.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_458045.1; -.
NP_807258.1; -.
3D structure databases
SMR P0A1E2; 4-444.
ModBase P0A1E2.
Enzyme and pathway databases
BioCyc SENT209261:T3617-MON; -.
SENT220341:STY3877-MON; -.
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 P0A1E2.
Genome annotation databases
GeneID 1068278; -.
1250123; -.
GenomeReviews AL513382_GR; STY3877.
AE014613_GR; t3617.
KEGG stt:t3617; -.
sty:STY3877; -.
Phylogenomic databases
HOGENOM P0A1E2; -.
Genome annotation databases
CMR P0A1E2; STY3877.
Other
ProtoNet P0A1E2.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
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_0000109951
REGION   113   114  2     S-adenosyl-L-methionine 2 binding (By similarity). 
METAL   62    62        Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity). 
METAL   66    66        Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity). 
METAL   69    69        Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity). 
BINDING   56    56        S-adenosyl-L-methionine 1 (By similarity). 
BINDING   68    68        S-adenosyl-L-methionine 2; via carbonyl oxygen (By similarity). 
BINDING   112   112        S-adenosyl-L-methionine 1; via amide nitrogen and carbonyl oxygen (By similarity). 
BINDING   145   145        S-adenosyl-L-methionine 1 (By similarity). 
BINDING   172   172        S-adenosyl-L-methionine 2 (By similarity). 
BINDING   184   184        S-adenosyl-L-methionine 2 (By similarity). 
BINDING   209   209        S-adenosyl-L-methionine 2 (By similarity). 
Sequence information
Length: 457 AA [This is the length of the unprocessed precursor] Molecular weight: 52828 Da [This is the MW of the unprocessed precursor] CRC64: 5667B4FE76204DAB [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSEQQIDWDL ALIQKYNYSG PRYTSYPTAL EFSEDFEDAA FLQAVARYPE RPLSLYVHIP 

        70         80         90        100        110        120 
FCHKLCYFCG CNKIVTRQQH KADQYLDALE QEIRHRAPLF ADRHVSQLHW GGGTPTYLNK 

       130        140        150        160        170        180 
AQISRLMTLL RENFHFNTDA EISIEVDPRE IELDVLDHLR AEGFNRLSMG VQDFNKEVQR 

       190        200        210        220        230        240 
LVNREQDEEF IFALLNHARD IGFTSTNIDL IYGLPKQTPE SFAFTLKRVT ELNPDRLSVF 

       250        260        270        280        290        300 
NYAHLPTLFA AQRKIKDADL PSAQQKLDIL QETIVSLTQA GYQFIGMDHF ARPDDELAVA 

       310        320        330        340        350        360 
QREGVLHRNF QGYTTQGDTD LLGMGVSAIS MIGDGYMQNQ KELKRYYQQV DERGNALWRG 

       370        380        390        400        410        420 
ITLTRDDCIR RDVIKALICN FRLDFNAVEQ QWGLHFAEYF AEDLQLLSPL AKDGLVDISE 

       430        440        450 
KGIQVTAKGR LLIRNICMCF DAYLRQKARM QQFSRVI
P0A1E2 in FASTA format

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