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UniProtKB/Swiss-Prot entry P54304


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

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Entry information
Entry name HEMN_BACSU
Primary accession number P54304
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on August 4, 2003 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 65)
Name and origin of the protein
Protein name Oxygen-independent coproporphyrinogen III oxidase 1
Synonyms Coproporphyrinogenase
Coprogen oxidase
EC 1.3.99.22
Gene name
Name: hemN
Synonyms: yqeR
OrderedLocusNames: BSU25500
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=8757728 [NCBI, ExPASy, EBI, Israel, Japan]
Homuth G., Heinemann M., Zuber U., Schumann W.;
"The genes of lepA and hemN form a bicistronic operon in Bacillus subtilis.";
Microbiology 142:1641-1649(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168 / JH642;
PubMed=8969508 [NCBI, ExPASy, EBI, Israel, Japan]
Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y.;
"Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes.";
Microbiology 142:3103-3111(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 328-366.
STRAIN=168 / MB11;
PubMed=1339421 [NCBI, ExPASy, EBI, Israel, Japan]
Wetzstein M., Voelker U., Dedio J., Loebau S., Zuber U., Schiesswohl M., Herget C., Hecker M., Schumann W.;
"Cloning, sequencing, and molecular analysis of the dnaK locus from Bacillus subtilis.";
J. Bacteriol. 174:3300-3310(1992).
[5]
REGULATION.
PubMed=10498703 [NCBI, ExPASy, EBI, Israel, Japan]
Homuth G., Rompf A., Schumann W., Jahn D.;
"Transcriptional control of Bacillus subtilis hemN and hemZ.";
J. Bacteriol. 181:5922-5929(1999).
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
X91655; CAB61616.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D84432; BAA12461.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99117; CAB14492.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M84964; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
PIR B69640; B69640.
RefSeq NP_390428.1; -.
3D structure databases
ModBase P54304.
Enzyme and pathway databases
BioCyc BSUB224308:BSU2546-MON; -.
Organism-specific databases
SubtiList BG11395; hemN. [Micado]
Ontologies
GO
GO:0051989; Molecular function: coproporphyrinogen dehydrogenase activity (inferred from electronic annotation from EC).
QuickGo view.
Family and domain databases
InterPro IPR013785; Aldolase_TIM.
IPR006638; Elp3/MiaB/NifB.
IPR010723; HemN_C.
IPR004559; HemN_rel.
IPR007197; Radical_SAM.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 1.
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 TIGR00539; hemN_rel; 1.
BLOCKS P54304.
Genome annotation databases
GeneID 937845; -.
GenomeReviews AL009126_GR; BSU25500.
KEGG bsu:BSU25500; -.
NMPDR fig|224308.1.peg.2553; -.
Phylogenomic databases
HOGENOM P54304; -.
Genome annotation databases
CMR P54304; BSU25500.
Other
ProtoNet P54304.
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   366  366     Oxygen-independent coproporphyrinogen III oxidase 1. PRO_0000109939
REGION   61    62  2     S-adenosyl-L-methionine 2 binding (By similarity). 
METAL   11    11        Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity). 
METAL   15    15        Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity). 
METAL   18    18        Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity). 
BINDING   5     5        S-adenosyl-L-methionine 1 (By similarity). 
BINDING   17    17        S-adenosyl-L-methionine 2; via carbonyl oxygen (By similarity). 
BINDING   60    60        S-adenosyl-L-methionine 1; via amide nitrogen and carbonyl oxygen (By similarity). 
BINDING   94    94        S-adenosyl-L-methionine 1 (By similarity). 
BINDING   121   121        S-adenosyl-L-methionine 2 (By similarity). 
BINDING   133   133        S-adenosyl-L-methionine 2 (By similarity). 
BINDING   158   158        S-adenosyl-L-methionine 2 (By similarity). 
CONFLICT   94    94        D -> E (in Ref. 1; CAB61616). 
CONFLICT   175   175        I -> S (in Ref. 1; CAB61616). 
Sequence information
Length: 366 AA [This is the length of the unprocessed precursor] Molecular weight: 41562 Da [This is the MW of the unprocessed precursor] CRC64: 33F473B83A7CFA0E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKSAYIHIPF CEHICHYCDF NKYFIQSQPV DEYLNALEQE MINTIAKTGQ PDLKTIFIGG 

        70         80         90        100        110        120 
GTPTSLSEEQ LKKLMDMINR VLKPSSDLSE FAVDANPDDL SAEKLKILKE AGVNRLSFGV 

       130        140        150        160        170        180 
QTFEDDLLEK IGRVHKQKDV FTSFERAREI GFENISLDLM FGLPGQTLKH LEHSINTALS 

       190        200        210        220        230        240 
LDAEHYSVYS LIVEPKTVFY NLMQKGRLHL PPQEQEAEMY EIVMSKMEAH GIHQYEISNF 

       250        260        270        280        290        300 
AKAGMESKHN LTYWSNEQYF GFGAGAHGYI GGTRTVNVGP VKHYIDLIAE KGFPYRDTHE 

       310        320        330        340        350        360 
VTTEEQIEEE MFLGLRKTAG VSKKRFAEKY GRSLDGLFPS VLKDLAEKGL IHNSESAVYL 


THQGNY 

P54304 in FASTA format

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