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UniProtKB/Swiss-Prot entry Q796V8


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

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Entry information
Entry name HEMZ_BACSU
Primary accession number Q796V8
Secondary accession numbers O07537 O07538
Integrated into Swiss-Prot on February 1, 2005
Sequence was last modified on July 5, 2004 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 30)
Name and origin of the protein
Protein name Oxygen-independent coproporphyrinogen III oxidase 2
Synonyms Coproporphyrinogenase
Coprogen oxidase
EC 1.3.99.22
Gene name
Name: hemZ
Synonyms: yhaV, yhaW
OrderedLocusNames: BSU09840
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9579061 [NCBI, ExPASy, EBI, Israel, Japan]
Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H., Venema G., Bron S.;
"The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus subtilis chromosome contains several dysfunctional genes, the glyB marker, many genes encoding transporter proteins, and the ubiquitous hit gene.";
Microbiology 144:859-875(1998).
[2]
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).
[3]
SEQUENCE REVISION.
DOI=10.1101/gr.9.11.1116; PubMed=10568751 [NCBI, ExPASy, EBI, Israel, Japan]
Medigue C., Rose M., Viari A., Danchin A.;
"Detecting and analyzing DNA sequencing errors: toward a higher quality of the Bacillus subtilis genome sequence.";
Genome Res. 9:1116-1127(1999).
[4]
CHARACTERIZATION, AND 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
Y14080; CAA74454.1; ALT_FRAME; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y14080; CAA74441.1; ALT_FRAME; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99109; CAB12823.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A69820; A69820.
H69819; H69819.
RefSeq NP_388865.1; -.
3D structure databases
ModBase Q796V8.
Enzyme and pathway databases
BioCyc BSUB224308:YHAW-MON; -.
Organism-specific databases
SubtiList BG12999; hemZ. [Micado]
Family and domain databases
InterPro IPR006638; Elp3/MiaB/NifB.
IPR007197; Radical_SAM.
Graphical view of domain structure.
Pfam PF04055; Radical_SAM; 1.
Pfam graphical view of domain structure.
SMART SM00729; Elp3; 1.
SMART graphical view of domain structure.
BLOCKS Q796V8.
Genome annotation databases
GeneID 937935; -.
GenomeReviews AL009126_GR; BSU09840.
KEGG bsu:BSU09840; -.
NMPDR fig|224308.1.peg.984; -.
Phylogenomic databases
HOGENOM Q796V8; -.
Genome annotation databases
CMR Q796V8; BSU09840.
Other
ProtoNet Q796V8.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
4Fe-4S; Complete proteome; 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   501  501     Oxygen-independent coproporphyrinogen III oxidase 2. PRO_0000109955
REGION   234   235  2     S-adenosyl-L-methionine 2 binding (By similarity). 
METAL   180   180        Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity). 
METAL   184   184        Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity). 
METAL   187   187        Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity). 
BINDING   174   174        S-adenosyl-L-methionine 1 (By similarity). 
BINDING   186   186        S-adenosyl-L-methionine 2; via carbonyl oxygen (By similarity). 
BINDING   233   233        S-adenosyl-L-methionine 1; via amide nitrogen and carbonyl oxygen (By similarity). 
BINDING   267   267        S-adenosyl-L-methionine 1 (By similarity). 
BINDING   295   295        S-adenosyl-L-methionine 2 (By similarity). 
BINDING   307   307        S-adenosyl-L-methionine 2 (By similarity). 
BINDING   332   332        S-adenosyl-L-methionine 2 (By similarity). 
Sequence information
Length: 501 AA [This is the length of the unprocessed precursor] Molecular weight: 57527 Da [This is the MW of the unprocessed precursor] CRC64: 8E4C2373D1D9190D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MQIKIEGIHD DRLHRPLQNI ANLFYEECEL AYGGEEPADF VISLALSQTD EHVTVSGEVK 

        70         80         90        100        110        120 
GTGIKEQHTK FFSPDMTEKE AFKQVKNTIS YVYLNLLQAH TGITQKWGIL TGIRPTKLLH 

       130        140        150        160        170        180 
KKLQSGMSKE QAHAELKKDY LIHDEKIMLM QEIVDRQLAA VPDLYRVKDE VSIYIGIPFC 

       190        200        210        220        230        240 
PTKCAYCTFP AYAIQGQAGR VGSFLWGLHY EMQKIGEWLK EHDVKVTTIY FGGGTPTSIT 

       250        260        270        280        290        300 
AEEMDLLYEE MVRSFPDVKN IREITVEAGR PDTITEEKLA VLNKYDIDRI SINPQSYENE 

       310        320        330        340        350        360 
TLKAIGRHHT VEETIEKYHL SRQHGMNNIN MDLIIGLPGE GVKEFRHSLS ETEKLMPESL 

       370        380        390        400        410        420 
TVHTLSFKRA SEMTRNKHKY KVAGREEVSQ MMEDAVAWTK EHGYVPYYLY RQKNILGNLE 

       430        440        450        460        470        480 
NVGYSLPGQE SIYNIMIMEE VQTIIGIGCG AASKFIDRDT GKITHFANPK DPKSYNERFE 

       490        500 
HYTDEKIKYL EQIFEKTTKQ H 

Q796V8 in FASTA format

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