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UniProtKB/Swiss-Prot entry P49852


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

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Entry information
Entry name HMP_BACSU
Primary accession number P49852
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 70)
Name and origin of the protein
Protein name Flavohemoprotein
Synonyms Hemoglobin-like protein
Flavohemoglobin
Nitric oxide dioxygenase
NO oxygenase
NOD
EC 1.14.12.17
Gene name
Name: hmp
Synonyms: ane3, ykiA
OrderedLocusNames: BSU13040
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], AND TRANSCRIPTIONAL REGULATION.
STRAIN=168;
PubMed=8682784 [NCBI, ExPASy, EBI, Israel, Japan]
Lacelle M., Kumano M., Kurita K., Yamane K., Zuber P., Nakano M.M.;
"Oxygen-controlled regulation of the flavohemoglobin gene in Bacillus subtilis.";
J. Bacteriol. 178:3803-3808(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
Devine K.M.;
"Sequence of the Bacillus subtilis genome between xlyA and ykoR.";
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
[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]
TRANSCRIPTIONAL REGULATION.
DOI=10.1128/JB.184.6.1783-1787.2002; PubMed=11872732 [NCBI, ExPASy, EBI, Israel, Japan]
Nakano M.M.;
"Induction of ResDE-dependent gene expression in Bacillus subtilis in response to nitric oxide and nitrosative stress.";
J. Bacteriol. 184:1783-1787(2002).
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
D78189; BAA11258.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ002571; CAA05584.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99110; CAB13161.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B69642; B69642.
RefSeq NP_389187.1; -.
3D structure databases
HSSP P04252; 1VHB. [HSSP ENTRY / PDB]
ModBase P49852.
Enzyme and pathway databases
BioCyc BSUB224308:BSU1306-MON; -.
Organism-specific databases
SubtiList BG11418; hmp. [Micado]
Ontologies
GO
GO:0008941; Molecular function: nitric oxide dioxygenase activity (inferred from electronic annotation from HAMAP).
GO:0005344; Molecular function: oxygen transporter activity (inferred from electronic annotation from HAMAP).
GO:0015671; Biological process: oxygen transport (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01252; -; 1.
PBIL [Tree]
InterPro IPR001709; FPN_cyt_redctse.
IPR012292; Globin.
IPR013316; Globin_annelid-type.
IPR000971; Globin_subset.
IPR008333; OxRdtase_FAD-bd.
IPR001433; OxRdtase_FAD/NAD_bd.
IPR001221; Phe_hydroxylase.
Graphical view of domain structure.
Gene3D G3DSA:1.10.490.10; Globin_related; 1.
Pfam PF00970; FAD_binding_6; 1.
PF00042; Globin; 1.
PF00175; NAD_binding_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00371; FPNCR.
PR00410; PHEHYDRXLASE.
PR01907; WORMGLOBIN.
PROSITE PS51384; FAD_FR; 1.
PS01033; GLOBIN; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P49852.
Genome annotation databases
GeneID 939891; -.
GenomeReviews AL009126_GR; BSU13040.
KEGG bsu:BSU13040; -.
NMPDR fig|224308.1.peg.1306; -.
Phylogenomic databases
HOGENOM P49852; -.
Genome annotation databases
CMR P49852; BSU13040.
Other
ProtoNet P49852.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Detoxification; FAD; Flavoprotein; Heme; Iron; Metal-binding; NAD; NADP; Oxidoreductase; Oxygen transport; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   399  399     Flavohemoprotein. PRO_0000052424
DOMAIN   152   255  104     FAD-binding FR-type. 
NP_BIND   206   209  4     FAD (By similarity). 
NP_BIND   268   273  6     NADP (By similarity). 
NP_BIND   388   391  4     FAD (By similarity). 
REGION   1   140  140     Globin. 
REGION   149   399  251     Reductase. 
REGION   259   399  141     NAD or NADP-binding. 
ACT_SITE   95    95        Charge relay system (By similarity). 
ACT_SITE   137   137        Charge relay system (By similarity). 
METAL   85    85        Iron (heme proximal ligand) (By similarity). 
BINDING   190   190        FAD (By similarity). 
SITE   29    29  1     Involved in heme-bound ligand stabilization and O-O bond activation (By similarity). 
SITE   84    84  1     Influences the redox potential of the prosthetic heme and FAD groups (By similarity). 
SITE   387   387  1     Influences the redox potential of the prosthetic heme and FAD groups (By similarity). 
Sequence information
Length: 399 AA [This is the length of the unprocessed precursor] Molecular weight: 44729 Da [This is the MW of the unprocessed precursor] CRC64: FFD3DD6C973301CF [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLDNKTIEII KSTVPVLQQH GETITGRFYD RMFQDHPELL NIFNQTNQKK KTQRTALANA 

        70         80         90        100        110        120 
VIAAAANIDQ LGNIIPVVKQ IGHKHRSIGI KPEHYPIVGK YLLIAIKDVL GDAATPDIMQ 

       130        140        150        160        170        180 
AWEKAYGVIA DAFIGIEKDM YEQAEEQAGG WKEYKPFVIA KKERESKEIT SFYLKPEDSK 

       190        200        210        220        230        240 
PLPEFQAGQY ISIKVRIPDS EYTHIRQYSL SDMPGKDYYR ISVKKDGVVS SYLHDGLQEG 

       250        260        270        280        290        300 
DSIEISAPAG DFVLDHASQK DLVLISAGVG ITPMISMLKT SVSKQPERQI LFIHAAKNSE 

       310        320        330        340        350        360 
YHALRHEVEE AAKHSAVKTA FVYREPTEED RAGDLHFHEG QIDQQFLKEL IANTDADYYI 

       370        380        390 
CGSPSFITAM HKLVSELGSA PESIHYELFG PQLSLAQSV 

P49852 in FASTA format

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View entry in raw text format (no links)
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