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UniProtKB/Swiss-Prot entry Q9RC40


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

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Entry information
Entry name HMP_BACHD
Primary accession number Q9RC40
Secondary accession numbers None
Integrated into Swiss-Prot on September 13, 2004
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 51)
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
OrderedLocusNames: BH1058
From
Bacillus halodurans [TaxID: 86665] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC BAA-125 / C-125 / DSM 18197 / FERM 7344 / JCM 9153;
DOI=10.1007/s007920050120; PubMed=10484179 [NCBI, ExPASy, EBI, Israel, Japan]
Takami H., Takaki Y., Nakasone K., Sakiyama T., Maeno G., Sasaki R., Hirama C., Fuji F., Masui N.;
"Genetic analysis of the chromosome of alkaliphilic Bacillus halodurans C-125.";
Extremophiles 3:227-233(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-125 / C-125 / DSM 18197 / FERM 7344 / JCM 9153;
DOI=10.1093/nar/28.21.4317; PubMed=11058132 [NCBI, ExPASy, EBI, Israel, Japan]
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis.";
Nucleic Acids Res. 28:4317-4331(2000).
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
AB024563; BAA83959.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000004; BAB04777.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B83782; B83782.
RefSeq NP_241924.1; -.
3D structure databases
HSSP P04252; 1VHB. [HSSP ENTRY / PDB]
ModBase Q9RC40.
Enzyme and pathway databases
BioCyc BHAL272558:BH1058-MON; -.
Ontologies
GO
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037; Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0008941; Molecular function: nitric oxide dioxygenase activity (inferred from electronic annotation from HAMAP).
GO:0019825; Molecular function: oxygen binding (inferred from electronic annotation from InterPro).
GO:0005344; Molecular function: oxygen transporter activity (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0015671; Biological process: oxygen transport (inferred from electronic annotation from HAMAP).
GO:0009636; Biological process: response to toxin (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_01252; -; 1.
PBIL [Tree]
InterPro IPR001834; Cyt_B5_reductase.
IPR001709; FPN_cyt_redctse.
IPR012292; Globin.
IPR000971; Globin_subset.
IPR008333; OxRdtase_FAD-bd.
IPR001433; OxRdtase_FAD/NAD_bd.
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 PR00406; CYTB5RDTASE.
PR00371; FPNCR.
PROSITE PS51384; FAD_FR; 1.
PS01033; GLOBIN; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q9RC40.
Genome annotation databases
GeneID 894032; -.
GenomeReviews BA000004_GR; BH1058.
KEGG bha:BH1058; -.
NMPDR fig|272558.1.peg.1058; -.
Phylogenomic databases
HOGENOM Q9RC40; -.
Genome annotation databases
CMR Q9RC40; BH1058.
Other
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   411  411     Flavohemoprotein. PRO_0000052422
DOMAIN   156   267  112     FAD-binding FR-type. 
NP_BIND   210   213  4     FAD (By similarity). 
NP_BIND   280   285  6     NADP (By similarity). 
NP_BIND   401   404  4     FAD (By similarity). 
REGION   3   142  140     Globin. 
REGION   153   411  259     Reductase. 
REGION   271   411  141     NAD or NADP-binding. 
ACT_SITE   99    99        Charge relay system (By similarity). 
ACT_SITE   141   141        Charge relay system (By similarity). 
METAL   89    89        Iron (heme proximal ligand) (By similarity). 
BINDING   194   194        FAD (By similarity). 
SITE   33    33  1     Involved in heme-bound ligand stabilization and O-O bond activation (By similarity). 
SITE   88    88  1     Influences the redox potential of the prosthetic heme and FAD groups (By similarity). 
SITE   400   400  1     Influences the redox potential of the prosthetic heme and FAD groups (By similarity). 
Sequence information
Length: 411 AA [This is the length of the unprocessed precursor] Molecular weight: 46565 Da [This is the MW of the unprocessed precursor] CRC64: 779B2F4AB64EA5DE [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSTATLSQET KQIVKATVPI LAEHGEAITK HFYKRMFSHH PELLNIFNQT HQKQGRQPQA 

        70         80         90        100        110        120 
LANSIYAAAE HIDNLEAILP VVSRIAHKHR SLNIKPEQYP IVGENLLAAM REVLGDAASD 

       130        140        150        160        170        180 
DVLEAWREAY ELIADVFIQV EKKMYEEASQ APGGWREFRS FVVEKKQRES ATITSFYLKP 

       190        200        210        220        230        240 
EDGKALASYK PGQYITVKVT IPGHEHTHMR QYSLSDAPEK GYYRITVKRE EGDGDLPPGI 

       250        260        270        280        290        300 
VSNYLHQHIH EGDVLEITAP AGDFTLQEEG ERPIVFISGG VGITPLMSMF NTLMQRGVKR 

       310        320        330        340        350        360 
EVIFIHAAIN GFYHAMHDHL AQTASQQENV HYAVCYERPT PGDRMNPFMK KEGFIDESFL 

       370        380        390        400        410 
RSILHDREAD FYFCGPVPFM KTIAQILKDW DVPEQQVHYE FFGPAGTLAS S 

Q9RC40 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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