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UniProtKB/Swiss-Prot entry Q87F90


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

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Entry information
Entry name HMP_XYLFT
Primary accession number Q87F90
Secondary accession numbers None
Integrated into Swiss-Prot on September 13, 2004
Sequence was last modified on June 1, 2003 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 36)
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: hmpA
OrderedLocusNames: PD_0038
From
Xylella fastidiosa (strain Temecula1 / ATCC 700964) [TaxID: 183190] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Xylella.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.185.3.1018-1026.2003; PubMed=12533478 [NCBI, ExPASy, EBI, Israel, Japan]
Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y., Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A., Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S., Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H., Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L., Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L., Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S., Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F., Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G., Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A., Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L., Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
"Comparative analyses of the complete genome sequences of Pierce's disease and citrus variegated chlorosis strains of Xylella fastidiosa.";
J. Bacteriol. 185:1018-1026(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
AE009442; AAO27945.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_778296.1; -.
3D structure databases
HSSP P04252; 2VHB. [HSSP ENTRY / PDB]
ModBase Q87F90.
Enzyme and pathway databases
BioCyc XFAS183190:PD_0038-MON; -.
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 IPR012292; Globin.
IPR000971; Globin_subset.
IPR008333; OxRdtase_FAD-bd.
IPR001433; OxRdtase_FAD/NAD_bd.
IPR000951; Ph_dOase_redase_FPNCR.
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 PR00409; PHDIOXRDTASE.
PROSITE PS51384; FAD_FR; 1.
PS01033; GLOBIN; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q87F90.
Genome annotation databases
GeneID 1144238; -.
GenomeReviews AE009442_GR; PD_0038.
KEGG xft:PD0038; -.
Phylogenomic databases
HOGENOM Q87F90; -.
Genome annotation databases
CMR Q87F90; PD_0038.
Other
ProtoNet Q87F90.
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   397  397     Flavohemoprotein. PRO_0000052454
DOMAIN   154   258  105     FAD-binding FR-type. 
NP_BIND   207   210  4     FAD (By similarity). 
NP_BIND   271   276  6     NADP (By similarity). 
NP_BIND   387   390  4     FAD (By similarity). 
REGION   1   140  140     Globin. 
REGION   151   397  247     Reductase. 
REGION   261   397  137     NAD or NADP-binding. 
ACT_SITE   97    97        Charge relay system (By similarity). 
ACT_SITE   139   139        Charge relay system (By similarity). 
METAL   87    87        Iron (heme proximal ligand) (By similarity). 
BINDING   192   192        FAD (By similarity). 
SITE   32    32  1     Involved in heme-bound ligand stabilization and O-O bond activation (By similarity). 
SITE   86    86  1     Influences the redox potential of the prosthetic heme and FAD groups (By similarity). 
SITE   386   386  1     Influences the redox potential of the prosthetic heme and FAD groups (By similarity). 
Sequence information
Length: 397 AA [This is the length of the unprocessed precursor] Molecular weight: 44089 Da [This is the MW of the unprocessed precursor] CRC64: 7C68FF4A44AC8EEC [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSASFSPHTI TLIKSTVPLL AEHGTTIIEA MYHRLFEDPQ IEALFNQANQ KNGTQIHALA 

        70         80         90        100        110        120 
GAILAYARNI DNPGVLASAI ERISQKHVGY AIHPEHYPHV ATALLGAIKQ VLGDVATSEV 

       130        140        150        160        170        180 
LEAWGEAYWF IANLLKDREA VIREGIMTKN GGWIHWRRFV ISKRIPESET ITSFMLHPED 

       190        200        210        220        230        240 
GGPVVPHQAG QYLTFRFDAA GMPGMKRNYS ISCGPNSDHY RITVKREHGT GASAFLHDQA 

       250        260        270        280        290        300 
KVGTIIECTP PVGDFFLPSV IERPIVLLSG GVGLTPMVSM MEQIAEAYPD AQVWYVHGTQ 

       310        320        330        340        350        360 
NRETHAMDAH IRALVSRHKH MKATTFYTQR SEADDAEAGF ITIDWLRANT PFQKADFYLC 

       370        380        390 
GPRPFLRTFV RDLIGAGVPA AQVHYEFFGP MDEEMAA 

Q87F90 in FASTA format

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