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UniProtKB/Swiss-Prot entry Q9PH91


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

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Entry information
Entry name HMP_XYLFA
Primary accession number Q9PH91
Secondary accession numbers None
Integrated into Swiss-Prot on September 13, 2004
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 45)
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: XF_0053
From
Xylella fastidiosa [TaxID: 2371] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Xylella.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=9a5c;
DOI=10.1038/35018003; PubMed=10910347 [NCBI, ExPASy, EBI, Israel, Japan]
Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M., Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S., Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S., Bueno M.R.P., Camargo A.A., Camargo L.E.A., Carraro D.M., Carrer H., Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M., Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H., Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S., Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H., Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D., Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E., Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F., Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N., Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F., Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y., Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O., Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A., de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R., Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B., Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G., Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M., da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z., Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D., Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S., Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.;
"The genome sequence of the plant pathogen Xylella fastidiosa.";
Nature 406:151-159(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
AE003849; AAF82866.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A82854; A82854.
RefSeq NP_297346.1; -.
3D structure databases
HSSP P04252; 1VHB. [HSSP ENTRY / PDB]
ModBase Q9PH91.
Enzyme and pathway databases
BioCyc XFAS160492:XF0053-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 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).
ProtoNet Q9PH91.
Genome annotation databases
GeneID 1125564; -.
GenomeReviews AE003849_GR; XF_0053.
KEGG xfa:XF0053; -.
NMPDR fig|160492.1.peg.53; -.
Phylogenomic databases
HOGENOM Q9PH91; -.
Genome annotation databases
CMR Q9PH91; XF_0053.
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   397  397     Flavohemoprotein. PRO_0000052453
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: 44144 Da [This is the MW of the unprocessed precursor] CRC64: C892E08EA8A5EC6B [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 ERIAQKHVGY AIHPEHYPHV ATALLGAIKK 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 MEQIAEAHPD AQVWYVHGTQ 

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

       370        380        390 
GPRPFLRTFV RDLIGAGVPA VQVHYEFFGP MDEEMAA 

Q9PH91 in FASTA format

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