Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q9PH91 (HMP_XYLFA)

Last modified June 16, 2009. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Flavohemoprotein
Alternative name(s):
    Hemoglobin-like protein
    Flavohemoglobin
    Nitric oxide dioxygenase
      Short name=NO oxygenase
      Short name=NOD
    EC=1.14.12.17
Gene names
Name: hmp
Ordered Locus Names: XF_0053
OrganismXylella fastidiosa [Complete proteome] [HAMAP]
Taxonomic identifier2371 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xylella

Hide | Top

Protein attributes

Sequence length397 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

Hide | Top

General annotation (Comments)

Function

Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O2 and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress By similarity.

Catalytic activity

2 NO + 2 O2 + NAD(P)H = 2 NO3- + NAD(P)+. HAMAP MF_01252

Cofactor

Binds 1 heme B (iron-protoporphyrin IX) group per subunit By similarity.

Binds 1 FAD per subunit By similarity.

Domain

Consists of two distinct domains; an N-terminal heme-containing oxygen-binding domain and a C-terminal reductase domain with binding sites for FAD and NAD(P)H. HAMAP MF_01252

Sequence similarities

Belongs to the globin family. Two-domain flavohemoproteins subfamily.

In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.

Contains 1 FAD-binding FR-type domain.

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 397397Flavohemoprotein HAMAP MF_01252
PRO_0000052453

Regions

Domain154 – 258105FAD-binding FR-type
Nucleotide binding207 – 2104FAD By similarity
Nucleotide binding271 – 2766NADP By similarity
Nucleotide binding387 – 3904FAD By similarity
Region1 – 140140Globin HAMAP MF_01252
Region151 – 397247Reductase HAMAP MF_01252
Region261 – 397137NAD or NADP-binding HAMAP MF_01252

Sites

Active site971Charge relay system By similarity
Active site1391Charge relay system By similarity
Metal binding871Iron (heme proximal ligand) By similarity
Binding site1921FAD By similarity
Site321Involved in heme-bound ligand stabilization and O-O bond activation By similarity
Site861Influences the redox potential of the prosthetic heme and FAD groups By similarity
Site3861Influences the redox potential of the prosthetic heme and FAD groups By similarity

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q9PH91-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: C892E08EA8A5EC6B

FASTA39744,144
        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

« Hide

Hide | Top

References

[1]"The genome sequence of the plant pathogen Xylella fastidiosa."
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. expand/collapse author list , 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.
Nature 406:151-159(2000) [PubMed: 10910347] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 9a5c.

Hide | Top

Cross-references

Sequence databases

AE003849 Genomic DNA. Translation: AAF82866.1.
PIRA82854.
RefSeqNP_297346.1.

3D structure databases

HSSPHSSP built from PDB template 1VHB based on UniProtKB P04252.
ModBaseSearch...

Genome annotation databases

GeneID1125564.
GenomeReviewsGene locus XF_0053 in contig AE003849_GR.
KEGGxfa:XF0053.
NMPDRfig|160492.1.peg.53.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ9PH91.
OMAQ9PH91. KHRSLGI.

Enzyme and pathway databases

BioCycXFAS160492:XF0053-MON.
BRENDA1.14.12.17. 278708.

Family and domain databases

HAMAPMF_01252.
[Tree]
InterProIPR017927. Fd_Rdtase_FAD-bd.
IPR012292. Globin.
IPR000971. Globin_subset.
IPR008333. OxRdtase_FAD-bd.
IPR001433. OxRdtase_FAD/NAD_bd.
IPR000951. Ph_dOase_redase_FPNCR.
[Graphical view]
Gene3DG3DSA:1.10.490.10. Globin_related. 1 hit.
PfamPF00970. FAD_binding_6. 1 hit.
PF00042. Globin. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSPR00409. PHDIOXRDTASE.
PROSITEPS51384. FAD_FR. 1 hit.
PS01033. GLOBIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameHMP_XYLFA
AccessionPrimary (citable) accession number: Q9PH91
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: October 1, 2000
Last modified: June 16, 2009
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents