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Reviewed, UniProtKB/Swiss-Prot Q7WHW5 (HMP_BORBR)

Last modified November 3, 2009. Version 39. 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

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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
Synonyms: fhp
Ordered Locus Names: BB3091
OrganismBordetella bronchiseptica (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP]
Taxonomic identifier518 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

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Protein attributes

Sequence length402 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 402402Flavohemoprotein HAMAP MF_01252
PRO_0000052425

Regions

Domain152 – 261110FAD-binding FR-type
Nucleotide binding206 – 2094FAD By similarity
Nucleotide binding274 – 2796NADP By similarity
Nucleotide binding395 – 3984FAD By similarity
Region1 – 138138Globin HAMAP MF_01252
Region149 – 402254Reductase HAMAP MF_01252
Region265 – 402138NAD or NADP-binding HAMAP MF_01252

Sites

Active site951Charge relay system By similarity
Active site1371Charge relay system By similarity
Metal binding851Iron (heme proximal ligand) By similarity
Binding site1901FAD By similarity
Site291Involved in heme-bound ligand stabilization and O-O bond activation By similarity
Site841Influences the redox potential of the prosthetic heme and FAD groups By similarity
Site3941Influences the redox potential of the prosthetic heme and FAD groups By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q7WHW5-1 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 0231E77F0A3C71E6

FASTA40243,723
        10         20         30         40         50         60 
MLSPEVRALV KATAPVLKEH GEALTRHFYT RMLGGNPELR QLFNQGHQQS GQQQQALAAA 

        70         80         90        100        110        120 
VAAYAEHIDD PSVLLPVVER IAHKHVSLGV RAEHYAIVGK HLLASIREVL GEAATDELID 

       130        140        150        160        170        180 
AWAAAYGQLA DLLIGRERAL YAAAASRDGG WTGWRAFKVV RKTPESAEIT SFYLAPADGG 

       190        200        210        220        230        240 
ATPDYLPGQY VSVRVYVPEL GLMQPRQYSL SEAPGMPGQL RISVKREAGS PAGMVSGTLH 

       250        260        270        280        290        300 
NRINEGDVLD VSPPQGDFTL DAEDGRPVVL LSGGVGLTPM VSMLNHLTAR DDGRQIRFVH 

       310        320        330        340        350        360 
ACREAGVHAM KEHINALAAK RPNVRKAVFY ERVGADDRRG VDYDYEGRVD LHAIRDEVIL 

       370        380        390        400 
PDADYYLCGP LPFMQAQRRA LADLGVAEHR IHAEVFGTGG VA

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Cross-references

Sequence databases

BX640446 Genomic DNA. Translation: CAE33583.1.
RefSeqNP_889627.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2663316.
GenomeReviewsGene locus BB3091 in contig BX470250_GR.
KEGGbbr:BB3091.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ7WHW5.
OMAKHRSLGI.

Enzyme and pathway databases

BioCycBBRO257310:BB3091-MON.
BRENDA1.14.12.17. 413.

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.
IPR001221. Phe_hydroxylase.
[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]
PRINTSPR00410. PHEHYDRXLASE.
PROSITEPS51384. FAD_FR. 1 hit.
PS01033. GLOBIN. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameHMP_BORBR
AccessionPrimary (citable) accession number: Q7WHW5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: October 1, 2003
Last modified: November 3, 2009
This is version 39 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)

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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