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Reviewed, UniProtKB/Swiss-Prot Q9I0H4 (HMP_PSEAE)

Last modified June 16, 2009. Version 49. 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: PA2664
OrganismPseudomonas aeruginosa [Complete proteome] [HAMAP]
Taxonomic identifier287 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

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Protein attributes

Sequence length393 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 – 393393Flavohemoprotein HAMAP MF_01252
PRO_0000052439

Regions

Domain153 – 256104FAD-binding FR-type
Nucleotide binding205 – 2084FAD By similarity
Nucleotide binding268 – 2736NADP By similarity
Nucleotide binding384 – 3874FAD By similarity
Region1 – 139139Globin HAMAP MF_01252
Region150 – 393244Reductase HAMAP MF_01252
Region260 – 393134NAD or NADP-binding HAMAP MF_01252

Sites

Active site951Charge relay system By similarity
Active site1381Charge relay system By similarity
Metal binding851Iron (heme proximal ligand) By similarity
Binding site1911FAD 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
Site3831Influences the redox potential of the prosthetic heme and FAD groups By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q9I0H4-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 6384A119B51AD82B

FASTA39343,658
        10         20         30         40         50         60 
MLSNAQRALI KATVPLLETG GEALITHFYR TMLGEYPEVR PLFNQAHQAS GDQPRALANG 

        70         80         90        100        110        120 
VLMYARHIDQ LQELGPLVAK VVNKHVSLQV LPEHYPIVGT CLLRAIREVL GEQIATDEVL 

       130        140        150        160        170        180 
EAWGAAYQQL ADLLIEAEES VYAASAQADG GWRGVRRFRV ARKQAESEEI TSFYLEPVDG 

       190        200        210        220        230        240 
QPLLAFQPGQ YIGLRLDIDG EEVRRNYSLS AASNGREYRI SVKREAGGRV SNYLHDRVAE 

       250        260        270        280        290        300 
GDELDLFPPA GDFVLRDSDK PLVLITAGVG ITPALAMLQE ALPQARPIRF IHCARHGGVH 

       310        320        330        340        350        360 
AFRDWIEDVS AQHEQVEHFF CYSEPRAGDS ADAEGLLSRE KLADWLPQER DLDAYFLGPR 

       370        380        390 
PFMAQVKRHL ADLGVPSQQC HYEFFGPAAA LDA

« Hide

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Cross-references

Sequence databases

AE004091 Genomic DNA. Translation: AAG06052.1.
PIRF83311.
RefSeqNP_251354.1.

3D structure databases

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

Genome annotation databases

GeneID882373.
GenomeReviewsGene locus PA2664 in contig AE004091_GR.
KEGGpae:PA2664.

Organism-specific databases

PseudoCAPPA2664.
CMRSearch...

Phylogenomic databases

HOGENOMQ9I0H4.
OMAQ9I0H4. KHRSLGI.

Enzyme and pathway databases

BioCycPAER208964:PA2664-MON.
BRENDA1.14.12.17. 354.

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_PSEAE
AccessionPrimary (citable) accession number: Q9I0H4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: March 1, 2001
Last modified: June 16, 2009
This is version 49 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