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Q47266 (HMP_DICD3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Flavohemoprotein
Alternative name(s):
Flavohemoglobin
Hemoglobin-like protein
Hemoprotein X
Nitric oxide dioxygenase
Short name=NO oxygenase
Short name=NOD
EC=1.14.12.17
Gene names
Name:hmp
Synonyms:hmpX
Ordered Locus Names:Dda3937_03368
OrganismDickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)) [Complete proteome] [HAMAP]
Taxonomic identifier198628 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeDickeya

Protein attributes

Sequence length395 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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. HAMAP MF_01252

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. HAMAP MF_01252

Subcellular location

Cytoplasm HAMAP MF_01252.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 395395Flavohemoprotein HAMAP MF_01252
PRO_0000052434

Regions

Domain150 – 255106FAD-binding FR-type
Nucleotide binding204 – 2074FAD By similarity
Nucleotide binding268 – 2736NADP By similarity
Nucleotide binding388 – 3914FAD By similarity
Region1 – 138138Globin HAMAP MF_01252
Region147 – 395249Reductase HAMAP MF_01252
Region259 – 395137NAD or NADP-binding HAMAP MF_01252

Sites

Active site951Charge relay system By similarity
Active site1351Charge relay system By similarity
Metal binding851Iron (heme proximal ligand) By similarity
Binding site1881FAD 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
Site3871Influences the redox potential of the prosthetic heme and FAD groups By similarity

Experimental info

Sequence conflict1231A → R in CAA53500. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q47266 [UniParc].

Last modified November 30, 2010. Version 2.
Checksum: 025225B7587745E6

FASTA39544,230
        10         20         30         40         50         60 
MLDQQTIATI KSTIPLLAET GPALTAHFYQ RMFHHNPELK DIFNMSNQRN GDQREALFNA 

        70         80         90        100        110        120 
ICAYATHIEN LPALLPAVER IAQKHASFNI QPEQYQIVGT HLLATLEEMF QPGQAVLDAW 

       130        140        150        160        170        180 
GKAYGVLANV FIQRESDIYQ QSAGQNGGWH GIRPFRIVAK QPQSSLITSF TLEPVDGGPI 

       190        200        210        220        230        240 
AAFRPGQYLA VYIRDKRFEY QEIRQYSLTN EPNGRYYRIA VKRETMGSVS GYLHDVAREG 

       250        260        270        280        290        300 
DVIELAAPHG DFYLEVTPET PVALISAGVG QTPMLSMLHS LKNQQHQADI FWLHAAENTE 

       310        320        330        340        350        360 
VHAFADEIAD VAATLPQLQS YVWYREASSE AARSAHAFHG LMALKDLPTP LPMTNLHCYL 

       370        380        390 
CGPVAFMQFA ARQLLELGIT ESQIHYECFG PHKVI 

« Hide

References

« Hide 'large scale' references
[1]"Flavohaemoglobin HmpX: a new pathogenicity determinant in Erwinia chrysanthemi strain 3937."
Favey S., Labesse G., Vouille V., Boccara M.
Microbiology 141:863-871(1995) [PubMed: 7773389] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 3937.
[2]"Complete genome sequence of Dickeya dadantii 3937."
International Erwinia Consortium
Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 3937.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X75893 Genomic DNA. Translation: CAA53500.1.
CP002038 Genomic DNA. Translation: ADM99548.1.
PIRS44277.
RefSeqYP_003884105.1. NC_014500.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID9734799.
GenomeReviewsGene locus Dda3937_03368 in contig CP002038_GR.
KEGGddd:Dda3937_03368.
PATRIC42318985. VBIDicDad25310_3305.

Organism-specific databases

CMRSearch...

Family and domain databases

HAMAPMF_01252. Hmp.
[Tree]
InterProIPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR009050. Globin-like.
IPR012292. Globin_dom.
IPR000971. Globin_subset.
IPR023950. Hmp.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR001221. Phe_hydroxylase.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
Gene3DG3DSA:1.10.490.10. Globin_related. 1 hit.
KOK05916.
PfamPF00970. FAD_binding_6. 1 hit.
PF00042. Globin. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSPR00371. FPNCR.
PR00410. PHEHYDRXLASE.
SUPFAMSSF46458. Globin_like. 1 hit.
SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
PS01033. GLOBIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHMP_DICD3
AccessionPrimary (citable) accession number: Q47266
Secondary accession number(s): E0SAY9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 30, 2010
Last modified: January 25, 2012
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families