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P40609 (HMP_VIBPA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 90. 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
Nitric oxide dioxygenase
Short name=NO oxygenase
Short name=NOD
EC=1.14.12.17
Gene names
Name:hmp
Ordered Locus Names:VP2809
OrganismVibrio parahaemolyticus [Complete proteome] [HAMAP]
Taxonomic identifier670 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

Protein attributes

Sequence length394 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

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 – 394394Flavohemoprotein HAMAP MF_01252
PRO_0000052450

Regions

Domain150 – 255106FAD-binding FR-type
Nucleotide binding204 – 2074FAD By similarity
Nucleotide binding268 – 2736NADP By similarity
Nucleotide binding387 – 3904FAD By similarity
Region1 – 136136Globin HAMAP MF_01252
Region147 – 394248Reductase HAMAP MF_01252
Region259 – 394136NAD 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
Site3861Influences the redox potential of the prosthetic heme and FAD groups By similarity

Experimental info

Sequence conflict1181D → G in AAA62190. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P40609 [UniParc].

Last modified April 4, 2003. Version 2.
Checksum: 2B65A6A71C8AB7AE

FASTA39444,410
        10         20         30         40         50         60 
MLSNQTIEIV KATAPLIAET GPKLTAHFYD RMFTHNPELK DIFNMSNQRN GDQREALFNA 

        70         80         90        100        110        120 
ICAYAANIEN LPALLGAVEK IAHKHTSFLI TKDQYQIVGK HLIATIDELF NPGQEVLDAW 

       130        140        150        160        170        180 
AEAYGVLANV FIQREEQIYQ ANASQEGGWR GLREFELVGK QLESEHICSF VFKPTDGSKV 

       190        200        210        220        230        240 
TKYKPGQYLG IYINSDKFEN QEIRQYSLSS SVQENTYRIS VKREQGGKVS NYLHDELNIG 

       250        260        270        280        290        300 
DKVKLAAPAG DFFMDVDTNT PVVLISAGVG LTPTLSMLES LTEHHAPVTW VHATENSKHH 

       310        320        330        340        350        360 
AFKEHVNQLV TAKENMNALI WYNQPTAEDK IGEDFHFTGF VNLHEIEAAL KQDNVQVYFC 

       370        380        390 
GPVGFMQHVA KQLQELGVPQ EQFHYECFGP HKVV

« Hide

References

« Hide 'large scale' references
[1]McCarter L.L.
Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BB22.
[2]"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
Lancet 361:743-749(2003) [PubMed: 12620739] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RIMD 2210633 / Serotype O3:K6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U09005 Genomic DNA. Translation: AAA62190.1.
BA000031 Genomic DNA. Translation: BAC61072.1.
RefSeqNP_799188.1. NC_004603.1.

3D structure databases

ProteinModelPortalP40609.
SMRP40609. Positions 1-394.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1190359.
GenomeReviewsGene locus VP2809 in contig BA000031_GR.
KEGGvpa:VP2809.
NMPDRfig|223926.1.peg.2809.
PATRIC20143818. VBIVibPar50997_2701.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG623097.
OMATWLHACE.
ProtClustDBPRK13289.

Enzyme and pathway databases

BioCycVPAR223926:VP2809-MONOMER.

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_VIBPA
AccessionPrimary (citable) accession number: P40609
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: April 4, 2003
Last modified: January 25, 2012
This is version 90 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

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