P40609 (HMP_VIBPA) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 90.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended 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 |
| ||||
| Organism | Vibrio parahaemolyticus [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 670 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio |
Protein attributes
| Sequence length | 394 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred 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. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Detoxification Oxygen transport Transport |
| Ligand | FAD Flavoprotein Heme Iron Metal-binding NAD NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | response to nitrosative stress Inferred from electronic annotation. Source: InterPro response to toxinInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | FAD binding Inferred from electronic annotation. Source: InterPro heme bindingInferred from electronic annotation. Source: InterPro nitric oxide dioxygenase activityInferred from electronic annotation. Source: EC oxygen bindingInferred from electronic annotation. Source: InterPro oxygen transporter activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 394 | 394 | Flavohemoprotein HAMAP MF_01252 | PRO_0000052450 | |||||
Regions | |||||||||
| Domain | 150 – 255 | 106 | FAD-binding FR-type | ||||||
| Nucleotide binding | 204 – 207 | 4 | FAD By similarity | ||||||
| Nucleotide binding | 268 – 273 | 6 | NADP By similarity | ||||||
| Nucleotide binding | 387 – 390 | 4 | FAD By similarity | ||||||
| Region | 1 – 136 | 136 | Globin HAMAP MF_01252 | ||||||
| Region | 147 – 394 | 248 | Reductase HAMAP MF_01252 | ||||||
| Region | 259 – 394 | 136 | NAD or NADP-binding HAMAP MF_01252 | ||||||
Sites | |||||||||
| Active site | 95 | 1 | Charge relay system By similarity | ||||||
| Active site | 135 | 1 | Charge relay system By similarity | ||||||
| Metal binding | 85 | 1 | Iron (heme proximal ligand) By similarity | ||||||
| Binding site | 188 | 1 | FAD By similarity | ||||||
| Site | 29 | 1 | Involved in heme-bound ligand stabilization and O-O bond activation By similarity | ||||||
| Site | 84 | 1 | Influences the redox potential of the prosthetic heme and FAD groups By similarity | ||||||
| Site | 386 | 1 | Influences the redox potential of the prosthetic heme and FAD groups By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 118 | 1 | D → G in AAA62190. Ref.1 | ||||||
Sequences
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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. |
| RefSeq | NP_799188.1. NC_004603.1. |
3D structure databases | |
| ProteinModelPortal | P40609. |
| SMR | P40609. Positions 1-394. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1190359. |
| GenomeReviews | Gene locus VP2809 in contig BA000031_GR. |
| KEGG | vpa:VP2809. |
| NMPDR | fig|223926.1.peg.2809. |
| PATRIC | 20143818. VBIVibPar50997_2701. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG623097. |
| OMA | TWLHACE. |
| ProtClustDB | PRK13289. |
Enzyme and pathway databases | |
| BioCyc | VPAR223926:VP2809-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01252. Hmp. [Tree] |
| InterPro | IPR017927. 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] |
| Gene3D | G3DSA:1.10.490.10. Globin_related. 1 hit. |
| KO | K05916. |
| Pfam | PF00970. FAD_binding_6. 1 hit. PF00042. Globin. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view] |
| PRINTS | PR00371. FPNCR. PR00410. PHEHYDRXLASE. |
| SUPFAM | SSF46458. Globin_like. 1 hit. SSF63380. Riboflavin_synthase_like_b-brl. 1 hit. |
| PROSITE | PS51384. FAD_FR. 1 hit. PS01033. GLOBIN. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HMP_VIBPA | ||||||||
| Accession | Primary (citable) accession number: P40609 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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