Flavohemoprotein - Vibrio parahaemolyticus

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Reviewed, UniProtKB/Swiss-Prot P40609 (HMP_VIBPA)

Last modified November 25, 2008. Version 69. History...

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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 names

Recommended 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
Ordered Locus Names:	VP2809

Organism

Vibrio parahaemolyticus [Complete proteome] [HAMAP]

Taxonomic identifier

670 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

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Protein attributes

Sequence length	394 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred 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 O(2) 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 O(2) + NAD(P)H = 2 NO(3)(-) + NAD(P)(+).
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.
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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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	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW oxygen transport Inferred from electronic annotation. Source: HAMAP response to toxin Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro nitric oxide dioxygenase activity Inferred from electronic annotation. Source: HAMAP oxygen binding Inferred from electronic annotation. Source: InterPro oxygen transporter activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 394

394

Flavohemoprotein

PRO_0000052450

Regions

Domain

150 – 255

106

FAD-binding FR-type

Nucleotide binding

204 – 207

FAD By similarity

Nucleotide binding

268 – 273

NADP By similarity

Nucleotide binding

387 – 390

FAD By similarity

Region

1 – 136

136

Globin

Region

147 – 394

248

Reductase

Region

259 – 394

136

NAD or NADP-binding

Sites

Active site

Charge relay system By similarity

Active site

135

Charge relay system By similarity

Metal binding

Iron (heme proximal ligand) By similarity

Binding site

188

FAD By similarity

Site

Involved in heme-bound ligand stabilization and O-O bond activation By similarity

Site

Influences the redox potential of the prosthetic heme and FAD groups By similarity

Site

386

Influences the redox potential of the prosthetic heme and FAD groups By similarity

Experimental info

Sequence conflict

118

D → G in AAA62190. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P40609-1 [UniParc].

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

394

44,410

        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

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References

	« Hide 'large scale' referencesShow '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.

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Cross-references

Sequence databases
	U09005 Genomic DNA. Translation: AAA62190.1. BA000031 Genomic DNA. Translation: BAC61072.1.
RefSeq	NP_799188.1.
3D structure databases
HSSP	HSSP built from PDB template 1GVH based on UniProtKB P24232.
ModBase	Search...
Genome annotation databases
GeneID	1190359.
GenomeReviews	Gene locus VP2809 in contig BA000031_GR.
KEGG	vpa:VP2809.
NMPDR	fig\|223926.1.peg.2809.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P40609.
Enzyme and pathway databases
BioCyc	VPAR223926:VP2809-MON.
Family and domain databases
HAMAP	MF_01252. [Tree]
InterPro	IPR001709. FPN_cyt_redctse. IPR012292. Globin. IPR000971. Globin_subset. IPR008333. OxRdtase_FAD-bd. IPR001433. OxRdtase_FAD/NAD_bd. IPR001221. Phe_hydroxylase. [Graphical view]
Gene3D	G3DSA:1.10.490.10. Globin_related. 1 hit.
Pfam	PF00970. FAD_binding_6. 1 hit. PF00042. Globin. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PRINTS	PR00371. FPNCR. PR00410. PHEHYDRXLASE.
PROSITE	PS51384. FAD_FR. 1 hit. PS01033. GLOBIN. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

HMP_VIBPA

Accession

Primary (citable) accession number: P40609

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	April 4, 2003
Last modified:	November 25, 2008
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (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

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents