Reviewed, UniProtKB/Swiss-Prot Q8DCU2 (HMP_VIBVU)

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:	VV1_1301

Organism

Vibrio vulnificus [Complete proteome] [HAMAP]

Taxonomic identifier

672 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

Protein attributes

Sequence length	394 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.

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 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 394	394	Flavohemoprotein HAMAP MF_01252		PRO_0000052451
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

Sequences

	Sequence		Length	Mass (Da)
	Q8DCU2-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 2CEF7EAAB9ADEEB8	FASTA	394	44,247
	10 20 30 40 50 60 MLSENTINIV KSTAPLLAET GPKLTAHFYQ RMFEHNPELK DIFNMSNQRN GDQREALFNA 70 80 90 100 110 120 ICAYASNIDN LPALLGAVEK IAHKHSSFLI TADQYQIVGG HLLATIDELF SPGQAVLDAW 130 140 150 160 170 180 AEAYGVLANV FIQREEQIYQ DNQSQTGGWR GLREFELVEK QYESAHICSF VFKPVDGGSV 190 200 210 220 230 240 VSFKPGQYLG IYINDEQFEN QEIRQYSLSS SVRPDCYRIS VKREEGGRVS NYLHDHLDVG 250 260 270 280 290 300 SKVKLAAPAG DFFLDAAPTA PVVLISAGVG LTPTLSMLES LTEHQAPVTW IHATENGQQH 310 320 330 340 350 360 AFKQHVKQLV ETHPHFNSLV WYNQPNSDDK IGDDFQFSGW VNLHEIETVL KQADVQVYFC 370 380 390 GPVGFMQFIA KQLLEMGVPE QQFHYECFGP HKVV

References

[1]	"Complete genome sequence of Vibrio vulnificus CMCP6." Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E. Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CMCP6.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016795 Genomic DNA. Translation: AAO09756.1.
RefSeq	NP_760229.1.
3D structure databases
HSSP	HSSP built from PDB template 1GVH based on UniProtKB P24232.
ModBase	Search...
Genome annotation databases
GeneID	1178228.
GenomeReviews	Gene locus VV1_1301 in contig AE016795_GR.
KEGG	vvu:VV1_1301.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8DCU2.
OMA	Q8DCU2. KHRSLGI.
Enzyme and pathway databases
BioCyc	VVUL216895:VV1_1301-MON.
BRENDA	1.14.12.17. 277169.
Family and domain databases
HAMAP	MF_01252. [Tree]
InterPro	IPR017927. Fd_Rdtase_FAD-bd. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. 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...

Entry information

Entry name

HMP_VIBVU

Accession

Primary (citable) accession number: Q8DCU2

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	March 1, 2003
Last modified:	June 16, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)