Q8GAZ4 (HMP_BURST) Reviewed, UniProtKB/Swiss-Prot

Names 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

Name:

hmp

Organism

Burkholderia sp. (strain TH2)

Taxonomic identifier

109791 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia

Protein attributes

Sequence length	393 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
Gene Ontology (GO)
Biological process	response to nitrosative stress Inferred from electronic annotation. Source: InterPro response to toxin Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro 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: EC oxygen binding Inferred from electronic annotation. Source: InterPro oxygen transporter activity Inferred 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 – 393	393	Flavohemoprotein HAMAP MF_01252		PRO_0000052428
Regions
	Domain	153 – 256	104	FAD-binding FR-type
	Nucleotide binding	205 – 208	4	FAD By similarity
	Nucleotide binding	268 – 273	6	NADP By similarity
	Nucleotide binding	385 – 388	4	FAD By similarity
	Region	1 – 139	139	Globin HAMAP MF_01252
	Region	150 – 393	244	Reductase HAMAP MF_01252
	Region	260 – 393	134	NAD or NADP-binding HAMAP MF_01252
Sites
	Active site	95	1	Charge relay system By similarity
	Active site	138	1	Charge relay system By similarity
	Metal binding	85	1	Iron (heme proximal ligand) By similarity
	Binding site	191	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	384	1	Influences the redox potential of the prosthetic heme and FAD groups By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8GAZ4 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: D17DB36399BB717B	FASTA	393	43,707
	10 20 30 40 50 60 MLSAEHRAIV KATVPLLESG GEALTTHFYK TMLAEYPSVR PLFNQAHQQS GDQPRALANA 70 80 90 100 110 120 VLMYARHIDQ LEQLGGLVSQ IVNKHVALNI LPEHYPIVGA CLLRAIREVL GAEIATDAVI 130 140 150 160 170 180 EAWGAAYQQL ADLLIGLEEN VYVEKETATG GWRGTRAFVV ARKVKESDEI TSFYLRPADG 190 200 210 220 230 240 GELLEFHPGQ YIGLKLIVDG EEIRRNYSLS AAANGREYRI SVKREPNGKA SNYLHDSVNE 250 260 270 280 290 300 GATLDLLTPS GDFTLEHNDK PLVLISGGVG ITPTLAMLNA ALQTSRPIHF IHATRHGGVH 310 320 330 340 350 360 AFRDHIDELA ARHPQLKRFY VYEKPRHDDE AHHAEGYIDE ARLIEWLPAT RDVDVYFLGP 370 380 390 KSFMQAVKRH LKTIGVPEKQ SRYEFFGPAS ALD

References

[1]	"Differential expression of two catechol 1,2-dioxygenases in Burkholderia sp. strain TH2." Suzuki K., Ichimura A., Ogawa N., Hasebe A., Miyashita K. J. Bacteriol. 184:5714-5722(2002) [PubMed: 12270830] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB035325 Genomic DNA. Translation: BAC16771.1.
3D structure databases
ProteinModelPortal	Q8GAZ4.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
HAMAP	MF_01252. Hmp. [Tree]
InterPro	IPR017927. Fd_Rdtase_FAD-bd. IPR009050. Globin-like. IPR012292. Globin_dom. IPR000971. Globin_subset. IPR023950. Hmp. IPR008333. OxRdtase_FAD-bd_dom. IPR001433. OxRdtase_FAD/NAD-bd. IPR000951. Ph_dOase_redase. IPR017938. Riboflavin_synthase-like_b-brl. [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	PR00409. PHDIOXRDTASE.
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_BURST

Accession

Primary (citable) accession number: Q8GAZ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	March 1, 2003
Last modified:	October 19, 2011
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program