Reviewed, UniProtKB/Swiss-Prot Q47266 (HMP_DICD3)

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
    Hemoprotein X

Gene names

Name:	hmp
Synonyms:	hmpX

Organism

Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))

Taxonomic identifier

198628 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Dickeya

Protein attributes

Sequence length	395 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 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)(+). HAMAP MF_01252
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per subunit By similarity. Binds 1 FAD per subunit By similarity.
Subcellular location	Cytoplasm. 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
Cellular component	Cytoplasm
Ligand	FAD Flavoprotein Heme Iron Metal-binding NAD NADP
Molecular function	Oxidoreductase
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
Cellular component	cytoplasm 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 395	395	Flavohemoprotein HAMAP MF_01252		PRO_0000052434
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	388 – 391	4	FAD By similarity
	Region	1 – 138	138	Globin HAMAP MF_01252
	Region	147 – 395	249	Reductase HAMAP MF_01252
	Region	259 – 395	137	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	387	1	Influences the redox potential of the prosthetic heme and FAD groups By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q47266-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 05C43167559CF6E6	FASTA	395	44,315
	10 20 30 40 50 60 MLDQQTIATI KSTIPLLAET GPALTAHFYQ RMFHHNPELK DIFNMSNQRN GDQREALFNA 70 80 90 100 110 120 ICAYATHIEN LPALLPAVER IAQKHASFNI QPEQYQIVGT HLLATLEEMF QPGQAVLDAW 130 140 150 160 170 180 GKRYGVLANV FIQRESDIYQ QSAGQNGGWH GIRPFRIVAK QPQSSLITSF TLEPVDGGPI 190 200 210 220 230 240 AAFRPGQYLA VYIRDKRFEY QEIRQYSLTN EPNGRYYRIA VKRETMGSVS GYLHDVAREG 250 260 270 280 290 300 DVIELAAPHG DFYLEVTPET PVALISAGVG QTPMLSMLHS LKNQQHQADI FWLHAAENTE 310 320 330 340 350 360 VHAFADEIAD VAATLPQLQS YVWYREASSE AARSAHAFHG LMALKDLPTP LPMTNLHCYL 370 380 390 CGPVAFMQFA ARQLLELGIT ESQIHYECFG PHKVI

References

[1]	"Flavohaemoglobin HmpX: a new pathogenicity determinant in Erwinia chrysanthemi strain 3937." Favey S., Labesse G., Vouille V., Boccara M. Microbiology 141:863-871(1995) [PubMed: 7773389] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	X75893 Genomic DNA. Translation: CAA53500.1.
PIR	S44277.
3D structure databases
HSSP	HSSP built from PDB template 1GVH based on UniProtKB P24232.
ModBase	Search...
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...

Entry information

Entry name

HMP_DICD3

Accession

Primary (citable) accession number: Q47266

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	November 25, 2008
This is version 61 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)