Reviewed, UniProtKB/Swiss-Prot Q7NSD8 (HMP_CHRVO)

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
Synonyms:	hmpA
Ordered Locus Names:	CV_3488

Organism

Chromobacterium violaceum [Complete proteome] [HAMAP]

Taxonomic identifier

536 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Chromobacterium

Protein attributes

Sequence length	404 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)(+).
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.

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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 404	404	Flavohemoprotein		PRO_0000052429
Regions
	Domain	152 – 263	112	FAD-binding FR-type
	Nucleotide binding	206 – 209	4	FAD By similarity
	Nucleotide binding	276 – 281	6	NADP By similarity
	Nucleotide binding	396 – 399	4	FAD By similarity
	Region	1 – 138	138	Globin
	Region	149 – 404	256	Reductase
	Region	267 – 404	138	NAD or NADP-binding
Sites
	Active site	95	1	Charge relay system By similarity
	Active site	137	1	Charge relay system By similarity
	Metal binding	85	1	Iron (heme proximal ligand) By similarity
	Binding site	190	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	395	1	Influences the redox potential of the prosthetic heme and FAD groups By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7NSD8-1 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: F17341E0EEBCD8C4	FASTA	404	44,215
	10 20 30 40 50 60 MLSEQTRSLV KATVPVLQQH GVALTSHFYR RMFEHNPELK NVFNQGHQHS GQQQQALAMA 70 80 90 100 110 120 VLAYARHIDD PSPLLPVLTR VAHKHVSLGI RAEHYPIVGK HLLASIRELL GEAAGDDLIQ 130 140 150 160 170 180 AWAEAYGLLA DTLIGIENGM YGDATSADGG WSGWRPFRVA KKEIESEEIA SFYLEPSDGG 190 200 210 220 230 240 ALPAFKPGQY VSVKRFVAEW GLSQPRQYSL SDAPNGEYLR ISVKREDAAQ GKPAGRVSNL 250 260 270 280 290 300 LHREVQVGDV LELSAPQGDF FLHEERDGPA VLISAGVGQT PMQAMLGQLL KRGGREVRFL 310 320 330 340 350 360 HAARHGGAHA MGAKVRQLAD RHPQLKVHVC YETPRAQDAI GVDYQAAGRL NLADVKGIAL 370 380 390 400 LPDADYYLCG PLGFMRAQRD SLRGLGVAAD RIHYEVFGSH PGDD

References

[1]

"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability." Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G. Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed: 14500782] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 12472 / DSM 30191 / IFO 12614 / JCM 1249 / NCIB 9131.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016825 Genomic DNA. Translation: AAQ61149.1.
RefSeq	NP_903158.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2549191.
GenomeReviews	Gene locus CV_3488 in contig AE016825_GR.
KEGG	cvi:CV_3488.
NMPDR	fig|243365.1.peg.3488.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7NSD8.
Enzyme and pathway databases
BioCyc	CVIO243365:CV_3488-MON.
Family and domain databases
HAMAP	MF_01252. [Tree]
InterPro	IPR012292. Globin. IPR000971. Globin_subset. IPR001032. Leghaemoglobin. IPR008333. OxRdtase_FAD-bd. IPR001433. OxRdtase_FAD/NAD_bd. [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	PR00188. PLANTGLOBIN.
PROSITE	PS51384. FAD_FR. 1 hit. PS01033. GLOBIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HMP_CHRVO

Accession

Primary (citable) accession number: Q7NSD8

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	December 15, 2003
Last modified:	November 25, 2008
This is version 39 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)