Reviewed, UniProtKB/Swiss-Prot Q73B49 (HMP_BACC1)

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:	BCE_1571

Organism

Bacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]

Taxonomic identifier

222523 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	402 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 – 402	402	Flavohemoprotein		PRO_0000052420
Regions
	Domain	150 – 260	111	FAD-binding FR-type
	Nucleotide binding	204 – 207	4	FAD By similarity
	Nucleotide binding	273 – 278	6	NADP By similarity
	Nucleotide binding	394 – 397	4	FAD By similarity
	Region	1 – 136	136	Globin
	Region	147 – 402	256	Reductase
	Region	264 – 402	139	NAD or NADP-binding
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	393	1	Influences the redox potential of the prosthetic heme and FAD groups By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q73B49-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: B7CC601EC87E3192	FASTA	402	44,954
	10 20 30 40 50 60 MLSEKTIEIV KSTVPLLQEK GVEITTRFYE ILFSEHPELL NIFNHTNQKK GRQQQALANA 70 80 90 100 110 120 VYAAATYIDN LEVIIPVVKQ IGHKHRSLGI KAEHYPIVGT CLLRAIKEVA GAPDEVLNAW 130 140 150 160 170 180 GEAYGVIADA FISIEAEMYE EAAHKEGGWK DFRNFVVVKK VKESDVITSF YLKPEDGGKV 190 200 210 220 230 240 SSFIPGQYVT VQINIEGETY THNRQYSLSD APGKEYYRIS VKKEKGVDTP DGKVSNYLHD 250 260 270 280 290 300 HVKEGDMLPV SAPAGDFVLN MDSTLPVVLI SGGVGITPMM SMLNTLIEQD SKRNVCFVHA 310 320 330 340 350 360 ALNSNTHAMK EHVEALDNEY EQVKAYTCYS APTEKDLEMK NFDKEGLIEA EWLQTIIPTT 370 380 390 400 EAEFYFCGPV AFMKHINATL TDLGVKQEHI HYEFFGPAAS LQ

References

[1]

"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1." Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D. Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE017194 Genomic DNA. Translation: AAS40500.1.
RefSeq	NP_977892.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2749014.
GenomeReviews	Gene locus BCE_1571 in contig AE017194_GR.
KEGG	bca:BCE_1571.
NMPDR	fig|222523.1.peg.1564.
TIGR	BCE_1571.
Phylogenomic databases
HOGENOM	Q73B49.
Family and domain databases
HAMAP	MF_01252. [Tree]
InterPro	IPR012292. Globin. IPR013316. Globin_annelid-type. 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	PR00410. PHEHYDRXLASE. PR01907. WORMGLOBIN.
PROSITE	PS51384. FAD_FR. 1 hit. PS01033. GLOBIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HMP_BACC1

Accession

Primary (citable) accession number: Q73B49

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	July 5, 2004
Last modified:	November 25, 2008
This is version 35 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)