Reviewed, UniProtKB/Swiss-Prot P49852 (HMP_BACSU)

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:	ane3, ykiA
Ordered Locus Names:	BSU13040

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	399 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

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.
Induction	By nitric oxide, nitrite, and under oxygen-limited conditions.
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 – 399	399	Flavohemoprotein		PRO_0000052424
Regions
	Domain	152 – 255	104	FAD-binding FR-type
	Nucleotide binding	206 – 209	4	FAD By similarity
	Nucleotide binding	268 – 273	6	NADP By similarity
	Nucleotide binding	388 – 391	4	FAD By similarity
	Region	1 – 140	140	Globin
	Region	149 – 399	251	Reductase
	Region	259 – 399	141	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	387	1	Influences the redox potential of the prosthetic heme and FAD groups By similarity

Sequences

	Sequence		Length	Mass (Da)
	P49852-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: FFD3DD6C973301CF	FASTA	399	44,729
	10 20 30 40 50 60 MLDNKTIEII KSTVPVLQQH GETITGRFYD RMFQDHPELL NIFNQTNQKK KTQRTALANA 70 80 90 100 110 120 VIAAAANIDQ LGNIIPVVKQ IGHKHRSIGI KPEHYPIVGK YLLIAIKDVL GDAATPDIMQ 130 140 150 160 170 180 AWEKAYGVIA DAFIGIEKDM YEQAEEQAGG WKEYKPFVIA KKERESKEIT SFYLKPEDSK 190 200 210 220 230 240 PLPEFQAGQY ISIKVRIPDS EYTHIRQYSL SDMPGKDYYR ISVKKDGVVS SYLHDGLQEG 250 260 270 280 290 300 DSIEISAPAG DFVLDHASQK DLVLISAGVG ITPMISMLKT SVSKQPERQI LFIHAAKNSE 310 320 330 340 350 360 YHALRHEVEE AAKHSAVKTA FVYREPTEED RAGDLHFHEG QIDQQFLKEL IANTDADYYI 370 380 390 CGSPSFITAM HKLVSELGSA PESIHYELFG PQLSLAQSV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Oxygen-controlled regulation of the flavohemoglobin gene in Bacillus subtilis." Lacelle M., Kumano M., Kurita K., Yamane K., Zuber P., Nakano M.M. J. Bacteriol. 178:3803-3808(1996) [PubMed: 8682784] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TRANSCRIPTIONAL REGULATION. Strain: 168.
[2]	"Sequence of the Bacillus subtilis genome between xlyA and ykoR." Devine K.M. Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"Induction of ResDE-dependent gene expression in Bacillus subtilis in response to nitric oxide and nitrosative stress." Nakano M.M. J. Bacteriol. 184:1783-1787(2002) [PubMed: 11872732] [Abstract] Cited for: TRANSCRIPTIONAL REGULATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D78189 Genomic DNA. Translation: BAA11258.1. AJ002571 Genomic DNA. Translation: CAA05584.1. Z99110 Genomic DNA. Translation: CAB13161.1.
PIR	B69642.
RefSeq	NP_389187.1.
3D structure databases
HSSP	HSSP built from PDB template 1VHB based on UniProtKB P04252.
ModBase	Search...
Genome annotation databases
GeneID	939891.
GenomeReviews	Gene locus BSU13040 in contig AL009126_GR.
KEGG	bsu:BSU13040.
NMPDR	fig|224308.1.peg.1306.
Organism-specific databases
SubtiList	BG11418. hmp. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P49852.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU1306-MON.
Family and domain databases
HAMAP	MF_01252. [Tree]
InterPro	IPR001709. FPN_cyt_redctse. 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	PR00371. FPNCR. PR00410. PHEHYDRXLASE. PR01907. WORMGLOBIN.
PROSITE	PS51384. FAD_FR. 1 hit. PS01033. GLOBIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HMP_BACSU

Accession

Primary (citable) accession number: P49852

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 25, 2008
This is version 72 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)