Flavohemoprotein - Bacillus halodurans

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Reviewed, UniProtKB/Swiss-Prot Q9RC40 (HMP_BACHD)

Last modified June 16, 2009. Version 56. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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:	BH1058

Organism

Bacillus halodurans [Complete proteome] [HAMAP]

Taxonomic identifier

86665 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length	411 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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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.
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.
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.

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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 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...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 411

411

Flavohemoprotein HAMAP MF_01252

PRO_0000052422

Regions

Domain

156 – 267

112

FAD-binding FR-type

Nucleotide binding

210 – 213

FAD By similarity

Nucleotide binding

280 – 285

NADP By similarity

Nucleotide binding

401 – 404

FAD By similarity

Region

3 – 142

140

Globin HAMAP MF_01252

Region

153 – 411

259

Reductase HAMAP MF_01252

Region

271 – 411

141

NAD or NADP-binding HAMAP MF_01252

Sites

Active site

Charge relay system By similarity

Active site

141

Charge relay system By similarity

Metal binding

Iron (heme proximal ligand) By similarity

Binding site

194

FAD By similarity

Site

Involved in heme-bound ligand stabilization and O-O bond activation By similarity

Site

Influences the redox potential of the prosthetic heme and FAD groups By similarity

Site

400

Influences the redox potential of the prosthetic heme and FAD groups By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q9RC40-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 779B2F4AB64EA5DE
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FASTA

411

46,565

        10         20         30         40         50         60 
MSTATLSQET KQIVKATVPI LAEHGEAITK HFYKRMFSHH PELLNIFNQT HQKQGRQPQA 

        70         80         90        100        110        120 
LANSIYAAAE HIDNLEAILP VVSRIAHKHR SLNIKPEQYP IVGENLLAAM REVLGDAASD 

       130        140        150        160        170        180 
DVLEAWREAY ELIADVFIQV EKKMYEEASQ APGGWREFRS FVVEKKQRES ATITSFYLKP 

       190        200        210        220        230        240 
EDGKALASYK PGQYITVKVT IPGHEHTHMR QYSLSDAPEK GYYRITVKRE EGDGDLPPGI 

       250        260        270        280        290        300 
VSNYLHQHIH EGDVLEITAP AGDFTLQEEG ERPIVFISGG VGITPLMSMF NTLMQRGVKR 

       310        320        330        340        350        360 
EVIFIHAAIN GFYHAMHDHL AQTASQQENV HYAVCYERPT PGDRMNPFMK KEGFIDESFL 

       370        380        390        400        410 
RSILHDREAD FYFCGPVPFM KTIAQILKDW DVPEQQVHYE FFGPAGTLAS S

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genetic analysis of the chromosome of alkaliphilic Bacillus halodurans C-125." Takami H., Takaki Y., Nakasone K., Sakiyama T., Maeno G., Sasaki R., Hirama C., Fuji F., Masui N. Extremophiles 3:227-233(1999) [PubMed: 10484179] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC BAA-125 / C-125 / DSM 18197 / FERM 7344 / JCM 9153.
[2]	"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis." Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K. Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-125 / C-125 / DSM 18197 / FERM 7344 / JCM 9153.

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Cross-references

Sequence databases
	AB024563 Genomic DNA. Translation: BAA83959.1. BA000004 Genomic DNA. Translation: BAB04777.1.
PIR	B83782.
RefSeq	NP_241924.1.
3D structure databases
HSSP	HSSP built from PDB template 1VHB based on UniProtKB P04252.
ModBase	Search...
Genome annotation databases
GeneID	894032.
GenomeReviews	Gene locus BH1058 in contig BA000004_GR.
KEGG	bha:BH1058.
NMPDR	fig\|272558.1.peg.1058.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9RC40.
OMA	Q9RC40. KHRSLGI.
Enzyme and pathway databases
BioCyc	BHAL272558:BH1058-MON.
BRENDA	1.14.12.17. 191865.
Family and domain databases
HAMAP	MF_01252. [Tree]
InterPro	IPR017927. Fd_Rdtase_FAD-bd. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR012292. Globin. IPR000971. Globin_subset. IPR001834. NADH-Cyt_B5_reductase. 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	PR00406. CYTB5RDTASE. PR00371. FPNCR.
PROSITE	PS51384. FAD_FR. 1 hit. PS01033. GLOBIN. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

HMP_BACHD

Accession

Primary (citable) accession number: Q9RC40

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 56 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)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents