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Q81FW4 (HMP_BACCR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Flavohemoprotein
Alternative name(s):
Flavohemoglobin
Hemoglobin-like protein
Nitric oxide dioxygenase
Short name=NO oxygenase
Short name=NOD
EC=1.14.12.17
Gene names
Name:hmp
Ordered Locus Names:BC_1448
OrganismBacillus cereus (strain ATCC 14579 / DSM 31)
Taxonomic identifier226900 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length402 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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. HAMAP MF_01252

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. 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 402402Flavohemoprotein HAMAP MF_01252
PRO_0000052421

Regions

Domain150 – 260111FAD-binding FR-type
Nucleotide binding204 – 2074FAD By similarity
Nucleotide binding273 – 2786NADP By similarity
Nucleotide binding394 – 3974FAD By similarity
Region1 – 136136Globin HAMAP MF_01252
Region147 – 402256Reductase HAMAP MF_01252
Region264 – 402139NAD or NADP-binding HAMAP MF_01252

Sites

Active site951Charge relay system By similarity
Active site1351Charge relay system By similarity
Metal binding851Iron (heme proximal ligand) By similarity
Binding site1881FAD By similarity
Site291Involved in heme-bound ligand stabilization and O-O bond activation By similarity
Site841Influences the redox potential of the prosthetic heme and FAD groups By similarity
Site3931Influences the redox potential of the prosthetic heme and FAD groups By similarity

Sequences

Sequence LengthMass (Da)Tools
Q81FW4 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: A637DE5D2030BC16

FASTA40244,944
        10         20         30         40         50         60 
MLSAKTIEIV KSTVPLLQEK GVEITTRFYQ ILFSEHPELL NIFNHTNQKK GRQQQALANA 

        70         80         90        100        110        120 
VYAAATYIDN LEAIIPVVKQ IGHKHRSLGI KAEHYPIVGT CLLRAIKEVA GAPDEVLNAW 

       130        140        150        160        170        180 
GEAYGVIADA FISIEAEMYE EAAHKEGGWK DFRNFVIVKK VKESDVITSF YLKPEDGGKV 

       190        200        210        220        230        240 
SSFIPGQYVT IQINIEGETY THNRQYSLSD APGKEYYRIS VKKEKGVDTP DGKVSNYLHG 

       250        260        270        280        290        300 
HVKEGDVLPV SAPAGDFVLN MDSTLPVVLI SGGVGITPMM SMLNTLIEQD SKRNVYFVHA 

       310        320        330        340        350        360 
AINSNTHAMK EHVKAVENEY EQVKAYTCYS APTEKDLEMK NFDKEGFIES EWLKTIIPTT 

       370        380        390        400 
EAEFYFCGPV AFMKHINAAL TDLSVKQEHI HYEFFGPATS LQ 

« Hide

References

[1]"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. expand/collapse author list , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.
Nature 423:87-91(2003) [PubMed: 12721630] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14579 / DSM 31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016877 Genomic DNA. Translation: AAP08429.1.
RefSeqNP_831228.1. NC_004722.1.

3D structure databases

ProteinModelPortalQ81FW4.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ81FW4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000031970; EBBACP00000031176; EBBACG00000031961.
GeneID1203797.
GenomeReviewsGene locus BC_1448 in contig AE016877_GR.
KEGGbce:BC1448.
PATRIC32598632. VBIBacCer54481_1425.

Phylogenomic databases

eggNOGCOG1018.
GeneTreeEBGT00050000001043.
HOGENOMHBG623097.
OMATWLHACE.
ProtClustDBPRK13289.

Enzyme and pathway databases

BioCycBCER226900:BC_1448-MONOMER.

Family and domain databases

HAMAPMF_01252. Hmp.
[Tree]
InterProIPR017927. Fd_Rdtase_FAD-bd.
IPR009050. Globin-like.
IPR012292. Globin_dom.
IPR000971. Globin_subset.
IPR023950. Hmp.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR001221. Phe_hydroxylase.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
Gene3DG3DSA:1.10.490.10. Globin_related. 1 hit.
KOK05916.
PfamPF00970. FAD_binding_6. 1 hit.
PF00042. Globin. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSPR00410. PHEHYDRXLASE.
SUPFAMSSF46458. Globin_like. 1 hit.
SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
PS01033. GLOBIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHMP_BACCR
AccessionPrimary (citable) accession number: Q81FW4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families