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Reviewed, UniProtKB/Swiss-Prot Q6HLA6 (HMP_BACHK)

Last modified June 16, 2009. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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: BT9727_1331
OrganismBacillus thuringiensis subsp. konkukian [Complete proteome] [HAMAP]
Taxonomic identifier180856 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length402 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 402402Flavohemoprotein HAMAP MF_01252
PRO_0000052423

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
Q6HLA6-1 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: F76860E408AC3132

FASTA40245,041
        10         20         30         40         50         60 
MLSEKTIEIV KSTVPLLQEK GVEITTRFYE ILFSEHPELL NIFNHTNQKK GRQQQALANA 

        70         80         90        100        110        120 
VYAAATYIDN LEAIIPVVKQ 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 
AINSNTHAMK EHVEAVDNEY EQVKAYTCYS APTEKDLEMK NFDKEGFVER EWLQTIIPTT 

       370        380        390        400 
EAEFYFCGPV PFMKHINAVL TDLGVKQEHI HYEFFGPAAS LQ 

« Hide

Cross-references

Sequence databases

AE017355 Genomic DNA. Translation: AAT63914.1.
RefSeqYP_035665.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2855081.
GenomeReviewsGene locus BT9727_1331 in contig AE017355_GR.
KEGGbtk:BT9727_1331.
NMPDRfig|281309.1.peg.1305.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ6HLA6.
OMAQ6HLA6. KHRSLGI.

Enzyme and pathway databases

BioCycBTHU281309:BT9727_1331-MON.

Family and domain databases

HAMAPMF_01252.
[Tree]
InterProIPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR012292. Globin.
IPR000971. Globin_subset.
IPR008333. OxRdtase_FAD-bd.
IPR001433. OxRdtase_FAD/NAD_bd.
IPR001221. Phe_hydroxylase.
[Graphical view]
Gene3DG3DSA:1.10.490.10. Globin_related. 1 hit.
PfamPF00970. FAD_binding_6. 1 hit.
PF00042. Globin. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSPR00371. FPNCR.
PR00410. PHEHYDRXLASE.
PROSITEPS51384. FAD_FR. 1 hit.
PS01033. GLOBIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHMP_BACHK
AccessionPrimary (citable) accession number: Q6HLA6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: July 19, 2004
Last modified: June 16, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

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