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Reviewed, UniProtKB/Swiss-Prot Q9KMY3 (HMP_VIBCH)

Last modified November 3, 2009. Version 61. 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

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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: VC_A0183
OrganismVibrio cholerae [Complete proteome] [HAMAP]
Taxonomic identifier666 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

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Protein attributes

Sequence length394 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred 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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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 394394Flavohemoprotein HAMAP MF_01252
PRO_0000052449

Regions

Domain152 – 262111FAD-binding FR-type
Nucleotide binding206 – 2094FAD By similarity
Nucleotide binding274 – 2796NADP By similarity
Nucleotide binding385 – 3884FAD By similarity
Region1 – 140140Globin HAMAP MF_01252
Region149 – 394246Reductase HAMAP MF_01252
Region265 – 394130NAD or NADP-binding HAMAP MF_01252

Sites

Active site951Charge relay system By similarity
Active site1371Charge relay system By similarity
Metal binding851Iron (heme proximal ligand) By similarity
Binding site1901FAD 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
Site3841Influences the redox potential of the prosthetic heme and FAD groups By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q9KMY3-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: DDA3490FAE28823A

FASTA39444,191
        10         20         30         40         50         60 
MLTQEHINII KSTIPLLESA GPALTQHFYQ RMFSHNPELK HIFNMTHQKT GRQSVALFEA 

        70         80         90        100        110        120 
IAAYAKHIDN LAALTSAVER IAHKHTSFNI QPEHYQIVGH HLLETLRELA PDAFTQPVEE 

       130        140        150        160        170        180 
AWTAAYFFLA QVFIDREGAL YLERKQALGG WRDGRTFVVR EKQVESAYVT SFVLVPADGG 

       190        200        210        220        230        240 
AVLDYQPGQY IGIEVTPEGS DYREIRQYSL SHASNGREYR ISVKREGVGS DNPGLVSHYL 

       250        260        270        280        290        300 
HNNVKVGDSV KLYAPAGDFF YVERERPVVL ISAGVGATPM QAILHTLAKQ NKSGVTYLYA 

       310        320        330        340        350        360 
CNSAKEHTFA QETAQLIAQQ GWMQQVWYRD ESADDVLQGE MQLAELILPI EDGDFYLCGP 

       370        380        390 
IGFMQYVVKQ LLALGVDKAR IHYEVFGPHA QLAA

« Hide

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Cross-references

Sequence databases

AE003853 Genomic DNA. Translation: AAF96096.1.
PIRF82491.
RefSeqNP_232583.1.

3D structure databases

HSSPHSSP built from PDB template 1GVH based on UniProtKB P24232.
ModBaseSearch...

Genome annotation databases

GeneID2611856.
GenomeReviewsGene locus VC_A0183 in contig AE003853_GR.
KEGGvch:VCA0183.
TIGRVC_A0183.

Phylogenomic databases

HOGENOMQ9KMY3.
OMAKHRSLGI.

Enzyme and pathway databases

BRENDA1.14.12.17. 19019.

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...

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Entry information

Entry nameHMP_VIBCH
AccessionPrimary (citable) accession number: Q9KMY3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: October 1, 2000
Last modified: November 3, 2009
This is version 61 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)

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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) · Sequences · References · Cross-references · Entry information · Relevant documents