Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q8FF30 (HMP_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
Synonyms:hmpA
Ordered Locus Names:c3075
OrganismEscherichia coli O6 [Complete proteome] [HAMAP]
Taxonomic identifier217992 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length396 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 – 396396Flavohemoprotein HAMAP MF_01252
PRO_0000052433

Regions

Domain150 – 255106FAD-binding FR-type
Nucleotide binding204 – 2074FAD By similarity
Nucleotide binding268 – 2736NADP By similarity
Nucleotide binding389 – 3924FAD By similarity
Region1 – 136136Globin HAMAP MF_01252
Region147 – 396250Reductase HAMAP MF_01252
Region259 – 396138NAD 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
Site3881Influences the redox potential of the prosthetic heme and FAD groups By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8FF30 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 46664A8ECA4F68B5

FASTA39643,850
        10         20         30         40         50         60 
MLDAQTIATV KATIPLLVET GPKLTAHFYD RMFTHNPELK EIFNMSNQRN GDQREALFNA 

        70         80         90        100        110        120 
IAAYASNIEN LPALLPAVEK IAQKHTSFQI KPEQYNIVGE HLLATLDEMF SPGQEVLDAW 

       130        140        150        160        170        180 
GKAYGVLANV FINREAEIYN ENASKAGGWE GTRDFRIVAK TPRSALITSF ELEPVDGGAV 

       190        200        210        220        230        240 
AEYRPGQYLG VWLKPEGFPH QEIRQYSLTR KPDGKGYRIA VKREEGGQVS NWLHNHANVG 

       250        260        270        280        290        300 
DVVKLVAPAG DFFMAVADDT PVTLISAGVG QTPMLAMLDT LAKAGHTAQV NWFHAAENGD 

       310        320        330        340        350        360 
VHAFADEVKE LGLSLPRFTA HTWYRQPNEA DRAKGQFDSE GLMDLSKLEG AFSDPTMQFY 

       370        380        390 
LCGPVGFMQF AAKQLVDLGV KQENIHYECF GPHKVL

« Hide

References

[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE014075 Genomic DNA. Translation: AAN81524.1.
RefSeqNP_754956.1. NC_004431.1.

3D structure databases

ProteinModelPortalQ8FF30.
SMRQ8FF30. Positions 1-396.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000044267; EBESCP00000042616; EBESCG00000043317.
GeneID1038776.
GenomeReviewsGene locus c3075 in contig AE014075_GR.
KEGGecc:c3075.
PATRIC18284000. VBIEscCol75197_2900.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000009404.
HOGENOMHBG623097.
OMATWLHACE.
ProtClustDBPRK13289.

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_ECOL6
AccessionPrimary (citable) accession number: Q8FF30
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: March 1, 2003
Last modified: January 25, 2012
This is version 61 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents