Flavohemoprotein - Escherichia coli O157:H7

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Q7ABK6 (HMP_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 57. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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:	Z3828, ECs3418

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	396 AA.
Sequence status	Complete.
Protein existence	Inferred 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.

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	response to nitrosative stress Inferred from electronic annotation. Source: InterPro response to toxin Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro nitric oxide dioxygenase activity Inferred from electronic annotation. Source: EC oxygen binding Inferred from electronic annotation. Source: InterPro oxygen transporter activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 396

396

Flavohemoprotein HAMAP MF_01252

PRO_0000052432

Regions

Domain

150 – 255

106

FAD-binding FR-type

Nucleotide binding

204 – 207

FAD By similarity

Nucleotide binding

268 – 273

NADP By similarity

Nucleotide binding

389 – 392

FAD By similarity

Region

1 – 136

136

Globin HAMAP MF_01252

Region

147 – 396

250

Reductase HAMAP MF_01252

Region

259 – 396

138

NAD or NADP-binding HAMAP MF_01252

Sites

Active site

Charge relay system By similarity

Active site

135

Charge relay system By similarity

Metal binding

Iron (heme proximal ligand) By similarity

Binding site

188

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

388

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

Sequences

Sequence

Length

Mass (Da)

Tools

Q7ABK6 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 49824A9B1444BD6B
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FASTA

396

43,838

        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 LGQSLPRFTA HTWYRQPSEA DRAKGQFDSE GLMDLSKLEG AFSDPTMQFY 

       370        380        390 
LCGPVGFMQF AAKQLVDLGV KQENIHYECF GPHKVL

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References

[1]	"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]	"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG57666.1. BA000007 Genomic DNA. Translation: BAB36841.1.
PIR	B91056. F85900.
RefSeq	NP_289108.1. NC_002655.2. NP_311445.1. NC_002695.1.
3D structure databases
ProteinModelPortal	Q7ABK6.
SMR	Q7ABK6. Positions 1-396.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000028060; EBESCP00000026953; EBESCG00000027112. EBESCT00000056662; EBESCP00000054490; EBESCG00000055710.
GeneID	914915. 959263.
GenomeReviews	Gene locus Z3828 in contig AE005174_GR. Gene locus ECs3418 in contig BA000007_GR.
KEGG	ece:Z3828. ecs:ECs3418.
PATRIC	18356272. VBIEscCol44059_3331.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000009404.
HOGENOM	HBG623097.
OMA	TWLHACE.
ProtClustDB	PRK13289.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS3418-MONOMER.
Family and domain databases
HAMAP	MF_01252. Hmp. [Tree]
InterPro	IPR017927. 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]
Gene3D	G3DSA:1.10.490.10. Globin_related. 1 hit.
KO	K05916.
Pfam	PF00970. FAD_binding_6. 1 hit. PF00042. Globin. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PRINTS	PR00410. PHEHYDRXLASE.
SUPFAM	SSF46458. Globin_like. 1 hit. SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITE	PS51384. FAD_FR. 1 hit. PS01033. GLOBIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HMP_ECO57

Accession

Primary (citable) accession number: Q7ABK6
Secondary accession number(s): Q8XA53

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	July 5, 2004
Last modified:	January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

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

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents