Flavohemoprotein - Escherichia coli O157:H7

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Reviewed, UniProtKB/Swiss-Prot Q7ABK6 (HMP_ECO57)

Last modified January 19, 2010. Version 44. History...

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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 names

Recommended 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
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

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Protein attributes

Sequence length	396 AA.
Sequence status	Complete.
Protein existence	Inferred 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. 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. HAMAP MF_01252 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.

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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	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW oxygen transport Inferred from electronic annotation. Source: HAMAP response to toxin Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	heme binding Inferred from electronic annotation. Source: InterPro nitric oxide dioxygenase activity Inferred from electronic annotation. Source: HAMAP oxygen binding Inferred from electronic annotation. Source: InterPro oxygen transporter activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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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

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Sequences

Sequence

Length

Mass (Da)

Tools

Q7ABK6-1 [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.

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.

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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. NP_311445.1.
3D structure databases
SMR	Q7ABK6. Positions 1-396.
ModBase	Search...
Genome annotation databases
GeneID	914915. 959263.
GenomeReviews	Gene locus Z3828 in contig AE005174_GR. Gene locus ECs3418 in contig BA000007_GR.
KEGG	ece:Z3828. ecs:ECs3418.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG623097.
OMA	KQIGHKH.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS3418-MONOMER.
Family and domain databases
HAMAP	MF_01252. Hmp. [Tree]
InterPro	IPR017927. Fd_Rdtase_FAD-bd. IPR012292. Globin. IPR009050. Globin-like. IPR000971. Globin_subset. 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.
Pfam	PF00970. FAD_binding_6. 1 hit. PF00042. Globin. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PRINTS	PR00410. PHEHYDRXLASE.
PROSITE	PS51384. FAD_FR. 1 hit. PS01033. GLOBIN. 1 hit. [Graphical view]
ProtoNet	Search...

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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 19, 2010
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (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)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents