Flavohemoprotein - Photorhabdus luminescens subsp. laumondii

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q7N215 (HMP_PHOLL)

Last modified February 9, 2010. Version 44. 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

Hide | Top

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:	plu3292

Organism

Photorhabdus luminescens subsp. laumondii [Complete proteome] [HAMAP]

Taxonomic identifier

141679 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Photorhabdus

Hide | Top

Protein attributes

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

Hide | Top

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.

Hide | Top

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...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 396

396

Flavohemoprotein HAMAP MF_01252

PRO_0000052437

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

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

Q7N215-1 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 400EC27CA60F4018
Show »

FASTA

396

44,961

        10         20         30         40         50         60 
MLDNQTIATV KSTIPLLSAT GPKLTAHFYE RMFKHNPELK NIFNMSHQLN GDQREALFNA 

        70         80         90        100        110        120 
ICAYAANIDN LKVLLPAVEK IAHKHASLNI QPEHYQIVGT HLLATLNEMF QPGNEILDAW 

       130        140        150        160        170        180 
GKAYGVLADI FINREEQIYH SGELTDGGWR GLRPFRINRK EVKSEVICSF EFAPQDGGKV 

       190        200        210        220        230        240 
MDYKPGQYLS IYLQDDSFAN REIRQYSLTA APNGSSYRIA IKREPQGIVS NHMHDKMQEG 

       250        260        270        280        290        300 
DTVWLTAPRG DFFLDIKPET PVTLISAGVG LTPMMSMLYH LHQQNHNSPI NWLHAAEHGG 

       310        320        330        340        350        360 
HHAFSHEVAA IAQAMPNFAG TIWYREPRDE DQQGIHYQHK GFMDLTVLNE ALKTEGMHFY 

       370        380        390 
FCGPVAFMQY VAKQLLDMGI DKQFIHYECF GPHKVI

« Hide

Hide | Top

References

[1]

"The genome sequence of the entomopathogenic bacterium Photorhabdus luminescens."
Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A., Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F., Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C., Lanois A., Powell K.

Kunst F.
Nat. Biotechnol. 21:1307-1313(2003) [PubMed: 14528314] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TT01.

Hide | Top

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX571870 Genomic DNA. Translation: CAE15666.1.
RefSeq	NP_930516.1.
3D structure databases
SMR	Q7N215. Positions 1-396.
ModBase	Search...
Genome annotation databases
GeneID	2803304.
KEGG	plu:plu3292.
NMPDR	fig\|243265.1.peg.3140.
Organism-specific databases
PhotoList	plu3292.
CMR	Search...
Phylogenomic databases
HOGENOM	HBG623097.
OMA	KQIGHKH.
Enzyme and pathway databases
BioCyc	PLUM243265:PLU3292-MONOMER.
BRENDA	1.14.12.17. 308689.
Family and domain databases
HAMAP	MF_01252. Hmp. [Tree]
InterPro	IPR017927. Fd_Rdtase_FAD-bd. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. 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	PR00371. FPNCR. PR00410. PHEHYDRXLASE.
PROSITE	PS51384. FAD_FR. 1 hit. PS01033. GLOBIN. 1 hit. [Graphical view]
ProtoNet	Search...

Hide | Top

Entry information

Entry name

HMP_PHOLL

Accession

Primary (citable) accession number: Q7N215

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	December 15, 2003
Last modified:	February 9, 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)

Hide | Top

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