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Q87F90 (HMP_XYLFT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:PD_0038
OrganismXylella fastidiosa (strain Temecula1 / ATCC 700964) [Complete proteome] [HAMAP]
Taxonomic identifier183190 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXylella

Protein attributes

Sequence length397 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 – 397397Flavohemoprotein HAMAP MF_01252
PRO_0000052454

Regions

Domain154 – 258105FAD-binding FR-type
Nucleotide binding207 – 2104FAD By similarity
Nucleotide binding271 – 2766NADP By similarity
Nucleotide binding387 – 3904FAD By similarity
Region1 – 140140Globin HAMAP MF_01252
Region151 – 397247Reductase HAMAP MF_01252
Region261 – 397137NAD or NADP-binding HAMAP MF_01252

Sites

Active site971Charge relay system By similarity
Active site1391Charge relay system By similarity
Metal binding871Iron (heme proximal ligand) By similarity
Binding site1921FAD By similarity
Site321Involved in heme-bound ligand stabilization and O-O bond activation By similarity
Site861Influences the redox potential of the prosthetic heme and FAD groups By similarity
Site3861Influences the redox potential of the prosthetic heme and FAD groups By similarity

Sequences

Sequence LengthMass (Da)Tools
Q87F90 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 7C68FF4A44AC8EEC

FASTA39744,089
        10         20         30         40         50         60 
MSASFSPHTI TLIKSTVPLL AEHGTTIIEA MYHRLFEDPQ IEALFNQANQ KNGTQIHALA 

        70         80         90        100        110        120 
GAILAYARNI DNPGVLASAI ERISQKHVGY AIHPEHYPHV ATALLGAIKQ VLGDVATSEV 

       130        140        150        160        170        180 
LEAWGEAYWF IANLLKDREA VIREGIMTKN GGWIHWRRFV ISKRIPESET ITSFMLHPED 

       190        200        210        220        230        240 
GGPVVPHQAG QYLTFRFDAA GMPGMKRNYS ISCGPNSDHY RITVKREHGT GASAFLHDQA 

       250        260        270        280        290        300 
KVGTIIECTP PVGDFFLPSV IERPIVLLSG GVGLTPMVSM MEQIAEAYPD AQVWYVHGTQ 

       310        320        330        340        350        360 
NRETHAMDAH IRALVSRHKH MKATTFYTQR SEADDAEAGF ITIDWLRANT PFQKADFYLC 

       370        380        390 
GPRPFLRTFV RDLIGAGVPA AQVHYEFFGP MDEEMAA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009442 Genomic DNA. Translation: AAO27945.1.
RefSeqNP_778296.1. NC_004556.1.

3D structure databases

ProteinModelPortalQ87F90.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ87F90.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1144238.
GenomeReviewsGene locus PD_0038 in contig AE009442_GR.
KEGGxft:PD0038.
PATRIC24147438. VBIXylFas71109_0060.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1018.
HOGENOMHBG623097.
OMATWLHACE.
ProtClustDBPRK13289.

Enzyme and pathway databases

BioCycXFAS183190:PD_0038-MONOMER.

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.
IPR000951. Ph_dOase_redase.
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]
PRINTSPR00409. PHDIOXRDTASE.
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_XYLFT
AccessionPrimary (citable) accession number: Q87F90
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 59 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