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Q6D245 (HMP_ERWCT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. 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
Ordered Locus Names:ECA3251
OrganismErwinia carotovora subsp. atroseptica (Pectobacterium atrosepticum) [Complete proteome] [HAMAP]
Taxonomic identifier29471 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePectobacterium

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_0000052435

Regions

Domain150 – 255106FAD-binding FR-type
Nucleotide binding204 – 2074FAD By similarity
Nucleotide binding268 – 2736NADP By similarity
Nucleotide binding389 – 3924FAD By similarity
Region1 – 138138Globin 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
Q6D245 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 7F2185F0FA36F34B

FASTA39644,356
        10         20         30         40         50         60 
MLDNHTIAIV KSTIPLLAET GPKLTAHFYD RMFTHNPELK DIFNMSNQRN GDQREALFNA 

        70         80         90        100        110        120 
ICAYATNIEN LAALLPAVER IAQKHTSFNI QADQYQIVGN HLLATLDEMF SPGQEVLDAW 

       130        140        150        160        170        180 
GKAYGVLANV FIQREDDIYR STETKTGGWS GVRPFRIVNK QLQSSVITSF TLEPTDGQPI 

       190        200        210        220        230        240 
ADFQPGQYLA IYIKHDSFAN QEIRQYSLTH APNGKSYRIA VKREAQGTVS GYLHDTAREG 

       250        260        270        280        290        300 
DIVHLAAPHG DFFLDIPTDT PVALISGGVG QTPMLGMLHT LKQQDHQAKV LWLHAAENGT 

       310        320        330        340        350        360 
AHAFTDEIEQ TGQALPHFDH HIWYREPQQT DRPGEDYHHS GLMQLASLKG ELTTPDMHYY 

       370        380        390 
LCGPVVFMQF VAQQLLAMGI PAEQLHYECF GPHKVV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX950851 Genomic DNA. Translation: CAG76149.1.
RefSeqYP_051340.1. NC_004547.2.

3D structure databases

ProteinModelPortalQ6D245.
SMRQ6D245. Positions 1-396.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2881853.
GenomeReviewsGene locus ECA3251 in contig BX950851_GR.
KEGGeca:ECA3251.
NMPDRfig|218491.3.peg.1953.
PATRIC20481837. VBIPecAtr54885_3294.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG623097.
OMATWLHACE.
ProtClustDBPRK13289.

Enzyme and pathway databases

BioCycECAR218491:ECA3251-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.
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_ERWCT
AccessionPrimary (citable) accession number: Q6D245
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: August 16, 2004
Last modified: January 25, 2012
This is version 54 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