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Protein
Submitted name:

Dehaloperoxidase A

Gene
N/A
Organism
Amphitrite ornata
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei56 – 561Heme (covalent)Combined sources
Metal bindingi90 – 901Iron (heme axial ligand); via tele nitrogenCombined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, PeroxidaseImported

Keywords - Biological processi

Oxygen transportUniRule annotation, Transport

Keywords - Ligandi

HemeCombined sources, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Submitted name:
Dehaloperoxidase AImported
OrganismiAmphitrite ornataImported
Taxonomic identifieri129555 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaAnnelidaPolychaetaScolecidaTerebellidaAmphitrite

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EW6X-ray1.78A/B2-138[»]
1EWAX-ray2.50A/B2-138[»]
2QFKX-ray1.62A/B2-138[»]
2QFNX-ray1.62A/B1-138[»]
3DR9X-ray1.26A/B2-138[»]
3K3UX-ray1.63A/B2-138[»]
3KUNX-ray1.26A/B2-138[»]
3KUOX-ray1.26A/B2-138[»]
3LB1X-ray1.76A/B2-138[»]
3LB2X-ray1.06A/B2-138[»]
3LB3X-ray1.85A/B2-138[»]
3LB4X-ray1.56A/B2-138[»]
3MOUX-ray1.71A/B2-138[»]
3MYMX-ray1.72A/B2-138[»]
3MYNX-ray2.19A/B2-138[»]
3O7NX-ray1.72A/B2-138[»]
3OJ1X-ray1.52A/B2-138[»]
3OK5X-ray1.72A/B2-138[»]
3ORDX-ray2.22A/B2-138[»]
4DWTX-ray2.05A/B2-138[»]
4DWUX-ray1.44A/B2-138[»]
4FH6X-ray1.44A/B2-138[»]
4FH7X-ray1.74A/B2-138[»]
4GZGX-ray1.49A/B2-138[»]
4HSWX-ray1.22A/B2-138[»]
4HSXX-ray1.12A/B2-138[»]
4ILZX-ray1.91A/B2-138[»]
4JACX-ray1.93A/B1-138[»]
4JYQX-ray1.80A/B2-138[»]
4KJTX-ray1.44A/B2-138[»]
4KMVX-ray1.44A/B2-138[»]
4KMWX-ray1.79A/B2-138[»]
4KN3X-ray1.78A/B2-138[»]
ProteinModelPortaliQ9NAV8.
SMRiQ9NAV8. Positions 2-138.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NAV8.

Family & Domainsi

Sequence similaritiesi

Belongs to the globin family.UniRule annotation

Family and domain databases

Gene3Di1.10.490.10. 1 hit.
InterProiIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin_dom.
[Graphical view]
PfamiPF00042. Globin. 1 hit.
[Graphical view]
SUPFAMiSSF46458. SSF46458. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9NAV8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGFKQDIATI RGDLRTYAQD IFLAFLNKYP DERRYFKNYV GKSDQELKSM
60 70 80 90 100
AKFGDHTEKV FNLMMEVADR ATDCVPLASD ANTLVQMKQH SSLTTGNFEK
110 120 130
LFVALVEYMR ASGQSFDSQS WDRFGKNLVS ALSSAGMK
Length:138
Mass (Da):15,660
Last modified:October 1, 2000 - v1
Checksum:iE63F8C82A7CB90A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF284381 mRNA. Translation: AAF97245.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF284381 mRNA. Translation: AAF97245.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EW6X-ray1.78A/B2-138[»]
1EWAX-ray2.50A/B2-138[»]
2QFKX-ray1.62A/B2-138[»]
2QFNX-ray1.62A/B1-138[»]
3DR9X-ray1.26A/B2-138[»]
3K3UX-ray1.63A/B2-138[»]
3KUNX-ray1.26A/B2-138[»]
3KUOX-ray1.26A/B2-138[»]
3LB1X-ray1.76A/B2-138[»]
3LB2X-ray1.06A/B2-138[»]
3LB3X-ray1.85A/B2-138[»]
3LB4X-ray1.56A/B2-138[»]
3MOUX-ray1.71A/B2-138[»]
3MYMX-ray1.72A/B2-138[»]
3MYNX-ray2.19A/B2-138[»]
3O7NX-ray1.72A/B2-138[»]
3OJ1X-ray1.52A/B2-138[»]
3OK5X-ray1.72A/B2-138[»]
3ORDX-ray2.22A/B2-138[»]
4DWTX-ray2.05A/B2-138[»]
4DWUX-ray1.44A/B2-138[»]
4FH6X-ray1.44A/B2-138[»]
4FH7X-ray1.74A/B2-138[»]
4GZGX-ray1.49A/B2-138[»]
4HSWX-ray1.22A/B2-138[»]
4HSXX-ray1.12A/B2-138[»]
4ILZX-ray1.91A/B2-138[»]
4JACX-ray1.93A/B1-138[»]
4JYQX-ray1.80A/B2-138[»]
4KJTX-ray1.44A/B2-138[»]
4KMVX-ray1.44A/B2-138[»]
4KMWX-ray1.79A/B2-138[»]
4KN3X-ray1.78A/B2-138[»]
ProteinModelPortaliQ9NAV8.
SMRiQ9NAV8. Positions 2-138.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NAV8.

Family and domain databases

Gene3Di1.10.490.10. 1 hit.
InterProiIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin_dom.
[Graphical view]
PfamiPF00042. Globin. 1 hit.
[Graphical view]
SUPFAMiSSF46458. SSF46458. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The crystal structure and amino acid sequence of dehaloperoxidase from Amphitrite ornata indicate common ancestry with globins."
    LaCount M.W., Zhang E., Chen Y.P., Han K., Whitton M.M., Lincoln D.E., Woodin S.A., Lebioda L.
    J. Biol. Chem. 275:18712-18716(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 2-138 IN COMPLEX WITH HEME.
  2. "Amphitrite ornata, a marine worm, contains two dehaloperoxidase genes."
    Han K., Woodin S.A., Lincoln D.E., Fielman K.T., Ely B.
    Mar. Biotechnol. 3:287-292(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  3. "X-ray crystal structural analysis of the binding site in the ferric and oxyferrous forms of the recombinant heme dehaloperoxidase cloned from Amphitrite ornata."
    de Serrano V., Chen Z., Davis M.F., Franzen S.
    Acta Crystallogr. D 63:1094-1101(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) OF 2-138 IN COMPLEX WITH HEME.
  4. "Distal histidine conformational flexibility in dehaloperoxidase from Amphitrite ornata."
    Chen Z., de Serrano V., Betts L., Franzen S.
    Acta Crystallogr. D 65:34-40(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.26 ANGSTROMS) OF 2-138 IN COMPLEX WITH HEME.
  5. "The V59W mutation blocks the distal pocket of the hemoglobin dehaloperoxidase from Amphitrite ornata."
    Davis M.F., de Serrano V., Gracz H., Vendreix F.A.P., Somasundram A., Negrerie M., Franzen S.
    Submitted (OCT-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 2-138 IN COMPLEX WITH HEME.
  6. "X-ray structure of the metcyano form of dehaloperoxidase from Amphitrite ornata: evidence for photoreductive dissociation of the iron-cyanide bond."
    de Serrano V.S., Davis M.F., Gaff J.F., Zhang Q., Chen Z., D'Antonio E.L., Bowden E.F., Rose R., Franzen S.
    Acta Crystallogr. D 66:770-782(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.26 ANGSTROMS) OF 2-138 IN COMPLEX WITH HEME.
  7. "Internal binding of halogenated phenols in dehaloperoxidase-hemoglobin inhibits peroxidase function."
    Thompson M.K., Davis M.F., de Serrano V., Nicoletti F.P., Howes B.D., Smulevich G., Franzen S.
    Biophys. J. 99:1586-1595(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.06 ANGSTROMS) OF 2-138 IN COMPLEX WITH HEME.
  8. "Characterization of the Inhibitor Binding Site of the Dehaloperoxidase-Hemoglobin from Amphitrite ornata using High-Pressure Xenon Derivatization."
    de Serrano V.S., Franzen S.
    Submitted (APR-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) OF 2-138 IN COMPLEX WITH HEME.
  9. "Mutation of Methionine-86 in Dehaloperoxidase-hemoglobin: Effects of the Asp-His-Fe Triad in a 3/3 Globin."
    D'Antonio E.L., D'Antonio J., Grazs H., de Serrano V.S., Thompson M.K., Ghiladi R.A., Franzen S., Bowden E.F.
    Submitted (MAY-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 2-138.
  10. "The V59W mutation blocks the distal pocket of the hemoglobin - dehaloperoxidase from Amphitirite ornata."
    Davis M.F., de Serrano V.S., Gracz H., Vendreix F.A.P., Somasundram A., Negrerie M., Franzen S.
    Submitted (JUL-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 2-138 IN COMPLEX WITH HEME.
  11. "Effect of the H55D mutation on the kinetics and structure of dehaloperoxidase-hemoglobin A."
    Zhao J., De Serrano V.S., S. Franzen.
    Submitted (AUG-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 2-138 IN COMPLEX WITH HEME.
  12. "Effect of the H55D mutation on the kinetics and structure of dehaloperoxidase-hemoglobin A."
    Zhao J., De Serrano V.S., Franzen S.
    Submitted (AUG-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 2-138.
  13. "Structural evidence for stabilization of inhibitor binding by a protein cavity in the dehaloperoxidase-hemoglobin from Amphitrite ornata."
    de Serrano V., Franzen S.
    Biopolymers 98:27-35(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS) OF 2-138.
  14. "A unique role for the distal histidine observed in carbonmonoxy dehaloperoxidase-hemoglobin A structures."
    de Serrano V.S., Zhao J., Franzen S.
    Submitted (FEB-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 2-138 IN COMPLEX WITH HEME.
  15. "The role of distal histidine in carbonmonoxide DHP structure."
    Zhao J., Franzen S.
    Submitted (SEP-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) OF 2-138 IN COMPLEX WITH HEME.
  16. "Role of polarity of the distal pocket in the control of inhibitor binding in dehaloperoxidase-hemoglobin."
    Plummer A., Thompson M.K., Franzen S.
    Biochemistry 52:2218-2227(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS) OF 2-138 IN COMPLEX WITH HEME.
  17. "Structural and kinetic study of an internal substrate binding site in dehaloperoxidase-hemoglobin A from Amphitrite ornata."
    Zhao J., de Serrano V., Zhao J., Le P., Franzen S.
    Biochemistry 52:2427-2439(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.44 ANGSTROMS) OF 2-138 IN COMPLEX WITH HEME.
  18. "Complexes of dual-function hemoglobin/dehaloperoxidase with substrate 2,4,6-trichlorophenol are inhibitory and indicate binding of halophenol to compound I."
    Wang C., Lovelace L.L., Sun S., Dawson J.H., Lebioda L.
    Biochemistry 52:6203-6210(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.44 ANGSTROMS) OF 2-138 IN COMPLEX WITH HEME.
  19. "The role of T56 in controlling the flexibility of the distal histidine in dehaloperoxidase-hemoglobin from Amphitrite ornata."
    Jiang S., Wright I., Swartz P., Franzen S.
    Biochim. Biophys. Acta 1834:2020-2029(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH HEME.
  20. "Observation of protein valves for the control of the internal flow of small molecules using time-resolved X-ray crystallography."
    Zhao J., Srajer V., Franzen S.
    Submitted (MAR-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-138 IN COMPLEX WITH HEME.
  21. "Influence of heme environment structure on dioxygen affinity for the dual function Amphitrite ornata hemoglobin/dehaloperoxidase. Insights into the evolutional structure-function adaptations."
    Sun S., Sono M., Wang C., Du J., Lebioda L., Dawson J.H.
    Arch. Biochem. Biophys. 545:108-115(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.44 ANGSTROMS) OF 2-138 IN COMPLEX WITH HEME.

Entry informationi

Entry nameiQ9NAV8_9ANNE
AccessioniPrimary (citable) accession number: Q9NAV8
Entry historyi
Integrated into UniProtKB/TrEMBL: October 1, 2000
Last sequence update: October 1, 2000
Last modified: May 27, 2015
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.