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Protein

Haloalkane dehalogenase

Gene

dhaA

Organism
Rhodococcus rhodochrous
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. Expresses halogenase activity against 1-chloroalkanes of chain length C3 to C10, and also shows a very weak activity with 1,2-dichloroethane.

Catalytic activityi

1-haloalkane + H2O = a primary alcohol + halide.

Pathwayi: haloalkane degradation

This protein is involved in the pathway haloalkane degradation, which is part of Xenobiotic degradation.
View all proteins of this organism that are known to be involved in the pathway haloalkane degradation and in Xenobiotic degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei106NucleophileBy similarity1
Active sitei130Proton donorBy similarity1
Active sitei272Proton acceptorBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Detoxification

Enzyme and pathway databases

BRENDAi3.8.1.5. 5395.
SABIO-RKP0A3G2.
UniPathwayiUPA00007.

Protein family/group databases

ESTHERirhoso-halo1. Haloalkane_dehalogenase-HLD2.

Names & Taxonomyi

Protein namesi
Recommended name:
Haloalkane dehalogenase (EC:3.8.1.5)
Gene namesi
Name:dhaA
Encoded oniPlasmid pRTL10 Publication
OrganismiRhodococcus rhodochrous
Taxonomic identifieri1829 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesNocardiaceaeRhodococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002167751 – 293Haloalkane dehalogenaseAdd BLAST293

Expressioni

Inductioni

By 1-haloalkanes.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1293
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi13 – 17Combined sources5
Beta strandi20 – 28Combined sources9
Beta strandi30 – 32Combined sources3
Beta strandi35 – 38Combined sources4
Helixi45 – 48Combined sources4
Turni49 – 51Combined sources3
Helixi52 – 55Combined sources4
Turni56 – 58Combined sources3
Beta strandi61 – 64Combined sources4
Helixi81 – 94Combined sources14
Beta strandi99 – 105Combined sources7
Helixi106 – 118Combined sources13
Helixi120 – 122Combined sources3
Beta strandi123 – 130Combined sources8
Beta strandi135 – 137Combined sources3
Helixi138 – 140Combined sources3
Helixi143 – 145Combined sources3
Helixi146 – 152Combined sources7
Beta strandi154 – 156Combined sources3
Helixi157 – 162Combined sources6
Helixi167 – 170Combined sources4
Helixi172 – 175Combined sources4
Beta strandi177 – 179Combined sources3
Helixi183 – 190Combined sources8
Helixi191 – 193Combined sources3
Helixi196 – 199Combined sources4
Helixi200 – 208Combined sources9
Helixi216 – 231Combined sources16
Beta strandi236 – 243Combined sources8
Beta strandi245 – 247Combined sources3
Helixi249 – 258Combined sources10
Beta strandi262 – 272Combined sources11
Helixi274 – 277Combined sources4
Helixi279 – 289Combined sources11
Helixi291 – 293Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2V9ZX-ray3.00A1-11[»]
A142-293[»]
3FBWX-ray1.23A1-293[»]
3RK4X-ray1.31A1-293[»]
3SK0X-ray1.78A1-293[»]
4E46X-ray1.26A1-293[»]
4F5ZX-ray1.20A1-293[»]
4F60X-ray1.45A1-293[»]
4FWBX-ray1.26A4-293[»]
4WCVX-ray1.69A1-293[»]
ProteinModelPortaliP0A3G2.
SMRiP0A3G2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A3G2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini34 – 158AB hydrolase-1Sequence analysisAdd BLAST125

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
HAMAPiMF_01231. Haloalk_dehal_type2. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
IPR023594. Haloalkane_dehalogenase_2.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PRINTSiPR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A3G2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEIGTGFPF DPHYVEVLGE RMHYVDVGPR DGTPVLFLHG NPTSSYLWRN
60 70 80 90 100
IIPHVAPSHR CIAPDLIGMG KSDKPDLDYF FDDHVRYLDA FIEALGLEEV
110 120 130 140 150
VLVIHDWGSA LGFHWAKRNP ERVKGIACME FIRPIPTWDE WPEFARETFQ
160 170 180 190 200
AFRTADVGRE LIIDQNAFIE GALPKCVVRP LTEVEMDHYR EPFLKPVDRE
210 220 230 240 250
PLWRFPNELP IAGEPANIVA LVEAYMNWLH QSPVPKLLFW GTPGVLIPPA
260 270 280 290
EAARLAESLP NCKTVDIGPG LHYLQEDNPD LIGSEIARWL PAL
Length:293
Mass (Da):33,246
Last modified:March 15, 2005 - v1
Checksum:i2B637C53E36BE9F3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF060871 Genomic DNA. Translation: AAC15838.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF060871 Genomic DNA. Translation: AAC15838.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2V9ZX-ray3.00A1-11[»]
A142-293[»]
3FBWX-ray1.23A1-293[»]
3RK4X-ray1.31A1-293[»]
3SK0X-ray1.78A1-293[»]
4E46X-ray1.26A1-293[»]
4F5ZX-ray1.20A1-293[»]
4F60X-ray1.45A1-293[»]
4FWBX-ray1.26A4-293[»]
4WCVX-ray1.69A1-293[»]
ProteinModelPortaliP0A3G2.
SMRiP0A3G2.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERirhoso-halo1. Haloalkane_dehalogenase-HLD2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00007.
BRENDAi3.8.1.5. 5395.
SABIO-RKP0A3G2.

Miscellaneous databases

EvolutionaryTraceiP0A3G2.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
HAMAPiMF_01231. Haloalk_dehal_type2. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
IPR023594. Haloalkane_dehalogenase_2.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PRINTSiPR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDHAA_RHORH
AccessioniPrimary (citable) accession number: P0A3G2
Secondary accession number(s): Q53042
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: November 2, 2016
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Plasmid

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.