P0A3G2 (DHAA_RHORH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Haloalkane dehalogenase
EC=3.8.1.5

Gene names

Name:

dhaA

Encoded on

Plasmid pRTL1

Organism

Rhodococcus rhodochrous

Taxonomic identifier

1829 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus

Protein attributes

Sequence length	293 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. HAMAP-Rule MF_01231
Catalytic activity	1-haloalkane + H2O = a primary alcohol + halide. HAMAP-Rule MF_01231
Pathway	Xenobiotic degradation; haloalkane degradation. HAMAP-Rule MF_01231
Subunit structure	Monomer.
Induction	By 1-haloalkanes. HAMAP-Rule MF_01231
Sequence similarities	Belongs to the haloalkane dehalogenase family. Type 2 subfamily.

Ontologies

Keywords
Biological process	Detoxification
Molecular function	Hydrolase
Technical term	3D-structure Plasmid
Gene Ontology (GO)
Biological_process	metabolic process Inferred from electronic annotation. Source: GOC response to toxin Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	haloalkane dehalogenase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 293

293

Haloalkane dehalogenase HAMAP-Rule MF_01231

PRO_0000216775

Sites

Active site

106

1

Nucleophile By similarity

Active site

130

1

Proton donor By similarity

Active site

272

1

Proton acceptor By similarity

Secondary structure

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293

Helix Strand Turn

Details...

Beta strand

13 – 17

5

Beta strand

20 – 28

9

Beta strand

30 – 32

3

Beta strand

35 – 38

4

Helix

45 – 48

4

Turn

49 – 51

3

Helix

52 – 55

4

Turn

56 – 58

3

Beta strand

61 – 64

4

Helix

81 – 94

14

Beta strand

99 – 105

7

Helix

106 – 118

13

Helix

120 – 122

3

Beta strand

123 – 130

8

Beta strand

135 – 137

3

Helix

138 – 140

3

Helix

143 – 145

3

Helix

146 – 152

7

Beta strand

154 – 156

3

Helix

157 – 162

6

Helix

167 – 170

4

Helix

172 – 175

4

Beta strand

177 – 179

3

Helix

183 – 190

8

Helix

191 – 193

3

Helix

196 – 199

4

Helix

200 – 208

9

Helix

216 – 231

16

Beta strand

236 – 243

8

Beta strand

245 – 247

3

Helix

249 – 258

10

Beta strand

262 – 272

11

Helix

274 – 277

4

Helix

279 – 289

11

Helix

291 – 293

3

Sequences

	Sequence		Length	Mass (Da)
	P0A3G2 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: 2B637C53E36BE9F3	FASTA	293	33,246
	10 20 30 40 50 60 MSEIGTGFPF DPHYVEVLGE RMHYVDVGPR DGTPVLFLHG NPTSSYLWRN IIPHVAPSHR 70 80 90 100 110 120 CIAPDLIGMG KSDKPDLDYF FDDHVRYLDA FIEALGLEEV VLVIHDWGSA LGFHWAKRNP 130 140 150 160 170 180 ERVKGIACME FIRPIPTWDE WPEFARETFQ AFRTADVGRE LIIDQNAFIE GALPKCVVRP 190 200 210 220 230 240 LTEVEMDHYR EPFLKPVDRE PLWRFPNELP IAGEPANIVA LVEAYMNWLH QSPVPKLLFW 250 260 270 280 290 GTPGVLIPPA EAARLAESLP NCKTVDIGPG LHYLQEDNPD LIGSEIARWL PAL

References

[1]	"The plasmid-located haloalkane dehalogenase gene from Rhodococcus rhodochrous NCIMB 13064." Kulakova A.N., Larkin M.J., Kulakov L.A. Microbiology 143:109-115(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: NCIMB 13064.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF060871 Genomic DNA. Translation: AAC15838.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2V9Z	X-ray	3.00	A	1-293	[»]
3FBW	X-ray	1.23	A	1-293	[»]
3RK4	X-ray	1.31	A	1-293	[»]
3SK0	X-ray	1.78	A	1-293	[»]
4E46	X-ray	1.26	A	1-293	[»]
4F5Z	X-ray	1.20	A	1-293	[»]
4F60	X-ray	1.45	A	1-293	[»]
4FWB	X-ray	1.26	A	4-293	[»]

ProteinModelPortal

P0A3G2.

SMR

P0A3G2. Positions 4-293.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

SABIO-RK

P0A3G2.

UniPathway

UPA00007.

Family and domain databases

HAMAP

MF_01231. Haloalk_dehal_type2.

InterPro

IPR000639. Epox_hydrolase-like.
IPR023594. Haloalkane_dehalogenase_2.
[Graphical view]

PRINTS

PR00412. EPOXHYDRLASE.

ProtoNet

Search...

Other

EvolutionaryTrace

P0A3G2.

Entry information

Entry name

DHAA_RHORH

Accession

Primary (citable) accession number: P0A3G2
Secondary accession number(s): Q53042

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	May 1, 2013
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program