P59336 (DHAA_RHOSD) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Haloalkane dehalogenase
EC=3.8.1.5

Gene names

Name:

dhaA

Organism

Rhodococcus sp. (strain TDTM0003)

Taxonomic identifier

269091 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	294 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. Has a broad substrate specificity, which includes primary, secondary and cyclic haloalkanes (chain length > C4). HAMAP-Rule MF_01231
Catalytic activity	1-haloalkane + H2O = a primary alcohol + halide. HAMAP-Rule MF_01231
Subunit structure	Monomer By similarity.
Sequence similarities	Belongs to the haloalkane dehalogenase family. Type 2 subfamily.

Ontologies

Keywords
Molecular function	Hydrolase
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	metabolic process Inferred from electronic annotation. Source: GOC
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 – 294

294

Haloalkane dehalogenase HAMAP-Rule MF_01231

PRO_0000216777

Sites

Active site

106

1

Nucleophile

Active site

130

1

Proton donor

Active site

272

1

Proton acceptor

Binding site

41

1

Halide

Binding site

107

1

Halide

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

294

Helix Strand Turn

Details...

Beta strand

13 – 17

5

Beta strand

20 – 28

9

Beta strand

30 – 33

4

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

107 – 118

12

Helix

120 – 122

3

Beta strand

123 – 130

8

Helix

138 – 140

3

Helix

143 – 152

10

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 – 276

3

Helix

279 – 289

11

Helix

290 – 293

4

Sequences

	Sequence		Length	Mass (Da)
	P59336 [UniParc]. Last modified February 22, 2003. Version 1. Checksum: 190E6B9944E5DBEF	FASTA	294	33,331
	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 GVLPKCVVRP 190 200 210 220 230 240 LTEVEMDHYR EPFLKPVDRE PLWRFPNEIP IAGEPANIVA LVEAYMNWLH QSPVPKLLFW 250 260 270 280 290 GTPGVLIPPA EAARLAESLP NCKTVDIGPG LHYLQEDNPD LIGSEIARWL PGLA

References

[1]

"Haloalkane dehalogenases: structure of a Rhodococcus enzyme." Newman J., Peat T.S., Richard R., Kan L., Swanson P.E., Affholter J.A., Holmes I.H., Schindler J.F., Unkefer C.J., Terwilliger T.C. Biochemistry 38:16105-16114(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BN6	X-ray	1.50	A	1-294	[»]
1BN7	X-ray	1.50	A	1-294	[»]
1CQW	X-ray	1.50	A	4-294	[»]

ProteinModelPortal

P59336.

SMR

P59336. Positions 4-294.

ModBase

Search...

Protein family/group databases

MEROPS

S33.990.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

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

P59336.

Entry information

Entry name

DHAA_RHOSD

Accession

Primary (citable) accession number: P59336

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 22, 2003
Last sequence update:	February 22, 2003
Last modified:	April 3, 2013
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program