P22643 (DHLA_XANAU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Haloalkane dehalogenase
EC=3.8.1.5

Gene names

Name:

dhlA

Organism

Xanthobacter autotrophicus

Taxonomic identifier

280 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Xanthobacteraceae › Xanthobacter

Protein attributes

Sequence length	310 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 terminally mono- and di- chlorinated and brominated alkanes (up to C4 only). The highest activity was found with 1,2-dichloroethane, 1,3-dichloropropane, and 1,2-dibromoethane. HAMAP-Rule MF_01230
Catalytic activity	1-haloalkane + H2O = a primary alcohol + halide. HAMAP-Rule MF_01230 1,2-dichloroethane + H2O = 2-chloroethanol + hydrogen chloride. HAMAP-Rule MF_01230
Enzyme regulation	Inhibited by thiol reagents such as p-chloromercuribenzoate and iodoacetamide. HAMAP-Rule MF_01230
Pathway	Xenobiotic degradation; 1,2-dichloroethane degradation; glycolate from 1,2-dichloroethane: step 1/4. HAMAP-Rule MF_01230
Subunit structure	Monomer.
Sequence similarities	Belongs to the haloalkane dehalogenase family. Type 1 subfamily.
Biophysicochemical properties	pH dependence: Optimum pH is 8.2. HAMAP-Rule MF_01230 Temperature dependence: Optimum temperature is 37 degrees Celsius.

Ontologies

Keywords
Biological process	Detoxification
Molecular function	Hydrolase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	1,2-dichloroethane catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway 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 – 310

310

Haloalkane dehalogenase HAMAP-Rule MF_01230

PRO_0000216771

Sites

Active site

124

1

Nucleophile

Active site

260

1

Proton donor

Active site

289

1

Proton acceptor

Binding site

125

1

Halide

Binding site

175

1

Halide

Secondary structure

1

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310

Helix Strand Turn

Details...

Helix

9 – 12

4

Beta strand

23 – 27

5

Beta strand

35 – 42

8

Beta strand

49 – 52

4

Helix

60 – 63

4

Turn

64 – 66

3

Helix

67 – 72

6

Beta strand

76 – 80

5

Beta strand

90 – 92

3

Helix

94 – 96

3

Helix

99 – 113

15

Beta strand

117 – 122

6

Helix

125 – 130

6

Helix

134 – 136

3

Helix

138 – 140

3

Beta strand

141 – 148

8

Turn

155 – 157

3

Helix

160 – 163

4

Turn

164 – 166

3

Turn

169 – 171

3

Helix

172 – 180

9

Helix

187 – 194

8

Helix

200 – 207

8

Helix

213 – 215

3

Helix

217 – 227

11

Helix

231 – 246

16

Beta strand

250 – 257

8

Beta strand

261 – 264

4

Helix

265 – 274

10

Beta strand

282 – 284

3

Helix

291 – 294

4

Helix

295 – 308

14

Sequences

	Sequence		Length	Mass (Da)
	P22643 [UniParc]. Last modified February 1, 1995. Version 2. Checksum: FB32C94BE5D8940C	FASTA	310	35,144
	10 20 30 40 50 60 MINAIRTPDQ RFSNLDQYPF SPNYLDDLPG YPGLRAHYLD EGNSDAEDVF LCLHGEPTWS 70 80 90 100 110 120 YLYRKMIPVF AESGARVIAP DFFGFGKSDK PVDEEDYTFE FHRNFLLALI ERLDLRNITL 130 140 150 160 170 180 VVQDWGGFLG LTLPMADPSR FKRLIIMNAC LMTDPVTQPA FSAFVTQPAD GFTAWKYDLV 190 200 210 220 230 240 TPSDLRLDQF MKRWAPTLTE AEASAYAAPF PDTSYQAGVR KFPKMVAQRD QACIDISTEA 250 260 270 280 290 300 ISFWQNDWNG QTFMAIGMKD KLLGPDVMYP MKALINGCPE PLEIADAGHF VQEFGEQVAR 310 EALKHFAETE

References

[1]	"Cloning of 1,2-dichloroethane degradation genes of Xanthobacter autotrophicus GJ10 and expression and sequencing of the dhlA gene." Janssen D.B., Pries F., van der Ploeg J., Kazemier B., Terpstra P., Witholt B. J. Bacteriol. 171:6791-6799(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: GJ10.
[2]	"Purification and characterization of hydrolytic haloalkane dehalogenase from Xanthobacter autotrophicus GJ10." Keuning S., Janssen D.B., Witholt B. J. Bacteriol. 163:635-639(1985) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-10.
[3]	"Crystallization of haloalkane dehalogenase from Xanthobacter autotrophicus GJ10." Rozeboom H.J., Kingma J., Janssen D.B., Dijkstra B.W. J. Mol. Biol. 200:611-612(1988) [PubMed] [Europe PMC] [Abstract] Cited for: CRYSTALLIZATION. Strain: GJ10.
[4]	"Crystal structure of haloalkane dehalogenase: an enzyme to detoxify halogenated alkanes." Franken S.M., Rozeboom H.J., Kalk K.H., Dijkstra B.W. EMBO J. 10:1297-1302(1991) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), SEQUENCE REVISION TO 120. Strain: GJ10.
[5]	"Refined X-ray structures of haloalkane dehalogenase at pH 6.2 and pH 8.2 and implications for the reaction mechanism." Verschueren K.H.G., Franken S.M., Rozeboom H.J., Kalk K.H., Dijkstra B.W. J. Mol. Biol. 232:856-872(1993) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[6]	"Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase." Verschueren K.H.G., Seljee F., Rozeboom H.J., Kalk K.H., Dijkstra B.W. Nature 363:693-698(1993) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). Strain: GJ10.
[7]	"Kinetic analysis and X-ray structure of haloalkane dehalogenase with a modified halide-binding site." Krooshof G.H., Ridder I.S., Tepper A.W.J.W., Vos G.J., Rozeboom H.J., Kalk K.H., Dijkstra B.W., Janssen D.B. Biochemistry 37:15013-15023(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS).
[8]	"Crystallographic and kinetic evidence of a collision complex formed during halide import in haloalkane dehalogenase." Pikkemaat M.G., Ridder I.S., Rozeboom H.J., Kalk K.H., Dijkstra B.W., Janssen D.B. Biochemistry 38:12052-12061(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[9]	"Haloalkane dehalogenase from Xanthobacter autotrophicus GJ10 refined at 1.15 A resolution." Ridder I.S., Rozeboom H.J., Dijkstra B.W. Acta Crystallogr. D 55:1273-1290(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS). Strain: GJ10.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M26950 Genomic DNA. Translation: AAA88691.1.

PIR

B43718.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B6G	X-ray	1.15	A	3-310	[»]
1BE0	X-ray	1.96	A	3-310	[»]
1BEE	X-ray	2.60	A	3-310	[»]
1BEZ	X-ray	2.10	A	3-310	[»]
1CIJ	X-ray	2.30	A	3-310	[»]
1EDB	X-ray	2.01	A	1-310	[»]
1EDD	X-ray	2.19	A	1-310	[»]
1EDE	X-ray	1.90	A	1-310	[»]
1HDE	X-ray	2.70	A/B	1-310	[»]
2DHC	X-ray	2.30	A	1-310	[»]
2DHD	X-ray	2.13	A	1-310	[»]
2DHE	X-ray	2.13	A	1-310	[»]
2EDA	X-ray	2.19	A	1-310	[»]
2EDC	X-ray	2.30	A	1-310	[»]
2HAD	X-ray	1.90	A	1-310	[»]
2PKY	X-ray	1.55	X	1-310	[»]
2YXP	X-ray	1.53	X	1-310	[»]

ProteinModelPortal

P22643.

SMR

P22643. Positions 1-310.

ModBase

Search...

Protein family/group databases

MEROPS

S33.990.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

UniPathway

UPA00265; UER00387.

Family and domain databases

HAMAP

MF_01230. Haloalk_dehal_type1.

InterPro

IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
IPR023489. Haloalkane_dehalogenase_1.
[Graphical view]

Pfam

PF00561. Abhydrolase_1. 1 hit.
[Graphical view]

PRINTS

PR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.

ProtoNet

Search...

Other

EvolutionaryTrace

P22643.

Entry information

Entry name

DHLA_XANAU

Accession

Primary (citable) accession number: P22643

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	February 1, 1995
Last modified:	April 3, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program