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Protein

Haloalkane dehalogenase

Gene

dhlA

Organism
Xanthobacter autotrophicus
Status
Reviewed-Annotation score: Annotation score: 5 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. 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.

Catalytic activityi

1-haloalkane + H2O = a primary alcohol + halide.
1,2-dichloroethane + H2O = 2-chloroethanol + hydrogen chloride.

Enzyme regulationi

Inhibited by thiol reagents such as p-chloromercuribenzoate and iodoacetamide.

pH dependencei

Optimum pH is 8.2.

Temperature dependencei

Optimum temperature is 37 degrees Celsius.

Pathwayi: 1,2-dichloroethane degradation

This protein is involved in step 1 of the subpathway that synthesizes glycolate from 1,2-dichloroethane.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Haloalkane dehalogenase (dhlA)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. no protein annotated in this organism
This subpathway is part of the pathway 1,2-dichloroethane degradation, which is itself part of Xenobiotic degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes glycolate from 1,2-dichloroethane, the pathway 1,2-dichloroethane degradation and in Xenobiotic degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei124Nucleophile1
Binding sitei125Halide1
Binding sitei175Halide1
Active sitei260Proton donor1
Active sitei289Proton acceptor1

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. 1641.
UniPathwayiUPA00265; UER00387.

Protein family/group databases

ESTHERixanau-halo1. Haloalkane_dehalogenase-HLD1.
MEROPSiS33.990.

Names & Taxonomyi

Protein namesi
Recommended name:
Haloalkane dehalogenase (EC:3.8.1.5)
Gene namesi
Name:dhlA
OrganismiXanthobacter autotrophicus
Taxonomic identifieri280 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesXanthobacteraceaeXanthobacter

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002167711 – 310Haloalkane dehalogenaseAdd BLAST310

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1310
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 12Combined sources4
Beta strandi23 – 27Combined sources5
Beta strandi35 – 42Combined sources8
Beta strandi49 – 52Combined sources4
Helixi60 – 63Combined sources4
Turni64 – 66Combined sources3
Helixi67 – 72Combined sources6
Beta strandi76 – 80Combined sources5
Beta strandi90 – 92Combined sources3
Helixi94 – 96Combined sources3
Helixi99 – 113Combined sources15
Beta strandi117 – 122Combined sources6
Helixi125 – 130Combined sources6
Helixi134 – 136Combined sources3
Helixi138 – 140Combined sources3
Beta strandi141 – 148Combined sources8
Turni155 – 157Combined sources3
Helixi160 – 163Combined sources4
Turni164 – 166Combined sources3
Turni169 – 171Combined sources3
Helixi172 – 180Combined sources9
Helixi187 – 194Combined sources8
Helixi200 – 207Combined sources8
Helixi213 – 215Combined sources3
Helixi217 – 227Combined sources11
Helixi231 – 246Combined sources16
Beta strandi250 – 257Combined sources8
Beta strandi261 – 264Combined sources4
Helixi265 – 274Combined sources10
Beta strandi282 – 284Combined sources3
Helixi291 – 294Combined sources4
Helixi295 – 308Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B6GX-ray1.15A3-310[»]
1BE0X-ray1.96A3-310[»]
1BEEX-ray2.60A3-310[»]
1BEZX-ray2.10A3-310[»]
1CIJX-ray2.30A3-310[»]
1EDBX-ray2.01A1-310[»]
1EDDX-ray2.19A1-310[»]
1EDEX-ray1.90A1-310[»]
1HDEX-ray2.70A/B1-310[»]
2DHCX-ray2.30A1-310[»]
2DHDX-ray2.13A1-310[»]
2DHEX-ray2.13A1-310[»]
2EDAX-ray2.19A1-310[»]
2EDCX-ray2.30A1-310[»]
2HADX-ray1.90A1-310[»]
2PKYX-ray1.55X1-310[»]
2YXPX-ray1.53X1-310[»]
ProteinModelPortaliP22643.
SMRiP22643.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22643.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini49 – 295AB hydrolase-1Sequence analysisAdd BLAST247

Sequence similaritiesi

Phylogenomic databases

KOiK01563.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
HAMAPiMF_01230. Haloalk_dehal_type1. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
IPR023489. Haloalkane_dehalogenase_1.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

P22643-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MINAIRTPDQ RFSNLDQYPF SPNYLDDLPG YPGLRAHYLD EGNSDAEDVF
60 70 80 90 100
LCLHGEPTWS YLYRKMIPVF AESGARVIAP DFFGFGKSDK PVDEEDYTFE
110 120 130 140 150
FHRNFLLALI ERLDLRNITL VVQDWGGFLG LTLPMADPSR FKRLIIMNAC
160 170 180 190 200
LMTDPVTQPA FSAFVTQPAD GFTAWKYDLV TPSDLRLDQF MKRWAPTLTE
210 220 230 240 250
AEASAYAAPF PDTSYQAGVR KFPKMVAQRD QACIDISTEA ISFWQNDWNG
260 270 280 290 300
QTFMAIGMKD KLLGPDVMYP MKALINGCPE PLEIADAGHF VQEFGEQVAR
310
EALKHFAETE
Length:310
Mass (Da):35,144
Last modified:February 1, 1995 - v2
Checksum:iFB32C94BE5D8940C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M26950 Genomic DNA. Translation: AAA88691.1.
PIRiB43718.

Genome annotation databases

KEGGiag:AAA88691.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M26950 Genomic DNA. Translation: AAA88691.1.
PIRiB43718.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B6GX-ray1.15A3-310[»]
1BE0X-ray1.96A3-310[»]
1BEEX-ray2.60A3-310[»]
1BEZX-ray2.10A3-310[»]
1CIJX-ray2.30A3-310[»]
1EDBX-ray2.01A1-310[»]
1EDDX-ray2.19A1-310[»]
1EDEX-ray1.90A1-310[»]
1HDEX-ray2.70A/B1-310[»]
2DHCX-ray2.30A1-310[»]
2DHDX-ray2.13A1-310[»]
2DHEX-ray2.13A1-310[»]
2EDAX-ray2.19A1-310[»]
2EDCX-ray2.30A1-310[»]
2HADX-ray1.90A1-310[»]
2PKYX-ray1.55X1-310[»]
2YXPX-ray1.53X1-310[»]
ProteinModelPortaliP22643.
SMRiP22643.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERixanau-halo1. Haloalkane_dehalogenase-HLD1.
MEROPSiS33.990.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAA88691.

Phylogenomic databases

KOiK01563.

Enzyme and pathway databases

UniPathwayiUPA00265; UER00387.
BRENDAi3.8.1.5. 1641.

Miscellaneous databases

EvolutionaryTraceiP22643.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
HAMAPiMF_01230. Haloalk_dehal_type1. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
IPR023489. Haloalkane_dehalogenase_1.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDHLA_XANAU
AccessioniPrimary (citable) accession number: P22643
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: February 1, 1995
Last modified: November 2, 2016
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.