Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Haloalkane dehalogenase

Gene

linB

Organism
Sphingomonas paucimobilis (Pseudomonas paucimobilis)
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 since not only monochloroalkanes (C3 to C10) but also dichloroalkanes (> C3), bromoalkanes, and chlorinated aliphatic alcohols were good substrates. Shows almost no activity with 1,2-dichloroethane, but very high activity with the brominated analog. Is involved in the degradation of the important environmental pollutant gamma-hexachlorocyclohexane (lindane) as it also catalyzes conversion of 1,3,4,6-tetrachloro-1,4-cyclohexadiene (1,4-TCDN) to 2,5-dichloro-2,5-cyclohexadiene-1,4-diol (2,5-DDOL) via the intermediate 2,4,5-trichloro-2,5-cyclohexadiene-1-ol (2,4,5-DNOL).

Catalytic activityi

1-haloalkane + H2O = a primary alcohol + halide.
1,4-TCDN + 2 H2O = 2,5-DDOL + 2 chloride.

Enzyme regulationi

Competitively inhibited by the key pollutants 1,2-dichloroethane (1,2-DCE) and 1,2-dichloropropane (1,2-DCP).

pH dependencei

Optimum pH is 8.2.

Pathwayi: gamma-hexachlorocyclohexane degradation

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei38Halide1
Active sitei108Nucleophile1
Binding sitei109Halide1
Active sitei132Proton donor1
Active sitei272Proton acceptor1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Detoxification

Enzyme and pathway databases

BioCyciMetaCyc:LINBPSEPA-MONOMER.
BRENDAi3.8.1.5. 2280.
SABIO-RKP51698.
UniPathwayiUPA00689.

Protein family/group databases

ESTHERisphpi-linb. Haloalkane_dehalogenase-HLD2.

Names & Taxonomyi

Protein namesi
Recommended name:
Haloalkane dehalogenase (EC:3.8.1.5)
Alternative name(s):
1,3,4,6-tetrachloro-1,4-cyclohexadiene hydrolase
1,4-TCDN chlorohydrolase
Gene namesi
Name:linB
OrganismiSphingomonas paucimobilis (Pseudomonas paucimobilis)
Taxonomic identifieri13689 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeSphingomonas

Subcellular locationi

  • Periplasm 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi38N → D, E, F or Q: Loss of activity. 1 Publication1
Mutagenesisi108D → A: Loss of activity. 1 Publication1
Mutagenesisi108D → N: 58% of wild-type activity. 1 Publication1
Mutagenesisi109W → L: Loss of activity. 1 Publication1
Mutagenesisi132E → Q: Loss of activity. 1 Publication1
Mutagenesisi151F → L, W or Y: Increase in activity. 1 Publication1
Mutagenesisi169F → L: 31% of wild-type activity. 1 Publication1
Mutagenesisi244E → Q: 38% of wild-type activity. 1 Publication1
Mutagenesisi272H → A: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00002167782 – 296Haloalkane dehalogenaseAdd BLAST295

Expressioni

Inductioni

Constitutively expressed.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1296
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi12 – 16Combined sources5
Beta strandi19 – 27Combined sources9
Beta strandi29 – 35Combined sources7
Helixi42 – 45Combined sources4
Turni46 – 48Combined sources3
Helixi49 – 52Combined sources4
Beta strandi55 – 61Combined sources7
Turni77 – 80Combined sources4
Helixi82 – 95Combined sources14
Beta strandi102 – 107Combined sources6
Helixi108 – 120Combined sources13
Helixi121 – 124Combined sources4
Beta strandi125 – 132Combined sources8
Helixi140 – 142Combined sources3
Helixi145 – 147Combined sources3
Helixi148 – 155Combined sources8
Helixi159 – 163Combined sources5
Turni164 – 166Combined sources3
Helixi168 – 171Combined sources4
Helixi173 – 176Combined sources4
Beta strandi178 – 180Combined sources3
Helixi184 – 191Combined sources8
Helixi192 – 194Combined sources3
Beta strandi196 – 198Combined sources3
Helixi199 – 201Combined sources3
Helixi202 – 206Combined sources5
Helixi208 – 210Combined sources3
Helixi218 – 231Combined sources14
Beta strandi238 – 245Combined sources8
Beta strandi247 – 250Combined sources4
Helixi251 – 257Combined sources7
Beta strandi261 – 272Combined sources12
Helixi274 – 276Combined sources3
Helixi279 – 293Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CV2X-ray1.58A1-296[»]
1D07X-ray2.00A1-296[»]
1G42X-ray1.80A1-296[»]
1G4HX-ray1.80A1-296[»]
1G5FX-ray1.80A1-296[»]
1IZ7X-ray1.58A2-296[»]
1IZ8X-ray2.00A2-296[»]
1K5PX-ray1.80A2-296[»]
1K63X-ray1.80A2-296[»]
1K6EX-ray1.85A2-296[»]
1MJ5X-ray0.95A1-296[»]
2BFNX-ray1.60A1-296[»]
4WDQX-ray1.58A2-296[»]
ProteinModelPortaliP51698.
SMRiP51698.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51698.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 155AB 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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P51698-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLGAKPFGE KKFIEIKGRR MAYIDEGTGD PILFQHGNPT SSYLWRNIMP
60 70 80 90 100
HCAGLGRLIA CDLIGMGDSD KLDPSGPERY AYAEHRDYLD ALWEALDLGD
110 120 130 140 150
RVVLVVHDWG SALGFDWARR HRERVQGIAY MEAIAMPIEW ADFPEQDRDL
160 170 180 190 200
FQAFRSQAGE ELVLQDNVFV EQVLPGLILR PLSEAEMAAY REPFLAAGEA
210 220 230 240 250
RRPTLSWPRQ IPIAGTPADV VAIARDYAGW LSESPIPKLF INAEPGALTT
260 270 280 290
GRMRDFCRTW PNQTEITVAG AHFIQEDSPD EIGAAIAAFV RRLRPA
Length:296
Mass (Da):33,108
Last modified:January 23, 2007 - v4
Checksum:i6EEE011B157DBAE1
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti81A → T in strain: B90. 1
Natural varianti112A → V in strain: B90. 1
Natural varianti134 – 135IA → VT in strain: B90. 2
Natural varianti138I → L in strain: B90. 1
Natural varianti247A → H in strain: B90. 1
Natural varianti253M → I in strain: B90. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14594 Genomic DNA. Translation: BAA03443.2.
AY150581 Genomic DNA. Translation: AAN64241.1.
PIRiA49896.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14594 Genomic DNA. Translation: BAA03443.2.
AY150581 Genomic DNA. Translation: AAN64241.1.
PIRiA49896.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CV2X-ray1.58A1-296[»]
1D07X-ray2.00A1-296[»]
1G42X-ray1.80A1-296[»]
1G4HX-ray1.80A1-296[»]
1G5FX-ray1.80A1-296[»]
1IZ7X-ray1.58A2-296[»]
1IZ8X-ray2.00A2-296[»]
1K5PX-ray1.80A2-296[»]
1K63X-ray1.80A2-296[»]
1K6EX-ray1.85A2-296[»]
1MJ5X-ray0.95A1-296[»]
2BFNX-ray1.60A1-296[»]
4WDQX-ray1.58A2-296[»]
ProteinModelPortaliP51698.
SMRiP51698.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERisphpi-linb. Haloalkane_dehalogenase-HLD2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00689.
BioCyciMetaCyc:LINBPSEPA-MONOMER.
BRENDAi3.8.1.5. 2280.
SABIO-RKP51698.

Miscellaneous databases

EvolutionaryTraceiP51698.

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 nameiLINB_SPHPI
AccessioniPrimary (citable) accession number: P51698
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 93 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Is not N-terminally processed during export, so it may be secreted into the periplasmic space via a hitherto unknown mechanism.

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.