Skip Header

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

P51698

- LINB_SPHPI

UniProt

P51698 - LINB_SPHPI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Haloalkane dehalogenase

Gene

linB

Organism
Sphingomonas paucimobilis (Pseudomonas paucimobilis)
Status
Reviewed - 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei38 – 381Halide
Active sitei108 – 1081Nucleophile
Binding sitei109 – 1091Halide
Active sitei132 – 1321Proton donor
Active sitei272 – 2721Proton acceptor

GO - Molecular functioni

  1. haloalkane dehalogenase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. response to toxic substance Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Detoxification

Enzyme and pathway databases

BioCyciMetaCyc:LINBPSEPA-MONOMER.
SABIO-RKP51698.
UniPathwayiUPA00689.

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

  1. periplasmic space Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi38 – 381N → D, E, F or Q: Loss of activity. 1 Publication
Mutagenesisi108 – 1081D → A: Loss of activity. 1 Publication
Mutagenesisi108 – 1081D → N: 58% of wild-type activity. 1 Publication
Mutagenesisi109 – 1091W → L: Loss of activity. 1 Publication
Mutagenesisi132 – 1321E → Q: Loss of activity. 1 Publication
Mutagenesisi151 – 1511F → L, W or Y: Increase in activity. 1 Publication
Mutagenesisi169 – 1691F → L: 31% of wild-type activity. 1 Publication
Mutagenesisi244 – 2441E → Q: 38% of wild-type activity. 1 Publication
Mutagenesisi272 – 2721H → A: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 296295Haloalkane dehalogenasePRO_0000216778Add
BLAST

Expressioni

Inductioni

Constitutively expressed.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
296
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 165Combined sources
Beta strandi19 – 279Combined sources
Beta strandi29 – 357Combined sources
Helixi42 – 454Combined sources
Turni46 – 483Combined sources
Helixi49 – 524Combined sources
Beta strandi55 – 617Combined sources
Turni77 – 804Combined sources
Helixi82 – 9514Combined sources
Beta strandi102 – 1076Combined sources
Helixi108 – 12013Combined sources
Helixi121 – 1244Combined sources
Beta strandi125 – 1328Combined sources
Helixi140 – 1423Combined sources
Helixi145 – 1473Combined sources
Helixi148 – 1558Combined sources
Helixi159 – 1635Combined sources
Turni164 – 1663Combined sources
Helixi168 – 1714Combined sources
Helixi173 – 1764Combined sources
Beta strandi178 – 1803Combined sources
Helixi184 – 1918Combined sources
Helixi192 – 1943Combined sources
Beta strandi196 – 1983Combined sources
Helixi199 – 2013Combined sources
Helixi202 – 2065Combined sources
Helixi208 – 2103Combined sources
Helixi218 – 23114Combined sources
Beta strandi238 – 2458Combined sources
Beta strandi247 – 2504Combined sources
Helixi251 – 2577Combined sources
Beta strandi261 – 27212Combined sources
Helixi274 – 2763Combined sources
Helixi279 – 29315Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP51698.
SMRiP51698. Positions 2-296.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51698.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
HAMAPiMF_01231. Haloalk_dehal_type2.
InterProiIPR029058. AB_hydrolase.
IPR000639. Epox_hydrolase-like.
IPR023594. Haloalkane_dehalogenase_2.
[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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti81 – 811A → T in strain: B90.
Natural varianti112 – 1121A → V in strain: B90.
Natural varianti134 – 1352IA → VT in strain: B90.
Natural varianti138 – 1381I → L in strain: B90.
Natural varianti247 – 2471A → H in strain: B90.
Natural varianti253 – 2531M → I in strain: B90.

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 .
PIRi A49896.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CV2 X-ray 1.58 A 1-296 [» ]
1D07 X-ray 2.00 A 1-296 [» ]
1G42 X-ray 1.80 A 1-296 [» ]
1G4H X-ray 1.80 A 1-296 [» ]
1G5F X-ray 1.80 A 1-296 [» ]
1IZ7 X-ray 1.58 A 2-296 [» ]
1IZ8 X-ray 2.00 A 2-296 [» ]
1K5P X-ray 1.80 A 2-296 [» ]
1K63 X-ray 1.80 A 2-296 [» ]
1K6E X-ray 1.85 A 2-296 [» ]
1MJ5 X-ray 0.95 A 1-296 [» ]
2BFN X-ray 1.60 A 1-296 [» ]
ProteinModelPortali P51698.
SMRi P51698. Positions 2-296.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00689 .
BioCyci MetaCyc:LINBPSEPA-MONOMER.
SABIO-RK P51698.

Miscellaneous databases

EvolutionaryTracei P51698.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
HAMAPi MF_01231. Haloalk_dehal_type2.
InterProi IPR029058. AB_hydrolase.
IPR000639. Epox_hydrolase-like.
IPR023594. Haloalkane_dehalogenase_2.
[Graphical view ]
PRINTSi PR00412. EPOXHYDRLASE.
SUPFAMi SSF53474. SSF53474. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Cloning and sequencing of a dehalogenase gene encoding an enzyme with hydrolase activity involved in the degradation of gamma-hexachlorocyclohexane in Pseudomonas paucimobilis."
    Nagata Y., Nariya T., Ohtomo R., Fukuda M., Yano K., Takagi M.
    J. Bacteriol. 175:6403-6410(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-16.
    Strain: UT26.
  2. Nagata Y., Nariya T., Ohtomo R., Fukuda M., Yano K., Takagi M.
    Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Cloning and characterization of lin genes responsible for the degradation of hexachlorocyclohexane isomers by Sphingomonas paucimobilis strain B90."
    Kumari R., Subudhi S., Suar M., Dhingra G., Raina V., Dogra C., Lal S., van der Meer J.R., Holliger C., Lal R.
    Appl. Environ. Microbiol. 68:6021-6028(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: B90.
  4. "Two different types of dehalogenases, LinA and LinB, involved in gamma-hexachlorocyclohexane degradation in Sphingomonas paucimobilis UT26 are localized in the periplasmic space without molecular processing."
    Nagata Y., Futamura A., Miyauchi K., Takagi M.
    J. Bacteriol. 181:5409-5413(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-10, SUBCELLULAR LOCATION.
  5. "Purification and characterization of a haloalkane dehalogenase of a new substrate class from a gamma-hexachlorocyclohexane-degrading bacterium, Sphingomonas paucimobilis UT26."
    Nagata Y., Miyauchi K., Damborsky J., Manova K., Ansorgova A., Takagi M.
    Appl. Environ. Microbiol. 63:3707-3710(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: UT26.
  6. "Identification of the catalytic triad in the haloalkane dehalogenase from Sphingomonas paucimobilis UT26."
    Hynkova K., Nagata Y., Takagi M., Damborsky J.
    FEBS Lett. 446:177-181(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-108; GLU-132; GLU-244 AND HIS-272.
    Strain: UT26.
  7. "Halide-stabilizing residues of haloalkane dehalogenases studied by quantum mechanic calculations and site-directed mutagenesis."
    Bohac M., Nagata Y., Prokop Z., Prokop M., Monincova M., Tsuda M., Koca J., Damborsky J.
    Biochemistry 41:14272-14280(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: QUANTUM MECHANIC STUDIES, MUTAGENESIS OF ASN-38; TRP-109; PHE-151 AND PHE-169.
  8. "Crystallization and preliminary X-ray diffraction analysis of haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26."
    Smatanova I.K., Nagata Y., Svensson L.A., Takagi M., Marek J.
    Acta Crystallogr. D 55:1231-1233(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
    Strain: UT26.
  9. "Crystal structure of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26."
    Marek J., Vevodova J., Smatanova I.K., Nagata Y., Svensson L.A., Newman J., Takagi M., Damborsky J.
    Biochemistry 39:14082-14086(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEX WITH 1,3-PROPANEDIOL.
    Strain: UT26.
  10. "Exploring the structure and activity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26: evidence for product- and water-mediated inhibition."
    Oakley A.J., Prokop Z., Bohac M., Kmunicek J., Jedlicka T., Monincova M., Kuta-Smatanova I., Nagata Y., Damborsky J., Wilce M.C.J.
    Biochemistry 41:4847-4855(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF COMPLEXES WITH 1,2-DICHLOROETHANE; 1,2-DICHLOROPROPANE AND BUTAN-1-OL.
    Strain: UT26.

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: October 29, 2014
This is version 84 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

External Data

Dasty 3