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Protein

(S)-2-haloacid dehalogenase

Gene
N/A
Organism
Pseudomonas sp. (strain YL)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolytic dehalogenation of small (S)-2-haloalkanoic acids to yield the corresponding (R)-2-hydroxyalkanoic acids. Acts on acids of short chain lengths, C2 to C4, with inversion of configuration at C-2.

Catalytic activityi

(S)-2-haloacid + H2O = (R)-2-hydroxyacid + halide.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei10 – 101Nucleophile

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
(S)-2-haloacid dehalogenase (EC:3.8.1.2)
Alternative name(s):
2-haloalkanoic acid dehalogenase
Halocarboxylic acid halidohydrolase
L-2-haloacid dehalogenase
L-DEX
OrganismiPseudomonas sp. (strain YL)
Taxonomic identifieri66693 [NCBI]
Taxonomic lineageiBacteriaProteobacteria

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi10 – 101D → A, E, G, N or S: Loss of activity. 1 Publication
Mutagenesisi180 – 1801D → E, G, N or S: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 232232(S)-2-haloacid dehalogenasePRO_0000079166Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
232
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 94Combined sources
Turni13 – 153Combined sources
Helixi19 – 2810Combined sources
Turni30 – 323Combined sources
Helixi33 – 5422Combined sources
Helixi60 – 7516Combined sources
Helixi81 – 899Combined sources
Helixi90 – 934Combined sources
Helixi100 – 10910Combined sources
Beta strandi113 – 1208Combined sources
Helixi122 – 13110Combined sources
Helixi135 – 1373Combined sources
Beta strandi139 – 1446Combined sources
Helixi145 – 1473Combined sources
Helixi154 – 16411Combined sources
Helixi168 – 1703Combined sources
Beta strandi171 – 1766Combined sources
Helixi178 – 18710Combined sources
Beta strandi191 – 1944Combined sources
Beta strandi203 – 2053Combined sources
Beta strandi209 – 2146Combined sources
Helixi215 – 2195Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JUDX-ray2.50A1-232[»]
1QH9X-ray2.50A1-232[»]
1ZRMX-ray2.00A1-232[»]
1ZRNX-ray1.83A1-232[»]
ProteinModelPortaliQ53464.
SMRiQ53464. Positions 3-222.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ53464.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di1.10.150.240. 1 hit.
3.40.50.1000. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
IPR006328. HAD_II.
IPR023198. PGP_dom2.
[Graphical view]
PfamiPF13419. HAD_2. 1 hit.
[Graphical view]
PRINTSiPR00413. HADHALOGNASE.
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01493. HAD-SF-IA-v2. 1 hit.
TIGR01428. HAD_type_II. 1 hit.

Sequencei

Sequence statusi: Complete.

Q53464-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDYIKGIAFD LYGTLFDVHS VVGRCDEAFP GRGREISALW RQKQLEYTWL
60 70 80 90 100
RSLMNRYVNF QQATEDALRF TCRHLGLDLD ARTRSTLCDA YLRLAPFSEV
110 120 130 140 150
PDSLRELKRR GLKLAILSNG SPQSIDAVVS HAGLRDGFDH LLSVDPVQVY
160 170 180 190 200
KPDNRVYELA EQALGLDRSA ILFVSSNAWD ATGARYFGFP TCWINRTGNV
210 220 230
FEEMGQTPDW EVTSLRAVVE LFETAAGKAE KG
Length:232
Mass (Da):26,177
Last modified:November 1, 1996 - v1
Checksum:iD276B5164B02E2C1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S74078 Genomic DNA. Translation: AAB32245.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S74078 Genomic DNA. Translation: AAB32245.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JUDX-ray2.50A1-232[»]
1QH9X-ray2.50A1-232[»]
1ZRMX-ray2.00A1-232[»]
1ZRNX-ray1.83A1-232[»]
ProteinModelPortaliQ53464.
SMRiQ53464. Positions 3-222.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ53464.

Family and domain databases

Gene3Di1.10.150.240. 1 hit.
3.40.50.1000. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
IPR006328. HAD_II.
IPR023198. PGP_dom2.
[Graphical view]
PfamiPF13419. HAD_2. 1 hit.
[Graphical view]
PRINTSiPR00413. HADHALOGNASE.
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01493. HAD-SF-IA-v2. 1 hit.
TIGR01428. HAD_type_II. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Comparative studies of genes encoding thermostable L-2-halo acid dehalogenase from Pseudomonas sp. strain YL, other dehalogenases, and two related hypothetical proteins from Escherichia coli."
    Nardi-Dei V., Kurihara T., Okamura T., Liu J.Q., Koshikawa H., Ozaki H., Terashima Y., Esaki N., Soda K.
    Appl. Environ. Microbiol. 60:3375-3380(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Comprehensive site-directed mutagenesis of L-2-halo acid dehalogenase to probe catalytic amino acid residues."
    Kurihara T., Liu J.-Q., Nardi-Dei V., Koshikawa H., Esaki N., Soda K.
    J. Biochem. 117:1317-1322(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  3. "Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An alpha/beta hydrolase structure that is different from the alpha/beta hydrolase fold."
    Hisano T., Hata Y., Fujii T., Liu J.-Q., Kurihara T., Esaki N., Soda K.
    J. Biol. Chem. 271:20322-20330(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  4. "Crystal structures of reaction intermediates of L-2-haloacid dehalogenase and implications for the reaction mechanism."
    Li Y.F., Hata Y., Fujii T., Hisano T., Nishihara M., Kurihara T., Esaki N.
    J. Biol. Chem. 273:15035-15044(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Entry informationi

Entry nameiHAD_PSEUY
AccessioniPrimary (citable) accession number: Q53464
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.