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Protein

(S)-2-haloacid dehalogenase 4A

Gene

hdl IVa

Organism
Burkholderia cepacia (Pseudomonas cepacia)
Status
Reviewed-Annotation score: Annotation score: 3 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-3.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei11 – 111NucleophileBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BRENDAi3.8.1.2. 1028.

Names & Taxonomyi

Protein namesi
Recommended name:
(S)-2-haloacid dehalogenase 4A (EC:3.8.1.2)
Alternative name(s):
2-haloalkanoic acid dehalogenase IVA
Halocarboxylic acid halidohydrolase IVA
L-2-haloacid dehalogenase IVA
Gene namesi
Name:hdl IVa
OrganismiBurkholderia cepacia (Pseudomonas cepacia)
Taxonomic identifieri292 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 231230(S)-2-haloacid dehalogenase 4APRO_0000079162Add
BLAST

Structurei

Secondary structure

1
231
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 104Combined sources
Turni14 – 163Combined sources
Helixi21 – 244Combined sources
Helixi27 – 304Combined sources
Helixi34 – 5421Combined sources
Helixi61 – 7515Combined sources
Helixi81 – 9313Combined sources
Helixi101 – 11010Combined sources
Beta strandi114 – 1218Combined sources
Helixi123 – 13210Combined sources
Helixi136 – 1383Combined sources
Beta strandi140 – 1445Combined sources
Helixi145 – 1473Combined sources
Helixi155 – 16511Combined sources
Helixi169 – 1713Combined sources
Beta strandi172 – 1776Combined sources
Helixi179 – 18810Combined sources
Beta strandi191 – 1955Combined sources
Beta strandi210 – 2156Combined sources
Helixi216 – 2183Combined sources
Helixi219 – 2235Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NO4X-ray1.93A/B2-231[»]
2NO5X-ray2.60A/B2-231[»]
ProteinModelPortaliQ51645.
SMRiQ51645. Positions 1-226.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ51645.

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.
TIGRFAMsiTIGR01549. HAD-SF-IA-v1. 1 hit.
TIGR01493. HAD-SF-IA-v2. 1 hit.
TIGR01509. HAD-SF-IA-v3. 1 hit.
TIGR01428. HAD_type_II. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q51645-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVDSLRACVF DAYGTLLDVH SAVMRNADEV GASAEALSML WRQRQLEYSW
60 70 80 90 100
TRTLMHQYAD FWQLTDEALT FALRTYHLED RKGLKDRLMS AYKELSAYPD
110 120 130 140 150
AAETLEKLKS AGYIVAILSN GNDEMLQAAL KASKLDRVLD SCLSADDLKI
160 170 180 190 200
YKPDPRIYQF ACDRLGVNPN EVCFVSSNAW DLGGAGKFGF NTVRINRQGN
210 220 230
PPEYEFAPLK HQVNSLSELW PLLAKNVTKA A
Length:231
Mass (Da):25,995
Last modified:January 23, 2007 - v3
Checksum:i75EBC85604B5F93C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66249 Genomic DNA. Translation: CAA46976.1.
PIRiS29096.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66249 Genomic DNA. Translation: CAA46976.1.
PIRiS29096.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NO4X-ray1.93A/B2-231[»]
2NO5X-ray2.60A/B2-231[»]
ProteinModelPortaliQ51645.
SMRiQ51645. Positions 1-226.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.8.1.2. 1028.

Miscellaneous databases

EvolutionaryTraceiQ51645.

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.
TIGRFAMsiTIGR01549. HAD-SF-IA-v1. 1 hit.
TIGR01493. HAD-SF-IA-v2. 1 hit.
TIGR01509. HAD-SF-IA-v3. 1 hit.
TIGR01428. HAD_type_II. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Molecular biology of the 2-haloacid halidohydrolase IVa from Pseudomonas cepacia MBA4."
    Murdiyatmo U., Asmara W., Tsang J.S.H., Baines A.J., Bull A.T., Hardman D.J.
    Biochem. J. 284:87-93(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-14.
    Strain: MBA4.

Entry informationi

Entry nameiHAD4_BURCE
AccessioniPrimary (citable) accession number: Q51645
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: October 14, 2015
This is version 71 of the entry and version 3 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. 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.