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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)DescriptionActionsGraphical viewLength
Active sitei11NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000791622 – 231(S)-2-haloacid dehalogenase 4AAdd BLAST230

Structurei

Secondary structure

1231
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 10Combined sources4
Turni14 – 16Combined sources3
Helixi21 – 24Combined sources4
Helixi27 – 30Combined sources4
Helixi34 – 54Combined sources21
Helixi61 – 75Combined sources15
Helixi81 – 93Combined sources13
Helixi101 – 110Combined sources10
Beta strandi114 – 121Combined sources8
Helixi123 – 132Combined sources10
Helixi136 – 138Combined sources3
Beta strandi140 – 144Combined sources5
Helixi145 – 147Combined sources3
Helixi155 – 165Combined sources11
Helixi169 – 171Combined sources3
Beta strandi172 – 177Combined sources6
Helixi179 – 188Combined sources10
Beta strandi191 – 195Combined sources5
Beta strandi210 – 215Combined sources6
Helixi216 – 218Combined sources3
Helixi219 – 223Combined sources5

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ51645.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

CDDicd02588. HAD_L2-DEX. 1 hit.
Gene3Di1.10.150.240. 1 hit.
3.40.50.1000. 1 hit.
InterProiView protein in InterPro
IPR006328. 2-HAD.
IPR036412. HAD-like_sf.
IPR006439. HAD-SF_hydro_IA.
IPR023214. HAD_sf.
IPR023198. PGP_dom2.
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.

Similar proteinsi

Entry informationi

Entry nameiHAD4_BURCE
AccessioniPrimary (citable) accession number: Q51645
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: October 25, 2017
This is version 77 of the entry and version 3 of the sequence. See 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