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Protein

(S)-2-haloacid dehalogenase

Gene

dhlB

Organism
Xanthobacter autotrophicus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolytic dehalogenation of small L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. Active with 2-halogenated carboxylic acids and converts only the L-isomer of 2-chloropropionic acid with inversion of configuration to produce D-lactate.

Catalytic activityi

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

pH dependencei

Optimum pH is 9.5.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei8Nucleophile1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BRENDAi3.8.1.2. 1641.

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
Gene namesi
Name:dhlB
OrganismiXanthobacter autotrophicus
Taxonomic identifieri280 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesXanthobacteraceaeXanthobacter

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000791591 – 253(S)-2-haloacid dehalogenaseAdd BLAST253

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1253
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 7Combined sources4
Turni11 – 13Combined sources3
Turni16 – 19Combined sources4
Helixi20 – 26Combined sources7
Helixi31 – 52Combined sources22
Helixi58 – 72Combined sources15
Helixi79 – 86Combined sources8
Helixi87 – 90Combined sources4
Helixi98 – 105Combined sources8
Beta strandi108 – 116Combined sources9
Helixi118 – 127Combined sources10
Helixi131 – 133Combined sources3
Beta strandi135 – 139Combined sources5
Helixi140 – 143Combined sources4
Helixi150 – 160Combined sources11
Helixi164 – 166Combined sources3
Beta strandi167 – 172Combined sources6
Helixi174 – 183Combined sources10
Beta strandi186 – 190Combined sources5
Helixi195 – 201Combined sources7
Beta strandi204 – 206Combined sources3
Helixi209 – 217Combined sources9
Beta strandi228 – 233Combined sources6
Helixi234 – 236Combined sources3
Helixi237 – 244Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AQ6X-ray1.95A/B1-253[»]
1QQ5X-ray1.52A/B1-253[»]
1QQ6X-ray2.10A/B1-253[»]
1QQ7X-ray1.70A/B1-253[»]
ProteinModelPortaliQ60099.
SMRiQ60099.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ60099.

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.
TIGR01509. HAD-SF-IA-v3. 1 hit.
TIGR01428. HAD_type_II. 1 hit.

Sequencei

Sequence statusi: Complete.

Q60099-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKAVVFDAY GTLFDVQSVA DATERAYPGR GEYITQVWRQ KQLEYSWLRA
60 70 80 90 100
LMGRYADFWG VTREALAYTL GTLGLEPDES FLADMAQAYN RLTPYPDAAQ
110 120 130 140 150
CLAELAPLKR AILSNGAPDM LQALVANAGL TDSFDAVISV DAKRVFKPHP
160 170 180 190 200
DSYALVEEVL GVTPAEVLFV SSNGFDVGGA KNFGFSVARV ARLSQEALAR
210 220 230 240 250
ELVSGTIAPL TMFKALRMRE ETYAEAPDFV VPALGDLPRL VRGMAGAHLA

PAV
Length:253
Mass (Da):27,469
Last modified:July 15, 1998 - v2
Checksum:iE2AB8DEED37A5716
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti84D → G (PubMed:1744048).Curated1
Sequence conflicti84D → G (PubMed:7580000).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81691 Genomic DNA. Translation: AAA27590.1.
X86084 Genomic DNA. Translation: CAA60039.1.
PIRiS52840.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81691 Genomic DNA. Translation: AAA27590.1.
X86084 Genomic DNA. Translation: CAA60039.1.
PIRiS52840.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AQ6X-ray1.95A/B1-253[»]
1QQ5X-ray1.52A/B1-253[»]
1QQ6X-ray2.10A/B1-253[»]
1QQ7X-ray1.70A/B1-253[»]
ProteinModelPortaliQ60099.
SMRiQ60099.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.8.1.2. 1641.

Miscellaneous databases

EvolutionaryTraceiQ60099.

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.
TIGR01509. HAD-SF-IA-v3. 1 hit.
TIGR01428. HAD_type_II. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHAD_XANAU
AccessioniPrimary (citable) accession number: Q60099
Secondary accession number(s): Q56757
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: November 2, 2016
This is version 82 of the entry and version 2 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.