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Protein

2-haloacrylate reductase

Gene

caa43

Organism
Burkholderia sp.
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the degradation of unsaturated organohalogen compounds. Catalyzes the NADPH-dependent reduction of the carbon-carbon double bond of 2-chloroacrylate to produce (S)-2-chloropropionate, which is probably further metabolized to (R)-lactate by (S)-2-haloacid dehalogenase. Can also use 2-bromoacrylate as substrate. Does not act on acrylate, methacrylate, 1,4-benzoquinone and 1,4-naphthoquinone.1 Publication

Catalytic activityi

(S)-2-chloropropanoate + NADP+ = 2-chloroacrylate + NADPH.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi153 – 159NADP1 Publication7

GO - Molecular functioni

GO - Biological processi

  • halogenated hydrocarbon catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18421.
BRENDAi1.3.1.103. 1033.

Names & Taxonomyi

Protein namesi
Recommended name:
2-haloacrylate reductase1 Publication (EC:1.3.1.1031 Publication)
Gene namesi
Name:caa431 Publication
OrganismiBurkholderia sp.
Taxonomic identifieri36773 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

Pathology & Biotechi

Biotechnological usei

(S)-2-chloropropionate is used in a large quantity as a synthetic precursor for the industrial production of aryloxyphenoxypropionic acid herbicides.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00004307522 – 3332-haloacrylate reductase1 PublicationAdd BLAST332

Structurei

Secondary structure

1333
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 9Combined sources7
Helixi13 – 15Combined sources3
Beta strandi16 – 20Combined sources5
Beta strandi30 – 40Combined sources11
Helixi42 – 48Combined sources7
Beta strandi67 – 75Combined sources9
Beta strandi87 – 90Combined sources4
Beta strandi92 – 94Combined sources3
Beta strandi98 – 105Combined sources8
Helixi106 – 108Combined sources3
Helixi120 – 138Combined sources19
Beta strandi148 – 151Combined sources4
Turni152 – 155Combined sources4
Helixi159 – 168Combined sources10
Beta strandi172 – 179Combined sources8
Helixi180 – 189Combined sources10
Beta strandi192 – 196Combined sources5
Turni197 – 199Combined sources3
Helixi202 – 210Combined sources9
Beta strandi215 – 220Combined sources6
Turni224 – 226Combined sources3
Helixi227 – 232Combined sources6
Beta strandi234 – 242Combined sources9
Helixi255 – 258Combined sources4
Turni259 – 263Combined sources5
Beta strandi266 – 268Combined sources3
Helixi272 – 275Combined sources4
Helixi279 – 294Combined sources16
Beta strandi302 – 307Combined sources6
Helixi308 – 310Combined sources3
Helixi311 – 320Combined sources10
Beta strandi325 – 330Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WLYX-ray1.30A1-333[»]
ProteinModelPortaliQ59I44.
SMRiQ59I44.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ59I44.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q59I44-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVMAAVIHKK GGPDNFVWEE VKVGSPGPGQ VRLRNTAIGV NFLDTYHRAG
60 70 80 90 100
IPHPLVVGEP PIVVGFEAAA VVEEVGPGVT DFTVGERVCT CLPPLGAYSQ
110 120 130 140 150
ERLYPAEKLI KVPKDLDLDD VHLAGLMLKG MTAQYLLHQT HKVKPGDYVL
160 170 180 190 200
IHAAAGGMGH IMVPWARHLG ATVIGTVSTE EKAETARKLG CHHTINYSTQ
210 220 230 240 250
DFAEVVREIT GGKGVDVVYD SIGKDTLQKS LDCLRPRGMC AAYGHASGVA
260 270 280 290 300
DPIRVVEDLG VRGSLFITRP ALWHYMSNRS EIDEGSKCLF DAVKAGVLHS
310 320 330
SVAKTFPLRE AAAAHKYMGG RQTIGSIVLL PQA
Length:333
Mass (Da):35,784
Last modified:April 26, 2005 - v1
Checksum:iD91E8DF63147CA42
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB196962 Genomic DNA. Translation: BAD91551.1.

Genome annotation databases

KEGGiag:BAD91551.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB196962 Genomic DNA. Translation: BAD91551.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WLYX-ray1.30A1-333[»]
ProteinModelPortaliQ59I44.
SMRiQ59I44.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:BAD91551.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18421.
BRENDAi1.3.1.103. 1033.

Miscellaneous databases

EvolutionaryTraceiQ59I44.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCAA43_BURSP
AccessioniPrimary (citable) accession number: Q59I44
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 29, 2014
Last sequence update: April 26, 2005
Last modified: November 2, 2016
This is version 54 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, 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.