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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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi153 – 1597NADP1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 3333322-haloacrylate reductase1 PublicationPRO_0000430752Add
BLAST

Structurei

Secondary structure

1
333
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 97Combined sources
Helixi13 – 153Combined sources
Beta strandi16 – 205Combined sources
Beta strandi30 – 4011Combined sources
Helixi42 – 487Combined sources
Beta strandi67 – 759Combined sources
Beta strandi87 – 904Combined sources
Beta strandi92 – 943Combined sources
Beta strandi98 – 1058Combined sources
Helixi106 – 1083Combined sources
Helixi120 – 13819Combined sources
Beta strandi148 – 1514Combined sources
Turni152 – 1554Combined sources
Helixi159 – 16810Combined sources
Beta strandi172 – 1798Combined sources
Helixi180 – 18910Combined sources
Beta strandi192 – 1965Combined sources
Turni197 – 1993Combined sources
Helixi202 – 2109Combined sources
Beta strandi215 – 2206Combined sources
Turni224 – 2263Combined sources
Helixi227 – 2326Combined sources
Beta strandi234 – 2429Combined sources
Helixi255 – 2584Combined sources
Turni259 – 2635Combined sources
Beta strandi266 – 2683Combined sources
Helixi272 – 2754Combined sources
Helixi279 – 29416Combined sources
Beta strandi302 – 3076Combined sources
Helixi308 – 3103Combined sources
Helixi311 – 32010Combined sources
Beta strandi325 – 3306Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WLYX-ray1.30A1-333[»]
ProteinModelPortaliQ59I44.
SMRiQ59I44. Positions 2-333.
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.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1WLYX-ray1.30A1-333[»]
ProteinModelPortaliQ59I44.
SMRiQ59I44. Positions 2-333.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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...

Publicationsi

  1. "2-Haloacrylate reductase, a novel enzyme of the medium chain dehydrogenase/reductase superfamily that catalyzes the reduction of a carbon-carbon double bond of unsaturated organohalogen compounds."
    Kurata A., Kurihara T., Kamachi H., Esaki N.
    J. Biol. Chem. 280:20286-20291(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-17 AND 115-129, X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, BIOTECHNOLOGY.
    Strain: WSImported.

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: May 11, 2016
This is version 52 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.