CAA43_BURSP
ID CAA43_BURSP Reviewed; 333 AA.
AC Q59I44;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=2-haloacrylate reductase {ECO:0000303|PubMed:15781461};
DE EC=1.3.1.103 {ECO:0000269|PubMed:15781461};
GN Name=caa43 {ECO:0000303|PubMed:15781461};
OS Burkholderia sp.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=36773;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-17 AND 115-129,
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOTECHNOLOGY.
RC STRAIN=WS {ECO:0000312|EMBL:BAD91551.1};
RX PubMed=15781461; DOI=10.1074/jbc.m414605200;
RA Kurata A., Kurihara T., Kamachi H., Esaki N.;
RT "2-Haloacrylate reductase, a novel enzyme of the medium chain
RT dehydrogenase/reductase superfamily that catalyzes the reduction of a
RT carbon-carbon double bond of unsaturated organohalogen compounds.";
RL J. Biol. Chem. 280:20286-20291(2005).
CC -!- FUNCTION: Involved in the degradation of unsaturated organohalogen
CC compounds. Catalyzes the NADPH-dependent reduction of the carbon-carbon
CC double bond of 2-chloroacrylate to produce (S)-2-chloropropionate,
CC which is probably further metabolized to (R)-lactate by (S)-2-haloacid
CC dehalogenase. Can also use 2-bromoacrylate as substrate. Does not act
CC on acrylate, methacrylate, 1,4-benzoquinone and 1,4-naphthoquinone.
CC {ECO:0000269|PubMed:15781461}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2-chloropropanoate + NADP(+) = 2-chloroacrylate + H(+) +
CC NADPH; Xref=Rhea:RHEA:36591, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:73934, ChEBI:CHEBI:73935;
CC EC=1.3.1.103; Evidence={ECO:0000269|PubMed:15781461};
CC -!- BIOTECHNOLOGY: (S)-2-chloropropionate is used in a large quantity as a
CC synthetic precursor for the industrial production of
CC aryloxyphenoxypropionic acid herbicides. {ECO:0000303|PubMed:15781461}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AB196962; BAD91551.1; -; Genomic_DNA.
DR PDB; 1WLY; X-ray; 1.30 A; A=1-333.
DR PDBsum; 1WLY; -.
DR AlphaFoldDB; Q59I44; -.
DR SMR; Q59I44; -.
DR KEGG; ag:BAD91551; -.
DR BioCyc; MetaCyc:MON-18421; -.
DR BRENDA; 1.3.1.103; 1033.
DR EvolutionaryTrace; Q59I44; -.
DR GO; GO:0102523; F:2-chloroacrylate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR GO; GO:0042206; P:halogenated hydrocarbon catabolic process; IDA:UniProtKB.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; NADP; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:15781461"
FT CHAIN 2..333
FT /note="2-haloacrylate reductase"
FT /evidence="ECO:0000269|PubMed:15781461"
FT /id="PRO_0000430752"
FT BINDING 153..159
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000303|PubMed:15781461"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:1WLY"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1WLY"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:1WLY"
FT STRAND 30..40
FT /evidence="ECO:0007829|PDB:1WLY"
FT HELIX 42..48
FT /evidence="ECO:0007829|PDB:1WLY"
FT STRAND 67..75
FT /evidence="ECO:0007829|PDB:1WLY"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:1WLY"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:1WLY"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:1WLY"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:1WLY"
FT HELIX 120..138
FT /evidence="ECO:0007829|PDB:1WLY"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:1WLY"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:1WLY"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:1WLY"
FT STRAND 172..179
FT /evidence="ECO:0007829|PDB:1WLY"
FT HELIX 180..189
FT /evidence="ECO:0007829|PDB:1WLY"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:1WLY"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:1WLY"
FT HELIX 202..210
FT /evidence="ECO:0007829|PDB:1WLY"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:1WLY"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:1WLY"
FT HELIX 227..232
FT /evidence="ECO:0007829|PDB:1WLY"
FT STRAND 234..242
FT /evidence="ECO:0007829|PDB:1WLY"
FT HELIX 255..258
FT /evidence="ECO:0007829|PDB:1WLY"
FT TURN 259..263
FT /evidence="ECO:0007829|PDB:1WLY"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:1WLY"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:1WLY"
FT HELIX 279..294
FT /evidence="ECO:0007829|PDB:1WLY"
FT STRAND 302..307
FT /evidence="ECO:0007829|PDB:1WLY"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:1WLY"
FT HELIX 311..320
FT /evidence="ECO:0007829|PDB:1WLY"
FT STRAND 325..330
FT /evidence="ECO:0007829|PDB:1WLY"
SQ SEQUENCE 333 AA; 35784 MW; D91E8DF63147CA42 CRC64;
MVMAAVIHKK GGPDNFVWEE VKVGSPGPGQ VRLRNTAIGV NFLDTYHRAG IPHPLVVGEP
PIVVGFEAAA VVEEVGPGVT DFTVGERVCT CLPPLGAYSQ ERLYPAEKLI KVPKDLDLDD
VHLAGLMLKG MTAQYLLHQT HKVKPGDYVL IHAAAGGMGH IMVPWARHLG ATVIGTVSTE
EKAETARKLG CHHTINYSTQ DFAEVVREIT GGKGVDVVYD SIGKDTLQKS LDCLRPRGMC
AAYGHASGVA DPIRVVEDLG VRGSLFITRP ALWHYMSNRS EIDEGSKCLF DAVKAGVLHS
SVAKTFPLRE AAAAHKYMGG RQTIGSIVLL PQA
