DEHA_RHOPA
ID DEHA_RHOPA Reviewed; 302 AA.
AC Q6NAM1;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Fluoroacetate dehalogenase;
DE EC=3.8.1.3;
GN OrderedLocusNames=RPA1163;
OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=258594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-98 / CGA009;
RX PubMed=14704707; DOI=10.1038/nbt923;
RA Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA Harrison F.H., Gibson J., Harwood C.S.;
RT "Complete genome sequence of the metabolically versatile photosynthetic
RT bacterium Rhodopseudomonas palustris.";
RL Nat. Biotechnol. 22:55-61(2004).
RN [2]
RP CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX DOI=10.1111/j.1751-7915.2009.00155.x;
RA Chan W.Y., Wong M., Guthrie J., Savchenko A.V., Yakunin A.F., Pai E.F.,
RA Edwards E.A.;
RT "Sequence- and activity-based screening of microbial genomes for novel
RT dehalogenases.";
RL Microb. Biotechnol. 3:107-120(2010).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF WILD-TYPE AND MUTANTS ASN-110 AND
RP ASN-280 IN COMPLEXES WITH FLUOROACETATE AND ANALOGS, CATALYTIC ACTIVITY,
RP FUNCTION, SUBUNIT, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF PHE-40; ASP-110; HIS-155; TRP-156; TRP-185; TYR-219 AND
RP HIS-280.
RX PubMed=21510690; DOI=10.1021/ja200277d;
RA Chan P.W., Yakunin A.F., Edwards E.A., Pai E.F.;
RT "Mapping the reaction coordinates of enzymatic defluorination.";
RL J. Am. Chem. Soc. 133:7461-7468(2011).
CC -!- FUNCTION: Catalyzes the hydrolytic defluorination of fluoroacetate to
CC produce glycolate. Has lower activity towards bromoacetate and
CC chloroacetate. {ECO:0000269|PubMed:21510690, ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a haloacetate + H2O = a halide anion + glycolate + H(+);
CC Xref=Rhea:RHEA:11044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:29805, ChEBI:CHEBI:85638; EC=3.8.1.3;
CC Evidence={ECO:0000269|PubMed:21510690, ECO:0000269|Ref.2};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.3 mM for fluoroacetate {ECO:0000269|PubMed:21510690,
CC ECO:0000269|Ref.2};
CC KM=1.4 mM for chloroacetate {ECO:0000269|PubMed:21510690,
CC ECO:0000269|Ref.2};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21510690}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Epoxide hydrolase
CC family. {ECO:0000305}.
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DR EMBL; BX572596; CAE26606.1; -; Genomic_DNA.
DR RefSeq; WP_011156727.1; NC_005296.1.
DR PDB; 3R3U; X-ray; 1.60 A; A/B/C/D=1-302.
DR PDB; 3R3V; X-ray; 1.50 A; A/B=1-302.
DR PDB; 3R3W; X-ray; 1.60 A; A/B=1-302.
DR PDB; 3R3X; X-ray; 1.80 A; A/B=1-302.
DR PDB; 3R3Y; X-ray; 1.15 A; A/B=1-302.
DR PDB; 3R3Z; X-ray; 1.70 A; A/B/C/D=1-302.
DR PDB; 3R40; X-ray; 1.05 A; A/B=1-302.
DR PDB; 3R41; X-ray; 1.05 A; A/B=1-302.
DR PDB; 5K3A; X-ray; 1.51 A; A/B=1-302.
DR PDB; 5K3B; X-ray; 1.58 A; A/B=1-302.
DR PDB; 5K3C; X-ray; 1.54 A; A/B=3-300.
DR PDB; 5K3D; X-ray; 1.45 A; A/B=4-300.
DR PDB; 5K3E; X-ray; 1.54 A; A/B=1-302.
DR PDB; 5K3F; X-ray; 1.54 A; A/B=1-302.
DR PDB; 5NYV; X-ray; 1.60 A; A/B=1-302.
DR PDB; 5O2G; X-ray; 2.10 A; A/B=1-302.
DR PDB; 5O2I; X-ray; 2.00 A; A/B=1-302.
DR PDB; 5SWN; X-ray; 1.54 A; A/B=4-300.
DR PDB; 5T4T; X-ray; 1.51 A; A/B=1-302.
DR PDB; 6FSX; X-ray; 1.80 A; A/B=1-302.
DR PDB; 6GXD; X-ray; 1.80 A; A/B=1-302.
DR PDB; 6GXF; X-ray; 1.80 A; A/B=1-302.
DR PDB; 6GXH; X-ray; 1.80 A; A/B=1-302.
DR PDB; 6GXL; X-ray; 1.80 A; A/B=1-302.
DR PDB; 6GXT; X-ray; 1.95 A; A/B=1-302.
DR PDB; 6MUH; X-ray; 1.80 A; A/B=1-302.
DR PDB; 6MUY; X-ray; 1.80 A; A/B=1-302.
DR PDB; 6MZZ; X-ray; 1.80 A; A/B=1-302.
DR PDB; 6N00; X-ray; 1.90 A; A/B=1-302.
DR PDB; 6QHP; X-ray; 1.80 A; A/B=1-302.
DR PDB; 6QHQ; X-ray; 1.74 A; A/B=1-302.
DR PDB; 6QHS; X-ray; 1.73 A; A/B=1-302.
DR PDB; 6QHT; X-ray; 1.73 A; A/B=1-302.
DR PDB; 6QHU; X-ray; 1.73 A; A/B=1-302.
DR PDB; 6QHV; X-ray; 1.72 A; A/B=1-302.
DR PDB; 6QHW; X-ray; 1.72 A; A/B=1-302.
DR PDB; 6QHX; X-ray; 1.85 A; A/B=1-302.
DR PDB; 6QHY; X-ray; 1.70 A; A/B=1-302.
DR PDB; 6QHZ; X-ray; 1.80 A; A/B=1-302.
DR PDB; 6QI0; X-ray; 1.73 A; A/B=1-302.
DR PDB; 6QI1; X-ray; 1.90 A; A/B=1-302.
DR PDB; 6QI2; X-ray; 1.73 A; A/B=1-302.
DR PDB; 6QI3; X-ray; 1.74 A; A/B=1-302.
DR PDB; 6QKS; X-ray; 1.60 A; A/B=1-302.
DR PDB; 6QKT; X-ray; 1.51 A; A/B=1-302.
DR PDB; 6QKU; X-ray; 1.51 A; A/B=1-302.
DR PDB; 6QKW; X-ray; 1.51 A; A/B=1-302.
DR PDB; 7A42; X-ray; 1.75 A; A/B=1-302.
DR PDB; 7A43; X-ray; 1.75 A; A/B=1-302.
DR PDBsum; 3R3U; -.
DR PDBsum; 3R3V; -.
DR PDBsum; 3R3W; -.
DR PDBsum; 3R3X; -.
DR PDBsum; 3R3Y; -.
DR PDBsum; 3R3Z; -.
DR PDBsum; 3R40; -.
DR PDBsum; 3R41; -.
DR PDBsum; 5K3A; -.
DR PDBsum; 5K3B; -.
DR PDBsum; 5K3C; -.
DR PDBsum; 5K3D; -.
DR PDBsum; 5K3E; -.
DR PDBsum; 5K3F; -.
DR PDBsum; 5NYV; -.
DR PDBsum; 5O2G; -.
DR PDBsum; 5O2I; -.
DR PDBsum; 5SWN; -.
DR PDBsum; 5T4T; -.
DR PDBsum; 6FSX; -.
DR PDBsum; 6GXD; -.
DR PDBsum; 6GXF; -.
DR PDBsum; 6GXH; -.
DR PDBsum; 6GXL; -.
DR PDBsum; 6GXT; -.
DR PDBsum; 6MUH; -.
DR PDBsum; 6MUY; -.
DR PDBsum; 6MZZ; -.
DR PDBsum; 6N00; -.
DR PDBsum; 6QHP; -.
DR PDBsum; 6QHQ; -.
DR PDBsum; 6QHS; -.
DR PDBsum; 6QHT; -.
DR PDBsum; 6QHU; -.
DR PDBsum; 6QHV; -.
DR PDBsum; 6QHW; -.
DR PDBsum; 6QHX; -.
DR PDBsum; 6QHY; -.
DR PDBsum; 6QHZ; -.
DR PDBsum; 6QI0; -.
DR PDBsum; 6QI1; -.
DR PDBsum; 6QI2; -.
DR PDBsum; 6QI3; -.
DR PDBsum; 6QKS; -.
DR PDBsum; 6QKT; -.
DR PDBsum; 6QKU; -.
DR PDBsum; 6QKW; -.
DR PDBsum; 7A42; -.
DR PDBsum; 7A43; -.
DR AlphaFoldDB; Q6NAM1; -.
DR SMR; Q6NAM1; -.
DR STRING; 258594.RPA1163; -.
DR ESTHER; rhopa-q6nam1; Haloacetate_dehalogenase.
DR PRIDE; Q6NAM1; -.
DR EnsemblBacteria; CAE26606; CAE26606; RPA1163.
DR GeneID; 66892184; -.
DR KEGG; rpa:RPA1163; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_020336_7_1_5; -.
DR OMA; LPTLDMW; -.
DR PhylomeDB; Q6NAM1; -.
DR BioCyc; RPAL258594:TX73_RS05935-MON; -.
DR BRENDA; 3.8.1.3; 5412.
DR EvolutionaryTrace; Q6NAM1; -.
DR Proteomes; UP000001426; Chromosome.
DR GO; GO:0018785; F:haloacetate dehalogenase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000639; Epox_hydrolase-like.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome.
FT CHAIN 1..302
FT /note="Fluoroacetate dehalogenase"
FT /id="PRO_0000398584"
FT DOMAIN 32..270
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 110
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:21510690"
FT ACT_SITE 280
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:21510690"
FT BINDING 111
FT /ligand="substrate"
FT BINDING 114
FT /ligand="substrate"
FT BINDING 155
FT /ligand="substrate"
FT BINDING 156
FT /ligand="substrate"
FT BINDING 219
FT /ligand="substrate"
FT SITE 134
FT /note="Important for enzyme activity"
FT MUTAGEN 40
FT /note="F->A: Reduced catalytic rate. Minor effect on
FT substrate affinity."
FT /evidence="ECO:0000269|PubMed:21510690"
FT MUTAGEN 110
FT /note="D->N: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:21510690"
FT MUTAGEN 155
FT /note="H->N: Reduced catalytic rate with fluoroacetate, but
FT increased catalytic rate with chloroacetate. Minor effect
FT on substrate affinity."
FT /evidence="ECO:0000269|PubMed:21510690"
FT MUTAGEN 156
FT /note="W->H: Reduced catalytic rate. Reduced substrate
FT affinity."
FT /evidence="ECO:0000269|PubMed:21510690"
FT MUTAGEN 185
FT /note="W->F: Reduced catalytic rate. Minor effect on
FT substrate affinity."
FT /evidence="ECO:0000269|PubMed:21510690"
FT MUTAGEN 219
FT /note="Y->F: Reduced catalytic rate. Minor effect on
FT substrate affinity."
FT /evidence="ECO:0000269|PubMed:21510690"
FT MUTAGEN 280
FT /note="H->N: Abolishes hydrolysis of covalent reaction
FT intermediate."
FT /evidence="ECO:0000269|PubMed:21510690"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:3R40"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:3R40"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:3R40"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:3R40"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:3R40"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:3R40"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:3R40"
FT HELIX 85..98
FT /evidence="ECO:0007829|PDB:3R40"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:3R40"
FT HELIX 111..122
FT /evidence="ECO:0007829|PDB:3R40"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:3R40"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:3R40"
FT HELIX 138..144
FT /evidence="ECO:0007829|PDB:3R40"
FT HELIX 147..152
FT /evidence="ECO:0007829|PDB:3R40"
FT HELIX 155..159
FT /evidence="ECO:0007829|PDB:3R40"
FT HELIX 165..170
FT /evidence="ECO:0007829|PDB:3R40"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:3R40"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:3R40"
FT HELIX 196..206
FT /evidence="ECO:0007829|PDB:3R40"
FT HELIX 209..223
FT /evidence="ECO:0007829|PDB:3R40"
FT HELIX 225..236
FT /evidence="ECO:0007829|PDB:3R40"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:3R40"
FT TURN 254..257
FT /evidence="ECO:0007829|PDB:3R41"
FT HELIX 261..267
FT /evidence="ECO:0007829|PDB:3R40"
FT STRAND 268..278
FT /evidence="ECO:0007829|PDB:3R40"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:3R40"
FT HELIX 287..299
FT /evidence="ECO:0007829|PDB:3R40"
SQ SEQUENCE 302 AA; 33692 MW; 3A1FAE748CF25167 CRC64;
MPDLADLFPG FGSEWINTSS GRIFARVGGD GPPLLLLHGF PQTHVMWHRV APKLAERFKV
IVADLPGYGW SDMPESDEQH TPYTKRAMAK QLIEAMEQLG HVHFALAGHD RGARVSYRLA
LDSPGRLSKL AVLDILPTYE YWQRMNRAYA LKIYHWSFLA QPAPLPENLL GGDPDFYVKA
KLASWTRAGD LSAFDPRAVE HYRIAFADPM RRHVMCEDYR AGAYADFEHD KIDVEAGNKI
PVPMLALWGA SGIAQSAATP LDVWRKWASD VQGAPIESGH FLPEEAPDQT AEALVRFFSA
AP
