DHAA_BRADU
ID DHAA_BRADU Reviewed; 310 AA.
AC P59337;
DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2003, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Haloalkane dehalogenase {ECO:0000255|HAMAP-Rule:MF_01231};
DE EC=3.8.1.5 {ECO:0000255|HAMAP-Rule:MF_01231};
GN Name=dhaA {ECO:0000255|HAMAP-Rule:MF_01231}; OrderedLocusNames=blr1087;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
CC -!- FUNCTION: Catalyzes hydrolytic cleavage of carbon-halogen bonds in
CC halogenated aliphatic compounds, leading to the formation of the
CC corresponding primary alcohols, halide ions and protons.
CC {ECO:0000255|HAMAP-Rule:MF_01231}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-haloalkane + H2O = a halide anion + a primary alcohol +
CC H(+); Xref=Rhea:RHEA:19081, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15734, ChEBI:CHEBI:16042, ChEBI:CHEBI:18060; EC=3.8.1.5;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01231};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01231}.
CC -!- INTERACTION:
CC P59337; P59337: dhaA; NbExp=2; IntAct=EBI-6967845, EBI-6967845;
CC -!- SIMILARITY: Belongs to the haloalkane dehalogenase family. Type 2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01231}.
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DR EMBL; BA000040; BAC46352.1; -; Genomic_DNA.
DR RefSeq; NP_767727.1; NC_004463.1.
DR RefSeq; WP_011083907.1; NZ_CP011360.1.
DR PDB; 3A2L; X-ray; 1.78 A; A/B=1-310.
DR PDB; 3A2M; X-ray; 1.84 A; A/B=1-310.
DR PDB; 3A2N; X-ray; 1.89 A; A/B/E/F=1-310.
DR PDB; 3AFI; X-ray; 1.75 A; A/B/E/F=1-310.
DR PDBsum; 3A2L; -.
DR PDBsum; 3A2M; -.
DR PDBsum; 3A2N; -.
DR PDBsum; 3AFI; -.
DR AlphaFoldDB; P59337; -.
DR SMR; P59337; -.
DR MINT; P59337; -.
DR STRING; 224911.27349338; -.
DR ESTHER; braja-dhaa; Haloalkane_dehalogenase-HLD2.
DR EnsemblBacteria; BAC46352; BAC46352; BAC46352.
DR GeneID; 64020952; -.
DR KEGG; bja:blr1087; -.
DR PATRIC; fig|224911.44.peg.484; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_020336_13_3_5; -.
DR InParanoid; P59337; -.
DR OMA; TLFCQDW; -.
DR PhylomeDB; P59337; -.
DR BRENDA; 3.8.1.5; 929.
DR EvolutionaryTrace; P59337; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0018786; F:haloalkane dehalogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR Gene3D; 3.40.50.1820; -; 1.
DR HAMAP; MF_01231; Haloalk_dehal_type2; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000639; Epox_hydrolase-like.
DR InterPro; IPR023594; Haloalkane_dehalogenase_2.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome.
FT CHAIN 1..310
FT /note="Haloalkane dehalogenase"
FT /id="PRO_0000216780"
FT DOMAIN 30..140
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 103
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01231"
FT ACT_SITE 127
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01231"
FT ACT_SITE 280
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01231"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:3AFI"
FT STRAND 17..25
FT /evidence="ECO:0007829|PDB:3AFI"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:3A2N"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:3AFI"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:3AFI"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:3AFI"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:3AFI"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:3AFI"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:3AFI"
FT HELIX 78..91
FT /evidence="ECO:0007829|PDB:3AFI"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:3AFI"
FT HELIX 104..115
FT /evidence="ECO:0007829|PDB:3AFI"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:3AFI"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:3AFI"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:3AFI"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:3AFI"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:3AFI"
FT HELIX 147..160
FT /evidence="ECO:0007829|PDB:3AFI"
FT HELIX 165..170
FT /evidence="ECO:0007829|PDB:3AFI"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:3AFI"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:3AFI"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:3AFI"
FT HELIX 191..198
FT /evidence="ECO:0007829|PDB:3AFI"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:3AFI"
FT HELIX 208..212
FT /evidence="ECO:0007829|PDB:3AFI"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:3AFI"
FT HELIX 224..239
FT /evidence="ECO:0007829|PDB:3AFI"
FT STRAND 244..251
FT /evidence="ECO:0007829|PDB:3AFI"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:3AFI"
FT HELIX 257..266
FT /evidence="ECO:0007829|PDB:3AFI"
FT STRAND 267..278
FT /evidence="ECO:0007829|PDB:3AFI"
FT HELIX 282..303
FT /evidence="ECO:0007829|PDB:3AFI"
SQ SEQUENCE 310 AA; 34089 MW; 7661684F109CF0FA CRC64;
MSKPIEIEIR RAPVLGSSMA YRETGAQDAP VVLFLHGNPT SSHIWRNILP LVSPVAHCIA
PDLIGFGQSG KPDIAYRFFD HVRYLDAFIE QRGVTSAYLV AQDWGTALAF HLAARRPDFV
RGLAFMEFIR PMPTWQDFHH TEVAEEQDHA EAARAVFRKF RTPGEGEAMI LEANAFVERV
LPGGIVRKLG DEEMAPYRTP FPTPESRRPV LAFPRELPIA GEPADVYEAL QSAHAALAAS
SYPKLLFTGE PGALVSPEFA ERFAASLTRC ALIRLGAGLH YLQEDHADAI GRSVAGWIAG
IEAVRPQLAA
