DHMA_PSYCK
ID DHMA_PSYCK Reviewed; 303 AA.
AC Q1QBB9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Haloalkane dehalogenase {ECO:0000255|HAMAP-Rule:MF_01230};
DE EC=3.8.1.5 {ECO:0000255|HAMAP-Rule:MF_01230};
GN Name=dhmA {ECO:0000255|HAMAP-Rule:MF_01230}; OrderedLocusNames=Pcryo_1253;
OS Psychrobacter cryohalolentis (strain ATCC BAA-1226 / DSM 17306 / VKM B-2378
OS / K5).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=335284;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1226 / DSM 17306 / VKM B-2378 / K5;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Sims D.R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Richardson P.;
RT "Complete sequence of chromosome of Psychrobacter cryohalolentis K5.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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_01230}.
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_01230};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01230}.
CC -!- SIMILARITY: Belongs to the haloalkane dehalogenase family. Type 1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01230}.
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DR EMBL; CP000323; ABE75034.1; -; Genomic_DNA.
DR RefSeq; WP_011513586.1; NC_007969.1.
DR PDB; 6F9O; X-ray; 1.05 A; A=1-303.
DR PDBsum; 6F9O; -.
DR AlphaFoldDB; Q1QBB9; -.
DR SMR; Q1QBB9; -.
DR STRING; 335284.Pcryo_1253; -.
DR ESTHER; psyck-q1qbb9; Haloalkane_dehalogenase-HLD1.
DR MEROPS; S33.990; -.
DR KEGG; pcr:Pcryo_1253; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_020336_13_3_6; -.
DR OMA; TLFCQDW; -.
DR BRENDA; 3.8.1.5; 13075.
DR Proteomes; UP000002425; Chromosome.
DR GO; GO:0018786; F:haloalkane dehalogenase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1820; -; 1.
DR HAMAP; MF_01230; Haloalk_dehal_type1; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000639; Epox_hydrolase-like.
DR InterPro; IPR023489; Haloalkane_dehalogenase_1.
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.
FT CHAIN 1..303
FT /note="Haloalkane dehalogenase"
FT /id="PRO_1000066842"
FT DOMAIN 48..192
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 123
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01230"
FT ACT_SITE 250
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01230"
FT ACT_SITE 280
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01230"
FT HELIX 8..11
FT /evidence="ECO:0007829|PDB:6F9O"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:6F9O"
FT STRAND 29..42
FT /evidence="ECO:0007829|PDB:6F9O"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:6F9O"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:6F9O"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:6F9O"
FT HELIX 66..71
FT /evidence="ECO:0007829|PDB:6F9O"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:6F9O"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:6F9O"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:6F9O"
FT HELIX 98..112
FT /evidence="ECO:0007829|PDB:6F9O"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:6F9O"
FT HELIX 124..135
FT /evidence="ECO:0007829|PDB:6F9O"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:6F9O"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:6F9O"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:6F9O"
FT HELIX 159..170
FT /evidence="ECO:0007829|PDB:6F9O"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:6F9O"
FT HELIX 176..182
FT /evidence="ECO:0007829|PDB:6F9O"
FT HELIX 190..197
FT /evidence="ECO:0007829|PDB:6F9O"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:6F9O"
FT HELIX 207..211
FT /evidence="ECO:0007829|PDB:6F9O"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:6F9O"
FT HELIX 225..235
FT /evidence="ECO:0007829|PDB:6F9O"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:6F9O"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:6F9O"
FT TURN 251..255
FT /evidence="ECO:0007829|PDB:6F9O"
FT HELIX 256..263
FT /evidence="ECO:0007829|PDB:6F9O"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:6F9O"
FT STRAND 275..281
FT /evidence="ECO:0007829|PDB:6F9O"
FT HELIX 282..299
FT /evidence="ECO:0007829|PDB:6F9O"
SQ SEQUENCE 303 AA; 34044 MW; 738070E2BB69A028 CRC64;
MKILRTPDSR FANLPDYNFD PHYLMVDDSE DSELRVHYLD EGPRDADPVL LLHGEPSWCY
LYRKMIPILT AAGHRVIAPD LPGFGRSDKP ASRTDYTYQR HVNWMQSVLD QLDLNNITLF
CQDWGGLIGL RLVAENPDRF ARVAAGNTML PTGDHDLGEG FRKWQQFSQE IPQFHVGGTI
KSGTVTKLSQ AVIDAYNAPF PDESYKEGAR QFPLLVPSTP DDPASENNRA AWIELSKWTK
PFITLFSDSD PVTAGGDRIM QKIIPGTKGQ AHTTIANGGH FLQEDQGEKV AKLLVQFIHD
NPR
