DHAA_MYCTU
ID DHAA_MYCTU Reviewed; 300 AA.
AC P9WMR9; L0TA36; Q50642;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Haloalkane dehalogenase 3;
DE EC=3.8.1.5;
GN Name=dhaA; OrderedLocusNames=Rv2579; ORFNames=MTCY227.22c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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. {ECO:0000250}.
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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the haloalkane dehalogenase family. Type 2
CC subfamily. {ECO:0000305}.
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DR EMBL; AL123456; CCP45375.1; -; Genomic_DNA.
DR PIR; B70725; B70725.
DR RefSeq; WP_003413363.1; NZ_NVQJ01000023.1.
DR RefSeq; YP_177890.1; NC_000962.3.
DR PDB; 2O2H; X-ray; 1.60 A; A=1-300.
DR PDB; 2O2I; X-ray; 1.50 A; A=1-300.
DR PDB; 2QVB; X-ray; 1.19 A; A/B=3-299.
DR PDBsum; 2O2H; -.
DR PDBsum; 2O2I; -.
DR PDBsum; 2QVB; -.
DR AlphaFoldDB; P9WMR9; -.
DR SMR; P9WMR9; -.
DR STRING; 83332.Rv2579; -.
DR iPTMnet; P9WMR9; -.
DR PaxDb; P9WMR9; -.
DR GeneID; 45426581; -.
DR GeneID; 888599; -.
DR KEGG; mtu:Rv2579; -.
DR TubercuList; Rv2579; -.
DR eggNOG; COG0596; Bacteria.
DR OMA; TLEWPRQ; -.
DR PhylomeDB; P9WMR9; -.
DR BRENDA; 3.8.1.5; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0018786; F:haloalkane dehalogenase activity; IDA:MTBBASE.
DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR GO; GO:0042206; P:halogenated hydrocarbon catabolic process; IDA:MTBBASE.
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; Acetylation; Hydrolase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..300
FT /note="Haloalkane dehalogenase 3"
FT /id="PRO_0000216783"
FT DOMAIN 32..155
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 109
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 133
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 273
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:21969609"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:2QVB"
FT STRAND 20..36
FT /evidence="ECO:0007829|PDB:2QVB"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:2QVB"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:2QVB"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:2QVB"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:2QVB"
FT HELIX 83..96
FT /evidence="ECO:0007829|PDB:2QVB"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:2QVB"
FT HELIX 110..121
FT /evidence="ECO:0007829|PDB:2QVB"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:2QVB"
FT STRAND 126..133
FT /evidence="ECO:0007829|PDB:2QVB"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:2QVB"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:2QVB"
FT HELIX 149..155
FT /evidence="ECO:0007829|PDB:2QVB"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:2QVB"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:2QVB"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:2QVB"
FT HELIX 185..192
FT /evidence="ECO:0007829|PDB:2QVB"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:2QVB"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:2QVB"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:2QVB"
FT HELIX 203..211
FT /evidence="ECO:0007829|PDB:2QVB"
FT HELIX 219..234
FT /evidence="ECO:0007829|PDB:2QVB"
FT STRAND 239..246
FT /evidence="ECO:0007829|PDB:2QVB"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:2QVB"
FT HELIX 252..259
FT /evidence="ECO:0007829|PDB:2QVB"
FT STRAND 261..273
FT /evidence="ECO:0007829|PDB:2QVB"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:2QVB"
FT HELIX 280..297
FT /evidence="ECO:0007829|PDB:2QVB"
SQ SEQUENCE 300 AA; 33728 MW; E8F4854749F22562 CRC64;
MTAFGVEPYG QPKYLEIAGK RMAYIDEGKG DAIVFQHGNP TSSYLWRNIM PHLEGLGRLV
ACDLIGMGAS DKLSPSGPDR YSYGEQRDFL FALWDALDLG DHVVLVLHDW GSALGFDWAN
QHRDRVQGIA FMEAIVTPMT WADWPPAVRG VFQGFRSPQG EPMALEHNIF VERVLPGAIL
RQLSDEEMNH YRRPFVNGGE DRRPTLSWPR NLPIDGEPAE VVALVNEYRS WLEETDMPKL
FINAEPGAII TGRIRDYVRS WPNQTEITVP GVHFVQEDSP EEIGAAIAQF VRRLRSAAGV
