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DHAA_AGRFC
ID   DHAA_AGRFC              Reviewed;         304 AA.
AC   Q8U671;
DT   22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 98.
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}; Synonyms=dha;
GN   OrderedLocusNames=Atu6064; ORFNames=AGR_pTi_130;
OS   Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS   (strain C58)).
OG   Plasmid pTiC58.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=176299;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11743193; DOI=10.1126/science.1066804;
RA   Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA   Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA   Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA   Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA   Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA   Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA   Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA   Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA   Gordon M.P., Olson M.V., Nester E.W.;
RT   "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT   C58.";
RL   Science 294:2317-2323(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743194; DOI=10.1126/science.1066803;
RA   Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA   Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA   Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA   Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA   Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT   "Genome sequence of the plant pathogen and biotechnology agent
RT   Agrobacterium tumefaciens C58.";
RL   Science 294:2323-2328(2001).
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   -!- SIMILARITY: Belongs to the haloalkane dehalogenase family. Type 2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01231}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK91024.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE007871; AAK91024.2; ALT_INIT; Genomic_DNA.
DR   PIR; AF3235; AF3235.
DR   RefSeq; NP_396583.2; NC_003065.3.
DR   PDB; 3WI7; X-ray; 1.70 A; A/B=1-304.
DR   PDB; 3WIB; X-ray; 1.95 A; A/B=1-304.
DR   PDBsum; 3WI7; -.
DR   PDBsum; 3WIB; -.
DR   AlphaFoldDB; Q8U671; -.
DR   SMR; Q8U671; -.
DR   ESTHER; agrtu-DHAA; Haloalkane_dehalogenase-HLD2.
DR   EnsemblBacteria; AAK91024; AAK91024; Atu6064.
DR   KEGG; atu:Atu6064; -.
DR   PATRIC; fig|176299.10.peg.5271; -.
DR   HOGENOM; CLU_020336_13_3_5; -.
DR   OMA; TLFCQDW; -.
DR   BRENDA; 3.8.1.5; 200.
DR   Proteomes; UP000000813; Plasmid Ti.
DR   GO; GO:0018786; F:haloalkane dehalogenase activity; IEA:UniProtKB-UniRule.
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; IPR023594; Haloalkane_dehalogenase_2.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Plasmid; Reference proteome.
FT   CHAIN           1..304
FT                   /note="Haloalkane dehalogenase"
FT                   /id="PRO_0000216779"
FT   DOMAIN          42..154
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        114
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01231"
FT   ACT_SITE        138
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   HELIX           14..16
FT                   /evidence="ECO:0007829|PDB:3WI7"
FT   STRAND          21..27
FT                   /evidence="ECO:0007829|PDB:3WI7"
FT   STRAND          30..37
FT                   /evidence="ECO:0007829|PDB:3WI7"
FT   STRAND          40..46
FT                   /evidence="ECO:0007829|PDB:3WI7"
FT   HELIX           53..56
FT                   /evidence="ECO:0007829|PDB:3WI7"
FT   HELIX           57..62
FT                   /evidence="ECO:0007829|PDB:3WI7"
FT   TURN            63..65
FT                   /evidence="ECO:0007829|PDB:3WI7"
FT   STRAND          66..72
FT                   /evidence="ECO:0007829|PDB:3WI7"
FT   HELIX           89..103
FT                   /evidence="ECO:0007829|PDB:3WI7"
FT   STRAND          107..114
FT                   /evidence="ECO:0007829|PDB:3WI7"
FT   HELIX           116..126
FT                   /evidence="ECO:0007829|PDB:3WI7"
FT   HELIX           128..130
FT                   /evidence="ECO:0007829|PDB:3WI7"
FT   STRAND          131..139
FT                   /evidence="ECO:0007829|PDB:3WI7"
FT   HELIX           146..148
FT                   /evidence="ECO:0007829|PDB:3WI7"
FT   HELIX           151..160
FT                   /evidence="ECO:0007829|PDB:3WI7"
FT   HELIX           165..170
FT                   /evidence="ECO:0007829|PDB:3WI7"
FT   HELIX           175..178
FT                   /evidence="ECO:0007829|PDB:3WI7"
FT   HELIX           180..183
FT                   /evidence="ECO:0007829|PDB:3WI7"
FT   HELIX           191..198
FT                   /evidence="ECO:0007829|PDB:3WI7"
FT   HELIX           205..207
FT                   /evidence="ECO:0007829|PDB:3WI7"
FT   HELIX           208..216
FT                   /evidence="ECO:0007829|PDB:3WI7"
FT   HELIX           224..231
FT                   /evidence="ECO:0007829|PDB:3WI7"
FT   HELIX           234..239
FT                   /evidence="ECO:0007829|PDB:3WI7"
FT   STRAND          244..251
FT                   /evidence="ECO:0007829|PDB:3WI7"
FT   STRAND          253..255
FT                   /evidence="ECO:0007829|PDB:3WI7"
FT   HELIX           257..266
FT                   /evidence="ECO:0007829|PDB:3WI7"
FT   STRAND          270..280
FT                   /evidence="ECO:0007829|PDB:3WI7"
FT   HELIX           282..285
FT                   /evidence="ECO:0007829|PDB:3WI7"
FT   HELIX           287..301
FT                   /evidence="ECO:0007829|PDB:3WI7"
SQ   SEQUENCE   304 AA;  34390 MW;  4783D160D4C86DFA CRC64;
     MKEHRHMTEK SPHSAFGDGA KAYDVPAFGL QIHTVEHGSG APIVFLHGNP TSSYLWRHIF
     RRLHGHGRLL AVDLIGYGQS SKPDIEYTLE NQQRYVDAWF DALDLRNVTL VLQDYGAAFG
     LNWASRNPDR VRAVAFFEPV LRNIDSVDLS PEFVTRRAKL RQPGEGEIFV QQENRFLTEL
     FPWFFLTPLA PEDLRQYQTP FPTPHSRKAI LAGPRNLPVD GEPASTVAFL EQAVNWLNTS
     DTPKLLLTFK PGFLLTDAIL KWSQVTIRNL EIEAAGAGIH FVQEEQPETI ARLLDAWLTR
     IAGN
 
 
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