ID A4PEU6_9SPHN Unreviewed; 296 AA.
AC A4PEU6;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Haloalkane dehalogenase {ECO:0000256|ARBA:ARBA00012065, ECO:0000256|HAMAP-Rule:MF_01231};
DE EC=3.8.1.5 {ECO:0000256|ARBA:ARBA00012065, ECO:0000256|HAMAP-Rule:MF_01231};
GN Name=linB {ECO:0000313|EMBL:BAF56671.1};
GN Synonyms=dhaA {ECO:0000256|HAMAP-Rule:MF_01231};
GN ORFNames=K663_22528 {ECO:0000313|EMBL:AMK20862.1}, K663_22543
GN {ECO:0000313|EMBL:AMK20865.1};
OS Sphingobium sp. MI1205.
OG Plasmid pMI3 {ECO:0000313|EMBL:AMK20862.1,
OG ECO:0000313|Proteomes:UP000060707}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=407020 {ECO:0000313|EMBL:BAF56671.1};
RN [1] {ECO:0000313|EMBL:BAF56671.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MI1205 {ECO:0000313|EMBL:BAF56671.1};
RX PubMed=17516046; DOI=10.1007/s00203-007-0251-8;
RA Ito M., Prokop Z., Klvana M., Otsubo Y., Tsuda M., Damborsky J., Nagata Y.;
RT "Degradation of beta-hexachlorocyclohexane by haloalkane dehalogenase LinB
RT from gamma-hexachlorocyclohexane-utilizing bacterium Sphingobium sp.
RT MI1205.";
RL Arch. Microbiol. 188:313-325(2007).
RN [2] {ECO:0007829|PDB:4H77, ECO:0007829|PDB:4H7D}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH CALCIUM.
RX PubMed=23564170; DOI=10.1128/JB.02020-12;
RA Okai M., Ohtsuka J., Imai L.F., Mase T., Moriuchi R., Tsuda M., Nagata K.,
RA Nagata Y., Tanokura M.;
RT "Crystal structure and site-directed mutagenesis analyses of haloalkane
RT dehalogenase LinB from Sphingobium sp. strain MI1205.";
RL J. Bacteriol. 195:2642-2651(2013).
RN [3] {ECO:0000313|Proteomes:UP000060707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI1205 {ECO:0000313|Proteomes:UP000060707};
RC PLASMID=pMI3 {ECO:0000313|Proteomes:UP000060707};
RA Tabata M.;
RT "Genome sequence of gamma-HCH degrading bacterium Sphingobium sp. MI1205.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AMK20862.1, ECO:0000313|Proteomes:UP000060707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI1205 {ECO:0000313|EMBL:AMK20862.1,
RC ECO:0000313|Proteomes:UP000060707};
RC PLASMID=pMI3 {ECO:0000313|EMBL:AMK20862.1,
RC ECO:0000313|Proteomes:UP000060707};
RX PubMed=27056230;
RA Tabata M., Ohhata S., Nikawadori Y., Sato T., Kishida K., Ohtsubo Y.,
RA Tsuda M., Nagata Y.;
RT "Complete Genome Sequence of a gamma-Hexachlorocyclohexane-Degrading
RT Bacterium, Sphingobium sp. Strain MI1205.";
RL Genome Announc. 4:0-0(2016).
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:0000256|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:0000256|HAMAP-Rule:MF_01231};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC Rule:MF_01231}.
CC -!- SIMILARITY: Belongs to the haloalkane dehalogenase family. Type 2
CC subfamily. {ECO:0000256|ARBA:ARBA00007213, ECO:0000256|HAMAP-
CC Rule:MF_01231}.
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DR EMBL; CP005192; AMK20862.1; -; Genomic_DNA.
DR EMBL; CP005192; AMK20865.1; -; Genomic_DNA.
DR EMBL; AB278602; BAF56671.1; -; Genomic_DNA.
DR EMBL; AB278602; BAF56673.1; -; Genomic_DNA.
DR RefSeq; WP_007682110.1; NZ_CP005192.1.
DR PDB; 4H77; X-ray; 1.60 A; A=1-296.
DR PDB; 4H7D; X-ray; 1.95 A; A=1-296.
DR PDB; 4H7E; X-ray; 1.80 A; A=1-296.
DR PDB; 4H7F; X-ray; 1.80 A; A=1-296.
DR PDB; 4H7H; X-ray; 2.10 A; A=1-296.
DR PDB; 4H7I; X-ray; 1.80 A; A=1-296.
DR PDB; 4H7J; X-ray; 1.80 A; A=1-296.
DR PDB; 4H7K; X-ray; 1.75 A; A=1-296.
DR PDBsum; 4H77; -.
DR PDBsum; 4H7D; -.
DR PDBsum; 4H7E; -.
DR PDBsum; 4H7F; -.
DR PDBsum; 4H7H; -.
DR PDBsum; 4H7I; -.
DR PDBsum; 4H7J; -.
DR PDBsum; 4H7K; -.
DR ESTHER; sphpi-q6vqx3; Haloalkane_dehalogenase-HLD2.
DR KEGG; spmi:K663_22528; -.
DR KEGG; spmi:K663_22543; -.
DR PATRIC; fig|407020.3.peg.4735; -.
DR OrthoDB; 9804723at2; -.
DR BRENDA; 3.8.1.5; 7695.
DR Proteomes; UP000060707; Plasmid pMI3.
DR GO; GO:0018786; F:haloalkane dehalogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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 PANTHER; PTHR43329; EPOXIDE HYDROLASE; 1.
DR PANTHER; PTHR43329:SF74; HALOALKANE DEHALOGENASE; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:4H77, ECO:0007829|PDB:4H7D};
KW Calcium {ECO:0007829|PDB:4H77, ECO:0007829|PDB:4H7D};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01231, ECO:0000313|EMBL:AMK20862.1};
KW Metal-binding {ECO:0007829|PDB:4H77, ECO:0007829|PDB:4H7D};
KW Plasmid {ECO:0000313|EMBL:AMK20862.1}.
FT DOMAIN 31..279
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 108
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01231"
FT ACT_SITE 132
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01231"
FT ACT_SITE 272
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01231"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007829|PDB:4H77, ECO:0007829|PDB:4H7D"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007829|PDB:4H77, ECO:0007829|PDB:4H7D"
SQ SEQUENCE 296 AA; 33230 MW; B14249854546F602 CRC64;
MSLGAKPFGE KKFIEIKGRR MAYIDEGTGD PILFQHGNPT SSYLWRNIMP HCAGLGRLIA
CDLIGMGDSD KLDPSGPERY TYAEHRDYLD ALWEALDLGD RVVLVVHDWG SVLGFDWARR
HRERVQGIAY MEAVTMPLEW ADFPEQDRDL FQAFRSQAGE ELVLQDNVFV EQVLPGLILR
PLSEAEMAAY REPFLAAGEA RRPTLSWPRQ IPIAGTPADV VAIARDYAGW LSESPIPKLF
INAEPGHLTT GRIRDFCRTW PNQTEITVAG AHFIQEDSPD EIGAAIAAFV RRLRPA
//
