ID A0A0Q4CPI5_9SPHN Unreviewed; 222 AA.
AC A0A0Q4CPI5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=(S)-2-haloacid dehalogenase {ECO:0000256|RuleBase:RU368077};
DE EC=3.8.1.2 {ECO:0000256|RuleBase:RU368077};
DE AltName: Full=2-haloalkanoic acid dehalogenase {ECO:0000256|RuleBase:RU368077};
DE AltName: Full=Halocarboxylic acid halidohydrolase {ECO:0000256|RuleBase:RU368077};
DE AltName: Full=L-2-haloacid dehalogenase {ECO:0000256|RuleBase:RU368077};
GN ORFNames=ASE58_08660 {ECO:0000313|EMBL:KQM27051.1};
OS Sphingomonas sp. Leaf9.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1735674 {ECO:0000313|EMBL:KQM27051.1, ECO:0000313|Proteomes:UP000051210};
RN [1] {ECO:0000313|EMBL:KQM27051.1, ECO:0000313|Proteomes:UP000051210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf9 {ECO:0000313|EMBL:KQM27051.1,
RC ECO:0000313|Proteomes:UP000051210};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM27051.1, ECO:0000313|Proteomes:UP000051210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf9 {ECO:0000313|EMBL:KQM27051.1,
RC ECO:0000313|Proteomes:UP000051210};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydrolytic dehalogenation of small (S)-2-
CC haloalkanoic acids to yield the corresponding (R)-2-hydroxyalkanoic
CC acids. {ECO:0000256|RuleBase:RU368077}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an (S)-2-haloacid + H2O = a (2R)-2-hydroxycarboxylate + a
CC halide anion + H(+); Xref=Rhea:RHEA:11192, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:58314,
CC ChEBI:CHEBI:137405; EC=3.8.1.2;
CC Evidence={ECO:0000256|RuleBase:RU368077};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. S-2-
CC haloalkanoic acid dehalogenase family. {ECO:0000256|RuleBase:RU368077}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQM27051.1}.
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DR EMBL; LMKC01000003; KQM27051.1; -; Genomic_DNA.
DR RefSeq; WP_055820041.1; NZ_LMKC01000003.1.
DR AlphaFoldDB; A0A0Q4CPI5; -.
DR OrthoDB; 9785638at2; -.
DR Proteomes; UP000051210; Unassembled WGS sequence.
DR GO; GO:0018784; F:(S)-2-haloacid dehalogenase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.150.750; -; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR006328; 2-HAD.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR023214; HAD_sf.
DR NCBIfam; TIGR01549; HAD-SF-IA-v1; 1.
DR NCBIfam; TIGR01493; HAD-SF-IA-v2; 1.
DR NCBIfam; TIGR01428; HAD_type_II; 1.
DR PANTHER; PTHR43316:SF3; HALOACID DEHALOGENASE, TYPE II (AFU_ORTHOLOGUE AFUA_2G07750)-RELATED; 1.
DR PANTHER; PTHR43316; HYDROLASE, HALOACID DELAHOGENASE-RELATED; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU368077}.
SQ SEQUENCE 222 AA; 24901 MW; 3B1D90FA2004CB0C CRC64;
MAGLRPKYIS FDCYGTLINF EMAPVARTLY ADRVAAEALD QFTADFSAYR LDEVLGAWKP
YRDVVESALR RTCARNGVEY RDSDTATVYA AVPTWRPHAD VVEPLKRVAA EYPLVILSNS
MVDLIPHSVE KLEAPFHAVY TAEEAQAYKP RMQAFEYMLD QLGCAPEDML HVSSSFRYDQ
MTAYDMGIKS KAFVDRGHEP VNPYYEVNVI PSLAGLPGLV GL
//
