ID A0A0L6CV74_9RHOB Unreviewed; 228 AA.
AC A0A0L6CV74;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
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 Name=hdl IVa {ECO:0000313|EMBL:KNX41667.1};
GN ORFNames=ROTO_17580 {ECO:0000313|EMBL:KNX41667.1};
OS Roseovarius tolerans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=74031 {ECO:0000313|EMBL:KNX41667.1, ECO:0000313|Proteomes:UP000037046};
RN [1] {ECO:0000313|Proteomes:UP000037046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EL-164 {ECO:0000313|Proteomes:UP000037046};
RA Voget S., Bruns H., Wagner-Doebler I., Schulz S., Daniel R.;
RT "Draft Genome Sequence of Roseovarius tolerans EL-164, a producer of N-
RT Acylated Alanine Methyl Esters (NAMEs).";
RL Submitted (JUL-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|ARBA:ARBA00008106,
CC 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:KNX41667.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LGVV01000019; KNX41667.1; -; Genomic_DNA.
DR RefSeq; WP_050662654.1; NZ_LGVV01000019.1.
DR AlphaFoldDB; A0A0L6CV74; -.
DR STRING; 74031.SAMN04488077_10416; -.
DR PATRIC; fig|74031.6.peg.1792; -.
DR OrthoDB; 7989657at2; -.
DR Proteomes; UP000037046; Unassembled WGS sequence.
DR GO; GO:0018784; F:(S)-2-haloacid dehalogenase activity; IEA:UniProtKB-UniRule.
DR CDD; cd02588; HAD_L2-DEX; 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 InterPro; IPR023198; PGP-like_dom2.
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 PRINTS; PR00413; HADHALOGNASE.
DR SFLD; SFLDF00045; 2-haloacid_dehalogenase; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU368077, ECO:0000313|EMBL:KNX41667.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037046}.
SQ SEQUENCE 228 AA; 24672 MW; 6792D92587F51341 CRC64;
MPITTCIFDA YGTLFDVAAA ARSAASEPGR ETFARHWPAI AEKWRLKQLQ YTWLRAVMGE
HVGFWQVTQD GLDWALEAEG LGGDADLRER LLQLYWELEA YPEVPTMLAA LKEAGKDTAI
LSNGAPDMLD GAVKSAGIGA LLDDVLSVES VGIFKPARVV YDLVGQRFGC APEEVLFVSS
NGWDACAAAG YGFNTVWVNR AGDPVDRLPA APDRQLTDLS GIPDLARG
//
