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Database: UniProt
Entry: Q92RC4_RHIME
LinkDB: Q92RC4_RHIME
Original site: Q92RC4_RHIME 
ID   Q92RC4_RHIME            Unreviewed;       220 AA.
AC   Q92RC4;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 108.
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=dhe {ECO:0000313|EMBL:CAC45540.1};
GN   ORFNames=SMc00103 {ECO:0000313|EMBL:CAC45540.1};
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834 {ECO:0000313|EMBL:CAC45540.1, ECO:0000313|Proteomes:UP000001976};
RN   [1] {ECO:0000313|EMBL:CAC45540.1, ECO:0000313|Proteomes:UP000001976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021 {ECO:0000313|EMBL:CAC45540.1,
RC   ECO:0000313|Proteomes:UP000001976};
RX   PubMed=11481430; DOI=10.1073/pnas.161294398;
RA   Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA   Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA   Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA   Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA   Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT   "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT   meliloti strain 1021.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN   [2] {ECO:0000313|Proteomes:UP000001976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021 {ECO:0000313|Proteomes:UP000001976};
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
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}.
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DR   EMBL; AL591688; CAC45540.1; -; Genomic_DNA.
DR   RefSeq; NP_385074.1; NC_003047.1.
DR   RefSeq; WP_003537251.1; NC_003047.1.
DR   AlphaFoldDB; Q92RC4; -.
DR   EnsemblBacteria; CAC45540; CAC45540; SMc00103.
DR   GeneID; 61602434; -.
DR   KEGG; sme:SMc00103; -.
DR   PATRIC; fig|266834.11.peg.2368; -.
DR   eggNOG; COG1011; Bacteria.
DR   HOGENOM; CLU_045011_3_1_5; -.
DR   OrthoDB; 7989657at2; -.
DR   Proteomes; UP000001976; Chromosome.
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; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU368077, ECO:0000313|EMBL:CAC45540.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001976}.
SQ   SEQUENCE   220 AA;  24490 MW;  DCE0B6E5A8D007AF CRC64;
     MSYAAYVFDA YGTLFDVHAA VRRHAEAIGP DGQAFSELWR AKQLEYSWVR SLMGAYVDFW
     ELTEQSLDYA FQRFPSADPK LKKPLLDAYW ALDCYPEVPA VLKGLKELGA RIAILSNGSP
     AMLASAVKNA ALDIIIDDVF SVDAVKAFKT APAVYDLVTT SYRLYPQAVS FQSSNRWDIA
     GATKFGFRTV WINRADGPDE YKDHGPSLIL PSLESLQFGI
//
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