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Database: UniProt
Entry: D3P4N8_AZOS1
LinkDB: D3P4N8_AZOS1
Original site: D3P4N8_AZOS1 
ID   D3P4N8_AZOS1            Unreviewed;       222 AA.
AC   D3P4N8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   24-JAN-2024, entry version 64.
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   OrderedLocusNames=AZL_c03240 {ECO:0000313|EMBL:BAI75617.1};
OS   Azospirillum sp. (strain B510).
OG   Plasmid pAB510c {ECO:0000313|EMBL:BAI75617.1,
OG   ECO:0000313|Proteomes:UP000002040}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=137722 {ECO:0000313|EMBL:BAI75617.1, ECO:0000313|Proteomes:UP000002040};
RN   [1] {ECO:0000313|EMBL:BAI75617.1, ECO:0000313|Proteomes:UP000002040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B510 {ECO:0000313|EMBL:BAI75617.1,
RC   ECO:0000313|Proteomes:UP000002040};
RC   PLASMID=pAB510c {ECO:0000313|EMBL:BAI75617.1};
RX   PubMed=20047946; DOI=10.1093/dnares/dsp026;
RA   Kaneko T., Minamisawa K., Isawa T., Nakatsukasa H., Mitsui H.,
RA   Kawaharada Y., Nakamura Y., Watanabe A., Kawashima K., Ono A., Shimizu Y.,
RA   Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M., Nakazaki N.,
RA   Nakayama S., Yamada M., Tabata S., Sato S.;
RT   "Complete genomic structure of the cultivated rice endophyte Azospirillum
RT   sp. B510.";
RL   DNA Res. 17:37-50(2010).
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}.
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DR   EMBL; AP010949; BAI75617.1; -; Genomic_DNA.
DR   RefSeq; WP_012977447.1; NC_013857.1.
DR   AlphaFoldDB; D3P4N8; -.
DR   KEGG; azl:AZL_c03240; -.
DR   HOGENOM; CLU_045011_3_2_5; -.
DR   OrthoDB; 9785638at2; -.
DR   Proteomes; UP000002040; Plasmid pAB510c.
DR   GO; GO:0018784; F:(S)-2-haloacid dehalogenase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd02588; HAD_L2-DEX; 1.
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; IPR041492; HAD_2.
DR   InterPro; IPR023214; HAD_sf.
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; PF13419; HAD_2; 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, ECO:0000313|EMBL:BAI75617.1};
KW   Plasmid {ECO:0000313|EMBL:BAI75617.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002040}.
SQ   SEQUENCE   222 AA;  25091 MW;  D46D128B8FD50B10 CRC64;
     MSQFRPKYVT FDCHGTLINF QMAEAARDLY GSILDAARMT EFIRNFAAYR LDEIMGDWKP
     YAEVVHNSLE RTCKRNNVAF REEDARMVYE RVPTWGPHAD VPAGLAKVAK EIPLVILSNA
     MNDQIPSNVA KLGAPFHAVY TAEQAQAYKP RFKAFEYMFD MLGCGPEDIL HCSSSFRYDL
     MSAHDLGIRN KVWVNRGHEP ANPYYGYVEI ADISGLPGVV GL
//
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