ID A0A1F8P427_9CHLR Unreviewed; 268 AA.
AC A0A1F8P427;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 18.
DE RecName: Full=Haloacid dehalogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2Z14_03065 {ECO:0000313|EMBL:OGO17926.1};
OS Chloroflexi bacterium RBG_16_48_8.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797641 {ECO:0000313|EMBL:OGO17926.1, ECO:0000313|Proteomes:UP000177106};
RN [1] {ECO:0000313|EMBL:OGO17926.1, ECO:0000313|Proteomes:UP000177106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR000915-3};
CC Note=Divalent metal ions. Mg(2+) is the most effective.
CC {ECO:0000256|PIRSR:PIRSR000915-3};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC {ECO:0000256|PIRNR:PIRNR000915}.
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:OGO17926.1}.
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DR EMBL; MGNI01000116; OGO17926.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8P427; -.
DR STRING; 1797641.A2Z14_03065; -.
DR Proteomes; UP000177106; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR006357; HAD-SF_hydro_IIA.
DR InterPro; IPR023214; HAD_sf.
DR NCBIfam; TIGR01549; HAD-SF-IA-v1; 1.
DR NCBIfam; TIGR01460; HAD-SF-IIA; 1.
DR PANTHER; PTHR19288; 4-NITROPHENYLPHOSPHATASE-RELATED; 1.
DR PANTHER; PTHR19288:SF46; HALOACID DEHALOGENASE-LIKE HYDROLASE DOMAIN-CONTAINING PROTEIN 2; 1.
DR Pfam; PF13344; Hydrolase_6; 1.
DR Pfam; PF13242; Hydrolase_like; 1.
DR PIRSF; PIRSF000915; PGP-type_phosphatase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|PIRSR:PIRSR000915-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000915-3}.
FT ACT_SITE 13
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT ACT_SITE 15
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT BINDING 15
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT BINDING 212
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
SQ SEQUENCE 268 AA; 29076 MW; 34F623A93B9A2805 CRC64;
MKELHSLQGL IIDLDGVIWR GEKLLTGVLP FFNELHSRSI PYIFATNNAT TTPRKLCQRA
HGLGFEMREE QIITSSQAAV SLLCQQLQEG AAIYVIGEEG IQEALEAAHF QLTHSADHAQ
AVVVAMDRRV NWDKMAEAAY AIANGAIFLG TNSDPSFPTE RGFAPGNGAI LNALQLTTNV
VPIVVGKPEP FLFLHALDHL GTKPEYTLVV GDRLTTDILG GINAGMMTAL LLTGVTSPEA
LAESSIQPDF VYETLDVLVK SLRQEPKT
//
