ID   A0A0Q9LZC0_9BACL        Unreviewed;       264 AA.
AC   A0A0Q9LZC0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Haloacid dehalogenase {ECO:0000313|EMBL:KRE59498.1};
GN   ORFNames=ASL11_25005 {ECO:0000313|EMBL:KRE59498.1};
OS   Paenibacillus sp. Soil750.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1736398 {ECO:0000313|EMBL:KRE59498.1, ECO:0000313|Proteomes:UP000051252};
RN   [1] {ECO:0000313|EMBL:KRE59498.1, ECO:0000313|Proteomes:UP000051252}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil750 {ECO:0000313|EMBL:KRE59498.1,
RC   ECO:0000313|Proteomes:UP000051252};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE59498.1, ECO:0000313|Proteomes:UP000051252}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil750 {ECO:0000313|EMBL:KRE59498.1,
RC   ECO:0000313|Proteomes:UP000051252};
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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:KRE59498.1}.
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DR   EMBL; LMSD01000034; KRE59498.1; -; Genomic_DNA.
DR   RefSeq; WP_056620913.1; NZ_LMSD01000034.1.
DR   AlphaFoldDB; A0A0Q9LZC0; -.
DR   STRING; 1736398.ASL11_25005; -.
DR   OrthoDB; 9809962at2; -.
DR   Proteomes; UP000051252; Unassembled WGS sequence.
DR   GO; GO:0036424; F:L-phosphoserine phosphatase activity; IEA:InterPro.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   Gene3D; 1.20.120.710; Haloacid dehalogenase hydrolase-like domain; 1.
DR   HAMAP; MF_02240; PSP; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR044266; PSP_YsaA.
DR   NCBIfam; TIGR01549; HAD-SF-IA-v1; 1.
DR   PANTHER; PTHR46470; N-ACYLNEURAMINATE-9-PHOSPHATASE; 1.
DR   PANTHER; PTHR46470:SF5; PHOSPHOSERINE PHOSPHATASE; 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;
SQ   SEQUENCE   264 AA;  29387 MW;  BEB4B3B9D9DF234B CRC64;
     MTLKAVLFDL DDTLLWDDRS VEEAFAATCA EAAKQVNGLN PEELEASVRK EARSLYESFD
     TFPFTKMIGI NPFEGLWANF TQGEDENFRK LEKLAPGYRT ESWTRGLAGL GIEDRDLGYK
     LGELFAAERR SRPYVYEETF RVLDELKGNY KLLLLTNGSP DLQKEKLAGV PEIAAYFDHI
     VISGEFGQGK PAAAIFNYAL GLLEINAEEG IMIGDKLTTD ILGSGSIGMR NIWINHHGLQ
     SGDEIVPAYE VSRLQEILPI ISNG
//