ID B1Y6J3_LEPCP Unreviewed; 231 AA.
AC B1Y6J3;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=HAD-superfamily hydrolase, subfamily IA, variant 3 {ECO:0000313|EMBL:ACB34829.1};
GN OrderedLocusNames=Lcho_2564 {ECO:0000313|EMBL:ACB34829.1};
OS Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS discophora (strain SP-6)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Leptothrix.
OX NCBI_TaxID=395495 {ECO:0000313|EMBL:ACB34829.1, ECO:0000313|Proteomes:UP000001693};
RN [1] {ECO:0000313|EMBL:ACB34829.1, ECO:0000313|Proteomes:UP000001693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51168 / LMG 8142 / SP-6
RC {ECO:0000313|Proteomes:UP000001693};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT "Complete sequence of Leptothrix cholodnii SP-6.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; CP001013; ACB34829.1; -; Genomic_DNA.
DR RefSeq; WP_012347585.1; NC_010524.1.
DR AlphaFoldDB; B1Y6J3; -.
DR STRING; 395495.Lcho_2564; -.
DR KEGG; lch:Lcho_2564; -.
DR eggNOG; COG1011; Bacteria.
DR HOGENOM; CLU_045011_8_2_4; -.
DR OrthoDB; 367448at2; -.
DR Proteomes; UP000001693; Chromosome.
DR GO; GO:0016791; F:phosphatase activity; IEA:UniProt.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR Gene3D; 1.20.120.1600; -; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR023214; HAD_sf.
DR NCBIfam; TIGR01549; HAD-SF-IA-v1; 1.
DR NCBIfam; TIGR01509; HAD-SF-IA-v3; 1.
DR PANTHER; PTHR46470; N-ACYLNEURAMINATE-9-PHOSPHATASE; 1.
DR PANTHER; PTHR46470:SF2; N-ACYLNEURAMINATE-9-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 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ACB34829.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001693}.
SQ SEQUENCE 231 AA; 25070 MW; E085F380C9679408 CRC64;
MTVLALTLDL DDTLWPIAPV IERAEQVTHA WLERQAPATA LRFGVPAMRE LRADVSRRHP
RLAHDLSQLR LIALRESLRA SGDDPALAEP AFEVFFAQRQ QVEFYADVIP ALDRLAARFP
LLALSNGNAE LAATGLSRWF CGSVSARSAG VAKPDVRIFR SACEQLGRAP AQVMHIGDDL
ALDVDGARAA GLQTAWVRRD GVQQPGGSTQ EAGRRHLQVS DLLALADLLG A
//
