ID A0A0D0GLS3_9SPHI Unreviewed; 616 AA.
AC A0A0D0GLS3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:KIO75331.1};
GN ORFNames=TH53_21205 {ECO:0000313|EMBL:KIO75331.1};
OS Pedobacter lusitanus.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1503925 {ECO:0000313|EMBL:KIO75331.1, ECO:0000313|Proteomes:UP000032049};
RN [1] {ECO:0000313|EMBL:KIO75331.1, ECO:0000313|Proteomes:UP000032049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NL19 {ECO:0000313|EMBL:KIO75331.1,
RC ECO:0000313|Proteomes:UP000032049};
RA Santos T., Caetano T., Covas C., Cruz A., Mendo S.;
RT "Draft genome sequence of Pedobacter sp. NL19 isolated from sludge of an
RT effluent treatment pond in an abandoned uranium mine.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR601952-2};
CC Note=Binds 1 Mg(2+) ion. {ECO:0000256|PIRSR:PIRSR601952-2};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR601952-2};
CC Note=Binds 2 Zn(2+) ions. {ECO:0000256|PIRSR:PIRSR601952-2};
CC -!- SIMILARITY: Belongs to the alkaline phosphatase family.
CC {ECO:0000256|RuleBase:RU003946}.
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:KIO75331.1}.
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DR EMBL; JXRA01000105; KIO75331.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0GLS3; -.
DR STRING; 1503925.TH53_21205; -.
DR Proteomes; UP000032049; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd16012; ALP; 1.
DR CDD; cd08577; PI-PLCc_GDPD_SF_unchar3; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR InterPro; IPR039559; AIM6_PI-PLC-like_dom.
DR InterPro; IPR001952; Alkaline_phosphatase.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1.
DR PANTHER; PTHR11596:SF5; ALKALINE PHOSPHATASE; 1.
DR Pfam; PF00245; Alk_phosphatase; 1.
DR PRINTS; PR00113; ALKPHPHTASE.
DR SMART; SM00098; alkPPc; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|PIRSR:PIRSR601952-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601952-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..616
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002211037"
FT ACT_SITE 338
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 297
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 297
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 389
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 391
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 505
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 510
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 514
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 552
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 553
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 616 AA; 68145 MW; 1F794B2678DC6457 CRC64;
MKKLSCYSFF ALLLLAANVQ AQQPLSFNSG HSHNDYKQNI PLLRAYYAGM GSIEADVFLK
DGQLFVAHEL KEIKPGATLL KQYLEPLYRL YKENGNHPYA DPKLKLQLVI DIKEDHEHVL
PALLKELKPF QDMVNKPLNP DAVSIVISGD MPKPENFKNY PAIISFDGRP TTVYTDEQLE
RVAMISDELK HYTVWNGKGT PTQTDADKLK MVIGAAHQKG KPFRFWATQD SPNTWLELEK
FGVDWINTDA PEKLKEFYLR KDKLTYTNPV AYPVYQPTYK SDGLNKKVKN IILLIGDGMG
LAQIHAGWIA NHGNLNITML RNSGFSQTAA ANSGNTDSAA GGSAIAMGEK TNNRYIGMGT
DDKKRTNLVD TLASYGLKSG IISAGDITDA TPAVFYAHQL DRSYSEAIAA DFLNSHVDIL
VGSNQKSFLQ NPDASLLSKL ENKGYTLSKS LSDFKLKDSG KQLVLLPDSA TRPVKDGRGD
MLAQSLKHTI KLLSANKKGF FIMTEGAQID YGGHVNDLKY VVTELHDFDK TVAEAVRFAD
QDGETLVLIT ADHETGGLTL LDAAAAEGRI EGEFSTNDHT NIMVPVYAYG PHSGDFTGTY
SNTEIFKKIL RLFTAR
//
