ID G8TM68_NIAKG Unreviewed; 621 AA.
AC G8TM68;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:AEV99841.1};
GN OrderedLocusNames=Niako_3540 {ECO:0000313|EMBL:AEV99841.1};
OS Niastella koreensis (strain DSM 17620 / KACC 11465 / NBRC 106392 /
OS GR20-10).
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Niastella.
OX NCBI_TaxID=700598 {ECO:0000313|EMBL:AEV99841.1, ECO:0000313|Proteomes:UP000005438};
RN [1] {ECO:0000313|EMBL:AEV99841.1, ECO:0000313|Proteomes:UP000005438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17620 / KACC 11465 / NBRC 106392 / GR20-10
RC {ECO:0000313|Proteomes:UP000005438};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Davenport K.,
RA Saunders E., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Niastella koreensis GR20-10.";
RL Submitted (DEC-2011) 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}.
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DR EMBL; CP003178; AEV99841.1; -; Genomic_DNA.
DR RefSeq; WP_014219755.1; NC_016609.1.
DR AlphaFoldDB; G8TM68; -.
DR STRING; 700598.Niako_3540; -.
DR KEGG; nko:Niako_3540; -.
DR PATRIC; fig|700598.3.peg.3624; -.
DR eggNOG; COG1785; Bacteria.
DR HOGENOM; CLU_445393_0_0_10; -.
DR OrthoDB; 9794455at2; -.
DR Proteomes; UP000005438; Chromosome.
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; 3.
DR Pfam; PF13653; GDPD_2; 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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..621
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003516923"
FT ACT_SITE 332
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 291
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 383
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 385
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 507
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 512
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 516
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 554
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 555
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 621 AA; 68825 MW; 535F3C1347465CC9 CRC64;
MNKLLFTLLI VLRTTAFSQP ANYTVANAHS HNDYEQPVPL LTAYNETFGS IEADIFWYNG
EILVAHSEKE LALHRTLEDM YLKPLQSFIE KNKGHIYADA ARHLQFMIDI KTDSVTTLNK
LVELLRKYPV LTQCSTLQIA ISGNRPEVSA YASYPSFIWF DGELQKEYPA AALARVVMLS
ADLKKYTMWN GKGIIPSPQW DTLQKLVSHA HALNKRVRFW GAPDFTNAWI QLMRLQVDYI
NTDSIKALSD FLRKMPSNSF KNKTGYKPYQ PTFLHDGVDK PVKNILLFIG DGTGLAQLYA
GYTANKGALN VFNMRNIGFS KTSSYDCYVT DSAPGSTAFA SGEKTNNRHV GVDHTGVAIP
LLPVFLKTKN IKTGLVTCGD ITDATPADFY AHQTDRENSI AIIHDLKKAD IDLLMGSGRE
SLANVALLEG NVKDAGSDSA FQELSPEFTV VHSVDSVKDV PGKKWVVVDP KAGLPVLRGR
EHWLEQAFSK AVKTLSRNKA GFFLMTEGAQ VDYGGHANDL SYVASEVMDF DQVIGKAMQF
ADADGQTLVI VTADHETGGL SLLAGDYSNG YVSGNFSTND HTATPVPVFA YGPQSFRFRG
VYENTELFYR MMAALNIPIR K
//