ID A0A1T5N9I7_9BACT Unreviewed; 609 AA.
AC A0A1T5N9I7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:SKC97157.1};
GN ORFNames=SAMN05660461_0859 {ECO:0000313|EMBL:SKC97157.1};
OS Chitinophaga ginsengisegetis.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=393003 {ECO:0000313|EMBL:SKC97157.1, ECO:0000313|Proteomes:UP000190166};
RN [1] {ECO:0000313|EMBL:SKC97157.1, ECO:0000313|Proteomes:UP000190166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18108 {ECO:0000313|EMBL:SKC97157.1,
RC ECO:0000313|Proteomes:UP000190166};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUZZ01000001; SKC97157.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5N9I7; -.
DR STRING; 393003.SAMN05660461_0859; -.
DR Proteomes; UP000190166; 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; 3.
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 Reference proteome {ECO:0000313|Proteomes:UP000190166};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..609
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011962104"
FT ACT_SITE 336
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 295
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 499
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 504
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 508
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 546
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 547
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 609 AA; 66918 MW; B434E184971B5021 CRC64;
MKKALFILSG VIMATGASAQ IKQYTMAQAH SHNDYERATP FYAAASLQFG SIEADIHLKD
GVLYVAHDAG AIQPFRTFKE LYLLPVLRQF SLYNGKPYAG NAPMQLLIDL KTAGTPTLQA
LQELLLPYRN YFDRNTNPSA VKLVISGNVP PVAEWPKYDP IFFFDGRPDS VYPAALQQRV
AMLSVDFHSY STWNGKGTLV PEEMKKVTTV INKAHQQGYA FRFWGAPSTR STYYKLMDLG
ADWIGTDHPE ELYDVMHNTP RTTASGMPVH EVYTPSFVSD ATKVRSKNVI LMIGDGTGLA
EMFSGYTANK GALNIFQMRQ LGLSKTQSTD NYHTDSAAGG SAMGTGTKTH NRAIGLDNTY
VSIPVIPEIL APKGIQSGVI VTEEITGATP ASFYGHTSDR DSTYTLEKQL LSSKLQLAVG
GGREELEKDF GGQLASSGIR IYDNLDNWDA TTKNRTLVVL SNKVVTSMRN GRGNYLKTAL
KKALQQLNAS GKGFFLMVEG SRIDHGGHLN DLDYLVREML DFDEAVGEAL RFADQDKQTT
VIVTADHETG GLALMDGDIA TGTLRGHFAT NDHTGIPVMV FAYGPNSNLF RGVYENNEIF
HKMLKCFGK
//
