ID A0A0S2FU08_9GAMM Unreviewed; 567 AA.
AC A0A0S2FU08;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Alkaline phosphatase 3, intestine, not Mn requiring {ECO:0000313|EMBL:ALN86996.1};
DE EC=3.1.3.1 {ECO:0000313|EMBL:ALN86996.1};
GN Name=akp3 {ECO:0000313|EMBL:ALN86996.1};
GN ORFNames=LC55x_3739 {ECO:0000313|EMBL:ALN86996.1};
OS Lysobacter capsici.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=435897 {ECO:0000313|EMBL:ALN86996.1};
RN [1] {ECO:0000313|EMBL:ALN86996.1, ECO:0000313|Proteomes:UP000059881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=55 {ECO:0000313|EMBL:ALN86996.1,
RC ECO:0000313|Proteomes:UP000059881};
RX PubMed=26597042; DOI=10.1186/s12864-015-2191-z;
RA de Bruijn I., Cheng X., de Jager V., Exposito R.G., Watrous J., Patel N.,
RA Postma J., Dorrestein P.C., Kobayashi D., Raaijmakers J.M.;
RT "Comparative genomics and metabolic profiling of the genus Lysobacter.";
RL BMC Genomics 16:991-991(2015).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP011130; ALN86996.1; -; Genomic_DNA.
DR RefSeq; WP_057922214.1; NZ_CP011130.1.
DR AlphaFoldDB; A0A0S2FU08; -.
DR STRING; 435897.LC55x_3739; -.
DR KEGG; lcp:LC55x_3739; -.
DR PATRIC; fig|435897.5.peg.3732; -.
DR Proteomes; UP000059881; Chromosome.
DR GO; GO:0004035; F:alkaline phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16012; ALP; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR001952; Alkaline_phosphatase.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
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 PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:ALN86996.1};
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..567
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006597584"
FT REGION 416..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 129
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 79
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 349
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 358
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 395
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 503
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 567 AA; 60150 MW; 8322AF19E431B191 CRC64;
MSKLRSASVL LVPALLTACA AAAPTRSDAP GAGVAVDVPA IQHPQGETPA WWYRDGAAQA
AQRGASSAKA KNVILFVGDG MSLTTVAAAR ILAGQLKGAP GEENRLSWER FPSTALSKTY
NTDSQTPDSA GTMSAMATGV KTRAGVLSIG QKGLRGDCAA ALQAPMLTLW ELAASQGLAT
GVVTTTRVTH ATPGATFSHS ADRNWENDMD LPDKAKSEGC IDIARQMIES PYGTGPDVLM
GGGRGNFMTV EQRDPEYDDK VGQRLDGRDL IATWKQRHPG GEYVWNAKQF AAAPKDKPLF
ALFEPDHMQF DHDRPQDGAG EPSLAEMTVA AIERLKKVKG DNGFVLLVEG GRIDHAHHMG
NAYRALTDTI ALSEAVEAAN KATSADDTLI LVTADHSHTL SFVGYPTRGN PMLGKVRGSS
GEDGDPSDYA RDALGKPYTT LNYSNGPGYT GASSQQPEGP HKFPHTASGM QEIEKGRPDL
SNVDTQAPDY MQEALVPTTA ETHGGDDVGI WARGPGSSAV RGSVEQNTIY HFLLQSMPKL
RASLCAKGDC DANQVPVMLP KADQFKN
//
