ID A0A0U5FFQ6_XANCI Unreviewed; 566 AA.
AC A0A0U5FFQ6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Alkaline phosphatase, placental-like {ECO:0000313|EMBL:CEG17234.1};
DE EC=3.1.3.1 {ECO:0000313|EMBL:CEG17234.1};
GN Name=ALPPL {ECO:0000313|EMBL:CEG17234.1};
GN ORFNames=XAC3562_610106 {ECO:0000313|EMBL:CEG17234.1};
OS Xanthomonas citri pv. citri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=611301 {ECO:0000313|EMBL:CEG17234.1, ECO:0000313|Proteomes:UP000052230};
RN [1] {ECO:0000313|Proteomes:UP000052230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Regsiter Alias;
RL Submitted (SEP-2014) 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:CEG17234.1}.
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; CCXZ01000157; CEG17234.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U5FFQ6; -.
DR KEGG; xcf:J172_02932; -.
DR KEGG; xcm:J164_02924; -.
DR KEGG; xcn:J169_02939; -.
DR KEGG; xcr:J163_02924; -.
DR KEGG; xcu:J159_02924; -.
DR KEGG; xcw:J162_02927; -.
DR Proteomes; UP000052230; Unassembled WGS sequence.
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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:CEG17234.1};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..566
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006856882"
FT REGION 437..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 128
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 78
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 188
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 346
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 391
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 498
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 566 AA; 59860 MW; 00208ABD9A13E252 CRC64;
MRYRLPTLAA LTTLCVAACA STTGSGTSAP ASVRVEVPPV THPAGETPQW WYRSGAARAA
GNGAMAGKAR NVILFLGDGM SLTTVAAARI LDGQRKGGPG EENLLSWEQF PATAFSKTYN
TDSQTPDSAG TMTSITTGVK SHMGAIGVSS GNRSDCADSL NKGLLSWLQL ADSAGMATGI
VTTTRLTHAT PAATYAHSPD RNWENDTDLP ESARAAGCQD IAQQLLSTAR YGRGPQVVLG
GGRSQFQSVQ ERDPEYDDKV GLRLDGRDLV AEWKQAHPQG AYVWNEQQLQ AASGAPALLG
LFEPDHMQFD HDRNRTPQGE PSLTEMTRTA IQSLSREPNG FVLMVEGGRI DHANHAGNAY
RALDETVSLS DAVRVAVQTA PPDTLIIVTA DHSHTLNFVG YPVRGNPILG KVRGTGGEEG
DRSQLATDLA GQPYTTLSYA NGPGYTGASN AQPAGPKKYP HEPSSSEPAT GRPDLSHVDT
EAPSYMQEAL VPTKSESHGG EDVGIWATGP GSAAFRGTLE ENVIYHVIVQ ATPRLRERLC
KAGTCNAAGV PVELPKPATF EAAVKR
//
