ID A0A068QP18_9GAMM Unreviewed; 478 AA.
AC A0A068QP18;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:CDG16361.1};
DE EC=3.1.3.1 {ECO:0000313|EMBL:CDG16361.1};
GN Name=phoA {ECO:0000313|EMBL:CDG16361.1};
GN ORFNames=XDD1_0658 {ECO:0000313|EMBL:CDG16361.1};
OS Xenorhabdus doucetiae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=351671 {ECO:0000313|EMBL:CDG16361.1, ECO:0000313|Proteomes:UP000032721};
RN [1] {ECO:0000313|EMBL:CDG16361.1, ECO:0000313|Proteomes:UP000032721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FRM16 / DSM 17909 {ECO:0000313|Proteomes:UP000032721};
RA Genoscope - CEA;
RL Submitted (JUL-2013) 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|ARBA:ARBA00005984, ECO:0000256|RuleBase:RU003946}.
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DR EMBL; FO704550; CDG16361.1; -; Genomic_DNA.
DR RefSeq; WP_045968570.1; NZ_VNHN01000027.1.
DR AlphaFoldDB; A0A068QP18; -.
DR STRING; 351671.XDD1_0658; -.
DR KEGG; xdo:XDD1_0658; -.
DR HOGENOM; CLU_008539_0_1_6; -.
DR OrthoDB; 9794455at2; -.
DR Proteomes; UP000032721; 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; IPR018299; Alkaline_phosphatase_AS.
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; PS00123; ALKALINE_PHOSPHATASE; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601952-3};
KW Hydrolase {ECO:0000313|EMBL:CDG16361.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, 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};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601952-2}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..478
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001652123"
FT ACT_SITE 131
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 80
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 351
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 398
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 399
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 441
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT DISULFID 197..207
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-3"
FT DISULFID 315..365
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-3"
SQ SEQUENCE 478 AA; 51007 MW; E5E542FC69A191AC CRC64;
MSRHYEKKRL AAVIAVLMSG VIAPSWATGD ANHIIEQPRA AQGNITEFGG ARRLTQDQTQ
ALKAALNNHK AKNVILFIGD GMGDSEITLA RNYAEGAGGF FKGIDALPFT GQYTHYSLDK
KTHKPNYVTD SAASATAWAT GVKTYNGALG IDVFGKSHQS LLTLAKKNGK ATGNITTAEI
QDATPAALYA HVTNRKCYGP EETSKICATD ALENGGKGSI TEQLLAVRAD VTLGGGAKSF
TQQSVSGVNK GKTLQQQALE QGYQWVTDAQ SLAAVKNANQ QTPLLGLFHE GNMDVAWQGP
KAVYHGNINE KPVKCAVNSK LDPNAPTLAQ MTEKTIDLLK KNNNGFFLQV ESASIDKQDH
KSNPCAQIGE TVALDKAVQV GLKFAKEHGN TLVIVTADHA HASQIIEPDV KSPGLTRSLI
TKDGAIMTVN YGNSEGDTQE HTGTQLRVAA YGPYAANVVG LTDQTDLFFT LRDAMGLK
//
