ID A0A085AE25_9ENTR Unreviewed; 471 AA.
AC A0A085AE25;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:KFC08470.1};
DE EC=3.1.3.- {ECO:0000313|EMBL:KFC08470.1};
DE EC=3.1.3.1 {ECO:0000313|EMBL:KFC08470.1};
GN Name=phoA {ECO:0000313|EMBL:KFC08470.1};
GN ORFNames=GTGU_01387 {ECO:0000313|EMBL:KFC08470.1};
OS Trabulsiella guamensis ATCC 49490.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Trabulsiella.
OX NCBI_TaxID=1005994 {ECO:0000313|EMBL:KFC08470.1, ECO:0000313|Proteomes:UP000028630};
RN [1] {ECO:0000313|EMBL:KFC08470.1, ECO:0000313|Proteomes:UP000028630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49490 {ECO:0000313|EMBL:KFC08470.1,
RC ECO:0000313|Proteomes:UP000028630};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (MAY-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|ARBA:ARBA00005984, 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:KFC08470.1}.
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DR EMBL; JMTB01000051; KFC08470.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A085AE25; -.
DR eggNOG; COG1785; Bacteria.
DR OrthoDB; 9794455at2; -.
DR Proteomes; UP000028630; 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; 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:KFC08470.1};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..471
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001786271"
FT ACT_SITE 124
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 73
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 344
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 353
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 434
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT DISULFID 190..200
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-3"
FT DISULFID 308..358
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-3"
SQ SEQUENCE 471 AA; 49339 MW; 3B78CA4E860D1D88 CRC64;
MRYSAIFIAL LPLLTAPVIG AEMTSTAVLD NRAAQGDITT PGGARRLSAD QTDAIRASIN
SGKAKNIILL IGDGMGDSEI TAARNYAEGA GGYFKGIDAL PLTGQYTHYA LDKKTGKPDY
VTDSAASATA WSTGVKTYNG ALGVDIHEKD HTTILEMAKA AGLKTGNVST AELQDATPAA
LVSHVTSRKC YGPVVTSEKC PGNALEKGGK GSITEQLLNA RADVTLGGGA KTFSETATAG
EWQGKTLREQ AQARGYQLVS DASSLDAITE ANQDKPLLGL FSEGNMPVRW EGPKASFHGN
IDKPAVTCTP NPKRDASVPT LAQMTEKAIS LLSNGEKGFF LQVEGASIDK QDHAANPCGQ
IGETVDLDEA VQKALEFAKK DGNTLVIVTA DHAHASQIIP ADTKAPGLSQ ALNTKDGAVM
AMTYGNSEEE SMEHTGAQLR IAAYGPHAAN VIGLTDQTDL FYTMKDALAL K
//
