ID E0TDX9_PARBH Unreviewed; 502 AA.
AC E0TDX9;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Alkaline phosphatase family protein {ECO:0000313|EMBL:ADM10428.1};
GN OrderedLocusNames=PB2503_11924 {ECO:0000313|EMBL:ADM10428.1};
OS Parvularcula bermudensis (strain ATCC BAA-594 / HTCC2503 / KCTC 12087).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Parvularculales;
OC Parvularculaceae; Parvularcula.
OX NCBI_TaxID=314260 {ECO:0000313|EMBL:ADM10428.1, ECO:0000313|Proteomes:UP000001302};
RN [1] {ECO:0000313|Proteomes:UP000001302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-594 / HTCC2503 / KCTC 12087
RC {ECO:0000313|Proteomes:UP000001302};
RA Kang D.-M., Oh H.-M., Cho J.-C.;
RT "Genome sequence of Parvularcula bermudensis HTCC2503.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADM10428.1, ECO:0000313|Proteomes:UP000001302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-594 / HTCC2503 / KCTC 12087
RC {ECO:0000313|Proteomes:UP000001302};
RX PubMed=21037002; DOI=10.1128/JB.01205-10;
RA Oh H.M., Kang I., Vergin K.L., Kang D., Rhee K.H., Giovannoni S.J.,
RA Cho J.C.;
RT "Complete genome sequence of strain HTCC2503T of Parvularcula bermudensis,
RT the type species of the order "Parvularculales" in the class
RT Alphaproteobacteria.";
RL J. Bacteriol. 193:305-306(2011).
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; CP002156; ADM10428.1; -; Genomic_DNA.
DR RefSeq; WP_013301402.1; NC_014414.1.
DR AlphaFoldDB; E0TDX9; -.
DR STRING; 314260.PB2503_11924; -.
DR KEGG; pbr:PB2503_11924; -.
DR eggNOG; COG1785; Bacteria.
DR HOGENOM; CLU_008539_4_1_5; -.
DR OrthoDB; 9794455at2; -.
DR Proteomes; UP000001302; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
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 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:UP000001302};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..502
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003140545"
FT ACT_SITE 106
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 56
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 167
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 169
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 324
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 371
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 463
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 502 AA; 53048 MW; 9608813DBFC600A4 CRC64;
MVLAVIAASA LAMQSASVSP AGPTDWVAQG EAALEAAKAV TPRVGRAKNA ILFIADGMDV
TTITAGRILA GQQQGKLGED HVLAFETLPF TALSKTYTTN MQTADSAGTA TAMLSGHKTK
SGVINVDQTV PRGDCAAAEG KALTSLMHVA AATDRQVGVV STARLTHATP ATVYASSADR
NWEADRDLPE EADGCTDIAT QLITAAQSFP IRVALGGGRR NFLPQSSVDP EYDDKTGARE
DGRNLTAEWT AIAPGYLYVW NAEQFGALSP TEEGAVLGLF EPSHMNYAVD RQDDAAGEPS
LSEMTSFAID KLSQHEEGYF LLVEGGRIDH AHHAGNAARA LNDLIAFDAA IETALQKVDL
DETLIIVTAD HGHTLVLQGY PHRGNPILGL VRSVNGAGAP IDTPFPGGDG KPYTTLVYGN
GPGSPFARPS SDQAIERQFV TDDEAQAIDY RQQSIVPGGS ETHGGQDVTI HAVGPQAHLI
RGTVEQNYIY YVIRDALTYQ AE
//
