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Database: UniProt
Entry: A0A0U2NGM0_9BURK
LinkDB: A0A0U2NGM0_9BURK
Original site: A0A0U2NGM0_9BURK 
ID   A0A0U2NGM0_9BURK        Unreviewed;       243 AA.
AC   A0A0U2NGM0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Acid phosphatase {ECO:0000256|PIRNR:PIRNR000897};
DE            EC=3.1.3.2 {ECO:0000256|PIRNR:PIRNR000897};
GN   ORFNames=AT302_20590 {ECO:0000313|EMBL:ALS61815.1};
OS   Pandoraea norimbergensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Pandoraea.
OX   NCBI_TaxID=93219 {ECO:0000313|EMBL:ALS61815.1, ECO:0000313|Proteomes:UP000060277};
RN   [1] {ECO:0000313|Proteomes:UP000060277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11628 {ECO:0000313|Proteomes:UP000060277};
RA   Ee R., Lim Y.-L., Yong D., Yin W.-F., Chan K.-G.;
RT   "Complete genome sequence of Pandoraea norimbergensis DSM 11628.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC         Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000897};
CC   -!- SIMILARITY: Belongs to the class A bacterial acid phosphatase family.
CC       {ECO:0000256|PIRNR:PIRNR000897}.
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DR   EMBL; CP013480; ALS61815.1; -; Genomic_DNA.
DR   RefSeq; WP_058378725.1; NZ_CP013480.3.
DR   AlphaFoldDB; A0A0U2NGM0; -.
DR   STRING; 93219.AT302_20590; -.
DR   KEGG; pnr:AT302_20590; -.
DR   OrthoDB; 9780507at2; -.
DR   Proteomes; UP000060277; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd03397; PAP2_acid_phosphatase; 1.
DR   Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR   InterPro; IPR001011; Acid_Pase_classA_bac.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   Pfam; PF01569; PAP2; 1.
DR   PIRSF; PIRSF000897; Acid_Ptase_ClsA; 1.
DR   PRINTS; PR00483; BACPHPHTASE.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR000897};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..243
FT                   /note="Acid phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006831525"
FT   DOMAIN          109..217
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
SQ   SEQUENCE   243 AA;  25955 MW;  DD57C2331C119CEC CRC64;
     MLPVSTRYGR PFVAALLLLS ALHAVQAAEL PHADYLSGAA PDLTVLVAPP PAPGTLAAAD
     DLRQVLALQR SRTAAQLALA DGDTHKSVFR FADVIGTDFR AERLPFTEAF FKRLAKEGAG
     PLKAAKDYWK RPRPYNVSAE VHPGIVTEGT SPSYPSGHAT FAYLSAVILA KIVPEKRAEI
     FARAEAYAQG RALGGVHYVS DVEAGKVSGT VIAAAMLANP AFRDDLMRAT RETREALSLP
     PLQ
//
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