ID   PPB1_PREIN              Reviewed;          20 AA.
AC   P81800;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   22-FEB-2023, entry version 44.
DE   RecName: Full=Alkaline phosphatase;
DE            Short=ALPase;
DE            EC=3.1.3.1;
DE   AltName: Full=PiALP;
DE   Flags: Fragment;
OS   Prevotella intermedia.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=28131 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC   STRAIN=ATCC 25611 / DSM 20706 / JCM 12248 / NCTC 13070 / VPI 4197;
RX   PubMed=9654126; DOI=10.1016/s0014-5793(98)00514-6;
RA   Ansai T., Awano S., Chen X., Fuchi T., Arimoto T., Akifusa S., Takehara T.;
RT   "Purification and characterization of alkaline phosphatase containing
RT   phosphotyrosyl phosphatase activity from the bacterium Prevotella
RT   intermedia.";
RL   FEBS Lett. 428:157-160(1998).
CC   -!- FUNCTION: Acts against tyrosine-phosphatases. {ECO:0000305}.
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=3.1.3.1;
CC   -!- ACTIVITY REGULATION: Completely inhibited by thiol-reducing agents,
CC       such as DTT and 2-mercaptoethanol. Activity was also inhibited by
CC       sodium orthovanadate, sodium molybdate, N-ethylmaleimide, EDTA and zinc
CC       ion, but was not inhibited by okadaic acid.
CC   -!- SUBUNIT: Homodimer; may be disulfide-linked. {ECO:0000305}.
CC   -!- PTM: The N-terminus is blocked.
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DR   AlphaFoldDB; P81800; -.
DR   STRING; 28131.BWX40_11465; -.
DR   GO; GO:0004035; F:alkaline phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0030945; F:protein tyrosine phosphatase activity, via thiol-phosphate intermediate; IDA:UniProtKB.
DR   GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hydrolase.
FT   CHAIN           <1..>20
FT                   /note="Alkaline phosphatase"
FT                   /id="PRO_0000058533"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000305"
FT   NON_TER         20
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   20 AA;  2053 MW;  A8D8A9276AE0ED83 CRC64;
     TDMLAVSVSS TDAIGHKYGT
//