ID   A0A0B1ZQP0_9SPHN        Unreviewed;       562 AA.
AC   A0A0B1ZQP0;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Alkaline phosphatase {ECO:0000256|PIRNR:PIRNR031924};
DE            EC=3.1.3.1 {ECO:0000256|PIRNR:PIRNR031924};
GN   ORFNames=LK12_04155 {ECO:0000313|EMBL:KHK93465.1};
OS   Novosphingobium malaysiense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1348853 {ECO:0000313|EMBL:KHK93465.1, ECO:0000313|Proteomes:UP000031057};
RN   [1] {ECO:0000313|EMBL:KHK93465.1, ECO:0000313|Proteomes:UP000031057}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUSC 273 {ECO:0000313|EMBL:KHK93465.1,
RC   ECO:0000313|Proteomes:UP000031057};
RA   Lee L.-H.;
RT   "Genome sequence of Novosphingobium malaysiense MUSC 273(T).";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Alkaline phosphatase with broad substrate specificity.
CC       {ECO:0000256|PIRNR:PIRNR031924}.
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         Evidence={ECO:0000256|PIRNR:PIRNR031924};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRNR:PIRNR031924};
CC       Note=Binds 2 Zn(2+) ions. {ECO:0000256|PIRNR:PIRNR031924};
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:KHK93465.1}.
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DR   EMBL; JTDI01000001; KHK93465.1; -; Genomic_DNA.
DR   RefSeq; WP_039279633.1; NZ_JTDI01000001.1.
DR   AlphaFoldDB; A0A0B1ZQP0; -.
DR   STRING; 1348853.LK12_04155; -.
DR   OrthoDB; 9766127at2; -.
DR   Proteomes; UP000031057; 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; cd16016; AP-SPAP; 1.
DR   Gene3D; 3.30.1360.150; -; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR026263; Alkaline_phosphatase_prok.
DR   InterPro; IPR002591; Phosphodiest/P_Trfase.
DR   PANTHER; PTHR10151:SF120; BIS(5'-ADENOSYL)-TRIPHOSPHATASE; 1.
DR   PANTHER; PTHR10151; ECTONUCLEOTIDE PYROPHOSPHATASE/PHOSPHODIESTERASE; 1.
DR   Pfam; PF01663; Phosphodiest; 1.
DR   PIRSF; PIRSF031924; Pi-irrepressible_AP; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR031924};
KW   Phosphoprotein {ECO:0000256|PIRSR:PIRSR031924-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031057};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRNR:PIRNR031924}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..562
FT                   /note="Alkaline phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002066028"
FT   ACT_SITE        93
FT                   /note="Phosphothreonine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031924-50"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031924-51"
FT   BINDING         175..177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031924-51"
SQ   SEQUENCE   562 AA;  59399 MW;  ABBDE5397E46ED81 CRC64;
     MRLSFSSLAL ATALLVSTPA FADNGAAPAA DTAAPAEAAA PAEAPQLILA ISVDQFSADL
     FAQYREHFSK GFARLLDGAV FPSGYQSHAA TETCPGHSTL LTGVHPARTG IIANDWYVPG
     ISRPDKEVYC VEDESNPKST SDEPVVSPKH LKAPTLGDLM KKANPAIINA AVSAKDRAAV
     MMSGHDTDAV YWFDDKGFTT FEDRKITPAV EAENAALSKL VDAGAGPLPV PGYCSAADRP
     VKVGDFTVGT YRFPQTAGDY KAYAKGPRLD AATGDLAIRM VDELGMGKDA VPDVLSVSFS
     QTDRVGHAFG HEGVEMCIQL AQLDATLGTL FDALDARGID YAVVLTADHG GFDAPDRLDQ
     QGYPAAKYIS PTLTGDALAA AVSKETGIVA PQGKLLYGGG SSGDIYLGAG LTDDQRKTVT
     DALVAMLKAN PEVDAVYTAD ELKSVPLPHG HPQDWTMIQR VRASFDPERS GDVLMMTKRG
     VVGIAHPGPG YVATHGSPWD YDRRVPIVFW RKGMTHEEQP APVETVDIAP TLASLVGLKE
     PAGTWDGRCL DIDGSEADTC AR
//