ID   A0A0E9MUW7_9SPHN        Unreviewed;       546 AA.
AC   A0A0E9MUW7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-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=SCH01S_52_00930 {ECO:0000313|EMBL:GAO40910.1};
OS   Sphingomonas changbaiensis NBRC 104936.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1219043 {ECO:0000313|EMBL:GAO40910.1, ECO:0000313|Proteomes:UP000033202};
RN   [1] {ECO:0000313|EMBL:GAO40910.1, ECO:0000313|Proteomes:UP000033202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 104936 {ECO:0000313|EMBL:GAO40910.1,
RC   ECO:0000313|Proteomes:UP000033202};
RA   Katano-Makiyama Y., Hosoyama A., Hashimoto M., Noguchi M., Tsuchikane K.,
RA   Ohji S., Yamazoe A., Ichikawa N., Kimura A., Fujita N.;
RT   "Whole genome shotgun sequence of Sphingomonas changbaiensis NBRC 104936.";
RL   Submitted (APR-2015) 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:GAO40910.1}.
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DR   EMBL; BBWU01000052; GAO40910.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0E9MUW7; -.
DR   STRING; 1219043.SCH01S_52_00930; -.
DR   Proteomes; UP000033202; 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; 2.
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:UP000033202};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRNR:PIRNR031924}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..546
FT                   /note="Alkaline phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002429753"
FT   ACT_SITE        73
FT                   /note="Phosphothreonine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031924-50"
FT   BINDING         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031924-51"
FT   BINDING         155..157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031924-51"
SQ   SEQUENCE   546 AA;  58489 MW;  DCD614179A3A31C1 CRC64;
     MRLRSIVTAV AVLLATAAQA QPPKPKLIVA ISIDQFSADL FSEYRQHFTG GLKRLSEGVV
     FPSGYQSHAA TETCPGHSTI LTGSRPYRTG IIANDWLDQS VARADKTVYC AEDETVPGSS
     SKDYTVSARH LLVPTLGERM KNADPATRVV SVAGKDRAAV MMGGHKVDQL WFWNGKDYVT
     TAGQPAPDAA IAPFRSALAA RLAQPQPALP VPDVCTSRDR AIPIGGGKTV GTWHFGRAAG
     DTTKFRASPE IDDANLTLAS ALIESMGLGR GPQTDIISIG ESATDYVGHT YGTEGVEMCI
     QLLALDKRLG AFFDQLDKSG VDYVVVLTAD HGGHDLPERN RIHAAPDAQR VDSRLDLKAI
     GAQIGRELKL TGPVLIPAGG DVYLDRAVPA KARAKAVARA AQLIKQSPLV EDVFVGADIA
     KMPQPTSPPE TWSFAERARA SYRPGRSGDL IVALKERVTP IPDPTKGYVA THGSFWDYDR
     RVPILFWWKG VQNFEQPLGV ETVDILPTLA SLIGLPVPPA EIDGRCLDLD ASAGDNCPVA
     APGTRR
//