ID A0A0N7Z5W5_9CYAN Unreviewed; 785 AA.
AC A0A0N7Z5W5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:GAQ00042.1};
DE EC=3.1.3.1 {ECO:0000313|EMBL:GAQ00042.1};
GN ORFNames=NIES2104_66070 {ECO:0000313|EMBL:GAQ00042.1};
OS Leptolyngbya sp. NIES-2104.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=1552121 {ECO:0000313|EMBL:GAQ00042.1, ECO:0000313|Proteomes:UP000052243};
RN [1] {ECO:0000313|EMBL:GAQ00042.1, ECO:0000313|Proteomes:UP000052243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2104 {ECO:0000313|EMBL:GAQ00042.1,
RC ECO:0000313|Proteomes:UP000052243};
RX PubMed=26494835; DOI=10.1093/dnares/dsv022;
RA Shimura Y., Hirose Y., Misawa N., Osana Y., Katoh H., Yamaguchi H.,
RA Kawachi M.;
RT "Comparison of the terrestrial cyanobacterium Leptolyngbya sp. NIES-2104
RT and the freshwater Leptolyngbya boryana PCC 6306 genomes.";
RL DNA Res. 22:403-412(2015).
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}.
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:GAQ00042.1}.
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DR EMBL; BBWW01000003; GAQ00042.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N7Z5W5; -.
DR STRING; 1552121.NIES2104_66070; -.
DR InParanoid; A0A0N7Z5W5; -.
DR Proteomes; UP000052243; Unassembled WGS sequence.
DR GO; GO:0004035; F:alkaline phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd16012; ALP; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 2.
DR InterPro; IPR001952; Alkaline_phosphatase.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1.
DR PANTHER; PTHR11596:SF5; ALKALINE PHOSPHATASE; 1.
DR Pfam; PF00245; Alk_phosphatase; 2.
DR Pfam; PF00353; HemolysinCabind; 4.
DR PRINTS; PR00113; ALKPHPHTASE.
DR SMART; SM00098; alkPPc; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR SUPFAM; SSF51120; beta-Roll; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:GAQ00042.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR601952-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601952-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT ACT_SITE 164
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 215
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 417
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 422
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 426
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 467
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 468
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 785 AA; 83485 MW; C6B37C4DA957CF4C CRC64;
MIGDGMGWEM ARAASIYQQI QQGNRGNTLD DFYTSGYGSS LNFQNLENKT LATTYGTTIA
DQRGTFSTGN SALLNNNELG ATLFPSINSP TASNPLRPGF EFDPTFNPGT TATGGARINQ
GAVGNLVGYD PRRGGAVPWD AAYYGGELPV GFEREYIKYS YPDSANTATT LYTGVKSYNN
AIAVDIYEQP LETLLVTAAQ NNKSTGLVSS VPIDHATPGA AAATVNRRAK YDSEFPDIDS
ILQQELRIYQ PTVLLGGGHP LSNTRDPLPD GVEPPNTFEF ITDDTYQYLR DNPTANRYGY
TFLERGENAA GTLADTATNL DPNAGDRLLG LYGARGQNGN LPVSTANGDY SRTGLDMFSV
FTTQGLNPDT KRPLLPGETD FEFISREVNE NPTLQQLSKA ALDVLGKDED GFWLMIEGGD
IDWAAHDNNI DNLIGTVIDF DKAVGSVVEW INANGGWEEN LLIVTADHDH YFTLNPNYPS
LLQTISAKAL TDIDDPAIAG NFWGSDPKVK YGWGNHSNRP VPVYYEGAGS EALSSFIGQG
YESYGFEIAG LPGVVDQSQL YKTMLTAITG STDRPLASGT IFGEEGDDLI YADVTDDTIF
AEEGTNYIYA NRGNNTVYSG AGNDLIYASF GDDSIYAGEG NNSVFAGAGR NTVFAGAGDD
YISTGTGDDL IYAGDGANII QSSLGNDTII SGSGNSVIDS GTGDDRVFVN GGNNRFVLNA
GAGSVTIYGF TPDSVFNRGI GLSASGSNPA PGLSFSVNNG DTLVNLGDDL LATLKGVQLN
ELPIA
//
