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Database: UniProt/TrEMBL
Entry: K9PHL8_9CYAN
LinkDB: K9PHL8_9CYAN
Original site: K9PHL8_9CYAN 
ID   K9PHL8_9CYAN            Unreviewed;       807 AA.
AC   K9PHL8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:AFY32022.1};
DE   Flags: Precursor;
GN   ORFNames=Cal7507_1562 {ECO:0000313|EMBL:AFY32022.1};
OS   Calothrix sp. PCC 7507.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC   Calothrix.
OX   NCBI_TaxID=99598 {ECO:0000313|EMBL:AFY32022.1, ECO:0000313|Proteomes:UP000010390};
RN   [1] {ECO:0000313|EMBL:AFY32022.1, ECO:0000313|Proteomes:UP000010390}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7507 {ECO:0000313|EMBL:AFY32022.1,
RC   ECO:0000313|Proteomes:UP000010390};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Teshima H., Chen A.,
RA   Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L., Pitluck S.,
RA   Woyke T., Kerfeld C.;
RT   "Finished genome of Calothrix sp. PCC 7507.";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
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};
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DR   EMBL; CP003943; AFY32022.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9PHL8; -.
DR   STRING; 99598.Cal7507_1562; -.
DR   KEGG; calo:Cal7507_1562; -.
DR   PATRIC; fig|99598.3.peg.1746; -.
DR   eggNOG; COG1785; Bacteria.
DR   eggNOG; COG2931; Bacteria.
DR   HOGENOM; CLU_018809_0_0_3; -.
DR   Proteomes; UP000010390; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR   CDD; cd16012; ALP; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 2.
DR   Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 1.
DR   InterPro; IPR001952; Alkaline_phosphatase.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
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; 1.
DR   PRINTS; PR00313; CABNDNGRPT.
DR   SMART; SM00098; alkPPc; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR   SUPFAM; SSF51120; beta-Roll; 1.
PE   4: Predicted;
KW   Magnesium {ECO:0000256|PIRSR:PIRSR601952-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601952-2};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010390};
KW   Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT   ACT_SITE        187
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         238
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         240
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         442
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         447
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         451
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         492
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         493
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   807 AA;  85780 MW;  AF3A06A50AB25B89 CRC64;
     MILYLKIISF VLAVVIFFHP LAFKISQQLN IGRLPFMAKN VIIMIGDGMG WEMARTAAIY
     KQIQDGKTGA TLNDFYTKGE GTGLNFQTLT GYGLVTTYGT TIADSNGVFS TGNSALDGTD
     PDTGESPVRA GFQFNPAFNP GTTASGGAKV SDGAVGNLVG YDPIKGGINP WTPGTDREYI
     KNSYPDSANT ATTLYTGVKS YNNAIGVDIF EDPLESILAT ATGIGKSTGL VSSVPIDHAT
     PGAAAANVNR RNKYDADFPS LDNILQQELR VYQPTVILGG GHPLSTPGDP LPVGVEPNTS
     NEFIGKDTYK ELSTKPTTNR YDYTFLERGQ DAAQKLADTA ATLDPEKGDR LLGLYGARGQ
     NGNLPVSSAN GDYSTTGLDM FSVFANQGDN AKVDTKRPLK PGETDAQFIA TERNQNPTLN
     DLTKAALNVL GKDPDGFWLM IEGGDIDWSA HDDNIDNLIG TTLDFDKSVG SVIDWINKNG
     GWEENLLIVT ADHDHYLTLN PEFPTLLQTK GAQALTDLDK SSEVGHYWGS DPNVKYGWGS
     HSNRPVPVYY QGAGSEVLDS LVGKGYEAYG YQIPGIQGLN DQTHIYQTML ASITEADQGK
     LVSGTVAGET LIAGVDLGGV HDTVFTGAGN DEVDLSFYNN ARQNRINTGS GDDIIYVSRK
     DRAFGGSGDD IFDATDAQGG NRLSGGDGDD IFYLGKDDRA SGGNGNDKFY VQSGGGNLIV
     GDAGADQFWI VSTELPATAN TIVDFQIGID VIGFLGSKSL GISASTLKLN QVGDNTDIAF
     NGKTLAVLND IQASSLNLNS SSQFVFA
//
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