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
//