ID K9QW07_NOSS7 Unreviewed; 1126 AA.
AC K9QW07;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:AFY48977.1};
GN OrderedLocusNames=Nos7524_3175 {ECO:0000313|EMBL:AFY48977.1};
OS Nostoc sp. (strain ATCC 29411 / PCC 7524).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=28072 {ECO:0000313|EMBL:AFY48977.1, ECO:0000313|Proteomes:UP000010378};
RN [1] {ECO:0000313|Proteomes:UP000010378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29411 / PCC 7524 {ECO:0000313|Proteomes:UP000010378};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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}.
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DR EMBL; CP003552; AFY48977.1; -; Genomic_DNA.
DR RefSeq; WP_015139412.1; NC_019684.1.
DR AlphaFoldDB; K9QW07; -.
DR STRING; 28072.Nos7524_3175; -.
DR KEGG; nop:Nos7524_3175; -.
DR PATRIC; fig|28072.8.peg.3466; -.
DR eggNOG; COG1785; Bacteria.
DR eggNOG; COG2931; Bacteria.
DR HOGENOM; CLU_289813_0_0_3; -.
DR OrthoDB; 570067at2; -.
DR Proteomes; UP000010378; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
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; 2.
DR PRINTS; PR00113; ALKPHPHTASE.
DR PRINTS; PR00313; CABNDNGRPT.
DR SMART; SM00098; alkPPc; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 2.
DR SUPFAM; SSF51120; beta-Roll; 1.
PE 3: Inferred from homology;
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:UP000010378};
KW Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT ACT_SITE 511
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 467
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 736
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 741
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 784
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 1126 AA; 118536 MW; FF5EB9A842323D04 CRC64;
MTNGNHVIFI HPDGTSPSHY ALARFVDEGP DGRLNWDQLS NAGVYLGHME DQLGGTSNGG
AVTHATGAKV YAESFGYELN NLPITSLSGS NKTIVEEARD AGKVTALVQS GAIFEPGTAA
FVAKTQEIVN SNGSRTVPRA QAAEIARQVI ESGVDFILSG GELNLLPVGT DGFHGTAAQY
DAISTNPLQR PTVNLIQLAI NRGYTVVYTE QQLRNLLDTT ITPVTPTKVL GVFAPVHTFN
DRPEEVLAQN GLPLYRETAP TIAEMLEITQ QLMEKHPNFS KGSITIVEEE GSDNFGNNNN
AAGTLEGVRR ADAAIGVAMD FIEKYPNTLL VTAADSDAGG LQVVDPRTAG QNVGNINNNP
ATSSRNVPLD GTTGANTLPF VSAPDANGDV FNFAVGWAGT PDFSGSIVAK AHGLNADKLP
ATVDNTGIYE LMYETLFNTE LAPRNPAPTP APQATRQTGN VIFIHPDGTS PSHFMALRNV
DKGPDGRLNW DKMTNAGVYL GHMENQLTGT SNAGAVTHAN GVKVFNESFG LNEDNSRITP
ASGKTGYTIL EEAIAAGKAT ALIQSGQMAE PGTAAFAAET TNRDGNNLRA RDKYAEIIEQ
VIRSGTDVIM GGGELYMLPI GTTGFHVTAE IDASETNPAF RPNINLIELA ESLGYTVVYT
EEQMNQVVNS NNPPTKLLGV FAAEDTFDDR REEQLGLNTD NPLPLYVATA PTVAEMLEAS
LKIVSTDPDG FFVVIEEEGT DNFANNNNAV GTIEAVRRAD AAIGVAMDYV NNQDPNTLVI
TAADSDAGGL QVFQFAPYVR PSGNFDTSNP NLANNQPEVP FINVNPTTTN NNRAFLDGVN
GSTASAERPW VPFASPNSID GPMGNFGVAW VGTPDFPGSI VSKAYGMNAD KLPSTVDNTG
IYDLMYQTLF GVTPEVAAAQ QQTELVAGTA GADTLIAAVD APFDGINDTV FTGAGNDEVD
AQTVSLPIAG RNRVNLGSGN DTIFVNRNDR VFGSAGNDEF DATDGKGGNR MSGGAGDDIF
RLGSGDRALG GDGNDEFYVQ SGGANLLSGG AGADQFWIAN VELPTSANTI LDFEKGVDVI
GVLGISRNTL TLNVINGNTE IGLGGQTVAI VNGVTGLDAN TNFVFV
//
