ID K9ZNF2_ANACC Unreviewed; 764 AA.
AC K9ZNF2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:AFZ60319.1};
GN OrderedLocusNames=Anacy_4979 {ECO:0000313|EMBL:AFZ60319.1};
OS Anabaena cylindrica (strain ATCC 27899 / PCC 7122).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Anabaena.
OX NCBI_TaxID=272123 {ECO:0000313|EMBL:AFZ60319.1, ECO:0000313|Proteomes:UP000010474};
RN [1] {ECO:0000313|Proteomes:UP000010474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27899 / PCC 7122 {ECO:0000313|Proteomes:UP000010474};
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};
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DR EMBL; CP003659; AFZ60319.1; -; Genomic_DNA.
DR RefSeq; WP_015216935.1; NZ_AP018166.1.
DR AlphaFoldDB; K9ZNF2; -.
DR STRING; 272123.Anacy_4979; -.
DR KEGG; acy:Anacy_4979; -.
DR PATRIC; fig|272123.3.peg.5402; -.
DR eggNOG; COG1785; Bacteria.
DR eggNOG; COG2931; Bacteria.
DR HOGENOM; CLU_018809_0_0_3; -.
DR OrthoDB; 9794455at2; -.
DR Proteomes; UP000010474; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR Gene3D; 2.160.20.160; -; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 2.
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; 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:UP000010474};
KW Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT ACT_SITE 155
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 206
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 208
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 407
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 412
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 457
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 458
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 764 AA; 81084 MW; C78B0D03EA53474E CRC64;
MAKNTIIMIG DGMGWEMARA AAIAKEIEAG ATGTTLADFY TEGKGTGLSF QNLSGYGLVT
TYGTTIAGNN GTFNVSNTAR NDANQTINTP TGTAPVREGF EFDPTFNPGT TPNGGAKVSE
GAVGNLVGYD PVQGGINPWT PGNNPEYIKY SYPDSANTAT TLYTGVKSYN GAIGVDIFEN
PVESILTQAT QQGKSTGLVS SVPIDHATPG AAAANVNNRN KFDEFGVIDT ILQQELGIYK
PTVLLGGGHP LSNVNNPLPA EVEPPSDHLY ISEETYAELK NNPTDNIYGY TFLERGPDAA
EVLAETASQL DPEKGDRLLG VYGARGQDGN LPVSSANGDY STTGLGMFTV FASQGQNPDT
VRPLLPGETD ESFIAREINE NPTLDDLTKA ALTVLEKDKD GFWLMVEAGD VDWSAHDDNI
DNMIGTMLDF DKSVQSVMNW IEANGGWEEN LLVVTADHDH YLTLNQDFPE LLRNQGGEAL
TDIDTVEGSG HYWGSSETTK YGWGTHTNRP VPVYYQGAGS EVLDGLVSQG YEAYGYDIPG
IDGLGDQTHI YQTMFAAVTE EAEKELVFGT SDSDTLIATV DIDGVQDTIF TGAGNDEIDF
AFNSDARRNR VNSGSGDDLI YVSRRDRAFG TEGNDEFDAT DSQGENRMSG GAGSDIFYLG
ADDRALGGDG DDKFYVQDGG NNLLSGGDGA DQFWILTGDL PGTANTVLDF ETGTDVLGIG
GQGAGFDFTD LTLSGNNIAV GNTIIAILIG INTTSLTAAD FAFV
//
