ID A0A1Q2HS08_9BACT Unreviewed; 543 AA.
AC A0A1Q2HS08;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Alkaline phosphatase 4 {ECO:0000313|EMBL:AQQ10013.1};
DE EC=3.1.3.1 {ECO:0000313|EMBL:AQQ10013.1};
DE Flags: Precursor;
GN Name=phoA_1 {ECO:0000313|EMBL:AQQ10013.1};
GN ORFNames=L21SP3_01835 {ECO:0000313|EMBL:AQQ10013.1};
OS Sedimentisphaera cyanobacteriorum.
OC Bacteria; Planctomycetota; Phycisphaerae; Sedimentisphaerales;
OC Sedimentisphaeraceae; Sedimentisphaera.
OX NCBI_TaxID=1940790 {ECO:0000313|EMBL:AQQ10013.1, ECO:0000313|Proteomes:UP000188273};
RN [1] {ECO:0000313|Proteomes:UP000188273}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L21-RPul-D3 {ECO:0000313|Proteomes:UP000188273};
RA Spring S., Bunk B., Sproer C., Klenk H.-P.;
RT "Comparative genomics and description of representatives of a novel lineage
RT of planctomycetes thriving in anoxic sediments.";
RL Submitted (FEB-2017) 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};
CC -!- SIMILARITY: Belongs to the alkaline phosphatase family.
CC {ECO:0000256|RuleBase:RU003946}.
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DR EMBL; CP019633; AQQ10013.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2HS08; -.
DR STRING; 1940790.L21SP3_01835; -.
DR KEGG; pbu:L21SP3_01835; -.
DR OrthoDB; 9794455at2; -.
DR Proteomes; UP000188273; Chromosome.
DR GO; GO:0004035; F:alkaline phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR CDD; cd16012; ALP; 1.
DR Gene3D; 1.10.60.40; -; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR InterPro; IPR001952; Alkaline_phosphatase.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1.
DR PANTHER; PTHR11596:SF5; ALKALINE PHOSPHATASE; 1.
DR Pfam; PF00245; Alk_phosphatase; 1.
DR PRINTS; PR00113; ALKPHPHTASE.
DR SMART; SM00098; alkPPc; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:AQQ10013.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR601952-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601952-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..543
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012727092"
FT ACT_SITE 131
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 68
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 183
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 185
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 320
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 368
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 369
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 500
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 543 AA; 58716 MW; A4633DD4F06CC00F CRC64;
MNLIKKSLLL LAAASAAVFA ASTPSSTYKV QADANKDGVV NNEDLSQMAS SWLGEDEGPK
YVFFFLGDGM ASPQIHATEA YLKQKLQADD PDNDLGASSL GTAGSELLTM SQFPVMGMQR
TYADNRFITG SAASATAFSC GHKTTINTIS MDPERTIDYV TIAEAAKDKG MKVGIVSSVS
IDHATPACYY AHNGYRGNYW DIANQLSDSG FDYFGGGGMK GERTKNGSRH YAPGKPSAAP
SNCPIQHAID NGYTVCENKA ELEAAAPGEK VFAYSKDYID GSWALPYDID RDPADASIAD
YTSEGIRLLE NSNGFFLMVE GGKIDWACHA NDAVTAIEDT IAFDNAVAEA YDFYLEHPDE
TLIVVSGDHE CGGMTLGAAG TGYDTFYEVF ENQTMSCDAF VAGPLADHKS VYGQDPWDNS
VDMNQDIKDK IENAFGLDYD AVSDFDRAQL EDAYDETMGG NAVPDSSENW KLYGYYDPLR
VAVTHIMNRN AGLAWTSYSH TAVPVPVMAL GSGQWKFDGY YENTAIADKL ADIMQVSLEE
AAQ
//
