ID A0A1G0RYB5_9BACT Unreviewed; 420 AA.
AC A0A1G0RYB5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:OGU65095.1};
DE Flags: Fragment;
GN ORFNames=A2W30_10255 {ECO:0000313|EMBL:OGU65095.1};
OS Ignavibacteria bacterium RBG_16_36_9.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1798435 {ECO:0000313|EMBL:OGU65095.1, ECO:0000313|Proteomes:UP000178123};
RN [1] {ECO:0000313|EMBL:OGU65095.1, ECO:0000313|Proteomes:UP000178123}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGU65095.1}.
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DR EMBL; MHAH01000151; OGU65095.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0RYB5; -.
DR Proteomes; UP000178123; Unassembled WGS sequence.
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; 1.
DR InterPro; IPR001952; Alkaline_phosphatase.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
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.
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 Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT ACT_SITE 68
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 24
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 268
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OGU65095.1"
SQ SEQUENCE 420 AA; 45523 MW; 30E2670C4C03F7BC CRC64;
LSISSKCQEN QLTTTGNVIF FHPDGTALAG WNAIRVLYYG PDGELNWDRL SQIGLYQGHT
KNTLTSSSEG GATMHAYGMK VELLSYGMDG KKLLTSRSGS SLSIMMEAKS KGINIGIINS
GKIVEPGTGV FVASDVSRAN EDAISKKIIE SGADLIFSGG EENLLPVGVE GKFGAGKRKD
GLNVIELAKQ LGYKVIYTRE ELASISNVVK KVLGIFARSH TFNDKSEEEL IQIGLHNYKP
EAPTLAEMTD AAIKFLSGKK GNFFFVVEEE GTDNFGNCNN ANGYFEALKR ADDAIGVALK
FYSKNPNTLI ITAADSEAGG MEIYGFLEQD MMPDQPLPEK SKNGAPLDGI NGTGTKPFLT
EKDKYGNQFQ FAVAWSTTDD VFGSVIARAE GLNSQLMKGK IDNTEIYRIM YATLFGIILK
//
