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Database: UniProt
Entry: A0A1U7MG46_9FIRM
LinkDB: A0A1U7MG46_9FIRM
Original site: A0A1U7MG46_9FIRM 
ID   A0A1U7MG46_9FIRM        Unreviewed;       532 AA.
AC   A0A1U7MG46;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Alkaline phosphatase 4 {ECO:0000313|EMBL:OLS56437.1};
DE            EC=3.1.3.1 {ECO:0000313|EMBL:OLS56437.1};
GN   Name=phoA_1 {ECO:0000313|EMBL:OLS56437.1};
GN   ORFNames=SPSPH_28360 {ECO:0000313|EMBL:OLS56437.1};
OS   Sporomusa sphaeroides DSM 2875.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Sporomusa.
OX   NCBI_TaxID=1337886 {ECO:0000313|EMBL:OLS56437.1, ECO:0000313|Proteomes:UP000186950};
RN   [1] {ECO:0000313|EMBL:OLS56437.1, ECO:0000313|Proteomes:UP000186950}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2875 {ECO:0000313|EMBL:OLS56437.1,
RC   ECO:0000313|Proteomes:UP000186950};
RA   Poehlein A., Daniel R.;
RT   "Genome sequence of Sporomusa sphaeroides DSM 2875.";
RL   Submitted (FEB-2016) 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|ARBA:ARBA00005984, 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:OLS56437.1}.
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DR   EMBL; LSLJ01000002; OLS56437.1; -; Genomic_DNA.
DR   RefSeq; WP_075756449.1; NZ_LSLJ01000002.1.
DR   AlphaFoldDB; A0A1U7MG46; -.
DR   STRING; 1337886.SPSPH_28360; -.
DR   Proteomes; UP000186950; Unassembled WGS sequence.
DR   GO; GO:0004035; F:alkaline phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd16012; ALP; 1.
DR   Gene3D; 1.10.60.40; -; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR001952; Alkaline_phosphatase.
DR   InterPro; IPR018299; Alkaline_phosphatase_AS.
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.
DR   PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:OLS56437.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, 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:UP000186950};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601952-2}.
FT   ACT_SITE        129
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         67
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         181
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
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         308
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         313
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         317
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         356
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         357
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         495
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   532 AA;  58521 MW;  8072C3AC0586A6F0 CRC64;
     MFKKKRLPLQ LVAICLVFFF CITFITGYSP ITAQADKRTA QEISSIAKTN VDQTGVKPKY
     IFLFIGDGMS FPQATALGHY NGTVDHNFVG TLNKPTRENI PKAEMPSFVN FPAVGAATTY
     DASKFITDSA SAATAIACSV KTLDGALGVD PYNKRVISIA EQLKAQAGYK IGIVTNVSLD
     HATPAGFYAH LPNRNSFYEI GLDLIASNFD FFGGGGFKQP TGKDKNQTHL FELAKQAGYN
     VANTYEDIKA LNSRSGKTIA INPVLDNPGD VAIHYNIDRD AGDLALADYV QKAIDVLGEK
     NSFFIMAEGG KIDWSSHAND AYTTIQEVKD LENAVNVAVA FAKKHPKETL IIVTGDHETG
     GFTLGYNGTQ YDTYLHLLQN QKLSFKRFAD EYVQQYRDNK VPFETAMADV KQLFGLMLPN
     DPAVAGMKDQ PLVLTAKEVA QLREAYAVSM IPYKQRQRDK EYQTTYSMYD QEPFQIVITR
     ILNSRSGLGW TSTAHTGLPV AVYALGTGQD VFNGFYDNTD ISKKIKTLVG LH
//
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