ID H0EFS7_GLAL7 Unreviewed; 538 AA.
AC H0EFS7;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Alkaline phosphatase {ECO:0000256|ARBA:ARBA00012647, ECO:0000256|RuleBase:RU003947};
DE EC=3.1.3.1 {ECO:0000256|ARBA:ARBA00012647, ECO:0000256|RuleBase:RU003947};
GN ORFNames=M7I_1334 {ECO:0000313|EMBL:EHL02541.1};
OS Glarea lozoyensis (strain ATCC 74030 / MF5533).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1104152 {ECO:0000313|EMBL:EHL02541.1, ECO:0000313|Proteomes:UP000005446};
RN [1] {ECO:0000313|EMBL:EHL02541.1, ECO:0000313|Proteomes:UP000005446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 74030 / MF5533 {ECO:0000313|Proteomes:UP000005446};
RX PubMed=22302591; DOI=10.1128/EC.05302-11;
RA Youssar L., Gruening B.A., Erxleben A., Guenther S., Huettel W.;
RT "Genome sequence of the fungus Glarea lozoyensis: the first genome sequence
RT of a species from the Helotiaceae family.";
RL Eukaryot. Cell 11:250-250(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1;
CC Evidence={ECO:0000256|RuleBase:RU003947};
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:EHL02541.1}.
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DR EMBL; AGUE01000021; EHL02541.1; -; Genomic_DNA.
DR AlphaFoldDB; H0EFS7; -.
DR HOGENOM; CLU_008539_6_0_1; -.
DR InParanoid; H0EFS7; -.
DR Proteomes; UP000005446; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 3.40.720.10; Alkaline Phosphatase, subunit A; 2.
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; 2.
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:0000256|RuleBase:RU003947};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR601952-2};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601952-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005446};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601952-2}.
FT TRANSMEM 51..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 145
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 198
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 311
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 462
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 538 AA; 58588 MW; 7281A87DE96C5845 CRC64;
MSPNPPLFAS DRRSSSSHSE ERAAAEDTAL LGNQRKDNSS PQQKSRFWRE IGLFAWALIA
TAAVIVLAVY SQHQGSSGDG KKTSPKGKKN LIFMVSDGMG PASLSMTRSF RQFQSGLPID
DVLVLDQHFI GSSRTRSSNS LVTDSAAGAT AFSCGMKSYN GAISKLPDHS SCGTVLEAAK
RAGYMTGLVV TTSITDATPA CFASHVDTRA EEDLIAQQEV GEHPLGRMVD LIFGGGRCHF
LPNTTSESCR GDGRDITKLA REKYGWNYID NRKDFDGIRS GSAVKLPLLG LFARYNFPYE
DSDKGFFLMI EGSRIDHAGH GNDPAAQVNE VLAYDKAFAS VLEFLDRSKT ESVLVSTSDH
ETGGLSIARQ LDPTYPEYLW YPEVLNNVSS TAEHSARRLA SYVAAGSKNV ESFIRKELVK
KGLGIKDATD AEIKTIIAAP NSYSFASMIS RRAQIGWSTH GHSAVDVNIY GTAGSERLNG
NHENTEVGKF LRDYLDLNVD AITKELNEKE KAKSASTEET IRPLVEMHSM PDGIDDEL
//
