ID J0WZ23_AURST Unreviewed; 678 AA.
AC J0WZ23;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=alkaline phosphatase {ECO:0000256|ARBA:ARBA00012647};
DE EC=3.1.3.1 {ECO:0000256|ARBA:ARBA00012647};
GN ORFNames=AURDEDRAFT_184995 {ECO:0000313|EMBL:EJD44547.1};
OS Auricularia subglabra (strain TFB-10046 / SS5) (White-rot fungus)
OS (Auricularia delicata (strain TFB10046)).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Auriculariaceae; Auricularia.
OX NCBI_TaxID=717982 {ECO:0000313|EMBL:EJD44547.1, ECO:0000313|Proteomes:UP000006514};
RN [1] {ECO:0000313|Proteomes:UP000006514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFB10046 {ECO:0000313|Proteomes:UP000006514};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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; JH687770; EJD44547.1; -; Genomic_DNA.
DR RefSeq; XP_007347296.1; XM_007347234.1.
DR AlphaFoldDB; J0WZ23; -.
DR KEGG; adl:AURDEDRAFT_184995; -.
DR eggNOG; KOG4126; Eukaryota.
DR InParanoid; J0WZ23; -.
DR OMA; YSGHKST; -.
DR OrthoDB; 35876at2759; -.
DR Proteomes; UP000006514; 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; 3.40.720.10; Alkaline Phosphatase, subunit A; 2.
DR InterPro; IPR001952; Alkaline_phosphatase.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1.
DR PANTHER; PTHR11596:SF72; 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 Reference proteome {ECO:0000313|Proteomes:UP000006514};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..678
FT /note="alkaline phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003741144"
FT ACT_SITE 228
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 287
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 289
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 445
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 456
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 497
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 498
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 629
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 678 AA; 73465 MW; 02274A26BEFBF4C7 CRC64;
MLSFGVKLLA LAALGGNAAY AQTFQRLGTC PTLGCVFPPD QADFMPGQVF DVRVEIHAPL
NGSEAFNNGA PDEKFSLTIQ RVGDRAGPKL ARDFWKCPEP GLEKWTFNYF EDLFAQDAKT
PTVVNVASKA YRQVALYTPG EYIATVHYYN TQKTVAHWTV RKPTTPRRKA KNVLFFIGDG
MTISMQTAAR LIAHKSVNGK YQSLLQLDQM DNLGHQMTHS IDSFITDSAN SATALNTGHK
SSVNALNVYA DSSPDPQDDP KVETLAEMFR RVKNGLIGIV TTAFVADATP AAIVAHTRDR
DQAGPIIDTF LRGEQNYSWP GVRGVDVLFG GGAENFLPGA ASFEGKDYYA EFAKAGYSVV
HDNAGLQKID KRKKALGIFS VSNMAKWVDR KVKTQNLKGQ QNSPTGDKTD ALDQPGLKEM
TLKAIDILHA RSKADKNQGW YLMSEAASIG EYKMMHVLDY HRALGELLEL DDAVRASIAH
LKKLGIYDDT LIVVTADHGH GFDVFGGVDT QYLHTAASDR QKRGAVGNYI NSGLSGYTVA
PGTAPTNNTV VIGAQGANFP VQWDPRYSLA AGVVAFPDHR ENYTTAPNGP RLPAVKGQNG
EGYVPNPADA QDGFGLTGTL PTNAAQGVHS LTDVAVYANG PGSEAFRGVY NNVDIFFKMA
DALGLATYKN TTSSGHWH
//
