ID B8N747_ASPFN Unreviewed; 652 AA.
AC B8N747;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=alkaline phosphatase {ECO:0000256|ARBA:ARBA00012647};
DE EC=3.1.3.1 {ECO:0000256|ARBA:ARBA00012647};
GN ORFNames=AFLA_019800 {ECO:0000313|EMBL:EED54728.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED54728.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED54728.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963474; EED54728.1; -; Genomic_DNA.
DR RefSeq; XP_002376000.1; XM_002375959.1.
DR AlphaFoldDB; B8N747; -.
DR STRING; 332952.B8N747; -.
DR EnsemblFungi; EED54728; EED54728; AFLA_019800.
DR VEuPathDB; FungiDB:AFLA_002443; -.
DR eggNOG; KOG4126; Eukaryota.
DR HOGENOM; CLU_008539_3_0_1; -.
DR OMA; YSGHKST; -.
DR Proteomes; UP000001875; 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; 1.
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 Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..652
FT /note="alkaline phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002875864"
FT ACT_SITE 221
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 281
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 283
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 434
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 439
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 443
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 484
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 485
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 610
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 652 AA; 72623 MW; 39EE2436F36225F5 CRC64;
MRFLSIAGAA LFASSAVAQT YQRLGGCPTL GCVFPPDQAD FLPGQYFDIR IEVHSPVNGS
EARQGQPDPD FKFTIAKKGE EGVAAAEYFE IDEPQLERWN FTWYEDLFAK DAQKPSLVNV
TAKAYRRVAL HEPGEYEATL TYYGQEKTVA NWLVRDLPEK RRAKNVVLFI GDGMTTNMIT
AARLIAHRSI NGKYLTKLQL DKFPVLGHQM THSMDSFITD SANSATALYT GHKTTVNALN
VYVDSSKDPF DDPKFETISE IFRRRYPDAG IGIVSTAFLA DATPAALAAH TRDRGEYDHV
ISAYYEGLTK YEWTDWDGPD VLLGAGAENF ITSEDAPRDY YKLFSEKEYS ISWNKTALQA
APNDTKALGV FSTSNLATWL DRNVYQENLR NQSNYPDGSK RDAEDLPGLK EMTLKAIDVL
NARHEDDGWF LMSEAASIDK QMHTLDYDRS LGELLELDDT VRATIEKLKA LGQLEDTLII
VTADHGHGFD VTGSVDTEYL NAQEDGRDKR RAIGTYQNSG LSQYTVRGPN ALRYSEGVHF
PARWDPRYTL HAGVVAFPDH QENYEVHKEG PRKPAVKRSG SDGYFANYKD AVTGFLINGT
LPVDADQGVH SLTDVPVFAQ GPCQELFGGV YSSVDIFFNM AECLGLADHG KN
//
