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Database: UniProt/TrEMBL
Entry: C5MB94_CANTT
LinkDB: C5MB94_CANTT
Original site: C5MB94_CANTT 
ID   C5MB94_CANTT            Unreviewed;       503 AA.
AC   C5MB94;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 62.
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=CTRG_03336 {ECO:0000313|EMBL:EER32911.1};
OS   Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294747 {ECO:0000313|EMBL:EER32911.1, ECO:0000313|Proteomes:UP000002037};
RN   [1] {ECO:0000313|EMBL:EER32911.1, ECO:0000313|Proteomes:UP000002037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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}.
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DR   EMBL; GG692398; EER32911.1; -; Genomic_DNA.
DR   RefSeq; XP_002549039.1; XM_002548993.1.
DR   AlphaFoldDB; C5MB94; -.
DR   STRING; 294747.C5MB94; -.
DR   EnsemblFungi; CTRG_03336-t43_1; CTRG_03336-t43_1-p1; CTRG_03336.
DR   GeneID; 8300292; -.
DR   KEGG; ctp:CTRG_03336; -.
DR   VEuPathDB; FungiDB:CTRG_03336; -.
DR   eggNOG; KOG4126; Eukaryota.
DR   HOGENOM; CLU_008539_6_0_1; -.
DR   OrthoDB; 35876at2759; -.
DR   Proteomes; UP000002037; 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   GO; GO:0019637; P:organophosphate metabolic process; IEA:UniProt.
DR   GO; GO:0006796; P:phosphate-containing compound metabolic process; IEA:UniProt.
DR   CDD; cd16012; ALP; 1.
DR   Gene3D; 1.10.1200.140; Alkaline phosphatase, crown domain; 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   InterPro; IPR042085; Ap_crown.
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:0000256|RuleBase:RU003947};
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:UP000002037};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601952-2}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..503
FT                   /note="Alkaline phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002955541"
FT   ACT_SITE        95
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         47
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         47
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         146
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         148
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         288
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         293
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         297
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         336
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         337
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   503 AA;  55223 MW;  EFA80B66B67D7DC3 CRC64;
     MAFIFPRLIN ISTLALAVYL YLFTNVEAIP VDNSQPKKKN IIFLVGDGFG PSGVNLARNY
     RQVEQGLSRR DLLNLDGHLI GTQRHSSNSS YITDSAAAGT ALATGKKTVN GYISVDPEQN
     PVGAIGEALK LQGYAVGLVV TTSVGDATPS VWAAHARTRR DQDLIVEQLV GEIHPLGHIP
     DLILGGGRDW FIGVNDGGKR PDNRSLIEEV QNNGTWTYVG DREGFDSYDE GRNATLPFLG
     LFAEDNFPYR IDRDDAEYPS LVEQTQFALN ALSNYTKDSD QGFFLMVESS RIDHAGHENC
     VQSHALEALE YDEVFGLVKN FTRETDVDTV VIATADHETG GLVLNLQGPR DFDPVFNATH
     SGEYLANEIA NYEGDDLLGF IRTTVIEEGL GLTNYTEEEV QRLADYVDNS SEGILYTTAL
     GVAIANLTSS RARVHWGSLQ HTSVDVDLYG FSNADYLTQK LLNVRTGLAG VHENTDFSVF
     IKSITDIDLD EVTELIADVP TRY
//
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