PHOA_ASPFU
ID PHOA_ASPFU Reviewed; 447 AA.
AC Q8X176; Q4WK63;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Acid phosphatase;
DE EC=3.1.3.2;
DE Flags: Precursor;
GN Name=phoA; ORFNames=AFUA_1G03570;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 260-274, INDUCTION,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12213928; DOI=10.1099/00221287-148-9-2819;
RA Bernard M., Mouyna I., Dubreucq G., Debeaupuis J.-P., Fontaine T.,
RA Vorgias C., Fuglsang C., Latge J.-P.;
RT "Characterization of a cell-wall acid phosphatase (PhoAp) in Aspergillus
RT fumigatus.";
RL Microbiology 148:2819-2829(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [3]
RP PROTEIN SEQUENCE OF 41-53; 164-176; 317-330 AND 347-350, AND GPI-ANCHOR.
RX PubMed=11545413;
RX DOI=10.1002/1522-2683(200108)22:13<2812::aid-elps2812>3.0.co;2-q;
RA Bruneau J.-M., Magnin T., Tagat E., Legrand R., Bernard M., Diaquin M.,
RA Fudali C., Latge J.-P.;
RT "Proteome analysis of Aspergillus fumigatus identifies
RT glycosylphosphatidylinositol-anchored proteins associated to the cell wall
RT biosynthesis.";
RL Electrophoresis 22:2812-2823(2001).
RN [4]
RP PROTEIN SEQUENCE OF 317-323, AND STRUCTURE OF GPI-ANCHOR.
RX PubMed=12626404; DOI=10.1093/glycob/cwg004;
RA Fontaine T., Magnin T., Melhert A., Lamont D., Latge J.-P.,
RA Ferguson M.A.J.;
RT "Structures of the glycosylphosphatidylinositol membrane anchors from
RT Aspergillus fumigatus membrane proteins.";
RL Glycobiology 13:169-177(2003).
CC -!- FUNCTION: Has both phosphomonoesterase and phosphodiesterase activity.
CC Cleaves a broad range of phosphate esters.
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=3.1.3.2;
CC -!- ACTIVITY REGULATION: Inhibited by NaF, molybdate and vanadate.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.45 mM for p-nitrophenyl phosphate {ECO:0000269|PubMed:12213928};
CC KM=2.3 mM for bis-(p-nitrophenyl) phosphate
CC {ECO:0000269|PubMed:12213928};
CC pH dependence:
CC Optimum pH is 4-6. Active from pH 3 to 7.
CC {ECO:0000269|PubMed:12213928};
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- INDUCTION: Repressed by phosphate. {ECO:0000269|PubMed:12213928}.
CC -!- PTM: The GPI-like anchor contains a phosphoceramide lipid group. The
CC anchor position has not been determined.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL88069.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF462065; AAL66381.1; -; Genomic_DNA.
DR EMBL; AAHF01000007; EAL88069.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_750107.1; XM_745014.1.
DR AlphaFoldDB; Q8X176; -.
DR STRING; 746128.CADAFUBP00000391; -.
DR GeneID; 3507810; -.
DR KEGG; afm:AFUA_1G03570; -.
DR eggNOG; ENOG502QSRP; Eukaryota.
DR HOGENOM; CLU_027977_2_0_1; -.
DR InParanoid; Q8X176; -.
DR OrthoDB; 890712at2759; -.
DR BRENDA; 3.1.3.2; 508.
DR Proteomes; UP000002530; Chromosome 1.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009395; P:phospholipid catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR007312; Phosphoesterase.
DR PANTHER; PTHR31956; PTHR31956; 1.
DR Pfam; PF04185; Phosphoesterase; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall biogenesis/degradation; Direct protein sequencing;
KW Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..419
FT /note="Acid phosphatase"
FT /id="PRO_0000245560"
FT PROPEP 420..447
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000245561"
FT ACT_SITE 215
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT LIPID 419
FT /note="GPI-like-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 329
FT /note="L -> C (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 447 AA; 48988 MW; 4B2FB1F0ECEF0D72 CRC64;
MKPSVATLLA TVSLVYAQTA TEKEPSLSAI ESAAASIQPY SPVSNVEGVA FNRFFQVWLE
NIDYEDAAAD ENMKWLASQG ILLTNFYAVT HPSEPNYCAA VGGDTFGMDN DNFNQIPANV
STVADLLDTK NIAWGEYQEH LPYPGFQGFN YSNQETYVND YVRKHNPLVL YDSVTKNSTR
LRQIKNFTSF EDDLANKKLP QWAFITPNMT NDAHDTNITF GAKWERSWIA PLLNNSYFMN
DTLILLTFDE DGTYSKSNKI FSVLLGGAIP DELKGTQDDT FYTHYSVIAS VSANWGLPSL
GRWDCGANIL EIVANKTGYV NYDVDTTNLR LNETYPGPMS AGEYSKYSPV WPNALTRGDC
SAGHGILDIV KETYANTEPT YNYSSPFPYD TASNYNTKVT ATKKNVTGTH RSSSSSSPSA
SSNAAVSAVA PAAGVSGLLL GLALNLL
