Acid phosphatase precursor - Aspergillus fumigatus

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Reviewed, UniProtKB/Swiss-Prot Q8X176 (PHOA_ASPFU)

Last modified October 13, 2009. Version 35. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information

Names and origin

Protein names

Recommended name:
Acid phosphatase
EC=3.1.3.2

Gene names

Name:	phoA
ORF Names:	AFUA_1G03570

Organism

Aspergillus fumigatus (Sartorya fumigata) [Complete proteome]

Taxonomic identifier

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	447 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Has both phosphomonoesterase and phosphodiesterase activity. Cleaves a broad range of phosphate esters.
Catalytic activity	A phosphate monoester + H₂O = an alcohol + phosphate.
Enzyme regulation	Inhibited by NaF, molybdate and vanadate.
Subcellular location	Cell membrane; Lipid-anchor › GPI-anchor. Ref.3 Ref.4
Induction	Repressed by phosphate. Ref.1
Post-translational modification	The GPI-like anchor contains a phosphoceramide lipid group. The anchor position has not been determined.
Biophysicochemical properties	Kinetic parameters: K_M=1.45 mM for p-nitrophenyl phophate K_M=2.3 mM for bis-(p-nitrophenyl) phophate pH dependence: Optimum pH is 4-6. Active from pH 3 to 7.
Sequence caution	The sequence EAL88069.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Cell membrane Membrane
Domain	Signal
Molecular function	Hydrolase
PTM	GPI-anchor Glycoprotein Lipoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	acid phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

17

Potential

Chain

402

Acid phosphatase

PRO_0000245560

Propeptide

28

Removed in mature form Potential

PRO_0000245561

Regions

Compositional bias

8

Poly-Ser

Sites

Active site

1

Proton donor By similarity

Amino acid modifications

Lipidation

1

GPI-like-anchor amidated serine Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

1

L → C AA sequence Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

Q8X176-1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 4B2FB1F0ECEF0D72
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447

48,988

        10         20         30         40         50         60 
MKPSVATLLA TVSLVYAQTA TEKEPSLSAI ESAAASIQPY SPVSNVEGVA FNRFFQVWLE 

        70         80         90        100        110        120 
NIDYEDAAAD ENMKWLASQG ILLTNFYAVT HPSEPNYCAA VGGDTFGMDN DNFNQIPANV 

       130        140        150        160        170        180 
STVADLLDTK NIAWGEYQEH LPYPGFQGFN YSNQETYVND YVRKHNPLVL YDSVTKNSTR 

       190        200        210        220        230        240 
LRQIKNFTSF EDDLANKKLP QWAFITPNMT NDAHDTNITF GAKWERSWIA PLLNNSYFMN 

       250        260        270        280        290        300 
DTLILLTFDE DGTYSKSNKI FSVLLGGAIP DELKGTQDDT FYTHYSVIAS VSANWGLPSL 

       310        320        330        340        350        360 
GRWDCGANIL EIVANKTGYV NYDVDTTNLR LNETYPGPMS AGEYSKYSPV WPNALTRGDC 

       370        380        390        400        410        420 
SAGHGILDIV KETYANTEPT YNYSSPFPYD TASNYNTKVT ATKKNVTGTH RSSSSSSPSA 

       430        440 
SSNAAVSAVA PAAGVSGLLL GLALNLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a cell-wall acid phosphatase (PhoAp) in Aspergillus fumigatus." Bernard M., Mouyna I., Dubreucq G., Debeaupuis J.-P., Fontaine T., Vorgias C., Fuglsang C., Latge J.-P. Microbiology 148:2819-2829(2002) [PubMed: 12213928] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 260-274, INDUCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[2]	"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus." Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. Denning D.W. Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Af293 / CBS 101355 / FGSC A1100.
[3]	"Proteome analysis of Aspergillus fumigatus identifies glycosylphosphatidylinositol-anchored proteins associated to the cell wall biosynthesis." Bruneau J.-M., Magnin T., Tagat E., Legrand R., Bernard M., Diaquin M., Fudali C., Latge J.-P. Electrophoresis 22:2812-2823(2001) [PubMed: 11545413] [Abstract] Cited for: PROTEIN SEQUENCE OF 41-53; 164-176; 317-330 AND 347-350, GPI-ANCHOR.
[4]	"Structures of the glycosylphosphatidylinositol membrane anchors from Aspergillus fumigatus membrane proteins." Fontaine T., Magnin T., Melhert A., Lamont D., Latge J.-P., Ferguson M.A.J. Glycobiology 13:169-177(2003) [PubMed: 12626404] [Abstract] Cited for: PROTEIN SEQUENCE OF 317-323, STRUCTURE OF GPI-ANCHOR.

Cross-references

Sequence databases
	AF462065 Genomic DNA. Translation: AAL66381.1. AAHF01000007 Genomic DNA. Translation: EAL88069.1. Sequence problems.
RefSeq	XP_750107.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q8X176.
Genome annotation databases
GeneID	3507810.
GenomeReviews	Gene locus phoA in contig CM000169_GR.
KEGG	afm:AFUA_1G03570.
Phylogenomic databases
HOGENOM	Q8X176.
Enzyme and pathway databases
BRENDA	3.1.3.2. 18841.
Family and domain databases
InterPro	IPR007312. Phosphoesterase. [Graphical view]
Pfam	PF04185. Phosphoesterase. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PHOA_ASPFU

Accession

Primary (citable) accession number: Q8X176
Secondary accession number(s): Q4WK63

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2006
Last sequence update:	March 1, 2002
Last modified:	October 13, 2009
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information