P34755 (PHYB_ASPAW) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-phytase B
EC=3.1.3.8

Alternative name(s):
Myo-inositol-hexaphosphate 3-phosphohydrolase B
pH 2.5 optimum acid phosphatase

Gene names

Name:	phyB
Synonyms:	aph

Organism

Aspergillus awamori (Black koji mold)

Taxonomic identifier

105351 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	479 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	Catalyzes the hydrolysis of inorganic orthophosphate from phytate.
Catalytic activity	Myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the histidine acid phosphatase family.

Ontologies

Keywords
Domain	Signal
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	dephosphorylation Inferred from electronic annotation. Source: GOC
Molecular_function	3-phytase activity Inferred from electronic annotation. Source: EC acid phosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

By similarity

Chain

20 – 479

460

3-phytase B

PRO_0000023975

Sites

Active site

82

1

Nucleophile

Active site

338

1

Proton donor

Amino acid modifications

Glycosylation

191

1

N-linked (GlcNAc...)

Glycosylation

315

1

N-linked (GlcNAc...)

Glycosylation

458

1

N-linked (GlcNAc...)

Disulfide bond

71 ↔ 387

Disulfide bond

128 ↔ 472

Disulfide bond

216 ↔ 441

Disulfide bond

225 ↔ 298

Disulfide bond

413 ↔ 421

Secondary structure

1

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479

Helix Strand Turn

Details...

Helix

41 – 43

3

Helix

45 – 47

3

Beta strand

71 – 81

11

Helix

89 – 103

15

Helix

112 – 119

8

Helix

127 – 129

3

Helix

141 – 156

16

Helix

157 – 159

3

Beta strand

162 – 164

3

Beta strand

166 – 173

8

Helix

174 – 188

15

Helix

189 – 191

3

Helix

192 – 195

4

Beta strand

196 – 201

6

Helix

205 – 207

3

Beta strand

210 – 213

4

Turn

224 – 227

4

Helix

234 – 245

12

Helix

253 – 266

14

Turn

267 – 269

3

Helix

276 – 278

3

Helix

281 – 298

18

Helix

306 – 323

18

Helix

325 – 328

4

Beta strand

330 – 336

7

Helix

338 – 348

11

Beta strand

359 – 361

3

Helix

370 – 372

3

Beta strand

379 – 387

9

Beta strand

395 – 403

9

Beta strand

406 – 408

3

Helix

417 – 419

3

Helix

423 – 433

11

Helix

437 – 440

4

Turn

453 – 455

3

Sequences

	Sequence		Length	Mass (Da)
	P34755 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: 4F8E0F3778CC3B08	FASTA	479	52,678
	10 20 30 40 50 60 MPRTSLLTLA CALATGASAF SYGAAIPQST QEKQFSQEFR DGYSILKHYG GNGPYSERVS 70 80 90 100 110 120 YGIARDPPTS CEVDQVIMVK RHGERYPSPS AGKDIEEALA KVYSINTTEY KGDLAFLNDW 130 140 150 160 170 180 TYYVPNECYY NAETTSGPYA GLLDAYNHGN DYKARYGHLW NGETVVPFFS SGYGRVIETA 190 200 210 220 230 240 RKFGEGFFGY NYSTNAALNI ISESEVMGAD SLTPTCDTDN DQTTCDNLTY QLPQFKVAAA 250 260 270 280 290 300 RLNSQNPGMN LTASDVYNLM VMASFELNAR PFSNWINAFT QDEWVSFGYV EDLNYYYCAG 310 320 330 340 350 360 PGDKNMAAVG AVYANASLTL LNQGPKEAGS LFFNFAHDTN ITPILAALGV LIPNEDLPLD 370 380 390 400 410 420 RVAFGNPYSI GNIVPMGGHL TIERLSCQAT ALSDEGTYVR LVLNEAVLPF NDCTSGPGYS 430 440 450 460 470 CPLANYTSIL NKNLPDYTTT CNVSASYPQY LSFWWNYNTT TELNYRSSPI ACQEGDAMD

References

[1]	"The cloning and sequencing of the genes encoding phytase (phy) and pH 2.5-optimum acid phosphatase (aph) from Aspergillus niger var. awamori." Piddington C.S., Houston C.S., Paloheimo M.T., Cantrell M.A., Miettinen-Oinonen A., Nevalainen H., Rambosek J.A. Gene 133:55-62(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ALK0243.
[2]	"Crystal structure of Aspergillus niger pH 2.5 acid phosphatase at 2.4-A resolution." Kostrewa D., Wyss M., D'Arcy A., van Loon A.P.G.M. J. Mol. Biol. 288:965-974(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L02420 Unassigned DNA. Translation: AAA16897.1.

PIR

JN0890.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QFX	X-ray	2.40	A/B	20-479	[»]

ProteinModelPortal

P34755.

SMR

P34755. Positions 33-479.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR000560. His_Pase_superF_clade-2.
IPR016274. Histidine_acid_Pase_euk.
[Graphical view]

Pfam

PF00328. His_Phos_2. 1 hit.
[Graphical view]

PIRSF

PIRSF000894. Acid_phosphatase. 1 hit.

PROSITE

PS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P34755.

Entry information

Entry name

PHYB_ASPAW

Accession

Primary (citable) accession number: P34755

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	April 3, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program