PHYT_BACSD
ID PHYT_BACSD Reviewed; 383 AA.
AC O66037;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=3-phytase;
DE EC=3.1.3.8;
DE AltName: Full=Myo-inositol-hexaphosphate 3-phosphohydrolase;
DE AltName: Full=Phytate 3-phosphatase;
DE Flags: Precursor;
GN Name=phy;
OS Bacillus sp. (strain DS11).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=86035;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 31-44 AND
RP 214-223.
RX PubMed=9595681; DOI=10.1111/j.1574-6968.1998.tb12997.x;
RA Kim Y.-O., Lee J.-K., Kim H.-K., Yu J.-H., Oh T.-K.;
RT "Cloning of the thermostable phytase gene (phy) from Bacillus sp. DS11 and
RT its overexpression in Escherichia coli.";
RL FEMS Microbiol. Lett. 162:185-191(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
RX PubMed=10089471; DOI=10.1107/s0907444998015285;
RA Ha N.-C., Kim Y.-O., Oh T.-K., Oh B.-H.;
RT "Preliminary X-ray crystallographic analysis of a novel phytase from a
RT Bacillus amyloliquefaciens strain.";
RL Acta Crystallogr. D 55:691-693(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=10655618; DOI=10.1038/72421;
RA Ha N.-C., Oh B.-C., Shin S., Kim H.-J., Oh T.-K., Kim Y.-O., Choi K.Y.,
RA Oh B.-H.;
RT "Crystal structures of a novel, thermostable phytase in partially and fully
RT calcium-loaded states.";
RL Nat. Struct. Biol. 7:147-153(2000).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol
CC 1,2,4,5,6-pentakisphosphate + phosphate; Xref=Rhea:RHEA:16989,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798,
CC ChEBI:CHEBI:58130; EC=3.1.3.8; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00997};
CC -!- SUBCELLULAR LOCATION: Secreted.
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DR EMBL; U85968; AAC38573.1; -; Genomic_DNA.
DR PDB; 1CVM; X-ray; 2.40 A; A=29-381.
DR PDB; 1H6L; X-ray; 1.80 A; A=29-381.
DR PDB; 1POO; X-ray; 2.10 A; A=29-383.
DR PDB; 1QLG; X-ray; 2.20 A; A=29-381.
DR PDB; 2POO; X-ray; 2.05 A; A=29-383.
DR PDBsum; 1CVM; -.
DR PDBsum; 1H6L; -.
DR PDBsum; 1POO; -.
DR PDBsum; 1QLG; -.
DR PDBsum; 2POO; -.
DR AlphaFoldDB; O66037; -.
DR SMR; O66037; -.
DR BRENDA; 3.1.3.8; 691.
DR EvolutionaryTrace; O66037; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016158; F:3-phytase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.120.10.30; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR003431; BP_Phytase.
DR Pfam; PF02333; Phytase; 1.
DR PROSITE; PS51662; BP_PHYTASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..30
FT /evidence="ECO:0000269|PubMed:9595681"
FT /id="PRO_0000022058"
FT CHAIN 31..383
FT /note="3-phytase"
FT /id="PRO_0000022059"
FT DOMAIN 31..362
FT /note="BPP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00997"
FT REGION 364..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:1H6L"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:1H6L"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:1H6L"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:1H6L"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:1H6L"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:1H6L"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:1H6L"
FT STRAND 98..109
FT /evidence="ECO:0007829|PDB:1H6L"
FT STRAND 112..121
FT /evidence="ECO:0007829|PDB:1H6L"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:1H6L"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:1H6L"
FT TURN 136..139
FT /evidence="ECO:0007829|PDB:1H6L"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:1H6L"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:1H6L"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:1H6L"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:1H6L"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:1H6L"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:1H6L"
FT STRAND 179..190
FT /evidence="ECO:0007829|PDB:1H6L"
FT STRAND 194..205
FT /evidence="ECO:0007829|PDB:1H6L"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:1H6L"
FT TURN 217..220
FT /evidence="ECO:0007829|PDB:1H6L"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:1H6L"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:1H6L"
FT STRAND 230..237
FT /evidence="ECO:0007829|PDB:1H6L"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:2POO"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:1H6L"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:1H6L"
FT STRAND 259..266
FT /evidence="ECO:0007829|PDB:1H6L"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:1H6L"
FT STRAND 272..278
FT /evidence="ECO:0007829|PDB:1H6L"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:1H6L"
FT STRAND 283..290
FT /evidence="ECO:0007829|PDB:1H6L"
FT STRAND 295..301
FT /evidence="ECO:0007829|PDB:1H6L"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:1H6L"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:1H6L"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:2POO"
FT STRAND 331..338
FT /evidence="ECO:0007829|PDB:1H6L"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:2POO"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:1H6L"
FT HELIX 356..359
FT /evidence="ECO:0007829|PDB:1H6L"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:1H6L"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:1QLG"
SQ SEQUENCE 383 AA; 41802 MW; DCB65188F7B61C8C CRC64;
MNHSKTLLLT AAAGLMLTCG AVSSQAKHKL SDPYHFTVNA AAETEPVDTA GDAADDPAIW
LDPKNPQNSK LITTNKKSGL AVYSLEGKML HSYHTGKLNN VDIRYDFPLN GKKVDIAAAS
NRSEGKNTIE IYAIDGKNGT LQSITDPNRP IASAIDEVYG FSLYHSQKTG KYYAMVTGKE
GEFEQYELNA DKNGYISGKK VRAFKMNSQT EGMAADDEYG SLYIAEEDEA IWKFSAEPDG
GSNGTVIDRA DGRHLTPDIE GLTIYYAADG KGYLLASSQG NSSYAIYERQ GQNKYVADFQ
ITDGPETDGT SDTDGIDVLG FGLGPEYPFG LFVAQDGENI DHGQKANQNF KMVPWERIAD
KIGFHPQVNK QVDPRKMTDR SGK
