PHYC_BACIU
ID PHYC_BACIU Reviewed; 383 AA.
AC O31097;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 89.
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=phyC; Synonyms=phyB13;
OS Bacillus subtilis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1423;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=VTT-E-68013;
RX PubMed=9603817; DOI=10.1128/aem.64.6.2079-2085.1998;
RA Kerovuo J., Lauraeus M., Nurminen P., Kalkkinen N., Apajalahti J.;
RT "Isolation, characterization, molecular gene cloning, and sequencing of a
RT novel phytase from Bacillus subtilis.";
RL Appl. Environ. Microbiol. 64:2079-2085(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=981;
RA Yao B., Yuan T., Wang Y., Fan Y.;
RT "Cloning of neutral phytase gene nphy from Bacillus subtilis and its
RT expression in Escherichia coli.";
RL Chin. J. Biotechnol. 17:11-15(2001).
CC -!- FUNCTION: Catalyzes the hydrolysis of inorganic orthophosphate from
CC phytate. Only phytate, ADP, and ATP were hydrolyzed (100, 75, and 50%
CC of the relative activity, respectively).
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Ca(2+) is required for its activity and/or stability.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.;
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- INDUCTION: By phytate.
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DR EMBL; AF029053; AAC31775.1; -; Genomic_DNA.
DR EMBL; AJ277890; CAB91845.1; -; Genomic_DNA.
DR PDB; 3AMR; X-ray; 1.25 A; A=29-383.
DR PDB; 3AMS; X-ray; 2.08 A; A=29-383.
DR PDBsum; 3AMR; -.
DR PDBsum; 3AMS; -.
DR AlphaFoldDB; O31097; -.
DR SMR; O31097; -.
DR BRENDA; 3.1.3.8; 658.
DR EvolutionaryTrace; O31097; -.
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..29
FT /id="PRO_0000022055"
FT CHAIN 30..383
FT /note="3-phytase"
FT /id="PRO_0000022056"
FT DOMAIN 30..362
FT /note="BPP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00997"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:3AMR"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:3AMR"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:3AMR"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:3AMR"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:3AMR"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:3AMR"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:3AMR"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:3AMR"
FT STRAND 98..109
FT /evidence="ECO:0007829|PDB:3AMR"
FT STRAND 112..121
FT /evidence="ECO:0007829|PDB:3AMR"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:3AMS"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:3AMR"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:3AMR"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:3AMR"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:3AMR"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:3AMR"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:3AMR"
FT STRAND 179..190
FT /evidence="ECO:0007829|PDB:3AMR"
FT STRAND 196..205
FT /evidence="ECO:0007829|PDB:3AMR"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:3AMR"
FT TURN 217..220
FT /evidence="ECO:0007829|PDB:3AMR"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:3AMR"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:3AMR"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:3AMR"
FT STRAND 245..255
FT /evidence="ECO:0007829|PDB:3AMR"
FT STRAND 259..266
FT /evidence="ECO:0007829|PDB:3AMR"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:3AMR"
FT STRAND 272..278
FT /evidence="ECO:0007829|PDB:3AMR"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:3AMR"
FT STRAND 283..290
FT /evidence="ECO:0007829|PDB:3AMR"
FT STRAND 295..301
FT /evidence="ECO:0007829|PDB:3AMR"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:3AMR"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:3AMR"
FT STRAND 331..338
FT /evidence="ECO:0007829|PDB:3AMR"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:3AMR"
FT HELIX 355..361
FT /evidence="ECO:0007829|PDB:3AMR"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:3AMR"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:3AMR"
SQ SEQUENCE 383 AA; 41923 MW; E9BEC2E4A48EB9CA CRC64;
MNHSKTLLLT AAAGLMLTCG AVSSQAKHKL SDPYHFTVNA AAETEPVDTA GDAADDPAIW
LDPKTPQNSK LITTNKKSGL VVYSLDGKML HSYNTGKLNN VDIRYDFPLN GKKVDIAAAS
NRSEGKNTIE IYAIDGKNGT LQSMTDPDHP IATAINEVYG FTLYHSQKTG KYYAMVTGKE
GEFEQYELKA DKNGYISGKK VRAFKMNSQT EGMAADDEYG RLYIAEEDEA IWKFSAEPDG
GSNGTVIDRA DGRHLTRDIE GLTIYYAADG KGYLMASSQG NSSYAIYDRQ GKNKYVADFR
ITDGPETDGT SDTDGIDVLG FGLGPEYPFG IFVAQDGENI DHGQKANQNF KIVPWERIAD
QIGFRPLANE QVDPRKLTDR SGK
