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Database: UniProt
Entry: I1CPN5_RHIO9
LinkDB: I1CPN5_RHIO9
Original site: I1CPN5_RHIO9 
ID   I1CPN5_RHIO9            Unreviewed;       437 AA.
AC   I1CPN5;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=3-phytase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=RO3G_15126 {ECO:0000313|EMBL:EIE90415.1};
OS   Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS   43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=246409 {ECO:0000313|EMBL:EIE90415.1, ECO:0000313|Proteomes:UP000009138};
RN   [1] {ECO:0000313|EMBL:EIE90415.1, ECO:0000313|Proteomes:UP000009138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880
RC   {ECO:0000313|Proteomes:UP000009138};
RX   PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA   Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA   Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA   Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA   Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA   Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA   Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT   "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT   whole-genome duplication.";
RL   PLoS Genet. 5:E1000549-E1000549(2009).
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DR   EMBL; CH476746; EIE90415.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1CPN5; -.
DR   SMR; I1CPN5; -.
DR   STRING; 246409.I1CPN5; -.
DR   VEuPathDB; FungiDB:RO3G_15126; -.
DR   eggNOG; KOG1382; Eukaryota.
DR   InParanoid; I1CPN5; -.
DR   OMA; RGRSDWC; -.
DR   OrthoDB; 2404758at2759; -.
DR   Proteomes; UP000009138; Unassembled WGS sequence.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR033379; Acid_Pase_AS.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR016274; Histidine_acid_Pase_euk.
DR   PANTHER; PTHR20963:SF8; MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE 1; 1.
DR   PANTHER; PTHR20963; MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE-RELATED; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   PIRSF; PIRSF000894; Acid_phosphatase; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR000894-2};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009138};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..437
FT                   /note="3-phytase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003638885"
FT   DISULFID        212..435
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT   DISULFID        262..276
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT   DISULFID        409..414
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ   SEQUENCE   437 AA;  50215 MW;  B5E1EF3F14E447B4 CRC64;
     MFRLFSGLWS VLALFISLAS LNKVEAKKHN DTSITLGWIM NHMGSSTNYP SYKFRHTVKD
     EITKEYDLEQ IQMIIRHGTR YPVSGDVEAI HDSITKLKES KAHLPWLKAV HNYDMYYEGL
     LNSRGQMEHY LMGQRLALRY PEFIKNLTYE GIISPQFAAY SSWSTRTSQS GHSFCMGAFK
     GQGHLGSDHA MGVPLLSYQE NNDTLIAFHK ACPKWKKDGK AITKQKTAFV NDKYLKPIAS
     RLSGSLGLNI STDDVENFYS ACQAEVSLYQ KSNTFCQLLT KEDVLNLEYI EDLKHYYKYS
     YGIPELNEDM ACDLGKDIIE NMNNTNDVKL NLKFGHTETV LPLRTLLGLY NDTLSSSSTE
     SEIEHRSFKL SKFGFYANNL MFQVLKHKST KERFVRVMEN EEVILFPGCK QKICPIDQFY
     AYMKPRINCD FTKNCSL
//
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