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INV1_PEA
ID   INV1_PEA                Reviewed;         555 AA.
AC   Q43089;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Beta-fructofuranosidase, cell wall isozyme;
DE            EC=3.2.1.26;
DE   AltName: Full=Acid invertase;
DE   AltName: Full=Sucrose hydrolase;
DE   Flags: Precursor;
GN   Name=BFRUCT1;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Little Marvel;
RA   Zhang L., Cohn N.S., Mitchell J.P.;
RT   "A cDNA clone encoding a cell Wall invertase from pea.";
RL   (er) Plant Gene Register PGR96-008(1996).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-fructofuranoside
CC         residues in beta-D-fructofuranosides.; EC=3.2.1.26;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10067};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR   EMBL; X85327; CAA59677.1; -; mRNA.
DR   PIR; T06491; T06491.
DR   AlphaFoldDB; Q43089; -.
DR   SMR; Q43089; -.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
DR   GO; GO:0004564; F:beta-fructofuranosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.115.10.20; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001362; Glyco_hydro_32.
DR   InterPro; IPR018053; Glyco_hydro_32_AS.
DR   InterPro; IPR013189; Glyco_hydro_32_C.
DR   InterPro; IPR013148; Glyco_hydro_32_N.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   Pfam; PF08244; Glyco_hydro_32C; 1.
DR   Pfam; PF00251; Glyco_hydro_32N; 1.
DR   SMART; SM00640; Glyco_32; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF75005; SSF75005; 1.
DR   PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..555
FT                   /note="Beta-fructofuranosidase, cell wall isozyme"
FT                   /id="PRO_0000033385"
FT   ACT_SITE        61
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT   ACT_SITE        140
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT   BINDING         58..61
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         120..121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         186..187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         241
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         277
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        154
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        337
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        435..481
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   555 AA;  62655 MW;  7B548E251CFD5D44 CRC64;
     MAISSIFLLS LFSLIYVIPI EATHHVYQTL ETLSSHHSSK SNHQPYRTAY HFQPLKNWIN
     DPNGPMRYGG FYHLFYQYNP KGAVWGNIVW AHSVSKDLVN WTPLDHAIHP SQPSDIKGCW
     SGSATILPGG KPAILYTGID PNNHQVQNIA IPKNMSDPLL REWKKSPKNP LMEPTIANKI
     NSSSFRDPTT SWLGKDGFWR VLIGSKIDTK GMAILYKSKN FVDWVEAKHP LHSAEGTGMW
     ECPDFYPVLD KNLLRTGVDT SRNGDDDVRH VLKVSLDDTK HDHYLIGSYD VVKDVFVPEN
     GFEDNGFVLR YDYGKYYASK TFFDDGKNRR ILLGWVNESS SVADDVKKGW SGIHTIPREI
     WLHESGKQLV QWPVKEIENL RMNPVNWPTK VIKGGERISI TGVDSVQADV EISFEISDLG
     KVESLRKWID PQLLCSQKGA GVKGGVGPFG LLVFASQGLK EYTAVFFRIF KYQDKNLVLM
     CSDQSRSSLN KDNDMTSYGT FVDVDPLHEK LSLRTLIDHS VVESFGGEGR ACVTARVYPT
     LAIHDKAMLK LTSEY
 
 
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