INV_SCHOC
ID INV_SCHOC Reviewed; 533 AA.
AC P24133;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Invertase;
DE EC=3.2.1.26;
DE AltName: Full=Beta-fructofuranosidase;
DE AltName: Full=Saccharase;
DE Flags: Precursor;
GN Name=INV;
OS Schwanniomyces occidentalis (Yeast) (Debaryomyces occidentalis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Schwanniomyces.
OX NCBI_TaxID=27300;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 2076;
RX PubMed=2688929; DOI=10.1007/bf00391470;
RA Klein R.D., Poorman R.A., Favreau M.A., Shea M.H., Hatzenbuhler N.T.,
RA Nulf S.C.;
RT "Cloning and sequence analysis of the gene encoding invertase from the
RT yeast Schwanniomyces occidentalis.";
RL Curr. Genet. 16:145-152(1989).
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; X17604; CAA35606.1; -; Genomic_DNA.
DR PIR; S13528; S13528.
DR PDB; 3KF3; X-ray; 1.90 A; A/B=27-533.
DR PDB; 3KF5; X-ray; 2.90 A; A/B=24-533.
DR PDBsum; 3KF3; -.
DR PDBsum; 3KF5; -.
DR AlphaFoldDB; P24133; -.
DR SMR; P24133; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR CLAE; SUC32A_DEBOC; -.
DR BRENDA; 3.2.1.26; 5620.
DR EvolutionaryTrace; P24133; -.
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 1: Evidence at protein level;
KW 3D-structure; Glycoprotein; Glycosidase; Hydrolase; Signal.
FT SIGNAL 1..22
FT CHAIN 23..533
FT /note="Invertase"
FT /id="PRO_0000033394"
FT ACT_SITE 50
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT BINDING 47..50
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 110..111
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 178..179
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 44..57
FT /evidence="ECO:0007829|PDB:3KF3"
FT TURN 58..61
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 62..70
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 78..92
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 108..116
FT /evidence="ECO:0007829|PDB:3KF3"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 135..143
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 146..160
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:3KF5"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:3KF3"
FT TURN 186..189
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:3KF3"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 202..213
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 229..239
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 245..253
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 263..271
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 293..297
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 302..310
FT /evidence="ECO:0007829|PDB:3KF3"
FT TURN 314..319
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 333..342
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 359..371
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:3KF5"
FT STRAND 387..397
FT /evidence="ECO:0007829|PDB:3KF3"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 407..415
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 424..430
FT /evidence="ECO:0007829|PDB:3KF3"
FT TURN 431..434
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 435..439
FT /evidence="ECO:0007829|PDB:3KF3"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 456..460
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 464..467
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 470..480
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 483..488
FT /evidence="ECO:0007829|PDB:3KF3"
FT TURN 489..492
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 493..498
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 507..514
FT /evidence="ECO:0007829|PDB:3KF3"
FT STRAND 520..532
FT /evidence="ECO:0007829|PDB:3KF3"
SQ SEQUENCE 533 AA; 60839 MW; C7CE833F30778088 CRC64;
MVQVLSVLVI PLLTLFFGYV ASSSIDLSVD TSEYNRPLIH FTPEKGWMND PNGLFYDKTA
KLWHLYFQYN PNATAWGQPL YWGHATSNDL VHWDEHEIAI GPEHDNEGIF SGSIVVDHNN
TSGFFNSSID PNQRIVAIYT NNIPDLQTQD IAFSLDGGYT FTKYENNPVI DVSSNQFRDP
KVFWHERFKS MDHGCSEIAR VKIQIFGSAN LKNWVLNSNF SSGYYGNQYG MSRLIEVPIE
NSDKSKWVMF LAINPGSPLG GSINQYFVGD FDGFQFVPDD SQTRFVDIGK DFYAFQTFSE
VEHGVLGLAW ASNWQYADQV PTNPWRSSTS LARNYTLRYV IQMLKLTANI DKSVLPDSIN
VVDKLKKKNV KLTNKKPIKT NFKGSTGLFD FNITFKVLNL NVSPGKTHFD ILINSQELNS
SVDSIKIGFD SSQSLFYIDR HIPNVEFPRK QFFTDKLAAY LEPLDYDQDL RVFSLYGIVD
KNIIELYFND GTVAMTNTFF MGEGKYPHDI QIVTDTEEPL FELESVIIRE LNK
