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Protein

Invertase 2

Gene

SUC2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei42PROSITE-ProRule annotation1 Publication1
Binding sitei60SubstrateBy similarity1
Binding sitei223SubstrateBy similarity1
Binding sitei311SubstrateBy similarity1

GO - Molecular functioni

  • beta-fructofuranosidase activity Source: SGD
  • inulinase activity Source: SGD
  • sucrose alpha-glucosidase activity Source: GO_Central

GO - Biological processi

  • fructan catabolic process Source: SGD
  • inulin catabolic process Source: SGD
  • raffinose catabolic process Source: SGD
  • sucrose catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciYEAST:YIL162W-MONOMER.

Protein family/group databases

CAZyiGH32. Glycoside Hydrolase Family 32.
mycoCLAPiSUC32B_YEAST.

Names & Taxonomyi

Protein namesi
Recommended name:
Invertase 2 (EC:3.2.1.26)
Alternative name(s):
Beta-fructofuranosidase 2
Saccharase
Gene namesi
Name:SUC2
Ordered Locus Names:YIL162W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IX

Organism-specific databases

EuPathDBiFungiDB:YIL162W.
SGDiS000001424. SUC2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • extracellular region Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi42D → N: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 191 PublicationAdd BLAST19
ChainiPRO_000003339920 – 532Invertase 2Add BLAST513

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi23N-linked (GlcNAc...); in isoform Secreted1 Publication1
Glycosylationi64N-linked (GlcNAc...); in isoform Secreted; partial1 Publication1
Glycosylationi97N-linked (GlcNAc...); in isoform Secreted1 Publication1
Glycosylationi111N-linked (GlcNAc...); in isoform Secreted1 Publication1
Glycosylationi118N-linked (GlcNAc...); in isoform Secreted1 Publication1
Glycosylationi165N-linked (GlcNAc...); in isoform Secreted; partial1 Publication1
Glycosylationi266N-linked (GlcNAc...); in isoform Secreted; partial1 Publication1
Glycosylationi275N-linked (GlcNAc...); in isoform Secreted; partial1 Publication1
Glycosylationi356N-linked (GlcNAc...); in isoform Secreted1 Publication1
Glycosylationi369N-linked (GlcNAc...); in isoform Secreted1 Publication1
Glycosylationi384N-linked (GlcNAc...); in isoform Secreted1 Publication1
Glycosylationi398N-linked (GlcNAc...); in isoform Secreted1 Publication1
Glycosylationi512N-linked (GlcNAc...); in isoform Secreted; partial1 Publication1

Post-translational modificationi

Isoform Secreted is glycosylated. Isoform Intracellular is not glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiP00724.

2D gel databases

COMPLUYEAST-2DPAGEP00724.

PTM databases

UniCarbKBiP00724.

Interactioni

Protein-protein interaction databases

BioGridi34830. 25 interactors.
DIPiDIP-5542N.
IntActiP00724. 2 interactors.
MINTiMINT-477961.

Structurei

Secondary structure

1532
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi30 – 32Combined sources3
Beta strandi36 – 49Combined sources14
Turni50 – 53Combined sources4
Beta strandi54 – 67Combined sources14
Beta strandi73 – 84Combined sources12
Beta strandi86 – 92Combined sources7
Beta strandi100 – 108Combined sources9
Helixi123 – 125Combined sources3
Beta strandi127 – 134Combined sources8
Beta strandi139 – 145Combined sources7
Beta strandi147 – 152Combined sources6
Beta strandi170 – 177Combined sources8
Turni178 – 181Combined sources4
Beta strandi182 – 189Combined sources8
Helixi190 – 192Combined sources3
Beta strandi194 – 205Combined sources12
Beta strandi207 – 212Combined sources6
Beta strandi223 – 234Combined sources12
Beta strandi239 – 247Combined sources9
Beta strandi257 – 265Combined sources9
Beta strandi270 – 275Combined sources6
Beta strandi278 – 280Combined sources3
Beta strandi283 – 285Combined sources3
Beta strandi287 – 291Combined sources5
Turni297 – 299Combined sources3
Beta strandi303 – 309Combined sources7
Turni311 – 315Combined sources5
Beta strandi316 – 318Combined sources3
Beta strandi320 – 323Combined sources4
Beta strandi329 – 343Combined sources15
Beta strandi345 – 354Combined sources10
Beta strandi374 – 382Combined sources9
Beta strandi387 – 397Combined sources11
Beta strandi410 – 416Combined sources7
Beta strandi418 – 423Combined sources6
Beta strandi425 – 430Combined sources6
Turni431 – 434Combined sources4
Beta strandi435 – 439Combined sources5
Helixi446 – 450Combined sources5
Beta strandi465 – 468Combined sources4
Beta strandi471 – 489Combined sources19
Turni490 – 493Combined sources4
Beta strandi494 – 499Combined sources6
Beta strandi503 – 505Combined sources3
Beta strandi510 – 517Combined sources8
Beta strandi521 – 530Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4EQVX-ray3.40A/B/C/D/E/F/G/H21-532[»]
ProteinModelPortaliP00724.
SMRiP00724.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni39 – 42Substrate bindingBy similarity4
Regioni102 – 103Substrate bindingBy similarity2
Regioni170 – 171Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the glycosyl hydrolase 32 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000181424.
InParanoidiP00724.
KOiK01193.
OMAiQANPETE.
OrthoDBiEOG092C1VN1.

Family and domain databases

Gene3Di2.120.10.10. 1 hit.
2.60.120.560. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001362. Glyco_hydro_32.
IPR018053. Glyco_hydro_32_AS.
IPR013189. Glyco_hydro_32_C.
IPR013148. Glyco_hydro_32_N.
IPR023296. Glyco_hydro_beta-prop.
IPR011040. Sialidases.
[Graphical view]
PfamiPF08244. Glyco_hydro_32C. 1 hit.
PF00251. Glyco_hydro_32N. 1 hit.
[Graphical view]
SMARTiSM00640. Glyco_32. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF75005. SSF75005. 1 hit.
PROSITEiPS00609. GLYCOSYL_HYDROL_F32. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform Secreted (identifier: P00724-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLLQAFLFLL AGFAAKISAS MTNETSDRPL VHFTPNKGWM NDPNGLWYDE
60 70 80 90 100
KDAKWHLYFQ YNPNDTVWGT PLFWGHATSD DLTNWEDQPI AIAPKRNDSG
110 120 130 140 150
AFSGSMVVDY NNTSGFFNDT IDPRQRCVAI WTYNTPESEE QYISYSLDGG
160 170 180 190 200
YTFTEYQKNP VLAANSTQFR DPKVFWYEPS QKWIMTAAKS QDYKIEIYSS
210 220 230 240 250
DDLKSWKLES AFANEGFLGY QYECPGLIEV PTEQDPSKSY WVMFISINPG
260 270 280 290 300
APAGGSFNQY FVGSFNGTHF EAFDNQSRVV DFGKDYYALQ TFFNTDPTYG
310 320 330 340 350
SALGIAWASN WEYSAFVPTN PWRSSMSLVR KFSLNTEYQA NPETELINLK
360 370 380 390 400
AEPILNISNA GPWSRFATNT TLTKANSYNV DLSNSTGTLE FELVYAVNTT
410 420 430 440 450
QTISKSVFAD LSLWFKGLED PEEYLRMGFE VSASSFFLDR GNSKVKFVKE
460 470 480 490 500
NPYFTNRMSV NNQPFKSEND LSYYKVYGLL DQNILELYFN DGDVVSTNTY
510 520 530
FMTTGNALGS VNMTTGVDNL FYIDKFQVRE VK
Length:532
Mass (Da):60,639
Last modified:July 21, 1986 - v1
Checksum:i7D8AB33E6772B775
GO
Isoform Intracellular (identifier: P00724-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: Missing.

Note: Produced by alternative initiation at Met-21 of isoform Secreted.
Show »
Length:512
Mass (Da):58,545
Checksum:iEC78825171A0E8D2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti51K → P in AAA73474 (PubMed:1888528).Curated1
Sequence conflicti409A → P AA sequence (PubMed:3284881).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0196111 – 20Missing in isoform Intracellular. CuratedAdd BLAST20

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46921 Genomic DNA. Translation: CAA87030.1.
U19781 Genomic DNA. Translation: AAA73474.1.
V01311 Genomic DNA. Translation: CAA24618.1.
K03294 Genomic DNA. Translation: AAA35127.1.
M13627 Genomic DNA. Translation: AAA35129.1.
BK006942 Genomic DNA. Translation: DAA08390.1.
PIRiA00899. IFBY.
RefSeqiNP_012104.1. NM_001179510.1. [P00724-1]

Genome annotation databases

EnsemblFungiiYIL162W; YIL162W; YIL162W. [P00724-1]
GeneIDi854644.
KEGGisce:YIL162W.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46921 Genomic DNA. Translation: CAA87030.1.
U19781 Genomic DNA. Translation: AAA73474.1.
V01311 Genomic DNA. Translation: CAA24618.1.
K03294 Genomic DNA. Translation: AAA35127.1.
M13627 Genomic DNA. Translation: AAA35129.1.
BK006942 Genomic DNA. Translation: DAA08390.1.
PIRiA00899. IFBY.
RefSeqiNP_012104.1. NM_001179510.1. [P00724-1]

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4EQVX-ray3.40A/B/C/D/E/F/G/H21-532[»]
ProteinModelPortaliP00724.
SMRiP00724.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34830. 25 interactors.
DIPiDIP-5542N.
IntActiP00724. 2 interactors.
MINTiMINT-477961.

Protein family/group databases

CAZyiGH32. Glycoside Hydrolase Family 32.
mycoCLAPiSUC32B_YEAST.

PTM databases

UniCarbKBiP00724.

2D gel databases

COMPLUYEAST-2DPAGEP00724.

Proteomic databases

PRIDEiP00724.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYIL162W; YIL162W; YIL162W. [P00724-1]
GeneIDi854644.
KEGGisce:YIL162W.

Organism-specific databases

EuPathDBiFungiDB:YIL162W.
SGDiS000001424. SUC2.

Phylogenomic databases

HOGENOMiHOG000181424.
InParanoidiP00724.
KOiK01193.
OMAiQANPETE.
OrthoDBiEOG092C1VN1.

Enzyme and pathway databases

BioCyciYEAST:YIL162W-MONOMER.

Miscellaneous databases

PROiP00724.

Family and domain databases

Gene3Di2.120.10.10. 1 hit.
2.60.120.560. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001362. Glyco_hydro_32.
IPR018053. Glyco_hydro_32_AS.
IPR013189. Glyco_hydro_32_C.
IPR013148. Glyco_hydro_32_N.
IPR023296. Glyco_hydro_beta-prop.
IPR011040. Sialidases.
[Graphical view]
PfamiPF08244. Glyco_hydro_32C. 1 hit.
PF00251. Glyco_hydro_32N. 1 hit.
[Graphical view]
SMARTiSM00640. Glyco_32. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF75005. SSF75005. 1 hit.
PROSITEiPS00609. GLYCOSYL_HYDROL_F32. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiINV2_YEAST
AccessioniPrimary (citable) accession number: P00724
Secondary accession number(s): D6VVC4, Q12671
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 30, 2016
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1780 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.