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Protein

Levansucrase

Gene

sacB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Sucrose + (6)-beta-D-fructofuranosyl-(2->)(n) alpha-D-glucopyranoside = glucose + (6)-beta-D-fructofuranosyl-(2->)(n+1) alpha-D-glucopyranoside.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei85SubstrateBy similarity1
Active sitei86NucleophileBy similarity1
Binding sitei164SubstrateBy similarity1
Sitei247Transition state stabilizerBy similarity1
Active sitei342Proton donor/acceptorBy similarity1
Binding sitei360SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciBSUB:BSU34450-MONOMER.
MetaCyc:BSU34450-MONOMER.
BRENDAi2.4.1.10. 658.
SABIO-RKP05655.

Protein family/group databases

CAZyiGH68. Glycoside Hydrolase Family 68.

Names & Taxonomyi

Protein namesi
Recommended name:
Levansucrase (EC:2.4.1.10)
Alternative name(s):
Beta-D-fructofuranosyl transferase
Sucrose 6-fructosyl transferase
Gene namesi
Name:sacB
Ordered Locus Names:BSU34450
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 29Add BLAST29
ChainiPRO_000001224930 – 473LevansucraseAdd BLAST444

Proteomic databases

PaxDbiP05655.
PRIDEiP05655.

Expressioni

Inductioni

Induced by sucrose.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100018666.

Structurei

Secondary structure

1473
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi43 – 45Combined sources3
Helixi48 – 52Combined sources5
Helixi54 – 57Combined sources4
Helixi61 – 63Combined sources3
Helixi70 – 72Combined sources3
Helixi77 – 79Combined sources3
Beta strandi83 – 91Combined sources9
Beta strandi95 – 97Combined sources3
Beta strandi103 – 111Combined sources9
Beta strandi120 – 127Combined sources8
Helixi133 – 135Combined sources3
Beta strandi137 – 142Combined sources6
Helixi147 – 150Combined sources4
Helixi156 – 158Combined sources3
Beta strandi161 – 169Combined sources9
Beta strandi175 – 183Combined sources9
Turni184 – 188Combined sources5
Beta strandi189 – 201Combined sources13
Beta strandi206 – 218Combined sources13
Beta strandi222 – 225Combined sources4
Helixi228 – 234Combined sources7
Helixi236 – 239Combined sources4
Beta strandi246 – 253Combined sources8
Beta strandi256 – 265Combined sources10
Beta strandi267 – 269Combined sources3
Helixi274 – 278Combined sources5
Helixi280 – 282Combined sources3
Helixi287 – 299Combined sources13
Helixi303 – 308Combined sources6
Beta strandi311 – 318Combined sources8
Beta strandi322 – 333Combined sources12
Turni335 – 337Combined sources3
Beta strandi342 – 349Combined sources8
Beta strandi352 – 360Combined sources9
Helixi361 – 363Combined sources3
Beta strandi374 – 383Combined sources10
Helixi391 – 393Combined sources3
Beta strandi395 – 400Combined sources6
Beta strandi404 – 406Combined sources3
Beta strandi410 – 416Combined sources7
Beta strandi419 – 431Combined sources13
Beta strandi435 – 438Combined sources4
Beta strandi441 – 443Combined sources3
Beta strandi447 – 452Combined sources6
Beta strandi455 – 458Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OYGX-ray1.50A30-473[»]
1PT2X-ray2.10A30-473[»]
2VDTX-ray3.20A34-472[»]
3BYJX-ray2.10A1-473[»]
3BYKX-ray2.10A1-473[»]
3BYLX-ray2.10A1-473[»]
3BYNX-ray2.10A1-473[»]
ProteinModelPortaliP05655.
SMRiP05655.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05655.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni246 – 247Substrate bindingBy similarity2
Regioni340 – 342Substrate bindingBy similarity3

Sequence similaritiesi

Belongs to the glycosyl hydrolase 68 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105EDQ. Bacteria.
ENOG410XR0E. LUCA.
HOGENOMiHOG000041220.
InParanoidiP05655.
KOiK00692.
OMAiVELNNDY.
PhylomeDBiP05655.

Family and domain databases

Gene3Di2.115.10.20. 1 hit.
InterProiIPR003469. Glyco_hydro_68.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PfamiPF02435. Glyco_hydro_68. 1 hit.
[Graphical view]
SUPFAMiSSF75005. SSF75005. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P05655-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNIKKFAKQA TVLTFTTALL AGGATQAFAK ETNQKPYKET YGISHITRHD
60 70 80 90 100
MLQIPEQQKN EKYQVPEFDS STIKNISSAK GLDVWDSWPL QNADGTVANY
110 120 130 140 150
HGYHIVFALA GDPKNADDTS IYMFYQKVGE TSIDSWKNAG RVFKDSDKFD
160 170 180 190 200
ANDSILKDQT QEWSGSATFT SDGKIRLFYT DFSGKHYGKQ TLTTAQVNVS
210 220 230 240 250
ASDSSLNING VEDYKSIFDG DGKTYQNVQQ FIDEGNYSSG DNHTLRDPHY
260 270 280 290 300
VEDKGHKYLV FEANTGTEDG YQGEESLFNK AYYGKSTSFF RQESQKLLQS
310 320 330 340 350
DKKRTAELAN GALGMIELND DYTLKKVMKP LIASNTVTDE IERANVFKMN
360 370 380 390 400
GKWYLFTDSR GSKMTIDGIT SNDIYMLGYV SNSLTGPYKP LNKTGLVLKM
410 420 430 440 450
DLDPNDVTFT YSHFAVPQAK GNNVVITSYM TNRGFYADKQ STFAPSFLLN
460 470
IKGKKTSVVK DSILEQGQLT VNK
Length:473
Mass (Da):52,971
Last modified:November 1, 1988 - v1
Checksum:i3FBF2F571B41D5B0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti12V → I in AAA22724 (PubMed:6424671).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14202 Genomic DNA. Translation: AAA22725.1.
Z94043 Genomic DNA. Translation: CAB08015.1.
AL009126 Genomic DNA. Translation: CAB15450.1.
K01987 Genomic DNA. Translation: AAA22724.1.
X02730 Genomic DNA. Translation: CAA26513.1.
PIRiS07309. A25040.
RefSeqiNP_391325.1. NC_000964.3.
WP_001022105.1. NZ_JNCM01000033.1.

Genome annotation databases

EnsemblBacteriaiCAB15450; CAB15450; BSU34450.
GeneIDi936413.
KEGGibsu:BSU34450.
PATRICi18978892. VBIBacSub10457_3609.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14202 Genomic DNA. Translation: AAA22725.1.
Z94043 Genomic DNA. Translation: CAB08015.1.
AL009126 Genomic DNA. Translation: CAB15450.1.
K01987 Genomic DNA. Translation: AAA22724.1.
X02730 Genomic DNA. Translation: CAA26513.1.
PIRiS07309. A25040.
RefSeqiNP_391325.1. NC_000964.3.
WP_001022105.1. NZ_JNCM01000033.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OYGX-ray1.50A30-473[»]
1PT2X-ray2.10A30-473[»]
2VDTX-ray3.20A34-472[»]
3BYJX-ray2.10A1-473[»]
3BYKX-ray2.10A1-473[»]
3BYLX-ray2.10A1-473[»]
3BYNX-ray2.10A1-473[»]
ProteinModelPortaliP05655.
SMRiP05655.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100018666.

Protein family/group databases

CAZyiGH68. Glycoside Hydrolase Family 68.

Proteomic databases

PaxDbiP05655.
PRIDEiP05655.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15450; CAB15450; BSU34450.
GeneIDi936413.
KEGGibsu:BSU34450.
PATRICi18978892. VBIBacSub10457_3609.

Phylogenomic databases

eggNOGiENOG4105EDQ. Bacteria.
ENOG410XR0E. LUCA.
HOGENOMiHOG000041220.
InParanoidiP05655.
KOiK00692.
OMAiVELNNDY.
PhylomeDBiP05655.

Enzyme and pathway databases

BioCyciBSUB:BSU34450-MONOMER.
MetaCyc:BSU34450-MONOMER.
BRENDAi2.4.1.10. 658.
SABIO-RKP05655.

Miscellaneous databases

EvolutionaryTraceiP05655.

Family and domain databases

Gene3Di2.115.10.20. 1 hit.
InterProiIPR003469. Glyco_hydro_68.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PfamiPF02435. Glyco_hydro_68. 1 hit.
[Graphical view]
SUPFAMiSSF75005. SSF75005. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSACB_BACSU
AccessioniPrimary (citable) accession number: P05655
Secondary accession number(s): P70984
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: November 2, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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.