Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Levansucrase

Gene

lsdA

Organism
Gluconacetobacter diazotrophicus (Acetobacter diazotrophicus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Releases fructooligosaccharides and levan, a high-molecular-mass fructosyl polymer, from sucrose. It acts more as a sucrose hydrolase than as a fructan polymerase.

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
Active sitei135NucleophileBy similarity1
Sitei309Transition state stabilizerBy similarity1
Active sitei401Proton donor/acceptorBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.4.1.10. 2464.
3.2.1.65. 2464.
SABIO-RKQ43998.

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:lsdA
OrganismiGluconacetobacter diazotrophicus (Acetobacter diazotrophicus)
Taxonomic identifieri33996 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGluconacetobacter

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30Sequence analysisAdd BLAST30
PropeptideiPRO_000001224531 – 511 PublicationAdd BLAST21
ChainiPRO_000001224652 – 584LevansucraseAdd BLAST533

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei31Pyrrolidone carboxylic acid1 Publication1
Disulfide bondi339 ↔ 3951 Publication

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Interactioni

Protein-protein interaction databases

STRINGi272568.Gdia_1531.

Structurei

Secondary structure

1584
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi90 – 93Combined sources4
Helixi95 – 99Combined sources5
Helixi113 – 115Combined sources3
Beta strandi132 – 140Combined sources9
Beta strandi146 – 149Combined sources4
Beta strandi152 – 160Combined sources9
Helixi168 – 170Combined sources3
Helixi172 – 174Combined sources3
Beta strandi176 – 185Combined sources10
Helixi188 – 190Combined sources3
Beta strandi198 – 204Combined sources7
Helixi208 – 212Combined sources5
Beta strandi219 – 232Combined sources14
Beta strandi237 – 249Combined sources13
Beta strandi255 – 272Combined sources18
Beta strandi277 – 289Combined sources13
Beta strandi293 – 296Combined sources4
Turni299 – 301Combined sources3
Beta strandi308 – 314Combined sources7
Beta strandi322 – 332Combined sources11
Helixi341 – 344Combined sources4
Helixi356 – 361Combined sources6
Helixi364 – 366Combined sources3
Beta strandi369 – 378Combined sources10
Beta strandi384 – 392Combined sources9
Turni394 – 396Combined sources3
Beta strandi401 – 408Combined sources8
Beta strandi411 – 418Combined sources8
Helixi420 – 422Combined sources3
Beta strandi431 – 443Combined sources13
Beta strandi446 – 448Combined sources3
Turni449 – 452Combined sources4
Beta strandi454 – 457Combined sources4
Beta strandi462 – 464Combined sources3
Beta strandi469 – 471Combined sources3
Beta strandi474 – 476Combined sources3
Turni478 – 481Combined sources4
Beta strandi482 – 489Combined sources8
Helixi490 – 492Combined sources3
Beta strandi493 – 503Combined sources11
Beta strandi505 – 509Combined sources5
Beta strandi513 – 518Combined sources6
Beta strandi521 – 524Combined sources4
Beta strandi542 – 545Combined sources4
Helixi548 – 551Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W18X-ray2.50A/B62-554[»]
ProteinModelPortaliQ43998.
SMRiQ43998.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ43998.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 68 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105EDQ. Bacteria.
ENOG410XR0E. LUCA.

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.

Q43998-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAHVRRKVAT LNMALAGSLL MVLGAQSALA QGNFSRQEAA RMAHRPGVMP
60 70 80 90 100
RGGPLFPGRS LAGVPGFPLP SIHTQQAYDP QSDFTARWTR ADALQIKAHS
110 120 130 140 150
DATVAAGQNS LPAQLTMPNI PADFPVINPD VWVWDTWTLI DKHADQFSYN
160 170 180 190 200
GWEVIFCLTA DPNAGYGFDD RHVHARIGFF YRRAGIPASR RPVNGGWTYG
210 220 230 240 250
GHLFPDGASA QVYAGQTYTN QAEWSGSSRL MQIHGNTVSV FYTDVAFNRD
260 270 280 290 300
ANANNITPPQ AIITQTLGRI HADFNHVWFT GFTAHTPLLQ PDGVLYQNGA
310 320 330 340 350
QNEFFNFRDP FTFEDPKHPG VNYMVFEGNT AGQRGVANCT EADLGFRPND
360 370 380 390 400
PNAETLQEVL DSGAYYQKAN IGLAIATDST LSKWKFLSPL ISANCVNDQT
410 420 430 440 450
ERPQVYLHNG KYYIFTISHR TTFAAGVDGP DGVYGFVGDG IRSDFQPMNY
460 470 480 490 500
GSGLTMGNPT DLNTAAGTDF DPSPDQNPRA FQSYSHYVMP GGLVESFIDT
510 520 530 540 550
VENRRGGTLA PTVRVRIAQN ASAVDLRYGN GGLGGYGDIP ANRADVNIAG
560 570 580
FIQDLFGQPT SGLAAQASTN NAQVLAQVRQ FLNQ
Length:584
Mass (Da):63,526
Last modified:November 1, 1996 - v1
Checksum:iCBFBF4139AD0B8CE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L41732 Genomic DNA. Translation: AAB36606.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L41732 Genomic DNA. Translation: AAB36606.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W18X-ray2.50A/B62-554[»]
ProteinModelPortaliQ43998.
SMRiQ43998.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272568.Gdia_1531.

Protein family/group databases

CAZyiGH68. Glycoside Hydrolase Family 68.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105EDQ. Bacteria.
ENOG410XR0E. LUCA.

Enzyme and pathway databases

BRENDAi2.4.1.10. 2464.
3.2.1.65. 2464.
SABIO-RKQ43998.

Miscellaneous databases

EvolutionaryTraceiQ43998.

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_GLUDI
AccessioniPrimary (citable) accession number: Q43998
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 80 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, Direct protein sequencing

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

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.