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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei135 – 1351NucleophileBy similarity
Sitei309 – 3091Transition state stabilizerBy similarity
Active sitei401 – 4011Proton donor/acceptorBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence analysisAdd
BLAST
Propeptidei31 – 51211 PublicationPRO_0000012245Add
BLAST
Chaini52 – 584533LevansucrasePRO_0000012246Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei31 – 311Pyrrolidone carboxylic acid1 Publication
Disulfide bondi339 ↔ 3951 Publication

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Interactioni

Protein-protein interaction databases

STRINGi272568.Gdia_1531.

Structurei

Secondary structure

1
584
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi90 – 934Combined sources
Helixi95 – 995Combined sources
Helixi113 – 1153Combined sources
Beta strandi132 – 1409Combined sources
Beta strandi146 – 1494Combined sources
Beta strandi152 – 1609Combined sources
Helixi168 – 1703Combined sources
Helixi172 – 1743Combined sources
Beta strandi176 – 18510Combined sources
Helixi188 – 1903Combined sources
Beta strandi198 – 2047Combined sources
Helixi208 – 2125Combined sources
Beta strandi219 – 23214Combined sources
Beta strandi237 – 24913Combined sources
Beta strandi255 – 27218Combined sources
Beta strandi277 – 28913Combined sources
Beta strandi293 – 2964Combined sources
Turni299 – 3013Combined sources
Beta strandi308 – 3147Combined sources
Beta strandi322 – 33211Combined sources
Helixi341 – 3444Combined sources
Helixi356 – 3616Combined sources
Helixi364 – 3663Combined sources
Beta strandi369 – 37810Combined sources
Beta strandi384 – 3929Combined sources
Turni394 – 3963Combined sources
Beta strandi401 – 4088Combined sources
Beta strandi411 – 4188Combined sources
Helixi420 – 4223Combined sources
Beta strandi431 – 44313Combined sources
Beta strandi446 – 4483Combined sources
Turni449 – 4524Combined sources
Beta strandi454 – 4574Combined sources
Beta strandi462 – 4643Combined sources
Beta strandi469 – 4713Combined sources
Beta strandi474 – 4763Combined sources
Turni478 – 4814Combined sources
Beta strandi482 – 4898Combined sources
Helixi490 – 4923Combined sources
Beta strandi493 – 50311Combined sources
Beta strandi505 – 5095Combined sources
Beta strandi513 – 5186Combined sources
Beta strandi521 – 5244Combined sources
Beta strandi542 – 5454Combined sources
Helixi548 – 5514Combined sources

3D structure databases

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

Publicationsi

  1. "Molecular characterization of the levansucrase gene from the endophytic sugarcane bacterium Acetobacter diazotrophicus SRT4."
    Arrieta J., Hernandez L., Coego A., Suarez V., Balmori E., Menendez C., Petit-Glatron M.-F., Chambert R., Selman-Housein G.
    Microbiology 142:1077-1085(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 52-61.
    Strain: SRT4 / CBS 550.94.
  2. "Structural characterization of Acetobacter diazotropicus levansucrase by matrix-assisted laser desorption/ionization mass spectrometry: identification of an N-terminal blocking group and a free-thiol cysteine residue."
    Betancourt L., Takao T., Hernandez L., Padron G., Shimonishi Y.
    J. Mass Spectrom. 34:169-174(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BOND, PYROGLUTAMATE FORMATION AT GLN-31.

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 11, 2015
This is version 78 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.