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Protein
Submitted name:

Sucrose isomerase SmuA from Protaminobacter rubrum

Gene

smuA

Organism
Serratia plymuthica
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

BRENDAi5.4.99.11. 5041.

Names & Taxonomyi

Protein namesi
Submitted name:
Sucrose isomerase SmuA from Protaminobacter rubrumImported (EC:5.4.99.11Imported)
Gene namesi
Name:smuAImported
OrganismiSerratia plymuthicaImported
Taxonomic identifieri82996 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GBDX-ray1.95A1-558[»]
3GBEX-ray1.70A1-558[»]
ProteinModelPortaliD0VX20.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiD0VX20.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 418406AamyInterPro annotationAdd
BLAST

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR032091. Malt_amylase_C.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 3 hits.
PfamiPF00128. Alpha-amylase. 1 hit.
PF16657. Malt_amylase_C. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

D0VX20-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
TIPKWWKEAV FYQVYPRSFK DTNGDGIGDI NGIIEKLDYL KALGIDAIWI
60 70 80 90 100
NPHYDSPNTD NGYDIRDYRK IMKEYGTMED FDRLISEMKK RNMRLMIDVV
110 120 130 140 150
INHTSDQNEW FVKSKSSKDN PYRGYYFWKD AKEGQAPNNY PSFFGGSAWQ
160 170 180 190 200
KDEKTNQYYL HYFAKQQPDL NWDNPKVRQD LYAMLRFWLD KGVSGLRFDT
210 220 230 240 250
VATYSKIPDF PNLTQQQLKN FAAEYTKGPN IHRYVNEMNK EVLSHYDIAT
260 270 280 290 300
AGEIFGVPLD QSIKFFDRRR DELNIAFTFD LIRLDRDSDQ RWRRKDWKLS
310 320 330 340 350
QFRQIIDNVD RTAGEYGWNA FFLDNHDNPR AVSHFGDDRP QWREPSAKAL
360 370 380 390 400
ATLTLTQRAT PFIYQGSELG MTNYPFKAID EFDDIEVKGF WHDYVETGKV
410 420 430 440 450
KADEFLQNVR LTSRDNSRTP FQWDGSKNAG FTSGKPWFKV NPNYQEINAV
460 470 480 490 500
SQVTQPDSVF NYYRQLIKIR HDIPALTYGT YTDLDPANDS VYAYTRSLGA
510 520 530 540 550
EKYLVVVNFK EQMMRYKLPD NLSIEKVIID SNSKNVVKKN DSLLELKPWQ

SGVYKLNQ
Length:558
Mass (Da):65,604
Last modified:December 15, 2009 - v1
Checksum:iD6303B9951A6CF15
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GBDX-ray1.95A1-558[»]
3GBEX-ray1.70A1-558[»]
ProteinModelPortaliD0VX20.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi5.4.99.11. 5041.

Miscellaneous databases

EvolutionaryTraceiD0VX20.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR032091. Malt_amylase_C.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 3 hits.
PfamiPF00128. Alpha-amylase. 1 hit.
PF16657. Malt_amylase_C. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Structural determinants of product specificity of sucrose isomerases."
    Ravaud S., Robert X., Watzlawick H., Haser R., Mattes R., Aghajari N.
    FEBS Lett. 583:1964-1968(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS).

Entry informationi

Entry nameiD0VX20_SERPL
AccessioniPrimary (citable) accession number: D0VX20
Entry historyi
Integrated into UniProtKB/TrEMBL: December 15, 2009
Last sequence update: December 15, 2009
Last modified: May 11, 2016
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sourcesImported

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.