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Protein
Submitted name:

Sucrose isomerase

Gene

mutB

Organism
Rhizobium sp. MX-45
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi22 – 221CalciumCombined sources
Metal bindingi24 – 241CalciumCombined sources
Metal bindingi26 – 261CalciumCombined sources
Metal bindingi28 – 281Calcium; via carbonyl oxygenCombined sources
Metal bindingi30 – 301CalciumCombined sources
Binding sitei144 – 1441GlucoseCombined sources
Binding sitei284 – 2841GlucoseCombined sources
Binding sitei327 – 3271GlucoseCombined sources
Binding sitei386 – 3861GlucoseCombined sources

GO - Molecular functioni

  1. catalytic activity Source: InterPro
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Ligandi

CalciumCombined sources, Metal-bindingCombined sources

Enzyme and pathway databases

BRENDAi5.4.99.11. 5351.

Names & Taxonomyi

Protein namesi
Submitted name:
Sucrose isomeraseImported (EC:5.4.11.99Imported)
Gene namesi
Name:mutBImported
OrganismiRhizobium sp. MX-45Imported
Taxonomic identifieri1071045 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GI6X-ray2.15A/B1-557[»]
4GI8X-ray1.95A/B1-557[»]
4GI9X-ray2.15A/B1-557[»]
4GIAX-ray2.01A/B1-557[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni254 – 2563Glucose bindingCombined sources

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR022567. DUF3459.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF11941. DUF3459. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

M1E1F3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
KPGAPWWKSA VFYQVYPRSF KDTNGDGIGD FKGLTEKLDY LKGLGIDAIW
60 70 80 90 100
INPHYASPNT DNGYDISDYR EVMKEYGTME DFDRLMAELK KRGMRLMVDV
110 120 130 140 150
VINHSSDQHE WFKSSRASKD NPYRDYYFWR DGKDGHEPNN YPSFFGGSAW
160 170 180 190 200
EKDPVTGQYY LHYLGRQQPD LNWDTPKLRE ELYAMLRFWL DKGVSGMRFD
210 220 230 240 250
TVATYSKTPG FPDLTPEQMK NFAEAYTQGP NLHRYLQEMH EKVFDHYDAV
260 270 280 290 300
TAGEIFGAPL NQVPLFIDSR RKELDMAFTF DLIRYDRALD RWHTIPRTLA
310 320 330 340 350
DFRQTIDKVD AIAGEYGWNT FFLGNHDNPR AVSHFGDDRP QWREASAKAL
360 370 380 390 400
ATVTLTQRGT PFIFQGDELG MTNYPFKTLQ DFDDIEVKGF FQDYVETGKA
410 420 430 440 450
TAEELLTNVA LTSRDNARTP FQWDDSANAG FTTGKPWLKV NPNYTEINAA
460 470 480 490 500
REIGDPKSVY SFYRNLISIR HETPALSTGS YRDIDPSNAD VYAYTRSQDG
510 520 530 540 550
ETYLVVVNFK AEPRSFTLPD GMHIAETLIE SSSPAAPAAG AASLELQPWQ

SGIYKVK
Length:557
Mass (Da):63,830
Last modified:April 3, 2013 - v1
Checksum:i536AFD407111E3E4
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GI6X-ray2.15A/B1-557[»]
4GI8X-ray1.95A/B1-557[»]
4GI9X-ray2.15A/B1-557[»]
4GIAX-ray2.01A/B1-557[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi5.4.99.11. 5351.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR022567. DUF3459.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF11941. DUF3459. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Mutations inducing an active-site aperture in Rhizobium sp. sucrose isomerase confer hydrolytic activity."
    Lipski A., Watzlawick H., Ravaud S., Robert X., Rhimi M., Haser R., Mattes R., Aghajari N.
    Acta Crystallogr. D 69:298-307(2012)
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH CALCIUM AND GLUCOSE.

Entry informationi

Entry nameiM1E1F3_9RHIZ
AccessioniPrimary (citable) accession number: M1E1F3
Entry historyi
Integrated into UniProtKB/TrEMBL: April 3, 2013
Last sequence update: April 3, 2013
Last modified: April 1, 2015
This is version 12 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

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 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.