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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 bindingi49 – 491CalciumCombined sources
Metal bindingi51 – 511CalciumCombined sources
Metal bindingi53 – 531CalciumCombined sources
Metal bindingi55 – 551Calcium; via carbonyl oxygenCombined sources
Metal bindingi57 – 571CalciumCombined sources
Binding sitei131 – 1311GlucoseCombined sources
Binding sitei191 – 1911GlucoseCombined sources
Binding sitei281 – 2811GlucoseCombined sources
Binding sitei441 – 4411GlucoseCombined 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
4GINX-ray1.90A1-584[»]
4H2CX-ray1.70A28-584[»]
4H7VX-ray1.80A/B28-584[»]
4H8HX-ray2.00A/B28-584[»]
4H8UX-ray2.00A/B28-584[»]
4H8VX-ray1.95A/B28-584[»]
4HA1X-ray2.20A/B28-584[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni88 – 914Glucose bindingCombined sources
Regioni353 – 3542Glucose 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.

M1E1F6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLMKRLFAAS LMLAFSSVSS VRAEEAVKPG APWWKSAVFY QVYPRSFKDT
60 70 80 90 100
NGDGIGDFKG LTEKLDYLKG LGIDAIWINP HYASPNTDNG YDISDYREVM
110 120 130 140 150
KEYGTMEDFD RLMAELKKRG MRLMVDVVIN HSSDQHEWFK SSRASKDNPY
160 170 180 190 200
RDYYFWRDGK DGHEPNNYPS FFGGSAWEKD PVTGQYYLHY FGRQQPDLNW
210 220 230 240 250
DTPKLREELY AMLRFWLDKG VSGMRFDTVA TYSKTPGFPD LTPEQMKNFA
260 270 280 290 300
EAYTQGPNLH RYLQEMHEKV FDHYDAVTAG EIFGAPLNQV PLFIDSRRKE
310 320 330 340 350
LDMAFTFDLI CYDRALDRWH TIPRTLADFR QTIDKVDAIA GEYGWNTFFL
360 370 380 390 400
GNHDNPRAVS HFGDDRPQWR EASAKALATV TLTQRGTPFI FQGDELGMTN
410 420 430 440 450
YPFKTLQDFD DIEVKGFFQD YVETGKATAE ELLTNVALTS RDNARTPFQW
460 470 480 490 500
DDSANAGFTT GKPWLKVNPN YTEINAAREI GDPKSVYSFY RNLISIRHET
510 520 530 540 550
PALSTGSYRD IDPSNADVYA YTRSQDGETY LVVVNFKAEP RSFTLPDGMH
560 570 580
IAETLIESSS PAAPAAGAAS LELQPWQSGI YKVK
Length:584
Mass (Da):66,739
Last modified:April 3, 2013 - v1
Checksum:iE26FB3B877608B86
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GINX-ray1.90A1-584[»]
4H2CX-ray1.70A28-584[»]
4H7VX-ray1.80A/B28-584[»]
4H8HX-ray2.00A/B28-584[»]
4H8UX-ray2.00A/B28-584[»]
4H8VX-ray1.95A/B28-584[»]
4HA1X-ray2.20A/B28-584[»]
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. "Insights into product binding in sucrose isomerases from crystal structures of MutB from Rhizobium sp."
    Lipski A., Watzlawick H., Ravaud S., Robert X., Haser R., Mattes R., Aghajari N.
    Submitted (SEP-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 28-584 IN COMPLEX WITH CALCIUM.
  2. "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(2013)
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 28-584 IN COMPLEX WITH CALCIUM.

Entry informationi

Entry nameiM1E1F6_9RHIZ
AccessioniPrimary (citable) accession number: M1E1F6
Entry historyi
Integrated into UniProtKB/TrEMBL: April 3, 2013
Last sequence update: April 3, 2013
Last modified: April 29, 2015
This is version 13 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.