| First appeared in release:||Release 3.0 (02/17/2006)|
|SwissProt: ||RHAA_ECOLI |
|TrEMBL: || |
|NCBI (GI): ||54041627 |
|Source organism:||Escherichia coli|
10 20 30 40 50 60
| | | | | |
MTTQLEQAWE LAKQRFAAVG IDVEEALRQL DRLPVSMHCW QGDDVSGFEN PEGSLTGGIQ - 60
ATGNYPGKAR NASELRADLE QAMRLIPGPK RLNLHAIYLE SDTPVSRDQI KPEHFKNWVE - 120
WAKANQLGLD FNPSCFSHPL SADGFTLSHA DDSIRQFWID HCKASRRVSA YFGEQLGTPS - 180
VMNIWIPDGM KDITVDRLAP RQRLLAALDE VISEKLNPAH HIDAVESKLF GIGAESYTVG - 240
SNEFYMGYAT SRQTALCLDA GHFHPTEVIS DKISAAMLYV PQLLLHVSRP VRWDSDHVVL - 300
LDDETQAIAS EIVRHDLFDR VHIGLDFFDA SINRIAAWVI GTRNMKKALL RALLEPTAEL - 360
RKLEAAGDYT ARLALLEEQK SLPWQAVWEM YCQRHDTPAG SEWLESVRAY EKEILSRRG
|Functional narrative |
Involved in carbohydrate degradation.
|Map of ordered and disordered regions|
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
|Name:||beta 1-alpha 1 loop|
|Location:||50 - 64|
|Modification type: ||Native |
|PDB: || |
|Structural/functional type: ||Function arises via a disorder to order transition |
|Functional classes: ||Molecular assembly |
|Functional subclasses: ||Substrate/ligand binding |
|Detection methods: |
- X-ray crystallography (298 K; citrate 0.2 M; Hepes (pH 6.4-7.4) 0.1 M; isopropanol (w/w) 10 %; PEG 8000 (22.5-30.0% (w/w)))
- Korndorfer IP, Fessner WD, Matthews BW. "The structure of rhamnose isomerase from Escherichia coli and its relation with xylose isomerase illustrates a change between inter and intra-subunit complementation during evolution." J Mol Biol. 2000; 300(4): 917-33. PubMed: 10891278
The Korndorfer et al. paper has a proline at residue 366, but SwissProt has an alanine at this position.
The Korndorfer et al. paper has an additional histidine tag on the N-terminus, which is completely disordered. The C-terminal glycine is also disordered in their experiment. These regions correspond to PDB files 1DE5 and 1DE6, but were not included as disordered regions in this DisProt entry.
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