| General information | | DisProt: | DP00429 | | Name: | L-rhamnose isomerase | | Synonym(s): | RHAA_ECOLI
EC 5.3.1.14
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | P32170 | | UniGene: | | | SwissProt: | RHAA_ECOLI | | TrEMBL: | | | NCBI (GI): | 54041627 | | Source organism: | Escherichia coli | | Sequence length: | 419 | | Percent disordered: | 4% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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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
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| Functional narrative |
Involved in carbohydrate degradation.
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| 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.
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| Region 1 | | Type: | Disordered | | Name: | beta 1-alpha 1 loop | | Location: | 50 - 64 | | Length: | 15 | | Region sequence: |
NPEGSLTGGIQATGN | | 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)))
| References:
- 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
| Comments:
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| Comments |
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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