Summary: L-rhamnose isomerase (RhaA)
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L-rhamnose isomerase (RhaA) Provide feedback
This family consists of several bacterial L-rhamnose isomerase proteins ( EC:184.108.40.206).
Korndorfer IP, Fessner WD, Matthews BW; , J Mol Biol 2000;300:917-933.: 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. PUBMED:10891278 EPMC:10891278
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This tab holds annotation information from the InterPro database.
InterPro entry IPR009308
This family consists of several bacterial L-rhamnose isomerase proteins (EC). This enzyme interconverts L-rhamnose and L-rhamnulose. In some species, including Escherichia coli, this is the first step in rhamnose catabolism. Sequential steps are catalyzed by rhamnulose kinase (rhaB), then rhamnulose-1-phosphate aldolase (rhaD) to yield glycerone phosphate and (S)-lactaldehyde. Bifunctional enzyme RhaA/RhaB from Bacillus clausii is also included in this entry. It contains both rhamnulokinase and L-rhamnose isomerase domains.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||L-rhamnose isomerase activity (GO:0008740)|
|manganese ion binding (GO:0030145)|
|Biological process||rhamnose metabolic process (GO:0019299)|
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This large superfamily of TIM barrel enzymes all contain a common phosphate binding site. The phosphate is found in a variety of cofactors and ligands such as FMN [1,2].
The clan contains the following 59 members:4HFCP_synth Ala_racemase_N ALAD Aldolase AP_endonuc_2 BtpA CdhD ComA CutC DAHP_synth_1 DAHP_synth_2 DeoC DHDPS DHO_dh DHquinase_I DUF2090 DUF561 DUF692 DUF993 Dus F_bP_aldolase FMN_dh G3P_antiterm Glu_syn_central Glu_synthase His_biosynth HMGL-like IGPS IMPDH KDGP_aldolase Lys-AminoMut_A MtrH NanE NAPRTase NeuB NMO OAM_alpha OMPdecase Orn_Arg_deC_N Oxidored_FMN PcrB PdxJ PRAI PRMT5_TIM Pterin_bind QRPTase_C Radical_SAM RhaA Ribul_P_3_epim SOR_SNZ Tagatose_6_P_K TAL_FSA ThiC_Rad_SAM ThiG TIM TMP-TENI Trp_syntA UvdE UxuA
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Pfam-B_10641 (release 9.0)|
|Number in seed:||5|
|Number in full:||515|
|Average length of the domain:||368.70 aa|
|Average identity of full alignment:||39 %|
|Average coverage of the sequence by the domain:||91.14 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||10|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the RhaA domain has been found. There are 28 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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