Summary: Ethanolamine utilisation protein EutN/carboxysome
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Ethanolamine utilisation protein EutN/carboxysome Provide feedback
The crystal structure of EutN contains a central five-stranded beta-barrel, with an alpha-helix at the open end of this barrel ( PDB:2HD3). The structure also contains three additional beta-strands, which help the formation of a tight hexamer, with a hole in the center. this suggests that EutN forms a pore, with an opening of 26 Angstrom in diameter on one face and 14 Angstrom on the other face . EutN is involved in the cobalamin-dependent degradation of ethanolamine .
Kofoid E, Rappleye C, Stojiljkovic I, Roth J; , J Bacteriol 1999;181:5317-5329.: The 17-gene ethanolamine (eut) operon of Salmonella typhimurium encodes five homologues of carboxysome shell proteins. PUBMED:10464203 EPMC:10464203
Forouhar F, Kuzin A, Seetharaman J, Lee I, Zhou W, Abashidze M, Chen Y, Yong W, Janjua H, Fang Y, Wang D, Cunningham K, Xiao R, Acton TB, Pichersky E, Klessig DF, Porter CW, Montelione GT, Tong L;, J Struct Funct Genomics. 2007;8:37-44.: Functional insights from structural genomics. PUBMED:17588214 EPMC:17588214
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR004992
The ethanolamine utilization protein EutN is involved in the cobalamin-dependent degradation of ethanolamine [PUBMED:10464203]. The crystal structure of EutN contains a central five-stranded beta-barrel, with an alpha-helix at the open end of this barrel (PDB: 2HD3). The structure also contains three additional beta-strands, which help the formation of a tight hexamer, with a hole in the centre. This suggests that EutN forms a pore, with an opening of 26 Amstrong in diameter on one face and 14 Amstrong on the other face [PUBMED:17588214].
This entry represents a family of related bacterial proteins with roles in ethanolamine and carbon dioxide metabolism.
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The OB (oligonucleotide/oligosaccharide binding) was defined by Murzin . The common part of the OB-fold, has a five-stranded beta-sheet coiled to form a closed beta-barrel. This barrel is capped by an alpha-helix located between the third and fourth strands .
The clan contains the following 45 members:BOF CSD DNA_ligase_OB DUF2110 DUF223 DUF3127 DUF35 EFP eIF-1a eIF-5a EutN_CcmL EXOSC1 mRNA_cap_C OB_NTP_bind OB_RNB OmdA Phage_DNA_bind POT1 RecO_N RecO_N_2 Rep-A_N Rep_fac-A_3 Rho_RNA_bind Ribosom_S12_S23 Ribosomal_L2 Ribosomal_S17 RNA_pol_Rbc25 RNA_pol_Rpb8 RuvA_N S1 S1-like S1_2 SSB Stn1 TEBP_beta Ten1 Ten1_2 TOBE TOBE_2 TOBE_3 TRAM tRNA_anti-codon tRNA_anti-like tRNA_anti_2 tRNA_bind
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Curation and family details
|Seed source:||Pfam-B_3053 (release 6.5)|
|Number in seed:||51|
|Number in full:||1340|
|Average length of the domain:||82.50 aa|
|Average identity of full alignment:||46 %|
|Average coverage of the sequence by the domain:||89.31 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||8|
|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 EutN_CcmL domain has been found. There are 33 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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