1LXN,1LXJ,1YQH,2EKY,1VK8


Conserved Protein Domain Family
Thiamine_BP

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pfam01910: Thiamine_BP 
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Thiamine-binding protein
The crystal structure of two of these members shows that this domain has a ferredoxin like fold and is likely to exists as at least homodimers. Sulphate ions are are located at the dimer interfaces, which are thought to confer additional stability. Although the function of this domain remains to be identified, its structure suggests a role in protein-protein interactions possibly regulated by the binding of small-molecule ligands. Solution of the structure of the hyperthermophilic anaerobic Thermotoga maritima sequence, UniProtKB:Q9WYV6, shows that this has a beta-alpha-beta-beta-alpha-beta ferredoxin-like fold and assembles as a homotetramer. It was possible to identify a pocket in each monmer that bound an unidentified ligand. It was also found that it bound charged thiamine though not hydroxymethyl pyrimidine. It is proposed that it is transporting charged thiamine around the cytoplasm. Under oxidative conditions this bacterium is under stress, and the transcriiptional unit within which this protein is expressed is up-regulated in these conditions, suggesting that the chelation of cytoplasmic thaimine is part of the response mechanism to such oxidatvie stress, which is mediated by this family.
Statistics
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Aligned: 93 rows
Threshold Bit Score: 72.5432
Threshold Setting Gi: 499643393
Created: 30-Apr-2019
Updated: 18-Jul-2019
Structure
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Program:
Drawing:
Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
1LXN_A          4 AELTVIPLGTC-STSLSSYVAAAVEALKKLNVRYEISGXGTLLEAEdLDELXEAVKAAHEAVLQAGSDRVYTTLKIDDRR 82  Methanothermob...
Q9WYV6          6 VSIKVVPA-VE-DGRLHEVIDRAIEKISSWGMKYEVGPSNTTVEGE-FEEIMDRVKELARYLEQF-AKRFVLQLDIDYKA 81  Thermotoga mar...
jgi:Caur_0427   6 VSFEVLPGGLPdKATTYAAVDAAIAVVAASGLTYRVCPMETTIEGD-YDAIMAVIKQAQEAVLAAGASRVFTLIKVDYDP 84  Chloroflexus a...
Q5E4V9         13 VAFQVIPR-LK-EGNNFEVVDKAIEVVKAANVPYQVGAMETTMKGE-LNYLLEVVKKAQQACYDAGALEVITNIKIHSKT 89  Aliivibrio fis...
Q5WKH7          6 AGIQLIPN-GK-EDHTGGIANKVIDVIEQSGLRHRVGPLETVVEGD-FDSLMALLRDVHQQAVQAGAEEVLTNVKMHYRT 82  Bacillus claus...
Q81Z92          7 MSFSVVPQAK--TKDVYSVVDKAIEVVQQSGVRYEVGAMETTLEGE-LDVLLDVVKRAQQACVDAGAEEVITSIKIHYRP 83  Bacillus anthr...
jgi:Dred_3206   6 VGFQVLPK-TK-GDNSYQIVDKAIEVVQKSGVKYEVGPMETVMEGE-LDVLIDIVKRAQEACITAGASEVMTYIKIHYRP 82  Desulfotomacul...
Q97J88          7 VSLQVLPV-VE-EKRLYEVVDKVIEYIKASGVKYIIGPMETTMEGD-LDTLLEIVKKAQEICVKEGSERVASVVKIDYKA 83  Clostridium ac...
Q8R9M3          6 LSLQVLPL-VP-EEKVYPIVDKVIKYIKSTGVNFMVGPMETTMEGE-LDILLDIVKKAQKICEEEGANRVISIIKLDYRS 82  Caldanaerobact...
1YQH_A         10 xSFSVVPQAK--TKDVYSVVDKAIEVVQQSGVRYEVGAXETTLEGE-LDVLLDVVKRAQQACVDAGAEEVITSIKIHYRP 86  Bacillus cereu...
1LXN_A         83 D-ADRGLRDKVESVK 96  Methanothermobacter thermautotrophicus
Q9WYV6         82 G-G-ITIEEKVSKYR 94  Thermotoga maritima
jgi:Caur_0427  85 N-G-SSIAEKLAKYE 97  Chloroflexus aurantiacus J-10-fl
Q5E4V9         90 EaA----TDTFCTYD 100 Aliivibrio fischeri ES114
Q5WKH7         83 S-G-VSLEDK----Q 91  Bacillus clausii KSM-K16
Q81Z92         84 S-TGVTIDEKVWKYr 97  Bacillus anthracis
jgi:Dred_3206  83 E-G-VTLDEKIAKYR 95  Desulfotomaculum reducens MI-1
Q97J88         84 E-G-VTMNEKVGKYK 96  Clostridium acetobutylicum
Q8R9M3         83 S-G-VTMEEKIKNYI 95  Caldanaerobacter subterraneus subsp. tengcongensis
1YQH_A         87 S-TGVTIDEKVWKYR 100 Bacillus cereus ATCC 14579
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