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1YAF

Structure of TenA from Bacillus subtilis

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0006772biological_processthiamine metabolic process
A0006790biological_processsulfur compound metabolic process
A0009228biological_processthiamine biosynthetic process
A0009229biological_processthiamine diphosphate biosynthetic process
A0016787molecular_functionhydrolase activity
A0044281biological_processsmall molecule metabolic process
A0050334molecular_functionthiaminase activity
B0005829cellular_componentcytosol
B0006772biological_processthiamine metabolic process
B0006790biological_processsulfur compound metabolic process
B0009228biological_processthiamine biosynthetic process
B0009229biological_processthiamine diphosphate biosynthetic process
B0016787molecular_functionhydrolase activity
B0044281biological_processsmall molecule metabolic process
B0050334molecular_functionthiaminase activity
C0005829cellular_componentcytosol
C0006772biological_processthiamine metabolic process
C0006790biological_processsulfur compound metabolic process
C0009228biological_processthiamine biosynthetic process
C0009229biological_processthiamine diphosphate biosynthetic process
C0016787molecular_functionhydrolase activity
C0044281biological_processsmall molecule metabolic process
C0050334molecular_functionthiaminase activity
D0005829cellular_componentcytosol
D0006772biological_processthiamine metabolic process
D0006790biological_processsulfur compound metabolic process
D0009228biological_processthiamine biosynthetic process
D0009229biological_processthiamine diphosphate biosynthetic process
D0016787molecular_functionhydrolase activity
D0044281biological_processsmall molecule metabolic process
D0050334molecular_functionthiaminase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000303|PubMed:18054064
ChainResidueDetails
ACYS135
BCYS135
CCYS135
DCYS135

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000303|PubMed:18054064
ChainResidueDetails
AGLU205
BGLU205
CGLU205
DGLU205

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:15709744, ECO:0000269|Ref.5
ChainResidueDetails
AASP44
DASP44
DTYR139
DTYR163
ATYR139
ATYR163
BASP44
BTYR139
BTYR163
CASP44
CTYR139
CTYR163

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Increases nucleophilicity of active site Cys => ECO:0000303|PubMed:18054064
ChainResidueDetails
ATYR47
BTYR47
CTYR47
DTYR47

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PDB entries from 2024-07-17

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