1J9B,1JZW


Conserved Protein Domain Family
ArsC_ArsC
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cd03034: ArsC_ArsC 
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Arsenate Reductase (ArsC) family, ArsC subfamily; arsenic reductases similar to that encoded by arsC on the R733 plasmid of Escherichia coli. E. coli ArsC catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)], the first step in the detoxification of arsenic, using reducing equivalents derived from glutathione (GSH) via glutaredoxin (GRX). ArsC contains a single catalytic cysteine, within a thioredoxin fold, that forms a covalent thiolate-As(V) intermediate, which is reduced by GRX through a mixed GSH-arsenate intermediate. This family of predominantly bacterial enzymes is unrelated to two other families of arsenate reductases which show similarity to low-molecular-weight acid phosphatases and phosphotyrosyl phosphatases.
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Statistics
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PSSM-Id: 239332
Aligned: 43 rows
Threshold Bit Score: 131.17
Created: 2-Mar-2005
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
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catalytic
Conserved site includes 4 residues -Click on image for an interactive view with Cn3D
Feature 1:catalytic residues [active site]
Evidence:
  • Structure:1JZW; Escherichia coli ArsC binds sulfate and sulfite ions (analogs of arsenate and arsenite); contacts at 3.5A
  • Structure:1J9B; Escherichia coli ArsC binds sulfate and arsorous acid; contacts at 3.5A
  • Comment:A triad of arginines is involved in activation of the catalytic cysteine, arsenate binding and stabilization of the transition state.
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Sequence Alignment
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Format: Row Display: Color Bits: Type Selection: 
Feature 1             #                                                #                      
1J9B_A      4 ITIYHNPAXGTSRNTLEMIRnSGTEPTIILYLENPPSRDELVKLIADMgi-svRALLRKNvepYEQLGLaedKFTDDQLI 82  Escherichia coli
1JZW_A      4 ITIYHNPAXGTSRNTLEMIRnSGTEPTIILYLENPPSRDELVKLIADMgi-svRALLRKNvepYEQLGLaedKFTDDQLI 82  Escherichia coli
CAG81129   44 ITLIHNPKCSKSCAALELLEqKQISPNVVQYLDTPLSVAEISSIVRKLdm-kpVELLRKGepqFSELNLgaaNTPDAEII 122 Yarrowia lipolytic...
NP_869816   2 TKIYHNPRCTKSRQALQLLEeRGVEAEVIKYMETPPSKKELAEIVKLLgi-paEALVRKKeplFKELNLgeqTLTNQQWI 80  Rhodopirellula bal...
YP_122658   4 ITIYHNPRCSKSRQALEILQnKGFEPIIIEYLKAPLDLEQLKRLRTHLa---lEDLVRTNenvFKELGLs--LANEAQVL 78  Legionella pneumop...
AAV96149    2 IEYWHNPRCSKSRQGLALLEeRGAEIELRRYLEDAPSLEELRATQAALgv-saIAMMRTGearFKELGLs-kSDPDAVLL 79  Silicibacter pomer...
AAQ58446    2 IRLYHNPKCSKSRAALSLLEeAGAEIEIVEYLKHPPSYEELDQLLGLLgl-epRELMRQKeeeYADLYLddiTLERKHLI 80  Chromobacterium vi...
P63622      4 IKIFHNPRCSKSRAALSLLEeRGIAAEVVKYLDTPPDLSELKDIFNKLglasaRGMMRVKddlYKELGLdnpNLDNDALL 83  Neisseria meningit...
P44589      3 VIIYHNPHCSKSRETLALLEnKGIQPIIELYLQKQYSVNELQSIAKKLgiddvRQMMRTKdelYKSLNLdnlDLSQAELF 82  Haemophilus influe...
NP_841710   5 ITIYQKPTCSKCREALSILKeSGREFDSINYYDDRLTVEVLRELVRKLgi-svRDLLRADe--PLARGTe--SVDDDELL 79  Nitrosomonas europ...

Feature 1                #            #        
1J9B_A     83 DFMLQHPILINRPIVVTPlGTRLCRpSEVVLDI 115 Escherichia coli
1JZW_A     83 DFMLQHPILINRPIVVTPlGTRLCRpSEVVLDI 115 Escherichia coli
CAG81129  123 DAMAKHPNLIERPILIVDdKAVIGRpTEKLNDL 155 Yarrowia lipolytica CLIB99
NP_869816  81 ATMVEHPKLIERPIVIHEgKAAIGRpTEKIAEI 113 Rhodopirellula baltica SH 1
YP_122658  79 EAMVKEPILMQRPIVTFKgKAAIGRpPEKILEL 111 Legionella pneumophila str. Paris
AAV96149   80 AAMAESPVLIERPLAIKGdRAVIGRpPEDMLSL 112 Silicibacter pomeroyi DSS-3
AAQ58446   81 AAMVDNPNLIERPIAIADgRAVIGRpPERVLNL 113 Chromobacterium violaceum ATCC 12472
P63622     84 RAIADHPALLERPIVLANgKAAVGRpLENIEAV 116 Neisseria meningitidis serogroup B
P44589     83 KAISEHSALIERPIVINGdKAKIGRpPETVLEI 115 Haemophilus influenzae
NP_841710  80 RLMAANPDLIQRPIVVRGdSAVLGRpPERIKKL 112 Nitrosomonas europaea ATCC 19718

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