1EU1,4DMR,1TMO


Conserved Protein Domain Family
MopB_CT_DMSOR-BSOR-TMAOR

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cd02793: MopB_CT_DMSOR-BSOR-TMAOR 
Click on image for an interactive view with Cn3D
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO.This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Statistics
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PSSM-Id: 239194
Aligned: 24 rows
Threshold Bit Score: 197.858
Created: 17-Jun-2005
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
molybdopterin
Conserved site includes 11 residues -Click on image for an interactive view with Cn3D
Feature 1:molybdopterin cofactor binding site
Evidence:
  • Structure:1EU1; Rhodobacter sphaeroides dimethylsulfoxide reductase (DMSOR) binds Mo and two MGD units
  • Comment:defined by 3.5 Angstrom contacts

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1             # ##  # ###                                                               
1EU1_A      635 YPLHVVASHPKsRLHSQLNg-tSLRDLyavaGHEPCLINPADAAARGIADGDVLRVFNDRGQILVGAKVSDaVMPGAIQI 713 Rhodobacter spha...
4DMR        677 YPLHIAASHPFnRLHSQLNg-tVLREGyavqGHEPCLMHPDDAAARGIADGDVVRVHNDRGQILTGVKVTDaVMKGVIQI 755 Rhodobacter caps...
1TMO        674 HPIWLQSCHPDkRLHSQMCesrEYRETyavnGREPVYISPVDAKARGIKDGDIVRVFNDRGQLLAGAVVSDnFPKGIVRI 753 Shewanella massilia
ZP_00276637 678 YPLHIDSSHPGsRLHSQLCg-tVLRGSyaikGREPCLMHPEDAKIRGIADGDIVRVFNDRGQMLVGVRLTDdIRRGVIRV 756 Ralstonia metall...
P33225      688 YPLHLQSVHPDfRLHSQLCeseTLRQQytvaGKEPVFINPQDASARGIRNGDVVRVFNARGQVLAGAVVSDrYAPGVARI 767 Escherichia coli
CAB72732    696 APFHLLTNHPRdRLHSQLCh-tSLRDTyaikDREPILINSKDAKKLGIKNGDVVRVFNKRGEVLAGAVVSDeIMQGVVRL 774 Campylobacter je...
NP_907962   703 FPLNLVSPHPKyRLHSQLNn-tWLRDLeevqGREPIWINPKDAQKRGIANGDVVRIFNKRGAILGGAVVTDyVMEGVVRM 781 Wolinella succin...
P44798      678 YPLALVTPHPYyRLHSQLAh-tSLRQKyavnDREPVMIHPEDAAARGIKDGDIVRIHSKRGQVLAGAAVTEnIIKGTVAL 756 Haemophilus infl...
ZP_00197475 623 GPLYLLTPQPQgRLHSQLDg-gVASLAektdGLERLRINTTDARALGIESGVTVLIRNDRGRCLAAADVSDdVMPGVVCL 701 Mesorhizobium sp...
NP_754178   674 KQLQLLTAHPAhRLHSQLNy-aELRKKyavaDREPITIHTEDAARFGIANGDLVRVWNKRGQILTGAVVTDgIKKGVVCV 752 Escherichia coli...
Feature 1        #                            #                ##        
1EU1_A      714 YEGGWYDPLdpse-------egtLDKYGDVNVLSLDVGTSKLaqGNCGQTILADVEK 763 Rhodobacter sphaeroides
4DMR        756 YEGGWYDPSdvte-------pgtLDKYGDVNVLSADIGTSKLaqGNCGQTVLAEVEK 805 Rhodobacter capsulatus
1TMO        754 HEGAWYGPVgkdgsteggaevgaLCSYGDPNTLTLDIGTSKLaqACSAYTCLVEFEK 810 Shewanella massilia
ZP_00276637 757 CEGGWYDPAepgk-------pgtLCRYGDVNNLTTGIGTSKLaqGNCGHTAMADVEK 806 Ralstonia metallidurans CH34
P33225      768 HEGAWYDPDkgge-------pgaLCKYGNPNVLTIDIGTSQLaqATSAHTTLVEIEK 817 Escherichia coli
CAB72732    775 CEGAWYDPNen-----------gLCKCGNANVLTMDIPTSKLanGNISHTGLVNIEK 820 Campylobacter jejuni subsp. jejuni NCTC...
NP_907962   782 QEGAWYDPVepgk-------agsLCKHGDVNVLIADIPTSELa-QGNQATALVEIEK 830 Wolinella succinogenes DSM 1740
P44798      757 HEGAWYDPMylge------sekpLCKNGCANVLTRDEGTSKLaqGNSPNTCIVQIEK 807 Haemophilus influenzae
ZP_00197475 702 PTGSRLQFAadg---------sdLEISGNPNVLTADIPASSFsqGCAAQSCRVWVER 749 Mesorhizobium sp. BNC1
NP_754178   753 HEGAWPDLEn------------gLCKNGSANVLTADIPSSQLanACAGNSALVYIEK 797 Escherichia coli CFT073

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