1FDO,1OGY,2NAP,1H0H,1KQF,1G8K,1Q16,1EU1,4DMR,1TMO,1VLE


Conserved Protein Domain Family
MopB_CT
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cd02775: MopB_CT 
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Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site. This hierarchy is of the conserved MopB_CT domain present in many, but not all, MopB homologs.
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Statistics
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PSSM-Id: 239176
Aligned: 389 rows
Threshold Bit Score: 41.1514
Created: 27-Jun-2005
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
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molybdopterin
Conserved site includes 10 residues -Click on image for an interactive view with Cn3D
Feature 1:molybdopterin cofactor binding site
Evidence:
  • Structure:1FDO; E. coli formate dehydrogenase H binds Mo and two molybdopterin guanine dinucleotide (MGD) units.
  • Structure:1HOH; Tungsten containing formate dehydrogenase from Desulfovibrio gigas binds W and two molybdopterin guanine dinucleotide (MGD) units.
  • Comment:defined by 3.5 Angstrom contacts
  • Comment:Molybdenum (or in some cases, tungsten) binds at the base of a funnel-shaped depression on one side of the molecule
  • Citation:PMID 9466935
  • Comment:The NADH-quinone oxidoreductase NuoG2-like protein domain (MopB_ CT_NDH-1_NuoG2-N7) is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site.
  • Comment:The putative hydrogenase-like homologs (MopB_CT_PHLH) also appear to lack the molybdopterin binding site.
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Sequence Alignment
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Format: Row Display: Color Bits: Type Selection: 
Feature 1        ## ####                                                                         
1FDO         582 EVgHYSCrsmtg-----ncaaLAALade------pgyAQINTEDAKRLGIEd------------eALVWVHSRKGkIITR 638  Escherichia coli
NP_949595    790 LHdAFTGgelsr-----asalLAARrpa-------prLLLHPDDAALHGFRd------------gAAVRVDGNPCaPVVT 845  Rhodopseudomon...
CAF23289     664 LKaVFAPalfdegirmkhdphLIQLvke-------prLRMHPNEAKKRGIMq------------gDTVRLTTNKGsLQAK 724  Parachlamydia ...
CAD77714     689 SEaLYDGrfan-------ngwLQELpqaltklvwdnaAVMSPRTAEALGIKh------------gLMVAIRRGDSsVELP 749  Rhodopirellula...
YP_145030    473 DArLFDGryre-------npyLQELprplsllvwdgaLLAGEREAEAWGLLegirarerradprrPLLRVRASGReALLP 545  Thermus thermo...
ZP_00397963  658 LGnQYQSgtqtr-----rnpaLRATl----------eLQVHPETARERSLKp------------gDLARVTTSHGtLDLP 710  Deinococcus ge...
AAV47412     592 EAdGYNTgvrs------rggeAGALv-----------ARIHPETVAEHSELvt-----------dETLTVETRRGsATVD 643  Haloarcula mar...
AAF40703     661 GVgIYHTdsivr-----rsapLQETshaa-----vpaARVNPNTLARLGLQd------------gQTAVAKQNGAsVSVA 718  Neisseria meni...
ZP_00099683  578 SPiTLNSqfyt-------idlLRRLenl-------plLLIHPDTGKQKNLAe------------gDLAKVYNEMGeLELP 631  Desulfitobacte...
ZP_00329582  548 TSaGLNSqf----------ynLGDVpe--------plALVNPRLAREQGLHs------------gSQARLYNEWGeIIIP 597  Moorella therm...

Feature 1                         #                #                     ##
1FDO         639 AQvsdr--pnkgAIYMTYqww---------igACNELVTEnlspi------tktpEYK 679  Escherichia coli
NP_949595    846 LDasv----prgTVVISAg------------sCQPRGPLRr-------------vKVE 874  Rhodopseudomonas palustris CGA009
CAF23289     725 IKwdgn--vaeqTVIIPLgfdlisa-hdldsnLINGLPIDiq-----------liESQ 768  Parachlamydia sp. UWE25
CAD77714     750 VYempgcapgviTTQIGYgrtrvgavggstemGVDPVGVNvspvr------ftdsMLY 801  Rhodopirellula baltica SH 1
YP_145030    546 LWp---------LPLLPEg------------sLVAPLSHFfh------------pEGT 570  Thermus thermophilus HB8
ZP_00397963  711 VAlnpg--lrpdTLFMPFhw----------eaSANLLTSPdrldp-----hsrmpAFK 751  Deinococcus geothermalis DSM 11300
AAV47412     644 IDrdag--vprgMVWLPIhh-----------pATNRLTLSdrdpq------sdepNFK 682  Haloarcula marismortui ATCC 43049
AAF40703     719 VKadag--lpenVVHLPLh-------------TENAALGAlmd----------tiELA 751  Neisseria meningitidis MC58
ZP_00099683  632 VSfsls--lppdIVLTYMgted------ihntLINTLLSFestdlgqifsgspgiAYN 681  Desulfitobacterium hafniense DCB-2
ZP_00329582  598 VVisel--vppqTILCHQrplp-------ggqVINDLTPPlatdmgtitssgpglAYY 646  Moorella thermoacetica ATCC 39073

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