1FDO,1H0H,1KQF,1OGY,2NAP


Conserved Protein Domain Family
MopB_CT_Fdh-Nap-like

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cd00508: MopB_CT_Fdh-Nap-like 
Click on image for an interactive view with Cn3D
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and other related proteins. Formate dehydrogenase H is a component of the anaerobic formate hydrogen lyase complex and catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. Formate dehydrogenase N (alpha subunit) is the major electron donor to the bacterial nitrate respiratory chain and nitrate reductases, Nap and Nas, catalyze the reduction of nitrate to nitrite. This CD (MopB_CT_Fdh-Nap-like) 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: 238282
Aligned: 129 rows
Threshold Bit Score: 96.8075
Created: 6-Mar-2002
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
molybdopterin
Conserved site includes 13 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

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                #####  ####                                                             
1FDO         571 DEYPMVLSTVREV-GHYSCrsmTGNCaALAALadepgYAQINTEDAKRLGIEDEALVWVHSRKGKIITRAQVsdrp-nkg 648  Escherichia coli
BAA74791     573 EEFPFNLNTGRGTvGQWHThtrTREIqAVTNIvsqkaYVDINRKDAEKLDIKENDEVLIHSSNGHTSKFIARltdnlkek 652  Clostridium pe...
AAF74559     595 DDYPMVLNTGRVQ-HQWHTltkTGKVpALNKLep-gpYLEIHPEDAARLGVAEKDQVAVRSRRGQAVLPARIsdrv-mpg 671  Pseudomonas pu...
NP_213150    545 EEGMFILLTGRLK-NNWHTmtrTGKSpELLKGei-ppFVIMNPRDAEELGIEEGEEVILSAKGKEITRVVRFgnv--krg 620  Aquifex aeolic...
BAC70041     596 DDFPFVLNTGRVQ-HQWHTltkTGKVaKLNKLnp-gpFVEVHPRDAAALGVVDGDSVEVASRRGRAVLPAVVtdrv-qpg 672  Streptomyces a...
CAD71546     631 EDYPIVLLTGRGTvSQWHTqtrTRQSpLLRSLypnqpYVEMHPRDAAELDVEHGDLVRVRSRRGHADATACLthsv-qpg 709  Rhodopirellula...
ZP_00215255  596 DTFPIVLNTGRLQ-HQWHTmtkTGKVaMLNKLnp-rpFVELHPDDASALGIAAKDSVEIRSARGRAVLPAVVterv-qrg 672  Burkholderia c...
ZP_00265697  583 ARFPLTLITGRLR-DQWHGmsrTGTAaQLFGHvs-eaVLSLHPDELRRHRLQPGDLVNLKSRRGAVIVAVASddsv-rpg 659  Pseudomonas fl...
ZP_00149628  566 SELPISLLSGRMR-DHWHGmsrTGTVpRLFNLed-epLLAMHPCDMRHRGLESGDLAKVTNGRGEMVVRVTDrpgl-vkg 642  Dechloromonas ...
YP_157667    587 ARYPLHLTTGRLR-DQWHGmsrSGKVaRLYNHvd-eaRIEMHADDLALRGLKSGDLVHVRSRRGDVVLRAEAssei-rsg 663  Azoarcus sp. EbN1
Feature 1             #            #               ##        
1FDO         649 AIYMTYQww-----igACNELVTENLSPitktpEYKYCAVRVEP 687  Escherichia coli
BAA74791     653 TLYAPIHy-------iETNLLTPSVFDPyskepSYKTVQVNIEK 689  Clostridium perfringens
AAF74559     672 NCFAPFHwndligeqlAINAATCDAVDPlslqpAFKHCAVALER 715  Pseudomonas putida
NP_213150    621 HIFAPFGypse--ygePTNLLTSDRTDPyskepDLKYSGVDVFV 662  Aquifex aeolicus VF5
BAC70041     673 CCFAPFHwndlfgeylSINAVTSDAVDPlsfqpEFKVCAVALAR 716  Streptomyces avermitilis MA-4680
CAD71546     710 QVFMPMHy-------eCTNQLTLSHFDPhsgqpSYKDCAVRIEP 746  Rhodopirellula baltica SH 1
ZP_00215255  673 NCFAPMHwndvygddlCINAVTNDAIDPesqqpELKYCAVALRR 716  Burkholderia cepacia R18194
ZP_00265697  660 QAFLPMHwgdr-flkgGVNSLTLPAFDPlskqpELKHSGVRLEP 702  Pseudomonas fluorescens PfO-1
ZP_00149628  643 RAWMPMHwgnqfmntpGANALASDATDPyskqpELKHAAVQIVK 686  Dechloromonas aromatica RCB
YP_157667    664 QAFIAMHwggnslnsaGANALTLRDFDPyskqpELKHAAVQVEK 707  Azoarcus sp. EbN1

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