2IWF,3SBP,1FWX,1QNI


Conserved Protein Domain Family
N2OR_C

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cd04223: N2OR_C 
Click on image for an interactive view with Cn3D
The C-terminal cupredoxin domain of Nitrous-oxide reductase
Nitrous-oxide reductase participates in nitrogen metabolism and catalyzes the last step in dissimilatory nitrate reduction, the two-electron reduction of N2O to N2. It contains copper ions as cofactors in the form of a binuclear CuA center at the site of electron entry and a tetranuclear CuZ centre at the active site. The C-terminus of Nitrous-oxide reductase is a cupredoxin domain.
Statistics
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PSSM-Id: 259885
Aligned: 27 rows
Threshold Bit Score: 168.953
Created: 19-Jun-2012
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
CuA binucleardimer interface
Conserved site includes 5 residues -Click on image for an interactive view with Cn3D
Feature 1: CuA binuclear site [ion binding site], 5 residue positions
Conserved feature residue pattern:H C C H MClick to see conserved feature residue pattern help
Evidence:
  • Structure:2IWF; Achromobacter cycloclastes Nitrous Oxide Reductase binds to coppers at CuA site.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                        #                               
2IWF_A       545 KVRVYMTSVAPSF-------SQPSFTVKE-GDEVTVIVTNLDEiDDLTHGFTMGNHGVAMEVG--PQQTSSVTFVAANPG 614 Achromobacter c...
3SBP_A       543 KVRVYMTSMAPAF-------GVQEFTVKQ-GDEVTVTITNIDQiEDVSHGFVVVNHGVSMEIS--PQQTSSITFVADKPG 612 Pseudomonas stu...
1FWX_A       498 KVRVYMSSVAPSF-------SIESFTVKE-GDEVTVIVTNLDEiDDLTHGFTMGNYGVAMEIG--PQMTSSVTFVAANPG 567 Paracoccus deni...
1QNI_A       486 KVRVYMTSVAPQY-------GMTDFKVKE-GDEVTVYITNLDMvEDVTHGFCMVNHGVSMEIS--PQQTASVTFTAGKPG 555 Marinobacter hy...
Q59105       549 KVTVKITSQAPAF-------SLREFKLKK-GDEVTLILTNLDKiEDLTHGFAIPKYNVNFIVN--PQETASVTFVADKPG 618 Ralstonia eutro...
YP_003812963 559 KVTVRLASQAPTF-------SMTEFRVKQ-GDEVTIILTNIDTiEDLTHGFAIHRYNINFIVN--PQETKSVTFVADKPG 628 gamma proteobac...
YP_001837801 543 TTHIYMTAIRSHF-------KPDIIEART-GETLYFHVTNLEQdYDIPHGFAIGGAPNMTNLLimPGETRTFKWVAPKPG 614 Leptospira bifl...
YP_001125843 519 EVHVYGIAMRSKFifdanakRPDVIEVNE-GDKVVVHLTNLDFdEDITHGFAINQYNLNMEIQ--PGQTNTIEFTADKPG 595 Geobacillus the...
YP_002760897 557 VVHVRMAAIRSHF-------APDNIEGVQvGDTVLFHVTNLEQdWDIPHGFAIQGATTSELLVm-PGETRTLRWVPKQIG 628 Gemmatimonas au...
EDP74727     133 EVHIYMSAIRSHF-------TPDNIEGIKvGDTVYFHVTNIEQdWDIPHGFAMFGAKAPNVLIm-PGETLTIKWKPEKPG 204 Hydrogenivirga ...
Feature 1             #   #   #  #        
2IWF_A       615 VYWYYCQWFCHALHMEMRGRMFVEP 639 Achromobacter cycloclastes
3SBP_A       613 LHWYYCSWFCHALHMEMVGRMMVEP 637 Pseudomonas stutzeri
1FWX_A       568 VYWYYCQWFCHALHMEMRGRMLVEP 592 Paracoccus denitrificans
1QNI_A       556 VYWYYCNWFCHALHMEMVGRMLVEA 580 Marinobacter hydrocarbonoclasticus
Q59105       619 VFWCYCTHFCHALHLEMRTRMIVEA 643 Ralstonia eutropha H16
YP_003812963 629 VYWAYCTHFCHALHLEMRLRMIVEP 653 gamma proteobacterium HdN1
YP_001837801 615 IYPFYCTDFCSALHQEMQQYIRVSP 639 Leptospira biflexa serovar Patoc strain 'Patoc 1 (Paris)'
YP_001125843 596 TYPLYCTNFCSALHQEMTGYLLVKP 620 Geobacillus thermodenitrificans NG80-2
YP_002760897 629 VYPMYCTDFCSALHQEMSGYVRVSP 653 Gemmatimonas aurantiaca T-27
EDP74727     205 VYPFYCTDFCSALHQEMQGYVRVSP 229 Hydrogenivirga sp. 128-5-R1-1

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