Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
CSCOP2 FamilyRespiratory nitrate reductase 1 gamma chain 8027146 4001750 SCOP2 (2022-06-29)
CSCOP2 SuperfamilyRespiratory nitrate reductase 1 gamma chain 8039525 3000332 SCOP2 (2022-06-29)
ASCOP2B SuperfamilyADC-like 8034109 3001132 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyFormate dehydrogenase/DMSO reductase, domains 1-3 8034108 3001453 SCOP2B (2022-06-29)
BSCOP2B Superfamily4Fe-4S ferredoxins 8034110 3000020 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
CNitrate_red_game1q16C1 A: alpha bundlesX: Transmembrane heme-binding four-helical bundle (From Homology)H: Transmembrane heme-binding four-helical bundleT: Respiratory nitrate reductase 1 gamma chainF: Nitrate_red_gamECOD (1.6)
AMolydop_bindinge1q16A1 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: double psiF: Molydop_bindingECOD (1.6)
ANarGe1q16A3 A: a+b two layersX: Formate dehydrogenase/DMSO reductase, domain 1 (From Topology)H: Formate dehydrogenase/DMSO reductase, domain 1 (From Topology)T: Formate dehydrogenase/DMSO reductase, domain 1F: NarGECOD (1.6)
AMolybdopterin_2nde1q16A4 A: a/b three-layered sandwichesX: Rossmann-likeH: Formate dehydrogenase/DMSO reductase, domains 2 and 3 (From Topology)T: Formate dehydrogenase/DMSO reductase, domains 2 and 3F: Molybdopterin_2ndECOD (1.6)
AMolybdopterin_1st_1e1q16A2 A: a/b three-layered sandwichesX: Rossmann-likeH: Formate dehydrogenase/DMSO reductase, domains 2 and 3 (From Topology)T: Formate dehydrogenase/DMSO reductase, domains 2 and 3F: Molybdopterin_1st_1ECOD (1.6)
BFer4_11e1q16B2 A: a+b two layersX: 4Fe-4S ferredoxin (From Topology)H: 4Fe-4S ferredoxin (From Topology)T: 4Fe-4S ferredoxinF: Fer4_11ECOD (1.6)
BNitr_red_bet_C_1e1q16B1 A: a+b two layersX: 4Fe-4S ferredoxin (From Topology)H: 4Fe-4S ferredoxin (From Topology)T: 4Fe-4S ferredoxinF: Nitr_red_bet_C_1ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF02665Nitrate reductase gamma subunit (Nitrate_red_gam)Nitrate reductase gamma subunit- Family
PF01568Molydopterin dinucleotide binding domain (Molydop_binding)Molydopterin dinucleotide binding domainThis domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entir ...This domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entire subunit. The formylmethanofuran dehydrogenase catalyses the first step in methane formation from CO2 in methanogenic archaea and has a molybdopterin dinucleotide cofactor [1]. This domain corresponds to the C-terminal domain IV in dimethyl sulfoxide (DMSO)reductase which interacts with the 2-amino pyrimidone ring of both molybdopterin guanine dinucleotide molecules [2].
Domain
PF00384Molybdopterin oxidoreductase (Molybdopterin)Molybdopterin oxidoreductase- Family
PF14710Respiratory nitrate reductase alpha N-terminal (Nitr_red_alph_N)Respiratory nitrate reductase alpha N-terminalThis is the N-terminal tail of the respiratory nitrate reductase alpha chain. The nitrate reductase complex is a dimer of heterotrimers each consisting of an alpha, beta and gamma chain. The N-terminal tail of the alpha chain interacts with the beta ...This is the N-terminal tail of the respiratory nitrate reductase alpha chain. The nitrate reductase complex is a dimer of heterotrimers each consisting of an alpha, beta and gamma chain. The N-terminal tail of the alpha chain interacts with the beta chain and contributes to the stability of the heterotrimer [1].
Domain
PF132474Fe-4S dicluster domain (Fer4_11)4Fe-4S dicluster domainSuperfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contai ...Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Domain
PF14711Respiratory nitrate reductase beta C-terminal (Nitr_red_bet_C)Respiratory nitrate reductase beta C-terminalThis domain occurs near the C-terminus of the respiratory nitrate reductase beta chain. The nitrate reductase complex is a dimer of heterotrimers each consisting of an alpha, beta and gamma chain. This domain plays a role in the interactions between ...This domain occurs near the C-terminus of the respiratory nitrate reductase beta chain. The nitrate reductase complex is a dimer of heterotrimers each consisting of an alpha, beta and gamma chain. This domain plays a role in the interactions between subunits and shielding of the Fe-S clusters [1]
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
Respiratory nitrate reductase 1 gamma chain
Respiratory nitrate reductase 1 alpha chain
Respiratory nitrate reductase 1 beta chain

Membrane Protein Annotation: PDBTM PDBTM Database Homepage

Membrane Protein Annotation: MemProtMD MemProtMD Database Homepage

Membrane Protein Annotation: mpstruc mpstruc Database Homepage

Protein Modification Annotation

Modified Residue(s)
ChainResidue(s)Description
FME Parent Component: MET

RESIDAA0021 , AA0566

PSI-MOD :  N-formyl-L-methionine residue MOD:00030 , N-formyl-L-methionine (Met) MOD:00482 , N-[(L-histidin-1'-yl)methyl]-L-methionine (fMet) MOD:01890 , N-[(L-histidin-1'-yl)methyl]-L-methionine (Met) MOD:01891