Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Gd1g8kg1 All beta proteins Double psi beta-barrel ADC-like Formate dehydrogenase/DMSO reductase, C-terminal domain Arsenite oxidase large subunit (Alcaligenes faecalis ) [TaxId: 511 ], SCOPe (2.08)
Gd1g8kg2 Alpha and beta proteins (a/b) Formate dehydrogenase/DMSO reductase, domains 1-3 Formate dehydrogenase/DMSO reductase, domains 1-3 Formate dehydrogenase/DMSO reductase, domains 1-3 Arsenite oxidase large subunit (Alcaligenes faecalis ) [TaxId: 511 ], SCOPe (2.08)
Ad1g8ka1 All beta proteins Double psi beta-barrel ADC-like Formate dehydrogenase/DMSO reductase, C-terminal domain Arsenite oxidase large subunit (Alcaligenes faecalis ) [TaxId: 511 ], SCOPe (2.08)
Ad1g8ka2 Alpha and beta proteins (a/b) Formate dehydrogenase/DMSO reductase, domains 1-3 Formate dehydrogenase/DMSO reductase, domains 1-3 Formate dehydrogenase/DMSO reductase, domains 1-3 Arsenite oxidase large subunit (Alcaligenes faecalis ) [TaxId: 511 ], SCOPe (2.08)
Cd1g8kc1 All beta proteins Double psi beta-barrel ADC-like Formate dehydrogenase/DMSO reductase, C-terminal domain Arsenite oxidase large subunit (Alcaligenes faecalis ) [TaxId: 511 ], SCOPe (2.08)
Cd1g8kc2 Alpha and beta proteins (a/b) Formate dehydrogenase/DMSO reductase, domains 1-3 Formate dehydrogenase/DMSO reductase, domains 1-3 Formate dehydrogenase/DMSO reductase, domains 1-3 Arsenite oxidase large subunit (Alcaligenes faecalis ) [TaxId: 511 ], SCOPe (2.08)
Ed1g8ke1 All beta proteins Double psi beta-barrel ADC-like Formate dehydrogenase/DMSO reductase, C-terminal domain Arsenite oxidase large subunit (Alcaligenes faecalis ) [TaxId: 511 ], SCOPe (2.08)
Ed1g8ke2 Alpha and beta proteins (a/b) Formate dehydrogenase/DMSO reductase, domains 1-3 Formate dehydrogenase/DMSO reductase, domains 1-3 Formate dehydrogenase/DMSO reductase, domains 1-3 Arsenite oxidase large subunit (Alcaligenes faecalis ) [TaxId: 511 ], SCOPe (2.08)
Bd1g8kb_ All beta proteins ISP domain ISP domain Rieske iron-sulfur protein (ISP) Arsenite oxidase Rieske subunit (Alcaligenes faecalis ) [TaxId: 511 ], SCOPe (2.08)
Dd1g8kd_ All beta proteins ISP domain ISP domain Rieske iron-sulfur protein (ISP) Arsenite oxidase Rieske subunit (Alcaligenes faecalis ) [TaxId: 511 ], SCOPe (2.08)
Fd1g8kf_ All beta proteins ISP domain ISP domain Rieske iron-sulfur protein (ISP) Arsenite oxidase Rieske subunit (Alcaligenes faecalis ) [TaxId: 511 ], SCOPe (2.08)
Hd1g8kh_ All beta proteins ISP domain ISP domain Rieske iron-sulfur protein (ISP) Arsenite oxidase Rieske subunit (Alcaligenes faecalis ) [TaxId: 511 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
GSCOP2B SuperfamilyFormate dehydrogenase/DMSO reductase, domains 1-3 8033012 3001453 SCOP2B (2022-06-29)
GSCOP2B SuperfamilyADC-like 8042518 3001132 SCOP2B (2022-06-29)
ASCOP2 FamilyFormate dehydrogenase/DMSO reductase, domains 1-3 8020632 4000801 SCOP2 (2022-06-29)
ASCOP2 FamilyFormate dehydrogenase/DMSO reductase, C-terminal domain 8030139 4002360 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyFormate dehydrogenase/DMSO reductase, domains 1-3 8033012 3001453 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyADC-like 8042518 3001132 SCOP2 (2022-06-29)
CSCOP2B SuperfamilyFormate dehydrogenase/DMSO reductase, domains 1-3 8033012 3001453 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyADC-like 8042518 3001132 SCOP2B (2022-06-29)
ESCOP2B SuperfamilyFormate dehydrogenase/DMSO reductase, domains 1-3 8033012 3001453 SCOP2B (2022-06-29)
ESCOP2B SuperfamilyADC-like 8042518 3001132 SCOP2B (2022-06-29)
BSCOP2 FamilyRieske iron-sulfur protein (ISP) 8029170 4001667 SCOP2 (2022-06-29)
BSCOP2 SuperfamilyISP domain 8041549 3000233 SCOP2 (2022-06-29)
DSCOP2B SuperfamilyISP domain 8041549 3000233 SCOP2B (2022-06-29)
FSCOP2B SuperfamilyISP domain 8041549 3000233 SCOP2B (2022-06-29)
HSCOP2B SuperfamilyISP domain 8041549 3000233 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
GMolydop_bindinge1g8kG1 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: double psiF: Molydop_bindingECOD (1.6)
GMolybdop_Fe4S4,arsenite_ox_Le1g8kG4 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: Molybdop_Fe4S4,arsenite_ox_LECOD (1.6)
GMolybdopterin_2nde1g8kG2 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)
GMolybdopterin_1st_1e1g8kG3 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)
AMolydop_bindinge1g8kA1 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: double psiF: Molydop_bindingECOD (1.6)
AMolybdop_Fe4S4,arsenite_ox_Le1g8kA2 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: Molybdop_Fe4S4,arsenite_ox_LECOD (1.6)
AMolybdopterin_2nde1g8kA3 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_1e1g8kA4 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)
CMolydop_bindinge1g8kC1 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: double psiF: Molydop_bindingECOD (1.6)
CMolybdop_Fe4S4,arsenite_ox_Le1g8kC4 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: Molybdop_Fe4S4,arsenite_ox_LECOD (1.6)
CMolybdopterin_2nde1g8kC2 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)
CMolybdopterin_1st_1e1g8kC3 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)
EMolydop_bindinge1g8kE1 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: double psiF: Molydop_bindingECOD (1.6)
EMolybdop_Fe4S4,arsenite_ox_Le1g8kE4 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: Molybdop_Fe4S4,arsenite_ox_LECOD (1.6)
EMolybdopterin_2nde1g8kE2 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)
EMolybdopterin_1st_1e1g8kE3 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)
Barsenite_ox_Se1g8kB1 A: beta sandwichesX: ISP domain (From Topology)H: ISP domain (From Topology)T: ISP domainF: arsenite_ox_SECOD (1.6)
BRieske_4e1g8kB2 A: few secondary structure elementsX: Trm112p-like (From Topology)H: Trm112p-like (From Topology)T: Trm112p-likeF: Rieske_4ECOD (1.6)
Darsenite_ox_Se1g8kD1 A: beta sandwichesX: ISP domain (From Topology)H: ISP domain (From Topology)T: ISP domainF: arsenite_ox_SECOD (1.6)
DRieske_4e1g8kD2 A: few secondary structure elementsX: Trm112p-like (From Topology)H: Trm112p-like (From Topology)T: Trm112p-likeF: Rieske_4ECOD (1.6)
Farsenite_ox_Se1g8kF1 A: beta sandwichesX: ISP domain (From Topology)H: ISP domain (From Topology)T: ISP domainF: arsenite_ox_SECOD (1.6)
FRieske_4e1g8kF2 A: few secondary structure elementsX: Trm112p-like (From Topology)H: Trm112p-like (From Topology)T: Trm112p-likeF: Rieske_4ECOD (1.6)
Harsenite_ox_Se1g8kH1 A: beta sandwichesX: ISP domain (From Topology)H: ISP domain (From Topology)T: ISP domainF: arsenite_ox_SECOD (1.6)
HRieske_4e1g8kH2 A: few secondary structure elementsX: Trm112p-like (From Topology)H: Trm112p-like (From Topology)T: Trm112p-likeF: Rieske_4ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
G3.30.200.200 Alpha Beta 2-Layer Sandwich Phosphorylase Kinase domain 1CATH (4.3.0)
G3.40.50.740 Alpha Beta 3-Layer(aba) Sandwich Rossmann fold CATH (4.3.0)
G3.40.228.10 Alpha Beta 3-Layer(aba) Sandwich Dimethylsulfoxide Reductase domain 2CATH (4.3.0)
G2.40.40.20 Mainly Beta Beta Barrel Barwin-like endoglucanases CATH (4.3.0)
A3.30.200.200 Alpha Beta 2-Layer Sandwich Phosphorylase Kinase domain 1CATH (4.3.0)
A3.40.50.740 Alpha Beta 3-Layer(aba) Sandwich Rossmann fold CATH (4.3.0)
A3.40.228.10 Alpha Beta 3-Layer(aba) Sandwich Dimethylsulfoxide Reductase domain 2CATH (4.3.0)
A2.40.40.20 Mainly Beta Beta Barrel Barwin-like endoglucanases CATH (4.3.0)
C2.60.40.4210 Mainly Beta Sandwich Immunoglobulin-like CATH (4.3.0)
C3.40.50.740 Alpha Beta 3-Layer(aba) Sandwich Rossmann fold CATH (4.3.0)
C3.40.228.10 Alpha Beta 3-Layer(aba) Sandwich Dimethylsulfoxide Reductase domain 2CATH (4.3.0)
C2.40.40.20 Mainly Beta Beta Barrel Barwin-like endoglucanases CATH (4.3.0)
E3.30.200.200 Alpha Beta 2-Layer Sandwich Phosphorylase Kinase domain 1CATH (4.3.0)
E3.40.50.740 Alpha Beta 3-Layer(aba) Sandwich Rossmann fold CATH (4.3.0)
E3.40.228.10 Alpha Beta 3-Layer(aba) Sandwich Dimethylsulfoxide Reductase domain 2CATH (4.3.0)
E2.40.40.20 Mainly Beta Beta Barrel Barwin-like endoglucanases CATH (4.3.0)
B2.102.10.10 Mainly Beta 3-layer Sandwich Rieske Iron-sulfur Protein Rieske [2Fe-2S] iron-sulphur domainCATH (4.3.0)
D2.102.10.10 Mainly Beta 3-layer Sandwich Rieske Iron-sulfur Protein Rieske [2Fe-2S] iron-sulphur domainCATH (4.3.0)
F2.102.10.10 Mainly Beta 3-layer Sandwich Rieske Iron-sulfur Protein Rieske [2Fe-2S] iron-sulphur domainCATH (4.3.0)
H2.102.10.10 Mainly Beta 3-layer Sandwich Rieske Iron-sulfur Protein Rieske [2Fe-2S] iron-sulphur domainCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, C, E, G
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
A, C, E, G
PF18465Rieske 3Fe-4S (Rieske_3)Rieske 3Fe-4SThis domain is comprised of the iron-sulphur cluster and Rieske subunit found in the large subunit of arsenite oxidase. Arsenite oxidase is a 100 kDa molybdenum- and iron-sulfur-containing protein located on the outer surface of the inner membrane of ...This domain is comprised of the iron-sulphur cluster and Rieske subunit found in the large subunit of arsenite oxidase. Arsenite oxidase is a 100 kDa molybdenum- and iron-sulfur-containing protein located on the outer surface of the inner membrane of Gram-negative organisms. The large subunit of arsenite oxidase is similar to other members of the dimethylsulfoxide (DMSO) reductase family of molybdenum enzymes. The large subunit of arsenite oxidase is divided into four domains, with domain I binding the [3Fe-4S] cluster . Domain I, consists of three antiparallel beta sheets and six helices. The [3Fe-4S] cluster is coordinated by the motif Cys21-X2-Cys24-X3-Cys28 near the interface with domains III and IV. A large, flattened funnel-like cavity bounded by domains I, II, and III leads to the molybdenum center Pfam:PF00384 located near the center of the molecule [1].
Domain
A, C, E, G
PF00384Molybdopterin oxidoreductase (Molybdopterin)Molybdopterin oxidoreductase- Family
B, D, F, H
PF00355Rieske [2Fe-2S] domain (Rieske)Rieske [2Fe-2S] domainThe rieske domain has a [2Fe-2S] centre. Two conserved cysteines coordinate one Fe ion, while the other Fe ion is coordinated by two conserved histidines. In hyperthermophilic archaea there is a SKTPCX(2-3)C motif at the C-terminus. The cysteines in ...The rieske domain has a [2Fe-2S] centre. Two conserved cysteines coordinate one Fe ion, while the other Fe ion is coordinated by two conserved histidines. In hyperthermophilic archaea there is a SKTPCX(2-3)C motif at the C-terminus. The cysteines in this motif form a disulphide bridge, which stabilises the protein [4].
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, C, E, G
ARSENITE OXIDASE
B, D, F, H
ARSENITE OXIDASE -

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

ChainsEnzyme NameDescriptionCatalytic Residues
E, F
arsenite oxidase  M-CSA #144

Arsenite oxidase oxidises arsenite (As(III)O33-)to the less toxic arsenate (As(V)O43-). The electrons produced are transferred towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin. Arsenite oxidase is a heterodimeric enzyme containing a large and a small subunit. The large catalytic subunit harbours the molybdopterin cofactor (comprising two molybdopterin guanosine dinucleotide cofactors bound to molybdenum), and a [3Fe-4S] cluster; the small subunit belongs to the structural class of the Rieske proteins and contains a Rieske-type [2Fe-2S] clusters.

Defined by 6 residues: CYS:E-24SER:E-98SER:E-99SER:E-238HIS:F-62HIS:F-81
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