The name of this superfamily has been modified since the most recent official CATH+ release (v4_4_0). At the point of the last release, this superfamily was: waiting to be named.

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
SC:1Dihydropyrimidine dehydrogenase [NADP(+)]SC:2Formate dehydrogenase iron-sulfur subunitSC:3Formate dehydrogenase iron-sulfur subunitSC:4Photosystem I iron-sulfur center4Fe-4S ferredoxinIron hydrogenase 1Adenylylsulfate reductase subunit betaFerredoxin, 4Fe-4SSC:5Pyruvate:ferredoxin (Flavodoxin) oxidoreductaseElectron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrialSC:6Respiratory nitrate reductase beta subunitNADH-ubiquinone oxidoreductase 75 kDa subunitDimethyl sulfoxide reductase subunit BRespiratory nitrate reductase beta subunitDimethyl sulfoxide reductase subunit BRespiratory nitrate reductase beta subunitFerredoxinElectron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrialFormate dehydrogenase iron-sulfur subunitCytochrome c nitrite reductase, Fe-S proteinElectron transfer flavoprotein-ubiquinone oxidoreductaseNADH-quinone oxidoreductaseEpoxyqueuosine reductaseCytochrome c nitrite reductase, Fe-S proteinFerredoxin-type protein NapGHydrogenase 2 operon protein HybAMauM/NapG family ferredoxin-type proteinFerredoxin-type protein NapFFerredoxin-type protein NapFNitrate reductase subunit betaElectron transport protein hydNElectron transport protein hydNFormate dehydrogenase iron-sulfur subunitPutative oxidoreductaseDihydropyrimidine dehydrogenase subunit BFormate dehydrogenase, alpha subunitAnaerobic sulfite reductase subunit AsrCFerredoxin4Fe-4S dicluster domain-containing proteinEpoxyqueuosine reductaseChaperone protein DnaJElectron transporter YccMElectron transfer flavoprotein-ubiquinone oxidoreductaseCytosolic Fe-S cluster assembly factor NAR1Respiratory nitrate reductase beta subunitIon-translocating oxidoreductase complex subunit CPeriplasmic [Fe] hydrogenase large subunitFormate dehydrogenase, alpha subunitFerredoxin4Fe-4S dicluster domain-containing proteinPeriplasmic [Fe] hydrogenase large subunitPeriplasmic [Fe] hydrogenaseNADH-ubiquinone oxidoreductase-G iron-sulfur binding regionFerredoxin-type protein NapFNADP-reducing hydrogenase subunit HndCTrichloroethene reductive dehalogenase4Fe-4S dicluster domain-containing proteinFerredoxin-type protein NapFProbable ferredoxin/ferredoxin--NADP reductaseRespiratory nitrate reductase beta subunitFerredoxin-like proteinCoB--CoM heterodisulfide reductase subunit A4Fe-4S binding domain containing proteinIron-sulfur cluster-binding proteinIon-translocating oxidoreductase complex subunit BReductive dehalogenase, putativeFerredoxin IIILong irondependent hydrogenase, putativeDihydropyrimidine dehydrogenase, putativeDNA-directed RNA polymerase II subunit, putativeIron-sulfur cluster-binding proteinFerredoxin-type protein NapF2-oxoglutarate:acceptor oxidoreductaseH(2):CoB-CoM heterodisulfide,ferredoxin reductase subunit ADNA-directed RNA polymerase I-like proteinDissimilatory sulfite reductase beta subunitCoB--CoM heterodisulfide reductase iron-sulfur subunit AIndolepyruvate oxidoreductase subunit IorAABC transporter relatedPyruvate formate-lyase 3 activating enzymeAnaerobic sulfite reductase subunit CNAD-dependent dihydropyrimidine dehydrogenase subunit PreAIndolepyruvate oxidoreductase subunit IorAFormate dehydrogenase 2 subunit beta (cytochrome c-553)
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FunFam 113:

There are 0 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

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