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CATH Superfamily 2.20.28.10

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_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.
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FunFam 5684: Rubrerythrin (RR) (Rubredoxin-dependent,iron-conta...

There are 7 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.

EC Term Annotations Evidence
NADH peroxidase. [EC: 1.11.1.1]
NADH + H(2)O(2) = NAD(+) + 2 H(2)O.
  • Ferricyanide, quinones, etc., can replace H(2)O(2).
 851 A0A015S2K9 A0A015T298 A0A015TMF0 A0A015U086 A0A015VMI2 A0A015W9Q1 A0A015WB30 A0A015XAT1 A0A015YAD0 A0A015YYI8
(841 more...)
NADH:ubiquinone reductase (Na(+)-transporting). [EC: 1.6.5.8]
NADH + ubiquinone + n Na(+)(In) = NAD(+) + ubiquinol + n Na(+)(Out).
    		 38 A0A069SF42 A0A073IAZ7 A0A078T0G8 A0A0F5ISU1 A0A0J6FFQ7 A0A0J9D6M8 A0A143XNZ1 A0A173RHV3 A0A174FNQ7 A0A174PAA3
    (28 more...)
    Magnesium-protoporphyrin IX monomethyl ester (oxidative) cyclase. [EC: 1.14.13.81]
    Magnesium-protoporphyrin IX 13-monomethyl ester + 3 NADPH + 3 O(2) = 3,8- divinyl protochlorophyllide + 3 NADP(+) + 5 H(2)O.
    • The enzyme participates in the biosynthesis of chlorophyllide a in aerobic organisms.
    • The same transformation is achieved in anaerobic organisms by EC 1.21.98.3.
    • Some facultative phototrophic bacteria, such as Rubrivivax gelatinosus, possess both enzymes.
    		 13 A0A0F0CQ80 A0A0F2J0Y7 A0A0F3GJ81 J9CPY3 J9G4P3 J9G8M9 J9GFH5 J9H866 K1RBH3 K1RZB5
    (3 more...)
    Ferredoxin hydrogenase. [EC: 1.12.7.2]
    H(2) + 2 oxidized ferredoxin = 2 reduced ferredoxin + 2 H(+).
    • Can use molecular hydrogen for the reduction of a variety of substances.
    • Formerly EC 1.12.1.1, EC 1.12.7.1, EC 1.18.3.1, EC 1.18.99.1, and EC 1.98.1.1.
    		 12 A0A174C785 A0A174FNF2 A0A174FNF2 A0A174ICI0 A0A1C5NYR9 A0A1C6KGP2 A0A1M4M822 E7GMS1 F9CZJ1 F9CZJ1
    (2 more...)
    Nitrite reductase (NAD(P)H). [EC: 1.7.1.4]
    Ammonia + 3 NAD(P)(+) + 2 H(2)O = nitrite + 3 NAD(P)H.
    • The enzymes from the fungi Neurospora crassa, Emericella nidulans and Candida nitratophila and the bacterium Aliivibrio fischeri can use either NADPH or NADH as electron donor.
    • Cf. EC 1.7.1.15.
    • Formerly EC 1.6.6.4.
    		 1 A0A0G3EH55
    Phosphopyruvate hydratase. [EC: 4.2.1.11]
    2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O.
    • Also acts on 3-phospho-D-erythronate.
    		 1 A0A128EHI7
    L-aspartate oxidase. [EC: 1.4.3.16]
    L-aspartate + O(2) = iminosuccinate + H(2)O(2).
    • L-aspartate oxidase catalyzes the first step in the de novo biosynthesis of NAD(+) in some bacteria.
    • O(2) can be replaced by fumarate as electron acceptor, yielding succinate.
    • The ability of the enzyme to use both O(2) and fumarate in cofactor reoxidation enables it to function under both aerobic and anaerobic conditions.
    • Iminosuccinate can either be hydrolyzed to form oxaloacetate and NH(3) or can be used by EC 2.5.1.72 in the production of quinolinate.
    		 1 U2EG96