NOVELTY - An enzyme involved in energetic metabolism, is new.    USE - The enzyme, nucleic acid, vector and cell are useful for catalyzing biomass modification, producing biofuel by fermentation, and/or metabolites or energy products, processing wood, pulp, agricultural wastes, organic wastes, beverages, detergents, resins, textiles, health products and drugs (all claimed). The biofuels include bioethanol, biomethanol, biopropanol and biobutanol. The metabolites include formate, acetate, succinate, fumarate and pyruvate. The enzymes are useful in paper industry, bakery industry, and detergent industry, chemical and medical fields. The amylase is useful in medical diagnosis. The amylase is also used for selecting successful integration of reporter construct in addition to antibiotic resistance.    ADVANTAGE - The enzymes have higher catalytic activity as compared to existing enzymes. The enzymes enable production energy products and metabolites at lower cost and/or improved levels. The enzymes have improved stability and activity.    DETAILED DESCRIPTION - INDEPENDENT CLAIMS are included for the following: (1) polypeptide comprising amino acid sequence of SEQ ID NOs: 1-12, 27-41, 58, 60, 62, 64, 66, 68, 70 and 72 or its fragments comprising at least 15 contiguous residues; (2) nucleic acid encoding the above-mentioned enzyme or polypeptide; (3) vector comprising the above-mentioned nucleic acid; (4) recombinant cell comprising the above-mentioned nucleic acid or vector; (5) method for modifying biomass, involves exposing biomass to the above-mentioned enzyme, nucleic acid, vector or recombinant; (6) method for producing metabolites or bioenergy products, involves exposing carbon source to the above-mentioned enzyme, nucleic acid, vector or recombinant cell; and (7) co-culture of at least two distinct microorganisms, where at least one of the microorganism is Deinococcurs bacterium and at least one of the microorganism is prokaryotic or eukaryotic cell, preferably yeast, and at least two microorganisms are symbiotic to each other and at least one Deinococcus bacterium exhibits enzymatic activity. Sequences not defined here may be found at ftp://ftp.wipo.int/pub/published_pct_sequences/publication.