Additional references for data included in Tables 3 The references for each subfamily are numbered inside the supplementary Tables S2a S2f, and listed a icon

Additional references for data included in Tables 3 The references for each subfamily are numbered inside the supplementary Tables S2a S2f, and listed a


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1Supplementary materials

Additional references for data included in Tables 3 - 8. The references for each subfamily are numbered inside the supplementary Tables S2a - S2f, and listed at the end of the Table S2f.


Table S2a. Main subfamilies that conform PDH family (COG1063) of MDR.

Subfamily







DHSO (sorbitol dehydrogenase)

Ref: [155-157]

BDH (2,3-butanediol dehydrogenase)

Ref: [158-160]

^ TDH (threonine dehydrogenase)

Ref: [161-164]

BCHC (2-desacetyl-2-hydroxyethyl bacteriochlorophyllide a dehydrogenase)

Ref: [165;166]

^ SORE (L-sorbose-1-phosphate reductase)

Ref: [167-171]

Secondary ADH

Ref: [172-177]

^ GATD (galactitol 1-phosphate dehydrogenase)

Ref: [178-180]

SSP and related (sensing starvation protein)

Ref: [181;182]

^ FDEH (5-exo-hydroxycamphor dehydrogenase)

Ref: [183;184]

BDOR (bi-domain oxidoreductase)

Ref: [185]

^ Archaea GDH (glucose dehydrogenase)

Ref:[186-189]

FADH (formaldehyde dehydrogenase-independent of cofactor-/formaldehyde dismutase)

Ref: [190-196]

References are listed at the end of suplementary material.




Table S2b. Main subfamilies that conform ADH family (COG1062) of MDR.

Subfamily







^ Aryl/Alkyl ADH: Firmicutes

Ref: [197;198]

Benzyl ADH

Ref: Acinetobacter calcoaceticus [199-201]; Acinetobacter sp. [202;203]; Pseudomonas putida [204-206]; Pseudomonas sp.[207;208]; Sphingomonas aromaticivorans [209]; Rhizobium tropici [210]

HNL (Hydroxynitrile lyase: acetone cyanohydrin lyase)

Ref: [211-214]

^ FADH: mycothiol-dependent (formaldehyde dehydrogenase dependent of mycothiol)

Ref: [215-217]

Class III ADH (formaldehyde dehydrogenase dependent of glutathion)

Ref: [218-238]

^ Animal ADH

Ref: Homo sapiens: ADHA_HUMAN [239-242], ADHB_HUMAN [239;243-254], ADHG_HUMAN [239;255;256], ADHP_HUMAN [257;258], ADH6_HUMAN [259], ADH7_HUMAN [260-267]; Papio hamadryas [268-273]; Macaca mulatta [274;275], Equus caballus: ADHE_HORSE [276-280], ADHS_HORSE [277-280]; Oryctolagus cuniculus [281-284]; Mus musculus: ADH7_MOUSE [285;286], ADHA_MOUSE [285;287-290]; Peromyscus maniculatus [291]; Rattus norvegicus: ADHA_RAT [292;293]; ADH7_RAT [294]; ADH2t_RAT_CAA62241 [295]; Geomys [296;297]; Gallus gallus [298;299]; Coturnix coturnix japonica [300;301]; Anas platyrhynchos [302]; Apterix australis [303]; Struthio camelus [304;305]; Alligator mississippiensis [306]; Uromastix hardwickii [307;308]; Naja naja [309]; Rana perezi [310-312]; Xenopus laevis [313]; Gadus callarias [314;315]

Plant ADH

Ref: ^ Pinus banksiana [316]; Washingtonia robusta [317]; Calamus usitatus and Phoenix reclinata [318]; grasses (Poaceae)[319], Zea mays [320-322], Zea luxurians and Zea diploperennis [323], Sorghum bicolor [324]; Tripsacum dactyloides [325], Oryza sativa [326;327]; Pennisetum americanum [328]; Pennisetum glaucum [329]; Dioscorea tokoro and Dioscorea tenuipes [330]; Rhynchoryza subulata and Leersia perrieri [331]; Hordeum vulgare [332]; Vitis vinifera [333;334]; Paeonia [335;336]; Solanum tuberosum [337;338]; Pisum sativum [339]; Lactuca sativa [340]; Lycopersicon esculentum [341-344]; Petunia hybrida [345;346]; Phaseolus acutifolius [347]; Nicotiana tabacum [348]; Pyrus communis [349]; Arabis gemmifera and Arabidopsis thaliana [350;351]; Gossypium [352-355]

References are listed at the end of suplementary material.




Table S2c. Main subfamilies that conform CADH family and Y-ADH family (COG1064) of MDR.

Subfamily







^ CADH and related (cinnamyl alcohol dehydrogenase)

Ref: [356-370]

ELI3 (elicitor-inducible defense-related proteins)

Ref: [356;359;371-378]

^ Yeast ADH and related

Ref: Kluyveromyces lactis [379-382]; Emericella nidulans [383-385]; Candida albicans [386]; Schizosaccharomyces pombe [387]; Saccharomyces cerevisiae [388-392]; Bacillus stearothermophilus [393-395]; Zymomonas mobilis [396;397]; Sinorhizobium meliloti [398]; Brucella abortus [399]

Fungi MTD (mannitol-1-phosphate dehydrogenase)

Ref: [400-403]

^ Fungi secondary ADH

Ref: [404-406]

Broad ADH (broad substrate specificity ADH)

Ref: [407-415]

References are listed at the end of suplementary material.




Table S2d. Main subfamilies that conform QOR family and NRBP family (COG0504) of MDR.

Subfamily







-crystallin/QOR (quinone oxidoreductase)

Ref: [416-427]

^ PIG3 and related (animal P53 Induced Gen 3: putative quinone oxidoreductase)

Ref: [428-430]

TED2 and related (quinone oxidoreductase involved in Tracheary Element Differentiation in plants)

Ref: [431-435]

^ NRBP1 (nuclear receptor binding protein/transcription factor)

Ref:[436-438]

Bifunctional QOR and related

Ref: [439-441]

VAT1

Ref: [442-448]

^ PER in actinomycetes (probable enoyl reductase in actinomycetes)

Ref: [449;450]

PKS-IAP (polyketide synthase-independent asociated proteins)

Ref: ^ Aspergillus terreus [451-453]; Cochliobolus carbonum [454-457]

QORL-1 (quinone oxidoreductase-like 1)

Ref: [458]

^ DINAP (dinoflagellate nuclear associated protein)

Ref: [459;460]

ARP (auxin regulated protein)

Ref: [461;462]

^ DI-QOR (dark induced-quinone oxidoreductase)

Ref: [463-466]

DI-QOR / ARP related

Unpurified protein; uncharacterized

^ AL (alginate lyase)

Ref: [467-470]

AST (membrane traffic protein)

Ref: [471]

^ BRP (bacteriocin-related proteins)

Ref: Lactococcus lactis [472]; Pediococcus pentosaceus[473]

CCAR (crotonyl-CoA reductase) and related

Ref: Streptomyces (Firmicutes) [474-478]; Pseudomonas (Proteobacteria:  subdivision) [479;480]; Methylobacterium (Proteobacteria:  subdivision) [481;482]

References are listed at the end of suplementary material.




Table S2e. Main subfamilies that conform LTD family (COG2130) of MDR.

Subfamily







LTD (Leucotriene B4 12-hydroxydehydrogenase)/PGR (15-Oxoprostaglandin 13-reductase)

Ref: [483-490]

^ AADH (allyl alcohol dehydrogenase)

Ref: [440;491;492]

LTD/AADH related

Uncharacterized proteins

References are listed at the end of suplementary material.




Table S2f. Main subfamilies that conform ER family (COG3321) of MDR.

Subfamily







^ Enoyl reductase (Fatty acid synthase -FAS-)

Ref: [493-505]

Enoyl reductase (modular polyketide synthase -PKS-)

Ref: [479;493;506-524]

^ Enoyl reductase (iterative polyketide synthase -PKS-)

Ref: [452;453;525;526]

ER -FAS: alveolata (enoyl reductase from type I fatty acid synthase in alveolata)

Ref: [527]

References are listed at the end of suplementary material.



^ Additional References


[155] Ng, K., Ye, R., Wu, X.C., & Wong, S.L. (1992) Sorbitol dehydrogenase from Bacillus subtilis. Purification, characterization, and gene cloning. J. Biol. Chem. 267, 24989-24994.

[156] Habenicht, A., Motejadded, H., Kiess, M., Wegerer, A., & Mattes, R. (1999) Xylose utilisation: cloning and characterisation of the xylitol dehydrogenase from Galactocandida mastotermitis. Biol. Chem. 380, 1405-1411.

[157] Johansson, K., El-Ahmad, M., Kaiser, C., Jornvall, H., Eklund, H., Hoog, J., & Ramaswamy, S. (2001) Crystal structure of sorbitol dehydrogenase. Chem. Biol. Interact. 130-132, 351-358.

[158] Gonzalez, E., Fernandez, M.R., Larroy, C., Sola, L., Pericas, M.A., Pares, X., & Biosca, J.A. (2000) Characterization of a (2R,3R)-2,3-butanediol dehydrogenase as the Saccharomyces cerevisiae YAL060W gene product. Disruption and induction of the gene. J. Biol. Chem. 275, 35876-35885.

[159] Gonzalez, E., Fernandez, M.R., Larroy, C., Pares, X., & Biosca, J.A. (2001) Characterization and functional role of Saccharomyces cerevisiae 2,3-butanediol dehydrogenase. Chem. Biol. Interact. 130-132, 425-434.

[160] Huang, M., Oppermann, F.B., & Steinbuchel, A. (1994) Molecular characterization of the Pseudomonas putida 2,3-butanediol catabolic pathway. FEMS Microbiol. Lett. 124, 141-150.

[161] Aronson, B.D., Somerville, R.L., Epperly, B.R., & Dekker, E.E. (1989) The primary structure of Escherichia coli L-threonine dehydrogenase. J. Biol. Chem. 264, 5226-5232.

[162] Epperly, B.R. & Dekker, E.E. (1991) L-threonine dehydrogenase from Escherichia coli. Identification of an active site cysteine residue and metal ion studies. J. Biol. Chem. 266, 6086-6092.

[163] Johnson, A.R., Chen, Y.W., & Dekker, E.E. (1998) Investigation of a catalytic zinc binding site in Escherichia coli L-threonine dehydrogenase by site-directed mutagenesis of cysteine-38. Arch. Biochem. Biophys. 358, 211-221.

[164] Weng, S.F., Liu, Y.S., Lin, J.W., & Tseng, Y.H. (1997) Transcriptional analysis of the threonine dehydrogenase gene of Xanthomonas campestris. Biochem. Biophys. Res. Commun. 240, 523-529.

[165] McGlynn, P. & Hunter, C.N. (1993) Genetic analysis of the bchC and bchA genes of Rhodobacter sphaeroides. Mol. Gen. Genet. 236, 227-234.

[166] Wellington, C.L. & Beatty, J.T. (1989) Promoter mapping and nucleotide sequence of the bchC bacteriochlorophyll biosynthesis gene from Rhodobacter capsulatus. Gene 83, 251-261.

[167] Anderson, R.L. & Simkins, R.A. (1982) L-Sorbose-1-phosphate reductase . Methods Enzymol. 89 (Pt D), 248-251.

[168] Kelker, N.E., Simkins, R.A., & Anderson, R.L. (1972) Pathway of L-sorbose metabolism in Aerobacter aerogenes. J. Biol. Chem. 247, 1479-1483.

[169] Reizer, J., Reizer, A., & Saier, M.H.J. (1995) Sorbose-1-P reductase (SorE) and the glucitol-6-P dehydrogenase (SorD) of the Klebsiella pneumoniae L-sorbose operon belong to the zinc-dependent dehydrogenase family and the short chain alcohol dehydrogenase family, respectively. Res. Microbiol. 146, 183-184.

[170] Wehmeier, U.F., Nobelmann, B., & Lengeler, J.W. (1992) Cloning of the Escherichia coli sor genes for L-sorbose transport and metabolism and physical mapping of the genes near metH and iclR. J. Bacteriol. 174, 7784-7790.

[171] Wehmeier, U.F. & Lengeler, J.W. (1994) Sequence of the sor-operon for L-sorbose utilization from Klebsiella pneumoniae KAY2026. Biochim. Biophys. Acta 1208, 348-351.

[172] Burdette, D. & Zeikus, J.G. (1994) Purification of acetaldehyde dehydrogenase and alcohol dehydrogenases from Thermoanaerobacter ethanolicus 39E and characterization of the secondary-alcohol dehydrogenase (2 degrees Adh) as a bifunctional alcohol dehydrogenase--acetyl-CoA reductive thioesterase. Biochem. J. 302, 163-170.

[173] Korkhin, Y., Kalb, G., Peretz, M., Bogin, O., Burstein, Y., & Frolow, F. (1998) NADP-dependent bacterial alcohol dehydrogenases: crystal structure, cofactor-binding and cofactor specificity of the ADHs of Clostridium beijerinckii and Thermoanaerobacter brockii. J. Mol. Biol. 278, 967-981.

[174] Li, C., Heatwole, J., Soelaiman, S., & Shoham, M. (1999) Crystal structure of a thermophilic alcohol dehydrogenase substrate complex suggests determinants of substrate specificity and thermostability. Proteins 37 , 619-627.

[175] Peretz, M. & Burstein, Y. (1989) Amino acid sequence of alcohol dehydrogenase from the thermophilic bacterium Thermoanaerobium brockii. Biochemistry 28, 6549-6555.

[176] Lo, H.S. & Chang, C.J. (1982) Purification and properties of NADP-linked, alcohol dehydrogenase from Entamoeba histolytica. J. Parasitol. 68, 372-377.

[177] Kumar, A., Shen, P.S., Descoteaux, S., Pohl, J. , Bailey, G., & Samuelson, J. (1992) Cloning and expression of an NADP(+)-dependent alcohol dehydrogenase gene of Entamoeba histolytica. Proc. Natl Acad. Sci. USA 89, 10188-10192.

[178] Markwell, J.P. & Anderson, R.L. (1981) Pathway of galactitol catabolism in Klebsiella pneumoniae: oxidation of L-galactitol-1-phosphate by a NAD-specific dehydrogenase. Arch. Biochem. Biophys. 209, 592-597.

[179] Nobelmann, B. & Lengeler, J.W. (1995) Sequence of the gat operon for galactitol utilization from a wild-type strain EC3132 of Escherichia coli. Biochim. Biophys. Acta 1262, 69-72.

[180] Nobelmann, B. & Lengeler, J.W. (1996) Molecular analysis of the gat genes from Escherichia coli and of their roles in galactitol transport and metabolism. J. Bacteriol. 178, 6790-6795.

[181] Huisman, G.W. & Kolter, R. (1994) Sensing starvation: a homoserine lactone--dependent signaling pathway in Escherichia coli. Science 265, 537-539.

[182] Babbit, P.C., Mrachko, G.T., Hasson, M.S., Huisman, G.W., Kolter, R., Ringe, D., Petsko, G.A., Kenyon, G.L., & Gerlt, J.A. (1995) Functionally diverse enzyme superfamily that abstracts the alpha-protons of carboxylic-acids. Science 267, 1159-1161.

[183] Aramaki, H., Koga, H., Sagara, Y., Hosoi, M., & Horiuchi, T. (1993) Complete nucleotide sequence of the 5-exo-hydroxycamphor dehydrogenase gene on the CAM plasmid of Pseudomonas putida (ATCC 17453). Biochim. Biophys. Acta 1174, 91-94.

[184] Koga, H., Aramaki, H., Yamaguchi, E., Takeuchi, K., Horiuchi, T., & Gunsalus, I.C. (1986) camR, a negative regulator locus of the cytochrome P-450cam hydroxylase operon. J. Bacteriol. 166, 1089-1095.

[185] Nakar, D. & Gutnick, D.L. (2001) Analysis of the wee gene cluster responsible for the biosynthesis of the polymeric bioemulsifier from the oil- degrading strain Acinetobacter lwoffii RAG-1. Microbiology 147, 1937-1946.

[186] Bonete, M.J., Pire, C., LLorca, F.I., & Camacho, M.L. (1996) Glucose dehydrogenase from the halophilic Archaeon Haloferax mediterranei: enzyme purification, characterisation and N-terminal sequence. FEBS Lett. 383, 227-229.

[187] Bright, J.R., Byrom, D., Danson, M.J., Hough, D.W., & Towner, P. (1993) Cloning, sequencing and expression of the gene encoding glucose dehydrogenase from the thermophilic archaeon Thermoplasma acidophilum. Eur. J. Biochem. 211, 549-554.

[188] John, J., Crennell, S.J., Hough, D.W., Danson, M.J., & Taylor, G.L. (1994) The crystal structure of glucose dehydrogenase from Thermoplasma acidophilum. Structure 2, 385-393.

[189] Smith, L.D., Budgen, N., Bungard, S.J., Danson, M.J., & Hough, D.W. (1989) Purification and characterization of glucose dehydrogenase from the thermoacidophilic archaebacterium Thermoplasma acidophilum. Biochem. J. 261, 973-977.

[190] Ito, K., Takahashi, M., Yoshimoto, T., & Tsuru, D. (1994) Cloning and high-level expression of the glutathione-independent formaldehyde dehydrogenase gene from Pseudomonas putida. J. Bacteriol. 176, 2483-2491.

[191] Oppenheimer, N.J., Henehan, G.T., Huete-Perez, J.A., & Ito, K. (1997) P. putida formaldehyde dehydrogenase. An alcohol dehydrogenase masquerading as an aldehyde dehydrogenase. Adv. Exp. Med. Biol. 414, 417-423.

[192] Tsuru, D., Oda, N., Matsuo, Y., Ishikawa, S., Ito, K., & Yoshimoto, T. (1997) Glutathione-independent formaldehyde dehydrogenase from Pseudomonas putida: survey of functional groups with special regard for cysteine residues. Biosci. Biotechnol. Biochem. 61, 1354-1357.

[193] Kato, N., Yamagami, T., Shimao, M., & Sakazawa, C. (1986) Formaldehyde dismutase, a novel NAD-binding oxidoreductase from Pseudomonas putida F61. Eur. J. Biochem. 156, 59-64.

[194] Mason, R.P. & Sanders, J.K. (1989) In vivo enzymology: a deuterium NMR study of formaldehyde dismutase in Pseudomonas putida F61a and Staphylococcus aureus. Biochemistry 28, 2160-2168.

[195] Piersma, S.R., de Vries, S., & Duine, J.A. (1997) Nicotinoprotein alcohol/aldehyde oxidoreductases. Enzymes with bound NAD(P) as cofactor. Adv. Exp. Med. Biol. 414, 425-434.

[196] Yanase, H., Noda, H., Aoki, K., Kita, K., & Kato, N. (1995) Cloning, sequence analysis, and expression of the gene encoding formaldehyde dismutase from Pseudomonas putida F61. Biosci. Biotechnol. Biochem. 59, 197-202.

[197] Poelarends, G.J., Kulakov, L.A., Larkin, M.J., van, H., V, & Janssen, D.B. (2000) Roles of horizontal gene transfer and gene integration in evolution of 1,3-dichloropropene- and 1,2-dibromoethane-degradative pathways. J. Bacteriol. 182, 2191-2199.

[198] Poelarends, G.J., Zandstra, M., Bosma, T., Kulakov, L.A., Larkin, M.J., Marchesi, J.R., Weightman, A.J., & Janssen, D.B. (2000) Haloalkane-utilizing Rhodococcus strains isolated from geographically distinct locations possess a highly conserved gene cluster encoding haloalkane catabolism. J. Bacteriol. 182, 2725-2731.

[199] MacKintosh, R.W. & Fewson, C.A. (1988) Benzyl alcohol dehydrogenase and benzaldehyde dehydrogenase II from Acinetobacter calcoaceticus. Substrate specificities and inhibition studies. Biochem. J. 255, 653-661.

[200] MacKintosh, R.W. & Fewson, C.A. (1988) Benzyl alcohol dehydrogenase and benzaldehyde dehydrogenase II from Acinetobacter calcoaceticus. Purification and preliminary characterization. Biochem. J. 250, 743-751.

[201] Gillooly, D.J., Robertson, A.G., & Fewson, C.A. (1998) Molecular characterization of benzyl alcohol dehydrogenase and benzaldehyde dehydrogenase II of Acinetobacter calcoaceticus. Biochem. J. 330, 1375-1381.

[202] Jones, R.M., Collier, L.S., Neidle, E.L., & Williams, P.A. (1999) areABC genes determine the catabolism of aryl esters in Acinetobacter sp. Strain ADP1. J. Bacteriol. 181, 4568-4575.

[203] Jones, R.M. & Williams, P.A. (2001) areCBA is an operon in Acinetobacter sp. strain ADP1 and Is controlled by AreR, a sigma(54)-dependent regulator. J. Bacteriol. 183, 405-409.

[204] Shaw, J.P. & Harayama, S. (1990) Purification and characterisation of TOL plasmid-encoded benzyl alcohol dehydrogenase and benzaldehyde dehydrogenase of Pseudomonas putida. Eur. J. Biochem. 191, 705-714.

[205] Shaw, J.P. & Harayama, S. (1992) Purification and characterisation of the NADH:acceptor reductase component of xylene monooxygenase encoded by the TOL plasmid pWW0 of Pseudomonas putida mt-2. Eur. J. Biochem. 209, 51-61.

[206] Shaw, J.P., Rekik, M., Schwager, F., & Harayama, S. (1993) Kinetic studies on benzyl alcohol dehydrogenase encoded by TOL plasmid pWWO. A member of the zinc-containing long chain alcohol dehydrogenase family. J. Biol. Chem. 268, 10842-10850.

[207] Peterson, J.A., Lu, J.Y., Geisselsoder, J., Graham-Lorence, S., Carmona, C., Witney, F., & Lorence, M.C. (1992) Cytochrome P-450terp. Isolation and purification of the protein and cloning and sequencing of its operon. J. Biol. Chem. 267, 14193-14203.

[208] Iurescia, S., Marconi, A.M., Tofani, D., Gambacorta, A., Paterno, A., Devirgiliis, C., van der Werf, M.J., & Zennaro, E. (1999) Identification and sequencing of beta-myrcene catabolism genes from Pseudomonas sp. strain M1. Appl. Environ. Microbiol. 65, 2871-2876.

[209] Romine, M.F., Stillwell, L.C., Wong, K.K., Thurston, S.J., Sisk, E.C., Sensen, C., Gaasterland, T., Fredrickson, J.K., & Saffer, J.D. (1999) Complete sequence of a 184-kilobase catabolic plasmid from Sphingomonas aromaticivorans F199. J. Bacteriol. 181, 1585-1602.

[210] Rosenblueth, M., Hynes, M.F., & Martinez-Romero, E. (1998) Rhizobium tropici teu genes involved in specific uptake of Phaseolus vulgaris bean-exudate compounds. Mol. Gen. Genet. 258, 587-598.

[211] Xu, L.L., Singh, B.K., & Conn, E.E. (1988) Purification and characterization of acetone cyanohydrin lyase from Linum usitatissimum. Arch. Biochem. Biophys. 263, 256-263.

[212] Trummler, K. & Wajant, H. (1997) Molecular cloning of acetone cyanohydrin lyase from flax (Linum usitatissimum). Definition of a novel class of hydroxynitrile lyases. J. Biol. Chem. 272, 4770-4774.

[213] Trummler, K., Roos, J., Schwaneberg, U., Effenberger, F., Forster, S., Pfizenmaier, K., & Wajant, H. (1998) Expression of the Zn2+-containing hydroxynitrile lyase from flax (^ Linum usitatissimum) in Pichia pastoris - utilization of the recombinant enzyme for enzymatic analysis and site-directed mutagenesis. Plant Sci. 139, 19-27.

[214] Breithaupt, H., Pohl, M., Bonigk, W., Heim, P., Schimz, K.L., & Kula, M.R. (1999) Cloning and expression of (R)-hydroxynitrile lyase from ^ Linum usitatissimum (flax). J. Mol. Catal. B-Enzym. 6, 315-332.

[215] Norin, A., Van Ophem, P.W., Piersma, S.R., Persson, B., Duine, J.A., & Jornvall, H. (1997) Mycothiol-dependent formaldehyde dehydrogenase, a prokaryotic medium-chain dehydrogenase/reductase, phylogenetically links different eukaroytic alcohol dehydrogenases--primary structure, conformational modelling and functional correlations. Eur. J. Biochem.




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