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. 2006 Dec;5(12):2062–2071. doi: 10.1128/EC.00205-06

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Copyright © 2006, American Society for Microbiology

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FIG.1. — Sequence comparison of glycine cleavage H proteins and dihydrolipoamide dehydrogenase (L protein) from different organisms using CLUSTALX. (A) Alignment of amino acid sequences deduced from two genes encoding glycine cleavage H proteins (TvH1 and TvH2) from Trichomonas vaginalis compared with H proteins from S. cerevisiae (Sc; P39726), B. subtilis (Bc; O32174), and P. sativum (Ps; P16048). The lysine (K) that binds lipoic acid is boxed. (B) Alignment of amino acid sequences deduced from the gene encoding dihydrolipoamide dehydrogenase (L protein) from T. vaginalis (Tv) compared with L proteins from S. cerevisiae (Sc; P09624), P. sativum (Ps; P31023), and B. subtilis (Bs; AAC05585). Asterisks and dots represent identities and similarities between the sequences, respectively. The hydrogenosomal presequence is marked in boldface type in the T. vaginalis protein sequences.

FIG.1. — Sequence comparison of glycine cleavage H proteins and dihydrolipoamide dehydrogenase (L protein) from different organisms using CLUSTALX. (A) Alignment of amino acid sequences deduced from two genes encoding glycine cleavage H proteins (TvH1 and TvH2) from Trichomonas vaginalis compared with H proteins from S. cerevisiae (Sc; P39726), B. subtilis (Bc; O32174), and P. sativum (Ps; P16048). The lysine (K) that binds lipoic acid is boxed. (B) Alignment of amino acid sequences deduced from the gene encoding dihydrolipoamide dehydrogenase (L protein) from T. vaginalis (Tv) compared with L proteins from S. cerevisiae (Sc; P09624), P. sativum (Ps; P31023), and B. subtilis (Bs; AAC05585). Asterisks and dots represent identities and similarities between the sequences, respectively. The hydrogenosomal presequence is marked in boldface type in the T. vaginalis protein sequences.