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Variation and Evolution of the Citric- Acid Cycle: a Genomic Perspective Martijn A

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Variation and Evolution of the Citric- Acid Cycle: a Genomic Perspective Martijn A R EVIEWS 14, 8605–8613 63 Karita, S., Sakka, K. and Ohmiya, K. (1997) in Rumen Microbes 57 Hayashi, H. et al. (1997) J. Bacteriol. 179, 4246–4253 and Digestive Physiology in Ruminants (Onodera, R. et al., eds), 58 Cornet, P. et al. (1983) Biotechnology 1, 589–594 pp. 47–57, Japan Sci. Soc. Press 59 Lemaire, M. and Béguin, P. (1993) J. Bacteriol. 175, 3353–3360 64 Tamaru, Y. et al. (1997) J. Ferment. Bioeng. 83, 201–205 60 Zverlov, V.V. et al. (1994) Biotechnol. Lett. 16, 29–34 65 Fanutti, C. et al. (1995) J. Biol. Chem. 270, 29314–29322 61 Kirby, J. et al. (1997) FEMS Microbiol. Lett. 149, 213–219 66 Li, X., Chen, H. and Ljungdahl, L. (1997) Appl. Environ. 62 Ohmiya, K. et al. (1997) Biotechnol. Genet. Eng. Rev. 14, 365–414 Microbiol. 63, 4721–4728 Variation and evolution of the citric- acid cycle: a genomic perspective Martijn A. Huynen, Thomas Dandekar and Peer Bork ompletely sequenced The presence of genes encoding enzymes display of the reaction steps genomes have provided involved in the citric-acid cycle has been for which genes can be found Ca new way of analysing studied in 19 completely sequenced in the selected genomes is the biochemical pathways in a genomes. In the majority of species, the given in Fig. 1. The first strik- species: using the presence of cycle appears to be incomplete or absent. ing feature in most of the genes encoding the enzymes Several distinct, incomplete cycles reflect genomes is the incompleteness that catalyse its reactions1,2. By adaptations to different environments. of the CAC. Only the four studying the variation in meta- Their distribution over the phylogenetic largest genomes, those of bolic pathways and the way tree hints at precursors in the evolution of Escherichia coli, Bacillus sub- that they are encoded in a the citric-acid cycle. tilis, Mycobacterium tubercu- rapidly growing set of se- losis and Saccharomyces cere- quenced genomes, we can elu- M.A. Huynen*, T. Dandekar and P. Bork are in the visiae, and the small genome cidate their evolution. Here, European Molecular Biology Laboratory, of Rickettsia prowazekii, en- Meyerhofstrasse 1, 69117 Heidelberg, Germany, and we present an investigation of in the Max-Delbrück-Centre for Molecular Medicine, code the genes for a complete the presence and absence of 13122 Berlin-Buch, Germany; CAC. In the other genomes, genes, in prokaryotes and yeast, M.A. Huynen is also in the Bioinformatics Group, the cycle has gaps or is com- that code for the enzymes in- Utrecht University, Padualaan 8, 3584 CH Utrecht, pletely absent. In these incom- The Netherlands. volved in the citric-acid cycle *tel: 149 6221 387372, plete cycles, the genes that are (CAC), including variations fax: 149 6221 387517, present generally code for such as the reductive CAC and e-mail: [email protected] reactions that are connected to the branched citric-acid path- each other, suggesting there way, the glyoxylate shunt, and in the reactions con- are functional connections between the genes. In in- necting the CAC to pyruvate and phosphoenolpyruvate. complete cycles, the last part of the oxidative cycle Our analysis has combined a thorough exami- (steps 6–8 in Fig. 1a), leading from succinate to nation of sequence data, which included improving oxaloactetate, is the most highly conserved, whereas the annotation of genes in the GenBank genome data- the initial steps (steps 1–3), from acetyl CoA to base, with an analysis of the biochemical data on the 2-ketoglutarate, show the least conservation. compared species. We examined the genomes of uni- When interpreting the role of incomplete CACs, it cellular organisms published to date, including those is important to realize that, as well as the oxidation of of four Archaea, 14 Bacteria and one Eukaryote. For acetyl CoA, the CAC also plays a role in the gener- an overview of the published genomes, including ation of intermediates for anabolic pathways. Specifi- references, see http://www.tigr.org/tdb/mdb/ cally, 2-ketoglutarate (between steps 3 and 4), ox- mdb.html. aloacetate (between steps 8 and 1) and succinyl CoA (between steps 5 and 6) are starting points for the Variability of the pathway synthesis of glutamate, aspartate and porphyrin, re- The genes involved in the CAC and its connections to spectively. The autotrophic species that are missing pyruvate and phosphoenolpyruvate in the various a small part of the CAC are still able to generate 2- genomes are indicated in Table 1 and a graphical ketoglutarate, oxaloacetate and succinyl CoA from 0966-842X/99/$ - see front matter © 1999 Elsevier Science. All rights reserved. PII: S0966-842X(99)01539-5 TRENDS IN MICROBIOLOGY 281 VOL. 7 NO. 7 JULY 1999 R EVIEWS Table 1. Citric-acid cycle enzymes and genesa,b Enzymesc Genes Species Escherichia Haemophilus Helicobacter Rickettsia Bacillus Mycobacterium Mycobacterium coli influenzae pylori prowazekii subtilis genitalium tuberculosis Citrate synthase (1) EC 4.1.3.7 gltA EC0720 – HP0026 RP844 citZ – TB0896 citA TB0889 Aconitase (2) EC 4.2.1.3 acnA EC1276 – – RP799 citB – TB1475 EC0771 acnB EC0118 – HP0779 – – –– Isocitrate dehydrogenase (3) EC 1.1.1.42 icdA EC1136 – HP0027 RP265 citC – TB3339 TB0066 2-ketoglutarate dehydrogenase (4) EC 1.2.4.2 sucA EC0726 HI1662 – RP180 odhA – TB1248 EC 2.3.1.61 sucB EC0727 HI1661 – RP179 odhB – TB1248 TB2215 2-ketoglutarate ferredoxin oxidoreductase (4) EC 1.2.7.3 korA – – HP0589 – – – TB2455d korB – – HP0590 – – – TB2454d korC – – HP0591 – – –– korD – – HP0588 – – – TB2455 Succinyl-CoA synthetase (5) EC 6.2.1.5 sucC EC0728 HI1196 – RP433 sucC – TB0951 sucD EC0729 HI1197 – RP432 sucD – TB0952 Succinyl-CoA–acetoacetate- CoA-transferase EC 2.8.3.5 scoA – – HP0691 – yxjD – TB2504 scoB – – HP0692 – yxjE – TB2503 Fumarate reductasef (6) EC 1.3.99.1 frdA EC4154 HI0835 HP0192 – sdhA – TB1552 TB0248 frdB EC4153 HI0834 HP0191 – sdhB – TB1553 TB0247 frdC EC4152 HI0833 HP0193 – sdhC – TB1554 frdD EC4151 HI0832 – – – – TB1555 Succinate dehydrogenase (6) EC 1.3.99.1 sdhA EC0723 – – RP128 – – TB3318 sdhB EC0724 – – RP044 – – TB3319 sdhC EC0721 – – RP126 – – TB3316 sdhD EC0722 – – RP127 – – TB3317 Fumarase (7) EC 4.2.1.2 fumA, B EC1612 – – –––– (Class I) EC4122 fumC EC1611 HI1398 HP1325 RP665 citG – TB1098 (Class II) Malate dehydrogenase (8) EC 1.1.1.37 mdh EC3236 HI1210 – RP376 citH MG460d TB1240 Archaeal EC0517 HI1031 – – yjmC –– type EC0801 EC3575 TRENDS IN MICROBIOLOGY 282 VOL. 7 NO. 7 JULY 1999 R EVIEWS Chlamydia Treponema Synechocystis Aquifex Archaeoglobus Methanococcus Methanobacterium Pyrococcus Saccharomyces trachomatis pallidum aeolicus fulgidus jannaschii thermoautotrophicum horikoshii cerevisiae ––gltA AQ0150(c) AF1340 – MT0962(c) – YNR001C MT1726(c) ––––– – – – YLR304C AQ1784 – – slr0665 – – – – – – ––icd AQ1512 AF0647 – – – YOR136W CT054 – – – – – – – YIL125W CT055 – – – – – – – YDR148C CT400 ––– – AF0469 MJ0276 MT1033 PH1662 – PH1666 ––– – AF0468 MJ0537 MT1034 PH1661 – PH1665 ––– – AF0471 MJ0536 MT1035 PH1660 – PH1663 ––– – AF0470 MJ0146 MT1032 PHunnote – CT821 – sucC AQ1620 AF1540 MJ0210 MT1036 – YGR244C AQ1306 AF2186 CT822 – sucD AQ1622 AF1539 MJ1246 MT0563 – YOR142W AQ1888 AF2185 ––– – – – – –– ––– – – – – –– CT592 – – AQ0594 AF0681 MJ0033 MT1502 – – CT591 – – AQ0655 AF0682 MJ0092 MT1850 – – AQ0553 CT593 – – – AF0684 –– –– ––– – AF0683 –– –– – – frdA – – – – – YJL045W – YKL148C – – sdhB – – – – – YLL041C sdhB – ––– – – – – – YMR118C ––– – –– – –– ––– AQ1780(n) AF1099(n) MJ1294(n) MT1735(n) PH1683(n) – MT0963(n) AQ1679(c) AF1098(c) MJ0617(c) MT1910(c) PH1684(c) CT855 – fumC – – – – – YPL262W CT376 – citH AQ1665 AF0855 MJ0490 MT0188 – YKL085W AQ1782 – – – – – MJ1425 MT1205 PH1277 – continued TRENDS IN MICROBIOLOGY 283 VOL. 7 NO. 7 JULY 1999 R EVIEWS Enzymesc Genes Species Escherichia Haemophilus Helicobacter Rickettsia Bacillus Mycobacterium Mycobacterium coli influenzae pylori prowazekii subtilis genitalium tuberculosis Isocitrate lyase (glyoxylate pathway) (9) EC 4.1.3.1 aceA EC4015 – – – – – TB0467 Malate synthase (glyoxylate pathway) (10) EC 4.1.3.2 aceB EC4014 – – – – –– Phosphoenol pyruvate glcB EC2976 – – – – – TB1837 carboxykinase (ATP) (11) EC 4.1.1.49 pckA EC3403 HI0809 – – pckA –– Phosphoenol pyruvate carboxykinase (GTP) (11) EC 4.1.1.32 pck –– – – – – TB0211 Phosphoenol pyruvate carboxylase (11) EC 4.1.1.31 ppc EC3956 HI1636 – – – –– Malic enzyme (12) EC 1.1.1.40 mez EC2463 HI1245 – RP373 ytsJ –– yqkJ EC 1.1.1.38 sfcA EC1479 – – – malS – TB2332 Pyruvate carboxylase/ oxaloacetate decarboxylaseg (13) EC 4.1.1.3 oadB –– – – –– – EC 6.3.1.4 pycA/–– – – pycA – TB2967 – accC EC 6.4.1.1 pycB/– – – pycA – TB2967 – oadA – Pyruvate dehydrogenase (14) EC 1.2.4.1 aceE EC0114 HI1233 – – – – TB2241 (E1) EC 1.2.4.1 pdhA – – – RP261 pdhA MG274 TB2497 (E1-a) EC 1.2.4.1 pdhB – – – RP262 pdhB MG273 TB2496 (E1-b) EC 2.3.1.12 aceF EC0115 HI1232 – RP530 pdhC MG272 TB2495 TB2215 EC 1.8.1.4 lpdA EC0116 HI1231 – RP460 pdhD MG271 TB0462 RP805 Pyruvate ferredoxin oxidoreductase EC 1.2.7.1 porA EC1378 – HP1110 – – – – porB EC1378 – HP1111 – – – – porC EC1378 – HP1108 – – – – porD EC1378 – HP1109 – – – – aIf a gene numbering system is available, the genes are indicated with their gene numbers, and the initials of the species (TB for M. tuberculosis); otherwise, gene names are used. Multiple copies of a gene that are a result of recent gene duplications or that do not have separate orthologs in multiple species are in one column. Genes that align only with part of a larger protein are indicated with a (c) for a carboxy-terminal alignment and an (n) for an amino-terminal alignment. bParalogous gene
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