Table 2.

Fold Prediction for Analogous Enzymes[i]

Enzyme activity (EC No.)Taxonomic representation[ii] PDB[ii] Predicted structural folds[iii]
bacteriaarchaeaeukaryotes
3-α-hydroxysteroid JN0829 AF1207HE27_HUMAN 1AHH Rossmann
 dehydrogenase  (EC 1.1.1.50)— — DIDH_RAT 1RAL TIM-barrel
17-β-hydroxysteroidYBBO_ECOLIAF1207 DHB1_HUMAN 1FDS Rossmann
 dehydrogenase  (EC 1.1.1.62)— — A56424 1RAL TIM-barrel
Protochlorophyllide BCHN_RHOCA — CHLN_CHLRE 3MIN nitrogenase Fe-Mo
 reductase (EC1.3.1.33)slr0506— PCR_ARATH — Rossmann
Hydrogenase (EC1.18.99.1) PHFL_DESVH FDHA_METFO 1171117 1FCA ferredoxin-like
PHNL_DESVM FRHA_METTH— 1FRV Ni-Fe hydrogenase
Chloramphenicol acetyl-  transferase (EC2.3.1.28) CAT_ECOLI — — 1CLA CoA-dependent  acetyltransferases
CAT4_ECOLI MJ1064YJV8_YEAST 1LXA single-stranded β-helix
Gluconokinase (EC2.7.1.12) GNTK_ECOLI — GNTK_SCHPO 1DVR P-loop-containing
GNTK_BACSU AF1752GLPK_YEAST 1GLA actin-like ATPase
Diacylglycerol kinase  (EC2.7.1.107) KDGL_ECOLI — — — not known; integral  membrane protein
— — KDGG_HUMAN 1CDL phosphofructokinase
FAD synthase (EC2.7.7.2) RIBF_CORAM — YDR236c 1GSG Rossmann
— MJ0973 FAD1_YEAST 1GPM adenine nucleotide  α-hydrolase
Glucan endo-1,3-β- E13B_BACCI — 1488257 1MAC ConA-like lectins/glucanases
 glucosidase (EC3.2.1.39)— AF0876 E13L-TOBAC 1GHR TIM-barrel
6-Phospho-β-glucosidase BGLB_ECOLI BGAL_SULSOBGLC_MAIZE 1PBG TIM-barrel
 (EC3.2.1.86) CELF_ECOLI — — 1LDG Rossmann
Asparaginase (EC3.5.1.1) ASG1_ECOLI MJ0020 ASG1_YEAST 3ECA glutaminase/asparaginase
ASPG_FLAME— ASPG_LUPAR 1APY Ntn hydrolases
Apyrase, ATP-diphosphatase  (EC3.6.1.5)USHA_ECOLIAF0876 APY_AEDAE 1KBP metallo-dependent  phosphatases
CD39_HUMAN 1DKG ribonuclease H-like
— — 1546841 1AKO DNase I-like
Diadenosine tetra-NTPA_ECOLIAF2200 AP4A_HUMAN 1MUT NTP pyrophosphorylase
 phosphatase  (EC 3.6.1.17)AF2211 APH1_SCHPO 1HXP HIT-like
Haloacetate dehalogenase DEH1_MORSP AF1706HYES_HUMAN 1BRO α/β-hydrolases
 (EC3.8.1.3) DEH2_MORSP MTH2091050822 1JUD haloacid dehalogenase
Prephenate dehydratase PHEA_ECOLI PHEA_METJA PHA2_YEAST 1FCA ferredoxin-like
 (EC4.2.1.51) PHEC_PSEAE AF0231— 2LAO periplasmic binding  protein-like
DNA-(apurinic or END3_ECOLI MJ0613 END3_SCHPO 2ABK DNA-glycosylase
 apyrimidinic site) lyase END4_ECOLI MTH1010 APN1_YEAST 1DID TIM-barrel
 (EC4.2.99.18)EX3_ECOLIMTH212 APE1_HUMAN 1AKO DNase I-like
Phosphoglycerate mutase PMG1_ECOLI — PMGE_HUMAN 3PGM phosphoglycerate mutase
 (EC5.4.2.1) PMGI_BACSU MTH1591 PMGI_TOBAC 1ALK alkaline phosphatase
Lysine-tRNA ligase SYK1_ECOLI — SYKC_YEAST 1LYL class II aaRS synthetases
 (EC6.1.1.6)BB0659 2645489 — 1GLN adenine nucleotide  α-hydrolase

[i] All designatins are as in Table 1. Only the apparent orthologs (Tatusov et al. 1996, 1997) are included. Proteins from recently sequenced genomes, not yet included in SwissProt, are listed under their original identifiers. The source organisms are as follows: (JN0829) Pseudomonas sp.; (A56424), mouse; (1546841)Rhodnius prolixus (Sarkis et al. 1986); (2645489)Methanococcus maripaludis (Ibba et al. 1997b); (MJ)Methanococcus jannaschii (Bult et al. 1996); (MTH)Methanobacterium thermoautotrophicum (Smith et al. 1997); (AF) Archaeolgbus fulgidus (Klenk et al. 1997); (BB)Borellia burgdorferi (Fraser et al. 1997).

[ii] The PDB codes in roman type indicate the structures that were used for fold prediction; italics indicate tentative fold predictions based on multiple iterative searches against the GenPept database. Only the folds of the catalytic domains are indicated.

[iii] Fold names are from the SCOP database [(Hubbard et al. 1997) http://scop.mrc-lmb.cam.ac.uk/scop].