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Proteins in PDB homologous to 1dbtA

Additional 1dbt chains
1dbtB

83 proteins (315 PDB structures) with E() < 0.001

Homologs in SwissProt


Acc   E.C. E() % id alen 60
&D
62
*K
1dbtA, 1dbtB, 1dbtCOrotidine 5'-Monophosphate Decarboxylase4.1.1.231.3e-101100.0237 &D*K
2yytA, 2yytB, 2yytC, 2yytD, 2yyuA, 2yyuBUncharacterized Conserved Protein From G4.1.1.231.1e-5960.9230 &D*K
3tfxA, 3tfxBOrotidine 5'-Phosphate Decarboxylase Fro4.1.1.232.6e-4045.9229 &D*K
3ldvA, 3ldvB, 3uwqA, 3uwqB1.77 Angstrom Resolution Orotidine 5'- P4.1.1.233.1e-3243.5223 &D*K
1eixA, 1eixB, 1eixC, 1eixD, 1l2uA, 1l2uBOrotidine 5'-Monophosphate Decarboxylase4.1.1.233.4e-3242.1228 &D*K
3tr2A, 3tr2BA Orotidine 5'-Phosphate Decarboxylase (4.1.1.231.9e-3039.7224 &D*K
1jjkA, 1jjkB, 1jjkC, 1jjkD, 1jjkE, 1jjkF, 1jjkG, 1jjkH, 1jjkI, 1jjkJ, 1jjkK, 1jjkL, 1jjkM, 1jjkN, 1jjkO, 1jjkPSelenomethionine Substitution Of Orotidi4.1.1.234.4e-3041.2228 &D*K
3ru6A, 3ru6B, 3ru6C, 3ru6D1.8 Angstrom Resolution Orotidine 5'-Pho4.1.1.235.9e-3039.6217 &D*K
1vqtAOrotidine 5'-Phosphate Decarboxylase (Tm4.1.1.232.2e-0729.9231 &D*K
3nqgA, 3nqgBThe Mutant V155d Of Orotidine 5'-Monopho4.1.1.233.3e-0723.6225 &D*K
2cz5A, 2cz5B, 2czdA, 2czdB, 2czeA, 2czeB, 2czfA, 2czfBOrotidine 5'-Phosphate Decarboxylase Fro4.1.1.235.8e-0725.0232 &D*K
3nqaA, 3nqaBThe Mutant F100a Of Orotidine 5'-Monopho4.1.1.236.5e-0723.6225 &D*K
3nqmA, 3nqmB, 3pc0A, 3pc0BThe Mutant V155s Of Orotidine 5'-Monopho4.1.1.231.3e-0623.1225 &D*K
3nqcA, 3nqcB, 3pbuA, 3pbuBThe Mutant I96s Of Orotidine 5'-Monophos4.1.1.231.3e-0623.1225 &D*K
3nqdA, 3nqdB, 3pbvA, 3pbvBThe Mutant I96t Of Orotidine 5'-Monophos4.1.1.231.5e-0623.1225 &D*K
3sj3A, 3sj3BThe Mutant R160a.Y206f Of Orotidine 5'- 4.1.1.231.8e-0623.1225 &D*K
3p61A, 3p61BThe Mutant R160a Of Orotidine 5'-Monopho4.1.1.231.8e-0623.1225 &D*K
1km2AOrotidine Monophosphate Mutant Q185a Wit4.1.1.232.3e-0623.1225 &D*K
1dv7AOrotidine Monophosphate Decarboxylase4.1.1.232.5e-0623.1225 &D*K
3p5yA, 3p5yBThe Mutant T159a Of Orotidine 5'-Monopho4.1.1.232.5e-0623.1225 &D*K
3p5zA, 3p5zBThe Mutant T159s Of Orotidine 5'-Monopho4.1.1.232.5e-0623.1225 &D*K
1lorAOrotidine 5'-Monophosphate Complexed Wit4.1.1.232.5e-0623.1225 &D*K
3g18A, 3g18B, 3g1aA, 3g1aB, 3g1dA, 3g1dB, 3g1fA, 3g1fB, 3g1fC, 3g1fD, 3g1fE, 3g1fF, 3g1fG, 3g1fH, 3g1fI, 3g1fJ, 3g1fK, 3g1fL, 3g1fM, 3g1hA, 3g1hB, 3g1hC, 3g1hD, 3g1hE, 3g1hF, 3g1hG, 3g1hH, 3g1hI, 3g1hJ, 3g1hK, 3g1hL, 3g1hM, 3ltpA, 3ltpBOrotidine 5'-Monophosphate Decarboxylase4.1.1.232.5e-0623.1225 &D*K
3rlvA, 3rlvBThe Mutant Y206f Of Orotidine 5'-Monopho2.5e-0623.1225 &D*K
3p60A, 3p60BThe Mutant T159v Of Orotidine 5'-Monopho4.1.1.232.5e-0623.1225 &D*K
3qf0A, 3qf0BThe Mutant T159v,Y206f Of Orotidine 5'- 2.5e-0623.1225 &D*K
1lolA, 1lolB, 1lp6A, 1lp6BOrotidine Monophosphate Decarboxylase Co4.1.1.232.5e-0623.1225 &D*K
1dvjA, 1dvjB, 1dvjC, 1dvjDOrotidine Monophosphate Decarboxylase Co4.1.1.232.8e-0623.1225 &D*K
3secA, 3ssjA, 3sw6A, 3thqA, 3thqBMethanothermobacter Thermautotrophicus O2.8e-0623.1225 &D*K
1x1zA, 1x1zB, 2e6yA, 2e6yB, 2zz1A, 2zz1B, 2zz6A, 2zz6B, 3w07AOrotidine 5'-Monophosphate Decarboxylase4.1.1.232.8e-0623.1225 &D*K
3lv6A, 3lv6BThe Mutant I218f Of Orotidine 5'-Monoph 4.1.1.232.9e-0622.2221 &D*K
3li1A, 3li1B, 3m47A, 3m47BThe Mutant I218a Of Orotidine 5'-Monoph 4.1.1.232.9e-0622.2221 &D*K
3sizA, 3sizB, 3sy5A, 3sy5BThe Mutant S127a Of Orotidine 5'-Monopho4.1.1.233.5e-0621.8225 &D*K
1km1A, 1km1BOrotidine Monophosphate Decarboxylase Mu4.1.1.233.9e-0621.8225 &D*K
3llfA, 3llfBThe Mutant S127p Of Orotidine 5'-Monoph 4.1.1.234.1e-0621.8225 &D*K
3nq7A, 3nq7BThe Mutant F71a Of Orotidine 5'-Monophos4.1.1.234.1e-0623.1225 &D*K
3nqfA, 3nqfB, 3pbyA, 3pbyBThe Mutant L123s Of Orotidine 5'-Monopho4.1.1.234.1e-0621.8225 &D*K
3qmrA, 3qmrBThe Mutant R160a,V182a Of Orotidine 5'- 4.1e-0623.1225 &D*K
3rluA, 3rluBThe Mutant K82a Of Orotidine 5'-Monophos4.9e-0623.9226 &D*K
3lldA, 3lldBThe Mutant S127g Of Orotidine 5'-Monoph 4.1.1.234.9e-0621.8225 &D*K
3nqeA, 3nqeB, 3pbwA, 3pbwBThe Mutant L123n Of Orotidine 5'-Monopho4.1.1.234.9e-0621.8225 &D*K
3lhzA, 3lhzB, 3m44A, 3m44BThe Mutant V201a Of Orotidine 5'-Monoph 4.1.1.235.8e-0622.7225 &D*K
3qmsA, 3qmsBThe Mutant T159v,V182a,Y206f Of Orotidin5.8e-0623.1225 &D*K
3lhuA, 3lhuBThe Mutant I199f Of Orotidine 5'-Monoph 4.1.1.235.8e-0622.7225 &D*K
3qezA, 3qezBThe Mutant T159v,V182a Of Orotidine 5'- 5.8e-0623.1225 &D*K
3qmtA, 3qmtBThe Mutant V182a,Y206f Of Orotidine 5'- 5.8e-0623.1225 &D*K
3lhwA, 3lhwB, 3m41A, 3m41BThe Mutant V182a Of Orotidine 5'-Monoph 4.1.1.235.8e-0623.1225 &D*K
3lhyA, 3lhyB, 3m43A, 3m43BThe Mutant I199a Of Orotidine 5'-Monoph 4.1.1.236.8e-0623.1225 &D*K
3lhtA, 3lhtBThe Mutant V201f Of Orotidine 5'-Monoph 4.1.1.236.8e-0622.7225 &D*K
3g1yA, 3g1yB, 3g22A, 3g22B, 3g24A, 3g24BThe Mutant D70n Of Orotidine 5'- Monopho4.1.1.236.8e-0622.7225 &N*K
3ltyA, 3ltyB, 3m5zA, 3m5zBThe Mutant V182a,I218a Of Orotidine 5'- 4.1.1.236.8e-0622.2221 &D*K
1km0A, 1km0B, 1km0C, 1km0DOrotidine Monophosphate Decarboxylase Mu4.1.1.237.6e-0622.7225 &N*K
1km5AOdcase Mutant D75n Complexed With 6-Azau4.1.1.237.6e-0622.7225 &D*K
2zz4A, 2zz4BCovalent Complex Of Orotidine Monophosph4.1.1.237.8e-0622.7225 &D*K
1km3AOdcase Mutant K42a Complexed With 6-azau4.1.1.238.9e-0622.7225 &D*K
1km4AOdcase Mutant K72a Complexed With Ump4.1.1.238.9e-0622.7225 &D*A
2zz2A, 2zz2B, 2zz7AOrotidine Monophosphate Decarboxylase K74.1.1.239.2e-0622.7225 &D*A
3li0A, 3li0BThe Mutant R203a Of Orotidine 5'-Monoph 4.1.1.231.1e-0522.7225 &D*K
3g1sA, 3g1sB, 3g1vA, 3g1vB, 3g1xA, 3g1xBThe Mutant D70g Of Orotidine 5'- Monopho4.1.1.231.1e-0522.7225 &G*K
3lv5A, 3lv5BThe Mutant I199e Of Orotidine 5'-Monoph 4.1.1.231.1e-0522.7225 &D*K
1klyAOrotidine Monophosphate Decarboxylase D74.1.1.231.2e-0522.7225 &G*K
3m1zA, 3m1zB, 3m5yA, 3m5yBThe Mutant V182a.V201a Of Orotidine 5'- 4.1.1.231.3e-0522.7225 &D*K
1klzAOrotidine Monophosphate Decarboxylase Mu4.1.1.231.5e-0522.7225 &A*K
2zz3A, 2zz3BCovalent Complex Of Orotidine Monophosph4.1.1.231.5e-0522.7225 &A*K
3ltsA, 3ltsB, 3m5xA, 3m5xBThe Mutant V182a,I199a Of Orotidine 5'- 4.1.1.231.6e-0523.1225 &D*K
3nq6A, 3nq6BThe Mutant P180a Of Orotidine 5'-Monopho4.1.1.231.6e-0522.7225 &D*K
3lhvA, 3lhvB, 3lhvC, 3lhvDThe Mutant V182a.I199a.V201a Of Orotidi 4.1.1.231.6e-0523.1225 &D*K
2qcdA, 2qceAThe Orotidine-5'-Monophosphate Decarboxy2.4.2.10, 4.1.1.231.9e-0525.1239 &D*K
2qccA, 2qccB, 2qcdB, 2qcgA, 2qcgB, 2qchA, 2qchB, 2qcnA, 2qcnB, 3ewzA, 3ewzB, 3ewzC, 3ewzD, 3ex1A, 3ex1B, 3ex2A, 3ex2B, 3ex3A, 3ex3B, 3ex4A, 3l0kA, 3l0kB, 3l0nA, 3l0nBThe Orotidine-5'-monophosphate Decarboxy2.4.2.10, 4.1.1.231.9e-0525.5239 &D*K
2jgyA, 2jgyB, 2v30A, 2v30BThe Human Orotidine-5'-Decarboxylase Dom2.4.2.10, 4.1.1.232.1e-0525.5239 &D*K
3g3mA, 3mi2A, 3mi2BHuman Orotidine 5'-Monophosphate Decarbo2.4.2.10, 4.1.1.232.1e-0525.1239 &D*K
3bk0A, 3bk0B, 3dbpA, 3dbpB, 3mo7AHuman Orotidine 5'-Monophosphate Decarbo2.4.2.10, 4.1.1.232.1e-0525.5239 &D*K
2p1fAHuman Ump Synthase (c-terminal Domain-or2.4.2.10, 4.1.1.232.2e-0525.1239 &D*K
2eawA, 2eawB, 3bggA, 3bgjA, 3bgjBHuman Ump Synthase (C-Terminal Domain- O2.4.2.10, 4.1.1.232.2e-0525.5239 &D*K
3bvjA, 3bvjB, 3g3dA, 3g3dB, 3mw7A, 3mw7B, 4hibA, 4hibB, 4hkpA, 4hkpBHuman Orotidine 5'-monophosphate Decarbo2.4.2.10, 4.1.1.232.4e-0525.5239 &D*K
1loqAOrotidine Monophosphate Decarboxylase Co4.1.1.233.1e-0522.7225 &D*K
3sguAMethanothermobacter Thermautotrophicus O3.4e-0522.7225 &D*K
1km6AOdcase Mutant D70ak72a Complexed With Om4.1.1.234.8e-0522.2225 &A*A
2zz5A, 2zz5BOrotidine Monophosphate Deacarboxylase D4.1.1.234.9e-0522.2225 &A*A
2qcmA, 2qcfAThe Orotidine-5'-Monophosphate Decarboxy2.4.2.10, 4.1.1.235.1e-0524.7239 &N*K
2qcmA, 2qcfAThe Orotidine-5'-Monophosphate Decarboxy2.4.2.10, 4.1.1.235.1e-0525.1239 &N*K
3ewxA, 3ewyAK314a Mutant Of Human Orotidyl-5'-Monoph2.4.2.10, 4.1.1.236e-0524.7239 &D*A
1losA, 1losB, 1losC, 1losDOrotidine Monophosphate Decarboxylase Mu4.1.1.236.9e-0522.7225 &D*K

Proteins identified as mutant are highlighted in maroon. Conservative changes in active site residues, e.g. &K, are marked in green. Non-conservative changes to active site residues (&A) are highlighted in red. Library sequence residues identical to MACie active site residues are shown in grey.

Likewise, E.C. numbers identical to the MACiE protein are shown in grey; differences in black.


Homologs in PDB for MACiE ID:


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