Proteins in PDB homologous to 1xelA

69 proteins (274 PDB structures) with E() < 0.001

Homologs in SwissProt

Acc   E.C. E() % id alen 124
1lrjA, 1nahA, 1naiA, 1udaA, 1udbA, 1xelAE. Coli Udp-Galactose 4-Epimerase Comple5.1.3.21e-144100.0338 &S*Y&K
1kvsAUdp-Galactose 4-Epimerase Complexed With5. &T*Y&K
1kvqAUdp-Galactose 4-Epimerase Complexed With5. &A*Y&K
1kvtAUdp-Galactose 4-Epimerase Complexed With5.1.3.23e-14499.7338 &V*Y&K
2udpA, 2udpB, 1udcAUdp-Galactose 4-Epimerase Complexed With5.1.3.23e-14499.7338 &S*Y&K
1a9zAUdp-Galactose 4-Epimerase Mutant S124aY15. &A*F&K
1kvuAUdp-Galactose 4-Epimerase Complexed With5. &S*F&K
1kvrAUdp-Galactose 4-Epimerase Complexed With5. &A*Y&K
1lrkA, 1lrlAEscherichia Coli Udp-Galactose 4-Epimera5. &S*Y&K
1a9yAUdp-Galactose 4-Epimerase Mutant S124aY15.1.3.21e-14399.1338 &A*F&K
3enkA, 3enkB1.9a Udp-glucose 4-epimerase From Burkho9.9e-7453.9334 &S*Y&K
1hzjA, 1hzjBHuman Udp-Galactose 4-Epimerase: Accommo5. &S*Y&K
1i3kA, 1i3kB, 1i3lA, 1i3lB, 1i3mA, 1i3mB, 1i3nA, 1i3nBMolecular Basis For Severe Epimerase-Def5.1.3.24e-7352.5341 &S*Y&K
1ek5A, 1ek6A, 1ek6BHuman Udp-Galactose 4-Epimerase In Compl5. &S*Y&K
1z45AThe Gal10 Fusion Protein Galactose Mutar5.1.3.2, &S*Y&K
1gy8A, 1gy8B, 1gy8C, 1gy8D, 2cnbA, 2cnbB, 2cnbC, 2cnbDTrypanosoma Brucei Udp-Galactose 4' Epim1.5e-4339.9383 &S*Y&K
2c20A, 2c20B, 2c20C, 2c20D, 2c20E, 2c20FUdp-Glucose 4-Epimerase6.2e-4336.7335 &T*Y&K
2p5uA, 2p5uB, 2p5uC, 2p5uD, 2p5yAThermus Thermophilus Hb8 Udp-Glucose 4- 4.2e-2232.9298 &T*Y&K
1orrA, 1orrB, 1orrC, 1orrDCdp-tyvelose 2-epimerase Complexed With &T*Y&K
3vpsA, 3vpsBA Novel Nad Dependent-Ndp-Hexosamine 5,68.7e-1930.4335 &T*Y&K
1sb8A, 1sb9APseudomonas Aeruginosa Udp-N-Acetylgluco1.1e-1829.4320 &S*Y&K
3rucA, 3rucB, 3rucC, 3rucDSpecific Recognition Of N-Acetylated Sub1.5e-1827.6344 &S*Y&K
3ru7A, 3ru7B, 3ru7C, 3ru7DSpecific Recognition Of N-Acetylated Sub3.3e-1827.2345 &S*Y&K
3ru9A, 3ru9B, 3ru9C, 3ru9D, 3ruaA, 3ruaB, 3ruaC, 3ruaD, 3rudA, 3rudB, 3rudC, 3rudD, 3rueA, 3rueB, 3rueS, 3rueBB, 3rufA, 3rufB, 3rufS, 3rufBB, 3ruhA, 3ruhB, 3ruhC, 3ruhDSpecific Recognition Of N-Acetylated Sub4.5e-1827.3344 &S*Y&K
3lu1A, 3lu1B, 3lu1C, 3lu1DCrystal Structure Analysis Of Wbgu: A Ud4.7e-1827.3344 &S*Y&K
4egbA, 4egbB, 4egbC, 4egbD, 4egbE, 4egbF, 4egbG, 4egbH3.0 Angstrom Resolution Dtdp-Glucose 4,61.1e-1727.1340 &T*Y&K
2hunA, 2hunBHypothetical Protein Ph0414 From Pyrococ5.5e-1729.6335 &T*Y&K
1r6dADesiv Double Mutant (Dtdp-Glucose 4,6- D4.6e-1627.7343 &T*Y&K
1r66ADesiv (Dtdp-Glucose 4,6-Dehydratase) Fro5.4e-1627.7343 &T*Y&K
1g1aA, 1g1aB, 1g1aC, 1g1aD, 1keuA, 1keuB, 1kewA, 1kewBThe Dtdp-D-Glucose 4,6-Dehydratase (Rmlb4.2.1.461.1e-1426.9364 &T*Y&K
3eheA, 3eheBUdp-Glucose 4 Epimerase (Gale-1) From Ar3.4e-1427.1314 &T*Y&K
4ef7A, 4ef7B, 4gllA, 4gllBUdp-Xylose Synthase5.1e-1424.6333 &T*Y&K
2pzkA, 2pzkB, 2pzlA, 2pzlB, 2pzmA, 2pzmBThe Bordetella Bronchiseptica Enzyme Wbm1.1e-1326.5336 &T*Y&K
3icpA, 3ko8AUdp-Galactose 4-Epimerase1.3e-1325.7343 &S*Y&K
2pzjA, 2q1sA, 2q1tA, 2q1uA, 2q1uBThe Bordetella Bronchiseptica Enzyme Wbm5e-1324.6338 &A*Y&K
1bxkA, 1bxkBDtdp-Glucose 4,6-Dehydratase From E. Col4.2.1.466.2e-1328.2355 &T*Y&K
3aw9A, 3aw9B, 3aw9CUdp-Galactose 4-Epimerase Mutant1.1e-1225.6344 &S*Y&K
2b69AHuman Udp-Glucoronic Acid Decarboxylase4.1.1.353.6e-1223.7333 &T*Y&K
1kepA, 1kepB, 1kerA, 1kerB, 1ketA, 1ketB, 1oc2A, 1oc2BThe Dtdp-D-Glucose 4,6-Dehydratase (Rmlb4.2.1.461.4e-1027.2345 &T*Y&K
2q1wA, 2q1wB, 2q1wCThe Bordetella Bronchiseptica Enzyme Wbm8.2e-1025.3312 &T*Y&K
2pk3A, 2pk3BA Gdp-4-Keto-6-Deoxy-D-Mannose Reductase1.4e-0922.7317 &S*Y&K
1t2aA, 1t2aB, 1t2aC, 1t2aDHuman Gdp-D-Mannose 4,6-Dehydratase4.2.1.474.4e-0923.6352 &T*Y&K
1db3AE.Coli Gdp-Mannose 4,6-Dehydratase4.2.1.475.1e-0925.5349 &T*Y&K
3sxpA, 3sxpB, 3sxpC, 3sxpD, 3sxpEHelicobacter Pylori Adp-L-Glycero-D-Mann6.6e-0928.0289 &S*Y&K
2z1mA, 2z1mB, 2z1mC, 2z1mD, 2z95A, 2z95B, 2z95C, 2z95DGdp-D-Mannose Dehydratase From Aquifex A1.1e-0723.3343 &T*Y&K
3m2pA, 3m2pB, 3m2pC, 3m2pD, 3m2pE, 3m2pFThe Udp-N-Acetylglucosamine 4-Epimerase 2.4e-0724.5314 &T*Y&K
1wvgA, 1wvgBCdp-D-Glucose 4,6-Dehydratase From Salmo3.4e-0723.9352 &S*Y&K
1rkxA, 1rkxB, 1rkxC, 1rkxDCrystal Structure At 1.8 Angstrom Of Cdp6.1e-0723.9348 &S*Y&K
1eq2A, 1eq2B, 1eq2C, 1eq2D, 1eq2E, 1eq2F, 1eq2G, 1eq2H, 1eq2I, 1eq2JThe Adp-L-Glycero-D-Mannoheptose 6- Epim5. &S*Y&K
2x6tA, 2x6tB, 2x6tC, 2x6tD, 2x6tE, 2x6tF, 2x6tG, 2x6tH, 2x6tI, 2x6tJ, 2x86A, 2x86B, 2x86C, 2x86D, 2x86E, 2x86F, 2x86G, 2x86H, 2x86I, 2x86J, 2x86K, 2x86L, 2x86M, 2x86N, 2x86O, 2x86P, 2x86Q, 2x86R, 2x86S, 2x86TAgme Bound To Adp-B-Mannose5. &S*F&K
3slgA, 3slgB, 3slgC, 3slgD, 3slgE, 3slgFPbgp3 Protein From Burkholderia Pseudoma3e-0623.5345 &T*Y&K
2c5eA, 2c5eBGdp-Mannose-3', 5' -Epimerase (Arabidops5. &S*Y&K
2c59A, 2c59BGdp-Mannose-3', 5' -Epimerase (Arabidops5. &S*Y&K
2c54A, 2c54BGdp-Mannose-3', 5' -Epimerase (Arabidops5.1.3.181e-0522.6337 &S*Y&R
2c5aA, 2c5aBGdp-Mannose-3', 5' -Epimerase (Arabidops5. &S*F&K
3a1nA, 3a1nB, 3a4vA, 3a4vBL-Threonine Dehydrogenase From Hyperther2.7e-0527.9179 &T*Y&K
2bllAApo-The C-Terminal Decarboxylase Domain, &T*Y&K
3a9wA, 3a9wB, 3ajrA, 3ajrBL-Threonine Bound L-Threonine Dehydrogen4.9e-0527.4179 &T*F&K
1z73AE. Coli Arna Dehydrogenase (decarboxylas1.1.1.305, &T*Y&K
1z74AE.Coli Arna Dehydrogenase (Decarboxylase1.1.1.305, &T*Y&K
1z7bAE.Coli Arna Dehydrogenase (Decarboxylase1.1.1.305, &T*Y&K
1u9jAE. Coli Arna (Pmri) Decarboxylase Domain1.1.1.305, &T*Y&K
1z75AArna Dehydrogenase (decarboxylase) Domai1.1.1.305, &T*Y&K
1bwsAGdp-4-Keto-6-Deoxy-D-Mannose EpimeraseRE1.1.1.2710.000223.8340 &S*Y&K
1z7eA, 1z7eB, 1z7eC, 1z7eD, 1z7eE, 1z7eFFull Length Arna1.1.1.305, &T*Y&K
1e6uAGdp 4-Keto-6-Deoxy-D-Mannose Epimerase R1.1.1.2710.0003122.9340 &S*Y&K
1bsvA, 1fxsA, 1gfsAGdp-Fucose Synthetase From Escherichia C1.1.1.2710.0004923.5340 &S*Y&K
1e7sAGdp 4-Keto-6-Deoxy-D-Mannose Epimerase R1.1.1.2710.0007723.2340 &S*Y&R
1e7qAGdp 4-Keto-6-Deoxy-D-Mannose Epimerase R1.1.1.2710.0008923.2340 &A*Y&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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