SitesBLAST
Comparing Ga0059261_2051 FitnessBrowser__Korea:Ga0059261_2051 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
4xg1B Psychromonas ingrahamii diaminopimelate decarboxylase with llp
43% identity, 99% coverage: 2:414/419 of query aligns to 1:415/418 of 4xg1B
- active site: K60 (= K61), H199 (= H200), E273 (= E275)
- binding (2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid: K60 (= K61), D79 (= D80), H199 (= H200), S202 (= S203), G239 (= G240), E273 (= E275), G275 (= G277), R276 (= R278), R310 (= R314), Y314 (= Y318), C345 (= C343), E346 (= E344), Y373 (= Y372)
- binding propane: A35 (= A35), E38 (= E38), E206 (= E207), I207 (≠ L208), A208 (= A209)
4xg1A Psychromonas ingrahamii diaminopimelate decarboxylase with llp
39% identity, 99% coverage: 2:414/419 of query aligns to 1:390/393 of 4xg1A
- active site: K55 (= K61), H178 (= H200), E246 (= E275)
- binding (2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid: K55 (= K61), D74 (= D80), S97 (= S103), H178 (= H200), S181 (= S203), G216 (= G240), E246 (= E275), G248 (= G277), R249 (= R278), R285 (= R314), Y289 (= Y318), C320 (= C343), E321 (= E344), Y348 (= Y372)
- binding propane: S121 (≠ L127), I122 (≠ E128)
B4XMC6 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Helicobacter pylori (Campylobacter pylori) (see paper)
38% identity, 90% coverage: 27:402/419 of query aligns to 13:388/405 of B4XMC6
- K46 (= K61) modified: N6-(pyridoxal phosphate)lysine
- I148 (= I163) mutation to A: Nearly no change in substrate affinity and 47-fold decrease in catalytic activity.; mutation to D: 2-fold decrease in substrate affinity and 235-fold decrease in catalytic activity.; mutation to F: 4-fold increase in substrate affinity and 23-fold decrease in catalytic activity.; mutation to G: Nearly no change in substrate affinity and 235-fold decrease in catalytic activity.; mutation to K: Nearly no change in substrate affinity and 55-fold decrease in catalytic activity.; mutation to L: 13-fold increase in substrate affinity and 40-fold decrease in catalytic activity.
- G225 (= G240) binding pyridoxal 5'-phosphate
- EPGR 259:262 (= EPGR 275:278) binding pyridoxal 5'-phosphate
- Y358 (= Y372) binding pyridoxal 5'-phosphate
1twiA Crystal structure of diaminopimelate decarboxylase from m. Jannaschii in co-complex with l-lysine (see paper)
35% identity, 99% coverage: 2:415/419 of query aligns to 5:430/434 of 1twiA
- active site: K69 (= K61), H210 (= H200), E290 (= E275)
- binding lysine: S213 (= S203), R293 (= R278), R329 (= R314), Y333 (= Y318), Y387 (= Y372)
- binding pyridoxal-5'-phosphate: A67 (= A59), K69 (= K61), D88 (= D80), N111 (≠ S103), H210 (= H200), S213 (= S203), G250 (= G240), E290 (= E275), G292 (= G277), R293 (= R278), Y387 (= Y372)
Q58497 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) (see paper)
35% identity, 98% coverage: 7:415/419 of query aligns to 14:434/438 of Q58497
- K73 (= K61) modified: N6-(pyridoxal phosphate)lysine
- S217 (= S203) binding pyridoxal 5'-phosphate
- G254 (= G240) binding pyridoxal 5'-phosphate
- EPGR 294:297 (= EPGR 275:278) binding pyridoxal 5'-phosphate
- Y391 (= Y372) binding pyridoxal 5'-phosphate
1tufA Crystal structure of diaminopimelate decarboxylase from m. Jannaschi (see paper)
35% identity, 98% coverage: 7:415/419 of query aligns to 10:430/434 of 1tufA
3c5qA Crystal structure of diaminopimelate decarboxylase (i148l mutant) from helicobacter pylori complexed with l-lysine
38% identity, 90% coverage: 27:402/419 of query aligns to 11:380/394 of 3c5qA
- active site: K44 (= K61), H183 (= H200), E257 (= E275)
- binding lysine: L146 (≠ I163), R260 (= R278), R294 (= R314), Y298 (= Y318), Y351 (= Y372)
- binding pyridoxal-5'-phosphate: K44 (= K61), D63 (= D80), H183 (= H200), S186 (= S203), G223 (= G240), E257 (= E275), P258 (= P276), G259 (= G277), R260 (= R278), Y351 (= Y372)
Q9X1K5 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
36% identity, 90% coverage: 26:402/419 of query aligns to 12:374/386 of Q9X1K5
- G214 (= G240) binding pyridoxal 5'-phosphate
- EIGR 246:249 (≠ EPGR 275:278) binding pyridoxal 5'-phosphate
- Y343 (= Y372) binding pyridoxal 5'-phosphate
2yxxA Crystal structure analysis of diaminopimelate decarboxylate (lysa)
36% identity, 90% coverage: 26:402/419 of query aligns to 11:373/385 of 2yxxA
- active site: K45 (= K61), H178 (= H200), E245 (= E275)
- binding pyridoxal-5'-phosphate: K45 (= K61), D64 (= D80), H178 (= H200), S181 (= S203), G213 (= G240), E245 (= E275), G247 (= G277), R248 (= R278), Y342 (= Y372)
6n2aA Meso-diaminopimelate decarboxylase from arabidopsis thaliana (isoform 1)
34% identity, 94% coverage: 1:394/419 of query aligns to 1:400/422 of 6n2aA
- binding lysine: K63 (= K61), R281 (= R278), R317 (= R314), Y321 (= Y318), C349 (= C343), E350 (= E344), Y378 (= Y372)
- binding pyridoxal-5'-phosphate: K63 (= K61), H202 (= H200), S205 (= S203), G242 (= G240), E278 (= E275), G280 (= G277), R281 (= R278), Y378 (= Y372)
P00861 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Escherichia coli (strain K12)
35% identity, 94% coverage: 11:402/419 of query aligns to 12:408/420 of P00861
- K54 (= K61) modified: N6-(pyridoxal phosphate)lysine
- G227 (= G240) binding pyridoxal 5'-phosphate
- EPGR 268:271 (= EPGR 275:278) binding pyridoxal 5'-phosphate
- Y378 (= Y372) binding pyridoxal 5'-phosphate
1ko0A Crystal structure of a d,l-lysine complex of diaminopimelate decarboxylase
35% identity, 94% coverage: 11:402/419 of query aligns to 11:407/419 of 1ko0A