SitesBLAST
Comparing Echvi_1295 FitnessBrowser__Cola:Echvi_1295 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)
P00861 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Escherichia coli (strain K12)
34% identity, 94% coverage: 15:398/410 of query aligns to 17:411/420 of P00861
- K54 (= K57) modified: N6-(pyridoxal phosphate)lysine
- G227 (= G227) binding
- EPGR 268:271 (≠ EPGK 268:271) binding
- Y378 (= Y365) binding
1ko0A Crystal structure of a d,l-lysine complex of diaminopimelate decarboxylase
34% identity, 94% coverage: 15:398/410 of query aligns to 16:410/419 of 1ko0A
- binding d-lysine: K53 (= K57), T156 (≠ V157), H190 (= H191), Y310 (= Y311), Y377 (= Y365)
- binding lysine: K53 (= K57), R270 (≠ K271), R306 (= R307), Y310 (= Y311), Y377 (= Y365)
- binding pyridoxal-5'-phosphate: A51 (= A55), K53 (= K57), H190 (= H191), G226 (= G227), E267 (= E268), P268 (= P269), G269 (= G270), R270 (≠ K271), Y377 (= Y365)
1knwA Crystal structure of diaminopimelate decarboxylase
34% identity, 94% coverage: 15:398/410 of query aligns to 16:410/421 of 1knwA
Q9X1K5 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
32% identity, 95% coverage: 15:403/410 of query aligns to 4:382/386 of Q9X1K5
2yxxA Crystal structure analysis of diaminopimelate decarboxylate (lysa)
32% identity, 95% coverage: 15:403/410 of query aligns to 3:381/385 of 2yxxA
- active site: K45 (= K57), H178 (= H191), E245 (= E268)
- binding pyridoxal-5'-phosphate: K45 (= K57), D64 (= D76), H178 (= H191), S181 (= S194), G213 (= G227), E245 (= E268), G247 (= G270), R248 (≠ K271), Y342 (= Y365)
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)
31% identity, 99% coverage: 3:406/410 of query aligns to 13:432/438 of Q58497
- K73 (= K57) modified: N6-(pyridoxal phosphate)lysine
- S217 (= S194) binding
- G254 (= G227) binding
- EPGR 294:297 (≠ EPGK 268:271) binding
- Y391 (= Y365) binding
1tufA Crystal structure of diaminopimelate decarboxylase from m. Jannaschi (see paper)
31% identity, 99% coverage: 3:406/410 of query aligns to 9:428/434 of 1tufA
1twiA Crystal structure of diaminopimelate decarboxylase from m. Jannaschii in co-complex with l-lysine (see paper)
31% identity, 99% coverage: 3:406/410 of query aligns to 9:428/434 of 1twiA
- active site: K69 (= K57), H210 (= H191), E290 (= E268)
- binding lysine: S213 (= S194), R293 (≠ K271), R329 (= R307), Y333 (= Y311), Y387 (= Y365)
- binding pyridoxal-5'-phosphate: A67 (= A55), K69 (= K57), D88 (= D76), N111 (≠ T99), H210 (= H191), S213 (= S194), G250 (= G227), E290 (= E268), G292 (= G270), R293 (≠ K271), Y387 (= Y365)
4xg1B Psychromonas ingrahamii diaminopimelate decarboxylase with llp
34% identity, 96% coverage: 10:403/410 of query aligns to 13:411/418 of 4xg1B
- active site: K60 (= K57), H199 (= H191), E273 (= E268)
- binding (2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid: K60 (= K57), D79 (= D76), H199 (= H191), S202 (= S194), G239 (= G227), E273 (= E268), G275 (= G270), R276 (≠ K271), R310 (= R307), Y314 (= Y311), C345 (= C337), E346 (= E338), Y373 (= Y365)
- binding propane: A35 (≠ Q32), E38 (≠ L35), E206 (≠ D198), I207 (≠ A199), A208 (≠ E200)
B4XMC6 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Helicobacter pylori (Campylobacter pylori) (see paper)
33% identity, 93% coverage: 22:403/410 of query aligns to 11:396/405 of B4XMC6
- K46 (= K57) modified: N6-(pyridoxal phosphate)lysine
- I148 (= I155) 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 (= G227) binding
- EPGR 259:262 (≠ EPGK 268:271) binding
- Y358 (= Y365) binding
3c5qA Crystal structure of diaminopimelate decarboxylase (i148l mutant) from helicobacter pylori complexed with l-lysine
34% identity, 93% coverage: 22:403/410 of query aligns to 9:388/394 of 3c5qA
- active site: K44 (= K57), H183 (= H191), E257 (= E268)
- binding lysine: L146 (≠ I155), R260 (≠ K271), R294 (= R307), Y298 (= Y311), Y351 (= Y365)
- binding pyridoxal-5'-phosphate: K44 (= K57), D63 (= D76), H183 (= H191), S186 (= S194), G223 (= G227), E257 (= E268), P258 (= P269), G259 (= G270), R260 (≠ K271), Y351 (= Y365)
6n2aA Meso-diaminopimelate decarboxylase from arabidopsis thaliana (isoform 1)
30% identity, 92% coverage: 25:403/410 of query aligns to 31:417/422 of 6n2aA
- binding lysine: K63 (= K57), R281 (≠ K271), R317 (= R307), Y321 (= Y311), C349 (= C337), E350 (= E338), Y378 (= Y365)
- binding pyridoxal-5'-phosphate: K63 (= K57), H202 (= H191), S205 (= S194), G242 (= G227), E278 (= E268), G280 (= G270), R281 (≠ K271), Y378 (= Y365)
4xg1A Psychromonas ingrahamii diaminopimelate decarboxylase with llp
32% identity, 98% coverage: 4:403/410 of query aligns to 1:386/393 of 4xg1A
- active site: K55 (= K57), H178 (= H191), E246 (= E268)
- binding (2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid: K55 (= K57), D74 (= D76), S97 (≠ T99), H178 (= H191), S181 (= S194), G216 (= G227), E246 (= E268), G248 (= G270), R249 (≠ K271), R285 (= R307), Y289 (= Y311), C320 (= C337), E321 (= E338), Y348 (= Y365)
- binding propane: S121 (≠ N122), I122 (= I123)
1hkvA Mycobacterium diaminopimelate dicarboxylase (lysa) (see paper)
28% identity, 97% coverage: 10:406/410 of query aligns to 25:445/446 of 1hkvA
- binding lysine: E375 (= E338), S376 (≠ T339)
- binding pyridoxal-5'-phosphate: A69 (= A55), K71 (= K57), R160 (= R142), H210 (= H189), H212 (= H191), G256 (= G226), G257 (= G227), E299 (= E268), G301 (= G270), R302 (≠ K271), Y404 (= Y365)
P9WIU7 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
28% identity, 97% coverage: 10:406/410 of query aligns to 26:446/447 of P9WIU7
- K72 (= K57) modified: N6-(pyridoxal phosphate)lysine
- C93 (≠ V78) modified: Interchain (with C-375)
- G258 (= G227) binding
- EPGR 300:303 (≠ EPGK 268:271) binding
- C375 (= C337) modified: Interchain (with C-72)
- Y405 (= Y365) binding
5x7nA Crystal structure of meso-diaminopimelate decarboxylase (dapdc) from corynebacterium glutamicum (see paper)
29% identity, 96% coverage: 10:402/410 of query aligns to 27:439/442 of 5x7nA
- binding lysine: K73 (= K57), R341 (= R307), Y345 (= Y311), Y402 (= Y365), M406 (= M369)
- binding pyridoxal-5'-phosphate: K73 (= K57), H115 (≠ T99), H214 (= H191), G254 (= G226), G255 (= G227), E297 (= E268), G299 (= G270), R300 (≠ K271), Y402 (= Y365)
5x7mA Crystal structure of meso-diaminopimelate decarboxylase (dapdc) from corynebacterium glutamicum (see paper)
29% identity, 96% coverage: 10:402/410 of query aligns to 27:439/443 of 5x7mA
8d5rA Structure of y430f d-ornithine/d-lysine decarboxylase complex with d- ornithine (see paper)
26% identity, 97% coverage: 11:406/410 of query aligns to 33:456/461 of 8d5rA
- binding n~2~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-d-ornithine: A78 (= A55), K80 (= K57), H210 (= H191), D213 (≠ S194), G251 (= G227), E299 (= E268), G301 (= G270), R302 (≠ K271), Y414 (= Y365)
- binding 1,4-diaminobutane: Q350 (≠ M309), H351 (≠ M310), D353 (= D312)
8d5dA Structure of y430f d-ornithine/d-lysine decarboxylase complex with d- arginine (see paper)
26% identity, 97% coverage: 11:406/410 of query aligns to 32:454/458 of 8d5dA
- binding (E)-N~2~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-D-arginine: K79 (= K57), H208 (= H191), D211 (≠ S194), G249 (= G227), E297 (= E268), G299 (= G270), R300 (≠ K271), D346 (≠ R307), F350 (≠ Y311), C377 (= C337), D378 (≠ E338), Y412 (= Y365)
8d88A Structure of y430f d-ornithine/d-lysine decarboxylase complex with d- lysine (see paper)
26% identity, 97% coverage: 11:406/410 of query aligns to 33:458/461 of 8d88A
- binding pentane-1,5-diamine: Q352 (≠ M309), H353 (≠ M310), D355 (= D312)
- binding N~2~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-D-lysine: A78 (= A55), K80 (= K57), H212 (= H191), D215 (≠ S194), G253 (= G227), E301 (= E268), G303 (= G270), R304 (≠ K271), Y416 (= Y365)
Query Sequence
>Echvi_1295 FitnessBrowser__Cola:Echvi_1295
MTIDNQQYQVQGVPLLDIASEYGTPVYVYDGQKILDQVATLQNAFSSVNLKIKYATKALS
NINILKLMKKAGTGVDAVSIEEVKLCLHVGYEPSEIMFTPNCVAFEEIQEAVDLGVMINI
DNIPMLEHFGTYYGNSVPLCIRLNPHILAGGNAKISVGHIDSKFGISILQLKHVLKIVEV
HNLKVAGLHVHTGSDILDAEVFLKGAEILFDAAKEFKDLQFLDFGGGFKVGYKEGDITTD
MVEVGRKVSAAFKEFCKNYGRELEIWFEPGKFLVSECGYLLVNANVVKSTPASTFIGVDS
GLNHLIRPMMYDAYHGVENISRVTGPDRVYTIVGYICETDTIAADRKLKEVKEGDVLAIK
NAGAYGFSMASNYNSRLRPAEVLVLDGKAHLIRARESFEDILRHQIDIGL
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory