SitesBLAST
Comparing WP_011767376.1 NCBI__GCF_000061505.1:WP_011767376.1 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
53% identity, 95% coverage: 21:424/424 of query aligns to 11:417/418 of 4xg1B
- active site: K60 (= K70), H199 (= H209), E273 (= E283)
- binding (2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid: K60 (= K70), D79 (= D89), H199 (= H209), S202 (= S212), G239 (= G249), E273 (= E283), G275 (= G285), R276 (= R286), R310 (= R322), Y314 (= Y326), C345 (= C352), E346 (= E353), Y373 (= Y380)
- binding propane: A35 (= A45), E38 (≠ T48), E206 (≠ D216), I207 (≠ P217), A208 (= A218)
4xg1A Psychromonas ingrahamii diaminopimelate decarboxylase with llp
49% identity, 95% coverage: 21:424/424 of query aligns to 9:392/393 of 4xg1A
- active site: K55 (= K70), H178 (= H209), E246 (= E283)
- binding (2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid: K55 (= K70), D74 (= D89), S97 (= S112), H178 (= H209), S181 (= S212), G216 (= G249), E246 (= E283), G248 (= G285), R249 (= R286), R285 (= R322), Y289 (= Y326), C320 (= C352), E321 (= E353), Y348 (= Y380)
- binding propane: S121 (= S136), I122 (≠ A137)
B4XMC6 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Helicobacter pylori (Campylobacter pylori) (see paper)
44% identity, 91% coverage: 31:417/424 of query aligns to 7:395/405 of B4XMC6
- K46 (= K70) modified: N6-(pyridoxal phosphate)lysine
- I148 (= I172) 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 (= G249) binding pyridoxal 5'-phosphate
- EPGR 259:262 (= EPGR 283:286) binding pyridoxal 5'-phosphate
- Y358 (= Y380) binding pyridoxal 5'-phosphate
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)
42% identity, 93% coverage: 31:423/424 of query aligns to 28:438/438 of Q58497
- K73 (= K70) modified: N6-(pyridoxal phosphate)lysine
- S217 (= S212) binding pyridoxal 5'-phosphate
- G254 (= G249) binding pyridoxal 5'-phosphate
- EPGR 294:297 (= EPGR 283:286) binding pyridoxal 5'-phosphate
- Y391 (= Y380) binding pyridoxal 5'-phosphate
1twiA Crystal structure of diaminopimelate decarboxylase from m. Jannaschii in co-complex with l-lysine (see paper)
42% identity, 93% coverage: 31:423/424 of query aligns to 24:434/434 of 1twiA
- active site: K69 (= K70), H210 (= H209), E290 (= E283)
- binding lysine: S213 (= S212), R293 (= R286), R329 (= R322), Y333 (= Y326), Y387 (= Y380)
- binding pyridoxal-5'-phosphate: A67 (= A68), K69 (= K70), D88 (= D89), N111 (≠ S112), H210 (= H209), S213 (= S212), G250 (= G249), E290 (= E283), G292 (= G285), R293 (= R286), Y387 (= Y380)
1tufA Crystal structure of diaminopimelate decarboxylase from m. Jannaschi (see paper)
42% identity, 93% coverage: 31:423/424 of query aligns to 24:434/434 of 1tufA
3c5qA Crystal structure of diaminopimelate decarboxylase (i148l mutant) from helicobacter pylori complexed with l-lysine
44% identity, 91% coverage: 31:417/424 of query aligns to 5:387/394 of 3c5qA
- active site: K44 (= K70), H183 (= H209), E257 (= E283)
- binding lysine: L146 (≠ I172), R260 (= R286), R294 (= R322), Y298 (= Y326), Y351 (= Y380)
- binding pyridoxal-5'-phosphate: K44 (= K70), D63 (= D89), H183 (= H209), S186 (= S212), G223 (= G249), E257 (= E283), P258 (= P284), G259 (= G285), R260 (= R286), Y351 (= Y380)
Q9X1K5 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
40% identity, 91% coverage: 28:412/424 of query aligns to 4:376/386 of Q9X1K5
- G214 (= G249) binding pyridoxal 5'-phosphate
- EIGR 246:249 (≠ EPGR 283:286) binding pyridoxal 5'-phosphate
- Y343 (= Y380) binding pyridoxal 5'-phosphate
2yxxA Crystal structure analysis of diaminopimelate decarboxylate (lysa)
40% identity, 91% coverage: 28:412/424 of query aligns to 3:375/385 of 2yxxA
- active site: K45 (= K70), H178 (= H209), E245 (= E283)
- binding pyridoxal-5'-phosphate: K45 (= K70), D64 (= D89), H178 (= H209), S181 (= S212), G213 (= G249), E245 (= E283), G247 (= G285), R248 (= R286), Y342 (= Y380)
6n2aA Meso-diaminopimelate decarboxylase from arabidopsis thaliana (isoform 1)
35% identity, 89% coverage: 38:414/424 of query aligns to 31:413/422 of 6n2aA
- binding lysine: K63 (= K70), R281 (= R286), R317 (= R322), Y321 (= Y326), C349 (= C352), E350 (= E353), Y378 (= Y380)
- binding pyridoxal-5'-phosphate: K63 (= K70), H202 (= H209), S205 (= S212), G242 (= G249), E278 (= E283), G280 (= G285), R281 (= R286), Y378 (= Y380)
1hkvA Mycobacterium diaminopimelate dicarboxylase (lysa) (see paper)
35% identity, 98% coverage: 5:420/424 of query aligns to 7:444/446 of 1hkvA
- binding lysine: E375 (= E353), S376 (= S354)
- binding pyridoxal-5'-phosphate: A69 (= A68), K71 (= K70), R160 (= R159), H210 (≠ A207), H212 (= H209), G256 (= G248), G257 (= G249), E299 (= E283), G301 (= G285), R302 (= R286), Y404 (= Y380)
P9WIU7 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
35% identity, 98% coverage: 5:420/424 of query aligns to 8:445/447 of P9WIU7
- K72 (= K70) modified: N6-(pyridoxal phosphate)lysine
- C93 (≠ V91) modified: Interchain (with C-375)
- G258 (= G249) binding pyridoxal 5'-phosphate
- EPGR 300:303 (= EPGR 283:286) binding pyridoxal 5'-phosphate
- C375 (= C352) modified: Interchain (with C-72)
- Y405 (= Y380) binding pyridoxal 5'-phosphate
5x7nA Crystal structure of meso-diaminopimelate decarboxylase (dapdc) from corynebacterium glutamicum (see paper)
35% identity, 93% coverage: 26:420/424 of query aligns to 30:442/442 of 5x7nA
- binding lysine: K73 (= K70), R341 (= R322), Y345 (= Y326), Y402 (= Y380), M406 (= M384)
- binding pyridoxal-5'-phosphate: K73 (= K70), H115 (≠ S112), H214 (= H209), G254 (= G248), G255 (= G249), E297 (= E283), G299 (= G285), R300 (= R286), Y402 (= Y380)
5x7mA Crystal structure of meso-diaminopimelate decarboxylase (dapdc) from corynebacterium glutamicum (see paper)
35% identity, 93% coverage: 26:420/424 of query aligns to 30:442/443 of 5x7mA
1knwA Crystal structure of diaminopimelate decarboxylase
33% identity, 91% coverage: 28:413/424 of query aligns to 16:410/421 of 1knwA
1ko0A Crystal structure of a d,l-lysine complex of diaminopimelate decarboxylase
33% identity, 91% coverage: 28:413/424 of query aligns to 16:410/419 of 1ko0A
- binding d-lysine: K53 (= K70), T156 (= T174), H190 (= H209), Y310 (= Y326), Y377 (= Y380)
- binding lysine: K53 (= K70), R270 (= R286), R306 (= R322), Y310 (= Y326), Y377 (= Y380)
- binding pyridoxal-5'-phosphate: A51 (= A68), K53 (= K70), H190 (= H209), G226 (= G249), E267 (= E283), P268 (= P284), G269 (= G285), R270 (= R286), Y377 (= Y380)
P00861 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Escherichia coli (strain K12)
33% identity, 91% coverage: 28:413/424 of query aligns to 17:411/420 of P00861
- K54 (= K70) modified: N6-(pyridoxal phosphate)lysine
- G227 (= G249) binding pyridoxal 5'-phosphate
- EPGR 268:271 (= EPGR 283:286) binding pyridoxal 5'-phosphate
- Y378 (= Y380) binding pyridoxal 5'-phosphate
8d5rA Structure of y430f d-ornithine/d-lysine decarboxylase complex with d- ornithine (see paper)
29% identity, 93% coverage: 21:416/424 of query aligns to 30:451/461 of 8d5rA
- binding n~2~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-d-ornithine: A78 (= A68), K80 (= K70), H210 (= H209), D213 (≠ S212), G251 (= G249), E299 (= E283), G301 (= G285), R302 (= R286), Y414 (= Y380)
- binding 1,4-diaminobutane: Q350 (≠ A324), H351 (≠ L325), D353 (= D327)
8d4iA Structure of y430f d-ornithine/d-lysine decarboxylase complex with putrescine (see paper)
29% identity, 93% coverage: 21:416/424 of query aligns to 30:453/462 of 8d4iA
8d88A Structure of y430f d-ornithine/d-lysine decarboxylase complex with d- lysine (see paper)
29% identity, 93% coverage: 21:416/424 of query aligns to 30:453/461 of 8d88A
- binding pentane-1,5-diamine: Q352 (≠ A324), H353 (≠ L325), D355 (= D327)
- binding N~2~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-D-lysine: A78 (= A68), K80 (= K70), H212 (= H209), D215 (≠ S212), G253 (= G249), E301 (= E283), G303 (= G285), R304 (= R286), Y416 (= Y380)
Query Sequence
>WP_011767376.1 NCBI__GCF_000061505.1:WP_011767376.1
MSSTASAAYPLPSLSDGPAGLMLEEVPLATLAERFGTPTYVYSRAALTAAFRDWQAALAG
RRSLVCYAVKANANLGVLSVFAQLGAGFDIVSGGELARVIAAGGRADRVVFSGVGKSRAE
MRQALAAGIRCFNVESAPELERLNEVAGELGQRAPIALRVNPDVDPKTHPYISTGLKSNK
FGVAFGEALELYRRAATLPHLRISGIACHIGSQLLDPAPVAEAAAKVLGLVDQLSAEGIV
LDHIDLGGGLGIRYRDETPPSVAAYLAPLLAAFGDRREEICFEPGRSLVGNAGLLLTRVE
YLKHGEEKNFAIVDAAMNDLARPALYDAYHEAVAVCRSDAPRQRYEIVGPICESGDFLAH
DRELALRDGDLVALLSAGAYGMTMSSNYNTRPRAAEVMVDGGQVHLVRERETVEALYAGE
HLLP
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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