SitesBLAST
Comparing WP_106719045.1 NCBI__GCF_003010935.1:WP_106719045.1 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
48% identity, 97% coverage: 2:411/421 of query aligns to 1:409/418 of 4xg1B
- active site: K60 (= K60), H199 (= H199), E273 (= E275)
- binding (2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid: K60 (= K60), D79 (= D79), H199 (= H199), S202 (= S202), G239 (= G239), E273 (= E275), G275 (= G277), R276 (= R278), R310 (= R314), Y314 (= Y318), C345 (= C346), E346 (= E347), Y373 (= Y375)
- binding propane: A35 (= A35), E38 (= E38), E206 (≠ D206), I207 (≠ L207), A208 (≠ E208)
4xg1A Psychromonas ingrahamii diaminopimelate decarboxylase with llp
45% identity, 97% coverage: 2:411/421 of query aligns to 1:384/393 of 4xg1A
- active site: K55 (= K60), H178 (= H199), E246 (= E275)
- binding (2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid: K55 (= K60), D74 (= D79), S97 (= S102), H178 (= H199), S181 (= S202), G216 (= G239), E246 (= E275), G248 (= G277), R249 (= R278), R285 (= R314), Y289 (= Y318), C320 (= C346), E321 (= E347), Y348 (= Y375)
- binding propane: S121 (= S126), I122 (≠ E127)
B4XMC6 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Helicobacter pylori (Campylobacter pylori) (see paper)
43% identity, 92% coverage: 27:415/421 of query aligns to 13:398/405 of B4XMC6
- K46 (= K60) modified: N6-(pyridoxal phosphate)lysine
- I148 (= I162) 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 (= G239) binding pyridoxal 5'-phosphate
- EPGR 259:262 (= EPGR 275:278) binding pyridoxal 5'-phosphate
- Y358 (= Y375) binding pyridoxal 5'-phosphate
3c5qA Crystal structure of diaminopimelate decarboxylase (i148l mutant) from helicobacter pylori complexed with l-lysine
44% identity, 92% coverage: 27:415/421 of query aligns to 11:390/394 of 3c5qA
- active site: K44 (= K60), H183 (= H199), E257 (= E275)
- binding lysine: L146 (≠ I162), R260 (= R278), R294 (= R314), Y298 (= Y318), Y351 (= Y375)
- binding pyridoxal-5'-phosphate: K44 (= K60), D63 (= D79), H183 (= H199), S186 (= S202), G223 (= G239), E257 (= E275), P258 (= P276), G259 (= G277), R260 (= R278), Y351 (= Y375)
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)
38% identity, 98% coverage: 7:418/421 of query aligns to 14:434/438 of Q58497
- K73 (= K60) modified: N6-(pyridoxal phosphate)lysine
- S217 (= S202) binding pyridoxal 5'-phosphate
- G254 (= G239) binding pyridoxal 5'-phosphate
- EPGR 294:297 (= EPGR 275:278) binding pyridoxal 5'-phosphate
- Y391 (= Y375) binding pyridoxal 5'-phosphate
1twiA Crystal structure of diaminopimelate decarboxylase from m. Jannaschii in co-complex with l-lysine (see paper)
38% identity, 98% coverage: 7:418/421 of query aligns to 10:430/434 of 1twiA
- active site: K69 (= K60), H210 (= H199), E290 (= E275)
- binding lysine: S213 (= S202), R293 (= R278), R329 (= R314), Y333 (= Y318), Y387 (= Y375)
- binding pyridoxal-5'-phosphate: A67 (= A58), K69 (= K60), D88 (= D79), N111 (≠ S102), H210 (= H199), S213 (= S202), G250 (= G239), E290 (= E275), G292 (= G277), R293 (= R278), Y387 (= Y375)
1tufA Crystal structure of diaminopimelate decarboxylase from m. Jannaschi (see paper)
38% identity, 98% coverage: 7:418/421 of query aligns to 10:430/434 of 1tufA
6n2aA Meso-diaminopimelate decarboxylase from arabidopsis thaliana (isoform 1)
37% identity, 96% coverage: 8:410/421 of query aligns to 10:414/422 of 6n2aA
- binding lysine: K63 (= K60), R281 (= R278), R317 (= R314), Y321 (= Y318), C349 (= C346), E350 (= E347), Y378 (= Y375)
- binding pyridoxal-5'-phosphate: K63 (= K60), H202 (= H199), S205 (= S202), G242 (= G239), E278 (= E275), G280 (= G277), R281 (= R278), Y378 (= Y375)
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, 92% coverage: 21:409/421 of query aligns to 7:379/386 of Q9X1K5
- G214 (= G239) binding pyridoxal 5'-phosphate
- EIGR 246:249 (≠ EPGR 275:278) binding pyridoxal 5'-phosphate
- Y343 (= Y375) binding pyridoxal 5'-phosphate
2yxxA Crystal structure analysis of diaminopimelate decarboxylate (lysa)
36% identity, 92% coverage: 21:409/421 of query aligns to 6:378/385 of 2yxxA
- active site: K45 (= K60), H178 (= H199), E245 (= E275)
- binding pyridoxal-5'-phosphate: K45 (= K60), D64 (= D79), H178 (= H199), S181 (= S202), G213 (= G239), E245 (= E275), G247 (= G277), R248 (= R278), Y342 (= Y375)
1hkvA Mycobacterium diaminopimelate dicarboxylase (lysa) (see paper)
33% identity, 97% coverage: 9:415/421 of query aligns to 21:444/446 of 1hkvA
- binding lysine: E375 (= E347), S376 (≠ T348)
- binding pyridoxal-5'-phosphate: A69 (= A58), K71 (= K60), R160 (= R149), H210 (≠ D197), H212 (= H199), G256 (= G238), G257 (= G239), E299 (= E275), G301 (= G277), R302 (= R278), Y404 (= Y375)
P9WIU7 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
33% identity, 97% coverage: 9:415/421 of query aligns to 22:445/447 of P9WIU7
- K72 (= K60) modified: N6-(pyridoxal phosphate)lysine
- C93 (≠ V81) modified: Interchain (with C-375)
- G258 (= G239) binding pyridoxal 5'-phosphate
- EPGR 300:303 (= EPGR 275:278) binding pyridoxal 5'-phosphate
- C375 (= C346) modified: Interchain (with C-72)
- Y405 (= Y375) binding pyridoxal 5'-phosphate
8d5rA Structure of y430f d-ornithine/d-lysine decarboxylase complex with d- ornithine (see paper)
30% identity, 98% coverage: 4:415/421 of query aligns to 23:455/461 of 8d5rA
- binding n~2~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-d-ornithine: A78 (= A58), K80 (= K60), H210 (= H199), D213 (≠ S202), G251 (= G239), E299 (= E275), G301 (= G277), R302 (= R278), Y414 (= Y375)
- binding 1,4-diaminobutane: Q350 (≠ T316), H351 (≠ L317), D353 (= D319)
8d5dA Structure of y430f d-ornithine/d-lysine decarboxylase complex with d- arginine (see paper)
30% identity, 98% coverage: 4:415/421 of query aligns to 22:453/458 of 8d5dA
- binding (E)-N~2~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-D-arginine: K79 (= K60), H208 (= H199), D211 (≠ S202), G249 (= G239), E297 (= E275), G299 (= G277), R300 (= R278), D346 (≠ R314), F350 (≠ Y318), C377 (= C346), D378 (≠ E347), Y412 (= Y375)
8d4iA Structure of y430f d-ornithine/d-lysine decarboxylase complex with putrescine (see paper)
30% identity, 98% coverage: 4:415/421 of query aligns to 23:457/462 of 8d4iA
8d88A Structure of y430f d-ornithine/d-lysine decarboxylase complex with d- lysine (see paper)
30% identity, 98% coverage: 4:415/421 of query aligns to 23:457/461 of 8d88A
- binding pentane-1,5-diamine: Q352 (≠ T316), H353 (≠ L317), D355 (= D319)
- binding N~2~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-D-lysine: A78 (= A58), K80 (= K60), H212 (= H199), D215 (≠ S202), G253 (= G239), E301 (= E275), G303 (= G277), R304 (= R278), Y416 (= Y375)
1knwA Crystal structure of diaminopimelate decarboxylase
31% identity, 91% coverage: 26:407/421 of query aligns to 24:409/421 of 1knwA
1ko0A Crystal structure of a d,l-lysine complex of diaminopimelate decarboxylase
31% identity, 91% coverage: 26:407/421 of query aligns to 24:409/419 of 1ko0A
- binding d-lysine: K53 (= K60), T156 (= T164), H190 (= H199), Y310 (= Y318), Y377 (= Y375)
- binding lysine: K53 (= K60), R270 (= R278), R306 (= R314), Y310 (= Y318), Y377 (= Y375)
- binding pyridoxal-5'-phosphate: A51 (= A58), K53 (= K60), H190 (= H199), G226 (= G239), E267 (= E275), P268 (= P276), G269 (= G277), R270 (= R278), Y377 (= Y375)
P00861 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Escherichia coli (strain K12)
31% identity, 91% coverage: 26:407/421 of query aligns to 25:410/420 of P00861
- K54 (= K60) modified: N6-(pyridoxal phosphate)lysine
- G227 (= G239) binding pyridoxal 5'-phosphate
- EPGR 268:271 (= EPGR 275:278) binding pyridoxal 5'-phosphate
- Y378 (= Y375) binding pyridoxal 5'-phosphate
5x7mA Crystal structure of meso-diaminopimelate decarboxylase (dapdc) from corynebacterium glutamicum (see paper)
30% identity, 99% coverage: 2:416/421 of query aligns to 16:443/443 of 5x7mA
Query Sequence
>WP_106719045.1 NCBI__GCF_003010935.1:WP_106719045.1
MNHFGYRDGVLHAEGVSIPDIAKAVGTPFYCYSTATIERHFKVFSAAFADMDTLVAYALK
ANSNQAVLKTLARLGSGADVVSEGEMRRALAAGIPAGKIVFSGVGKKQGEMDFALAAGIH
CFNVESEPELEMLSARAVAAGKIAPVSLRINPDVDAKTHKKISTGKSENKFGIPLAKASA
IYARASLLPGLKVTGVDMHIGSQITDLEPFDNAFRLLAELVAQLQADGHDIKHVDLGGGL
GIPYHFDNNPPPLPDAYAQIVQKHIKPLGLKTIFEPGRLIVGNAGILVTEVIYLKEGDAR
NFVIVDAAMNDLIRPTLYDAFHIMHPVKEPGANAPRIRGDVVGPVCETGDYLGLDRDLPR
PAPGDLIAIGTAGAYGAVQAGTYNTRLLVPEVLVNGDLFHVVRPRTTYDELIGLDSIPEW
L
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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