SitesBLAST
Comparing WP_012566228.1 NCBI__GCF_000016185.1:WP_012566228.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
1ko0A Crystal structure of a d,l-lysine complex of diaminopimelate decarboxylase
30% identity, 90% coverage: 33:413/422 of query aligns to 8:388/419 of 1ko0A
- binding d-lysine: K53 (= K85), T156 (≠ Y188), H190 (= H223), Y310 (= Y339), Y377 (= Y402)
- binding lysine: K53 (= K85), R270 (≠ D299), R306 (≠ E335), Y310 (= Y339), Y377 (= Y402)
- binding pyridoxal-5'-phosphate: A51 (= A83), K53 (= K85), H190 (= H223), G226 (= G261), E267 (= E296), P268 (= P297), G269 (= G298), R270 (≠ D299), Y377 (= Y402)
1knwA Crystal structure of diaminopimelate decarboxylase
30% identity, 90% coverage: 33:413/422 of query aligns to 8:388/421 of 1knwA
P00861 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Escherichia coli (strain K12)
30% identity, 90% coverage: 33:413/422 of query aligns to 9:389/420 of P00861
- K54 (= K85) modified: N6-(pyridoxal phosphate)lysine
- G227 (= G261) binding pyridoxal 5'-phosphate
- EPGR 268:271 (≠ EPGD 296:299) binding pyridoxal 5'-phosphate
- Y378 (= Y402) binding pyridoxal 5'-phosphate
4xg1B Psychromonas ingrahamii diaminopimelate decarboxylase with llp
26% identity, 92% coverage: 34:421/422 of query aligns to 11:392/418 of 4xg1B
- active site: K60 (= K85), H199 (= H223), E273 (= E296)
- binding (2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid: K60 (= K85), D79 (= D105), H199 (= H223), S202 (≠ A231), G239 (= G261), E273 (= E296), G275 (= G298), R276 (≠ D299), R310 (≠ E335), Y314 (= Y339), C345 (≠ N373), E346 (= E374), Y373 (= Y402)
- binding propane: A35 (≠ P58), E38 (≠ L61), E206 (≠ A235), I207 (≠ W236), A208 (= A237)
6n2aA Meso-diaminopimelate decarboxylase from arabidopsis thaliana (isoform 1)
26% identity, 87% coverage: 51:419/422 of query aligns to 31:395/422 of 6n2aA
- binding lysine: K63 (= K85), R281 (≠ D299), R317 (≠ E335), Y321 (= Y339), C349 (≠ N373), E350 (= E374), Y378 (= Y402)
- binding pyridoxal-5'-phosphate: K63 (= K85), H202 (= H223), S205 (≠ W226), G242 (= G261), E278 (= E296), G280 (= G298), R281 (≠ D299), Y378 (= Y402)
2yxxA Crystal structure analysis of diaminopimelate decarboxylate (lysa)
28% identity, 90% coverage: 41:421/422 of query aligns to 3:361/385 of 2yxxA
- active site: K45 (= K85), H178 (= H223), E245 (= E296)
- binding pyridoxal-5'-phosphate: K45 (= K85), D64 (= D105), H178 (= H223), S181 (≠ W226), G213 (= G261), E245 (= E296), G247 (= G298), R248 (≠ D299), Y342 (= Y402)
Q9X1K5 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
28% identity, 90% coverage: 41:421/422 of query aligns to 4:362/386 of Q9X1K5
- G214 (= G261) binding pyridoxal 5'-phosphate
- EIGR 246:249 (≠ EPGD 296:299) binding pyridoxal 5'-phosphate
- Y343 (= Y402) binding pyridoxal 5'-phosphate
3c5qA Crystal structure of diaminopimelate decarboxylase (i148l mutant) from helicobacter pylori complexed with l-lysine
24% identity, 90% coverage: 40:418/422 of query aligns to 1:367/394 of 3c5qA
- active site: K44 (= K85), H183 (= H223), E257 (= E296)
- binding lysine: L146 (≠ R187), R260 (≠ D299), R294 (≠ E335), Y298 (= Y339), Y351 (= Y402)
- binding pyridoxal-5'-phosphate: K44 (= K85), D63 (= D105), H183 (= H223), S186 (≠ W226), G223 (= G261), E257 (= E296), P258 (= P297), G259 (= G298), R260 (≠ D299), Y351 (= Y402)
B4XMC6 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Helicobacter pylori (Campylobacter pylori) (see paper)
24% identity, 90% coverage: 40:418/422 of query aligns to 3:374/405 of B4XMC6
- K46 (= K85) modified: N6-(pyridoxal phosphate)lysine
- I148 (≠ R187) 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 (= G261) binding pyridoxal 5'-phosphate
- EPGR 259:262 (≠ EPGD 296:299) binding pyridoxal 5'-phosphate
- Y358 (= Y402) binding pyridoxal 5'-phosphate
4xg1A Psychromonas ingrahamii diaminopimelate decarboxylase with llp
25% identity, 92% coverage: 34:421/422 of query aligns to 9:367/393 of 4xg1A
- active site: K55 (= K85), H178 (= H223), E246 (= E296)
- binding (2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid: K55 (= K85), D74 (= D105), S97 (≠ T128), H178 (= H223), S181 (≠ W226), G216 (= G261), E246 (= E296), G248 (= G298), R249 (≠ D299), R285 (≠ E335), Y289 (= Y339), C320 (≠ N373), E321 (= E374), Y348 (= Y402)
- binding propane: S121 (= S152), I122 (≠ L153)
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)
25% identity, 91% coverage: 34:415/422 of query aligns to 18:404/438 of Q58497
- K73 (= K85) modified: N6-(pyridoxal phosphate)lysine
- S217 (≠ A231) binding pyridoxal 5'-phosphate
- G254 (= G261) binding pyridoxal 5'-phosphate
- EPGR 294:297 (≠ EPGD 296:299) binding pyridoxal 5'-phosphate
- Y391 (= Y402) binding pyridoxal 5'-phosphate
1tufA Crystal structure of diaminopimelate decarboxylase from m. Jannaschi (see paper)
25% identity, 91% coverage: 34:415/422 of query aligns to 14:400/434 of 1tufA
1twiA Crystal structure of diaminopimelate decarboxylase from m. Jannaschii in co-complex with l-lysine (see paper)
25% identity, 91% coverage: 34:415/422 of query aligns to 14:400/434 of 1twiA
- active site: K69 (= K85), H210 (= H223), E290 (= E296)
- binding lysine: S213 (≠ A231), R293 (≠ D299), R329 (≠ E335), Y333 (= Y339), Y387 (= Y402)
- binding pyridoxal-5'-phosphate: A67 (= A83), K69 (= K85), D88 (= D105), N111 (≠ T128), H210 (= H223), S213 (≠ A231), G250 (= G261), E290 (= E296), G292 (= G298), R293 (≠ D299), Y387 (= Y402)
8d5dA Structure of y430f d-ornithine/d-lysine decarboxylase complex with d- arginine (see paper)
26% identity, 90% coverage: 26:403/422 of query aligns to 19:413/458 of 8d5dA
- binding (E)-N~2~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-D-arginine: K79 (= K85), H208 (= H223), D211 (≠ A231), G249 (= G261), E297 (= E296), G299 (= G298), R300 (≠ D299), D346 (≠ A348), F350 (≠ Q352), C377 (≠ N373), D378 (≠ E374), Y412 (= Y402)
8d5rA Structure of y430f d-ornithine/d-lysine decarboxylase complex with d- ornithine (see paper)
26% identity, 90% coverage: 26:403/422 of query aligns to 20:415/461 of 8d5rA
- binding n~2~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-d-ornithine: A78 (= A83), K80 (= K85), H210 (= H223), D213 (≠ A231), G251 (= G261), E299 (= E296), G301 (= G298), R302 (≠ D299), Y414 (= Y402)
- binding 1,4-diaminobutane: Q350 (≠ L350), H351 (= H351), D353 (= D353)
8d88A Structure of y430f d-ornithine/d-lysine decarboxylase complex with d- lysine (see paper)
26% identity, 90% coverage: 26:403/422 of query aligns to 20:417/461 of 8d88A
- binding pentane-1,5-diamine: Q352 (≠ L350), H353 (= H351), D355 (= D353)
- binding N~2~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-D-lysine: A78 (= A83), K80 (= K85), H212 (= H223), D215 (≠ A231), G253 (= G261), E301 (= E296), G303 (= G298), R304 (≠ D299), Y416 (= Y402)
8d4iA Structure of y430f d-ornithine/d-lysine decarboxylase complex with putrescine (see paper)
26% identity, 90% coverage: 26:403/422 of query aligns to 20:417/462 of 8d4iA
7ru7A Crystal structure of btrk, a decarboxylase involved in butirosin biosynthesis
23% identity, 90% coverage: 34:412/422 of query aligns to 1:379/412 of 7ru7A
1hkvA Mycobacterium diaminopimelate dicarboxylase (lysa) (see paper)
25% identity, 95% coverage: 14:412/422 of query aligns to 4:414/446 of 1hkvA
- binding lysine: E375 (= E374), S376 (≠ A375)
- binding pyridoxal-5'-phosphate: A69 (= A83), K71 (= K85), R160 (≠ N173), H210 (= H221), H212 (= H223), G256 (= G260), G257 (= G261), E299 (= E296), G301 (= G298), R302 (≠ D299), Y404 (= Y402)
P9WIU7 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
25% identity, 95% coverage: 14:412/422 of query aligns to 5:415/447 of P9WIU7
- K72 (= K85) modified: N6-(pyridoxal phosphate)lysine
- C93 (= C107) modified: Interchain (with C-375)
- G258 (= G261) binding pyridoxal 5'-phosphate
- EPGR 300:303 (≠ EPGD 296:299) binding pyridoxal 5'-phosphate
- C375 (≠ N373) modified: Interchain (with C-72)
- Y405 (= Y402) binding pyridoxal 5'-phosphate
Query Sequence
>WP_012566228.1 NCBI__GCF_000016185.1:WP_012566228.1
MTPDALAATSAAALPCAPALWWERPDLRYVGRDLHLAGRNLAELARQAGTPAYVYSGPRV
LENLRRLKAALESTGLPHAIRYAMKANRHGPLLTWMKASGLCGIDACSPNELRFAVQCGF
RPEEVSYTATSVSEADLAVLARHPETWVNADSLSTLRRLAAVSPGREIGIRVNPALGVGY
GENQLLRYSGERTSKFGIYRDRFEEALALAASHGLTVRGIHFHVGWGYLNAQLPAWAEVV
RECLWFLDRVPQARLVNLGGGLGVPHAAGDRPLDLEAWAAVIRDSFAGRGIEVWVEPGDY
VVKDAGVLLLQANTVERKRATTFVGVDGGFNLAVEPVFYRLPCEPVPARLHQDPARAWAA
DALAPVSIAGNINEALDLWAEALPFPAVEEGDVIAFLNAGGYAAAMGSNHCMRAQASEHL
LL
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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