SitesBLAST
Comparing WP_012466478.1 NCBI__GCF_000020465.1:WP_012466478.1 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)
4xg1B Psychromonas ingrahamii diaminopimelate decarboxylase with llp
39% identity, 98% coverage: 7:415/417 of query aligns to 3:413/418 of 4xg1B
- active site: K60 (= K63), H199 (= H202), E273 (= E277)
- binding (2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid: K60 (= K63), D79 (= D82), H199 (= H202), S202 (= S205), G239 (= G242), E273 (= E277), G275 (= G279), R276 (= R280), R310 (= R317), Y314 (= Y321), C345 (= C346), E346 (= E347), Y373 (= Y375)
- binding propane: A35 (≠ R38), E38 (= E41), E206 (≠ D209), I207 (≠ P210), A208 (≠ E211)
B4XMC6 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Helicobacter pylori (Campylobacter pylori) (see paper)
38% identity, 94% coverage: 22:411/417 of query aligns to 5:394/405 of B4XMC6
- K46 (= K63) modified: N6-(pyridoxal phosphate)lysine
- I148 (= I165) 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 (= G242) binding pyridoxal 5'-phosphate
- EPGR 259:262 (= EPGR 277:280) 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
38% identity, 94% coverage: 22:411/417 of query aligns to 3:386/394 of 3c5qA
- active site: K44 (= K63), H183 (= H202), E257 (= E277)
- binding lysine: L146 (≠ I165), R260 (= R280), R294 (= R317), Y298 (= Y321), Y351 (= Y375)
- binding pyridoxal-5'-phosphate: K44 (= K63), D63 (= D82), H183 (= H202), S186 (= S205), G223 (= G242), E257 (= E277), P258 (= P278), G259 (= G279), R260 (= R280), Y351 (= Y375)
1twiA Crystal structure of diaminopimelate decarboxylase from m. Jannaschii in co-complex with l-lysine (see paper)
38% identity, 95% coverage: 23:417/417 of query aligns to 23:429/434 of 1twiA
- active site: K69 (= K63), H210 (= H202), E290 (= E277)
- binding lysine: S213 (= S205), R293 (= R280), R329 (= R317), Y333 (= Y321), Y387 (= Y375)
- binding pyridoxal-5'-phosphate: A67 (≠ S61), K69 (= K63), D88 (= D82), N111 (≠ A105), H210 (= H202), S213 (= S205), G250 (= G242), E290 (= E277), G292 (= G279), R293 (= R280), Y387 (= Y375)
1tufA Crystal structure of diaminopimelate decarboxylase from m. Jannaschi (see paper)
38% identity, 95% coverage: 23:417/417 of query aligns to 23:429/434 of 1tufA
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, 95% coverage: 23:417/417 of query aligns to 27:433/438 of Q58497
- K73 (= K63) modified: N6-(pyridoxal phosphate)lysine
- S217 (= S205) binding pyridoxal 5'-phosphate
- G254 (= G242) binding pyridoxal 5'-phosphate
- EPGR 294:297 (= EPGR 277:280) binding pyridoxal 5'-phosphate
- Y391 (= Y375) binding pyridoxal 5'-phosphate
4xg1A Psychromonas ingrahamii diaminopimelate decarboxylase with llp
36% identity, 98% coverage: 7:415/417 of query aligns to 3:388/393 of 4xg1A
- active site: K55 (= K63), H178 (= H202), E246 (= E277)
- binding (2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid: K55 (= K63), D74 (= D82), S97 (≠ A105), H178 (= H202), S181 (= S205), G216 (= G242), E246 (= E277), G248 (= G279), R249 (= R280), R285 (= R317), Y289 (= Y321), C320 (= C346), E321 (= E347), Y348 (= Y375)
- binding propane: S121 (= S129), I122 (≠ L130)
6n2aA Meso-diaminopimelate decarboxylase from arabidopsis thaliana (isoform 1)
34% identity, 96% coverage: 11:410/417 of query aligns to 10:414/422 of 6n2aA
- binding lysine: K63 (= K63), R281 (= R280), R317 (= R317), Y321 (= Y321), C349 (= C346), E350 (= E347), Y378 (= Y375)
- binding pyridoxal-5'-phosphate: K63 (= K63), H202 (= H202), S205 (= S205), G242 (= G242), E278 (= E277), G280 (= G279), R281 (= R280), Y378 (= Y375)
2yxxA Crystal structure analysis of diaminopimelate decarboxylate (lysa)
36% identity, 95% coverage: 21:417/417 of query aligns to 3:385/385 of 2yxxA
- active site: K45 (= K63), H178 (= H202), E245 (= E277)
- binding pyridoxal-5'-phosphate: K45 (= K63), D64 (= D82), H178 (= H202), S181 (= S205), G213 (= G242), E245 (= E277), G247 (= G279), R248 (= R280), Y342 (= 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, 95% coverage: 21:417/417 of query aligns to 4:386/386 of Q9X1K5
- G214 (= G242) binding pyridoxal 5'-phosphate
- EIGR 246:249 (≠ EPGR 277:280) binding pyridoxal 5'-phosphate
- Y343 (= Y375) binding pyridoxal 5'-phosphate
1hkvA Mycobacterium diaminopimelate dicarboxylase (lysa) (see paper)
35% identity, 97% coverage: 12:416/417 of query aligns to 21:445/446 of 1hkvA
- binding lysine: E375 (= E347), S376 (= S348)
- binding pyridoxal-5'-phosphate: A69 (≠ S61), K71 (= K63), R160 (= R152), H210 (≠ D200), H212 (= H202), G256 (= G241), G257 (= G242), E299 (= E277), G301 (= G279), R302 (= R280), Y404 (= Y375)
P9WIU7 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
35% identity, 97% coverage: 12:416/417 of query aligns to 22:446/447 of P9WIU7
- K72 (= K63) modified: N6-(pyridoxal phosphate)lysine
- C93 (≠ N84) modified: Interchain (with C-375)
- G258 (= G242) binding pyridoxal 5'-phosphate
- EPGR 300:303 (= EPGR 277:280) binding pyridoxal 5'-phosphate
- C375 (= C346) modified: Interchain (with C-72)
- Y405 (= Y375) binding pyridoxal 5'-phosphate
5x7nA Crystal structure of meso-diaminopimelate decarboxylase (dapdc) from corynebacterium glutamicum (see paper)
31% identity, 99% coverage: 4:415/417 of query aligns to 15:442/442 of 5x7nA
- binding lysine: K73 (= K63), R341 (= R317), Y345 (= Y321), Y402 (= Y375), M406 (= M379)
- binding pyridoxal-5'-phosphate: K73 (= K63), H115 (≠ A105), H214 (= H202), G254 (= G241), G255 (= G242), E297 (= E277), G299 (= G279), R300 (= R280), Y402 (= Y375)
5x7mA Crystal structure of meso-diaminopimelate decarboxylase (dapdc) from corynebacterium glutamicum (see paper)
31% identity, 99% coverage: 4:415/417 of query aligns to 15:442/443 of 5x7mA
8d5dA Structure of y430f d-ornithine/d-lysine decarboxylase complex with d- arginine (see paper)
28% identity, 98% coverage: 7:416/417 of query aligns to 22:454/458 of 8d5dA
- binding (E)-N~2~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-D-arginine: K79 (= K63), H208 (= H202), D211 (≠ S205), G249 (= G242), E297 (= E277), G299 (= G279), R300 (= R280), D346 (≠ R317), F350 (≠ Y321), C377 (= C346), D378 (≠ E347), Y412 (= Y375)
8d5rA Structure of y430f d-ornithine/d-lysine decarboxylase complex with d- ornithine (see paper)
28% identity, 98% coverage: 7:416/417 of query aligns to 23:456/461 of 8d5rA
- binding n~2~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-d-ornithine: A78 (≠ S61), K80 (= K63), H210 (= H202), D213 (≠ S205), G251 (= G242), E299 (= E277), G301 (= G279), R302 (= R280), Y414 (= Y375)
- binding 1,4-diaminobutane: Q350 (≠ A319), H351 (≠ L320), D353 (≠ Q322)
8d88A Structure of y430f d-ornithine/d-lysine decarboxylase complex with d- lysine (see paper)
28% identity, 98% coverage: 7:416/417 of query aligns to 23:458/461 of 8d88A
- binding pentane-1,5-diamine: Q352 (≠ A319), H353 (≠ L320), D355 (≠ Q322)
- binding N~2~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-D-lysine: A78 (≠ S61), K80 (= K63), H212 (= H202), D215 (≠ S205), G253 (= G242), E301 (= E277), G303 (= G279), R304 (= R280), Y416 (= Y375)
8d4iA Structure of y430f d-ornithine/d-lysine decarboxylase complex with putrescine (see paper)
28% identity, 98% coverage: 7:416/417 of query aligns to 23:458/462 of 8d4iA
7ru7A Crystal structure of btrk, a decarboxylase involved in butirosin biosynthesis
28% identity, 93% coverage: 28:416/417 of query aligns to 15:411/412 of 7ru7A
1ko0A Crystal structure of a d,l-lysine complex of diaminopimelate decarboxylase
29% identity, 95% coverage: 11:407/417 of query aligns to 8:409/419 of 1ko0A
- binding d-lysine: K53 (= K63), T156 (= T167), H190 (= H202), Y310 (= Y321), Y377 (= Y375)
- binding lysine: K53 (= K63), R270 (= R280), R306 (= R317), Y310 (= Y321), Y377 (= Y375)
- binding pyridoxal-5'-phosphate: A51 (≠ S61), K53 (= K63), H190 (= H202), G226 (= G242), E267 (= E277), P268 (= P278), G269 (= G279), R270 (= R280), Y377 (= Y375)
Query Sequence
>WP_012466478.1 NCBI__GCF_000020465.1:WP_012466478.1
MSERTVFHYQDNVLCCEDVRLDELAGIYGTPLFVTSKRSLEGSLREFEAAFASLPHITCY
SVKANFNLSVISTLAGMGCGCDVNSGGELFRALKAGVSPEKIIFAGVGKKPEEIAFALEA
GVLMLKVESLSELEAIERIAAEKGLTAPVALRINPNVTAETHPYITTGDSKEKFGIDEAG
LEEAFSLLRRMKHVRLVCLDMHIGSQIFDPEYYVAATAVLLDIFETARSLGFSIEYLDIG
GGFPVTYDARKPATPITYFAEKLMPLLAAAGVPVIFEPGRFLVANASVLLSRILYKKTNH
TGKQFYIVDAGMTELIRPALYQSHHEVLTVIRHEKTVVADVVGPVCESSDFFARQRTIDD
AAEGELLAVMSSGAYAAVMSSNYNGRLRPAEVMVDGQEVTVIRRRETYEQLIANEVL
Or try a new SitesBLAST search
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