SitesBLAST
Comparing WP_012971281.1 NCBI__GCF_000025485.1:WP_012971281.1 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
60% identity, 98% coverage: 2:415/423 of query aligns to 1:417/418 of 4xg1B
- active site: K60 (= K60), H199 (= H199), E273 (= E273)
- 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 (= E273), G275 (= G275), R276 (= R276), R310 (= R312), Y314 (= Y316), C345 (= C343), E346 (= E344), Y373 (= Y371)
- binding propane: A35 (= A35), E38 (= E38), E206 (≠ D206), I207 (≠ L207), A208 (= A208)
4xg1A Psychromonas ingrahamii diaminopimelate decarboxylase with llp
56% identity, 98% coverage: 2:415/423 of query aligns to 1:392/393 of 4xg1A
- active site: K55 (= K60), H178 (= H199), E246 (= E273)
- 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 (= E273), G248 (= G275), R249 (= R276), R285 (= R312), Y289 (= Y316), C320 (= C343), E321 (= E344), Y348 (= Y371)
- binding propane: S121 (= S126), I122 (≠ E127)
B4XMC6 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Helicobacter pylori (Campylobacter pylori) (see paper)
44% identity, 93% coverage: 20:412/423 of query aligns to 6:399/405 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 273:276) binding pyridoxal 5'-phosphate
- Y358 (= Y371) binding pyridoxal 5'-phosphate
3c5qA Crystal structure of diaminopimelate decarboxylase (i148l mutant) from helicobacter pylori complexed with l-lysine
44% identity, 93% coverage: 20:412/423 of query aligns to 4:391/394 of 3c5qA
- active site: K44 (= K60), H183 (= H199), E257 (= E273)
- binding lysine: L146 (≠ I162), R260 (= R276), R294 (= R312), Y298 (= Y316), Y351 (= Y371)
- binding pyridoxal-5'-phosphate: K44 (= K60), D63 (= D79), H183 (= H199), S186 (= S202), G223 (= G239), E257 (= E273), P258 (= P274), G259 (= G275), R260 (= R276), Y351 (= Y371)
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)
39% identity, 98% coverage: 2:415/423 of query aligns to 9:435/438 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 273:276) binding pyridoxal 5'-phosphate
- Y391 (= Y371) binding pyridoxal 5'-phosphate
1tufA Crystal structure of diaminopimelate decarboxylase from m. Jannaschi (see paper)
39% identity, 98% coverage: 2:415/423 of query aligns to 5:431/434 of 1tufA
1twiA Crystal structure of diaminopimelate decarboxylase from m. Jannaschii in co-complex with l-lysine (see paper)
39% identity, 98% coverage: 2:415/423 of query aligns to 5:431/434 of 1twiA
- active site: K69 (= K60), H210 (= H199), E290 (= E273)
- binding lysine: S213 (= S202), R293 (= R276), R329 (= R312), Y333 (= Y316), Y387 (= Y371)
- binding pyridoxal-5'-phosphate: A67 (≠ S58), K69 (= K60), D88 (= D79), N111 (≠ S102), H210 (= H199), S213 (= S202), G250 (= G239), E290 (= E273), G292 (= G275), R293 (= R276), Y387 (= Y371)
Q9X1K5 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
39% identity, 92% coverage: 18:408/423 of query aligns to 4:381/386 of Q9X1K5
- G214 (= G239) binding pyridoxal 5'-phosphate
- EIGR 246:249 (≠ EPGR 273:276) binding pyridoxal 5'-phosphate
- Y343 (= Y371) binding pyridoxal 5'-phosphate
2yxxA Crystal structure analysis of diaminopimelate decarboxylate (lysa)
39% identity, 92% coverage: 18:408/423 of query aligns to 3:380/385 of 2yxxA
- active site: K45 (= K60), H178 (= H199), E245 (= E273)
- binding pyridoxal-5'-phosphate: K45 (= K60), D64 (= D79), H178 (= H199), S181 (= S202), G213 (= G239), E245 (= E273), G247 (= G275), R248 (= R276), Y342 (= Y371)
6n2aA Meso-diaminopimelate decarboxylase from arabidopsis thaliana (isoform 1)
36% identity, 91% coverage: 8:393/423 of query aligns to 10:400/422 of 6n2aA
- binding lysine: K63 (= K60), R281 (= R276), R317 (= R312), Y321 (= Y316), C349 (= C343), E350 (= E344), Y378 (= Y371)
- binding pyridoxal-5'-phosphate: K63 (= K60), H202 (= H199), S205 (= S202), G242 (= G239), E278 (= E273), G280 (= G275), R281 (= R276), Y378 (= Y371)
1hkvA Mycobacterium diaminopimelate dicarboxylase (lysa) (see paper)
33% identity, 96% coverage: 6:411/423 of query aligns to 18:444/446 of 1hkvA
- binding lysine: E375 (= E344), S376 (≠ T345)
- binding pyridoxal-5'-phosphate: A69 (≠ S58), K71 (= K60), R160 (= R149), H210 (≠ D197), H212 (= H199), G256 (= G238), G257 (= G239), E299 (= E273), G301 (= G275), R302 (= R276), Y404 (= Y371)
P9WIU7 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
33% identity, 96% coverage: 6:411/423 of query aligns to 19:445/447 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 273:276) binding pyridoxal 5'-phosphate
- C375 (= C343) modified: Interchain (with C-72)
- Y405 (= Y371) binding pyridoxal 5'-phosphate
5x7mA Crystal structure of meso-diaminopimelate decarboxylase (dapdc) from corynebacterium glutamicum (see paper)
31% identity, 96% coverage: 8:411/423 of query aligns to 22:442/443 of 5x7mA
5x7nA Crystal structure of meso-diaminopimelate decarboxylase (dapdc) from corynebacterium glutamicum (see paper)
31% identity, 96% coverage: 8:411/423 of query aligns to 22:442/442 of 5x7nA
- binding lysine: K73 (= K60), R341 (= R312), Y345 (= Y316), Y402 (= Y371), M406 (= M375)
- binding pyridoxal-5'-phosphate: K73 (= K60), H115 (≠ S102), H214 (= H199), G254 (= G238), G255 (= G239), E297 (= E273), G299 (= G275), R300 (= R276), Y402 (= Y371)
1ko0A Crystal structure of a d,l-lysine complex of diaminopimelate decarboxylase
33% identity, 91% coverage: 18:404/423 of query aligns to 16:410/419 of 1ko0A
- binding d-lysine: K53 (= K60), T156 (= T164), H190 (= H199), Y310 (= Y316), Y377 (= Y371)
- binding lysine: K53 (= K60), R270 (= R276), R306 (= R312), Y310 (= Y316), Y377 (= Y371)
- binding pyridoxal-5'-phosphate: A51 (≠ S58), K53 (= K60), H190 (= H199), G226 (= G239), E267 (= E273), P268 (= P274), G269 (= G275), R270 (= R276), Y377 (= Y371)
1knwA Crystal structure of diaminopimelate decarboxylase
33% identity, 91% coverage: 18:404/423 of query aligns to 16:410/421 of 1knwA
P00861 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Escherichia coli (strain K12)
33% identity, 91% coverage: 18:404/423 of query aligns to 17:411/420 of P00861
- K54 (= K60) modified: N6-(pyridoxal phosphate)lysine
- G227 (= G239) binding pyridoxal 5'-phosphate
- EPGR 268:271 (= EPGR 273:276) binding pyridoxal 5'-phosphate
- Y378 (= Y371) binding pyridoxal 5'-phosphate
7ru7A Crystal structure of btrk, a decarboxylase involved in butirosin biosynthesis
28% identity, 95% coverage: 11:413/423 of query aligns to 1:411/412 of 7ru7A
8d5rA Structure of y430f d-ornithine/d-lysine decarboxylase complex with d- ornithine (see paper)
28% identity, 96% coverage: 4:407/423 of query aligns to 23:451/461 of 8d5rA
- binding n~2~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-d-ornithine: A78 (≠ S58), K80 (= K60), H210 (= H199), D213 (≠ S202), G251 (= G239), E299 (= E273), G301 (= G275), R302 (= R276), Y414 (= Y371)
- binding 1,4-diaminobutane: Q350 (≠ A314), H351 (≠ L315), D353 (≠ Q317)
8d4iA Structure of y430f d-ornithine/d-lysine decarboxylase complex with putrescine (see paper)
28% identity, 96% coverage: 4:407/423 of query aligns to 23:453/462 of 8d4iA
Query Sequence
>WP_012971281.1 NCBI__GCF_000025485.1:WP_012971281.1
MDHFNDRDGLLHAEEVPLTEIAERFGTPCYVYSRATLERHWRAFERAFRDHPHLICFSVK
SNSNLAVLNVLARLGSGFDIVSVGELERVLAAGGDPARVVFSGVGKRADEIRRALEVGIR
CFNVESESELTRIDRIAGELGVRAPVSLRVNPDVDPQTHHYISTGLKENKFGIDIQEAES
VYALAAAMPNLKVVGIDCHIGSQLTDLAPFIDALGRVLALADRLCASGIAIEHLDLGGGL
GIRYREEHPPEPAAYAAAMSHLLADRPYEVILEPGRAIVGNAGVLLTQVEYLKHGPHKHF
AILDAAMNDLLRPALYQAGHEIVRVVQETDADPSRYDLVGPVCETGDFLGKDRTLALEEG
DLVAVRGAGAYGFTMSSNYNSRPRAAEVMVDGDRAYLVRAREQVADLYAGEQLLPSETPD
AAA
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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