SitesBLAST
Comparing Ga0059261_4188 FitnessBrowser__Korea:Ga0059261_4188 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)
7ru7A Crystal structure of btrk, a decarboxylase involved in butirosin biosynthesis
35% identity, 91% coverage: 33:404/407 of query aligns to 17:388/412 of 7ru7A
6knhC Crystal structure of sbnh in complex with citrate, a plp-dependent decarboxylase in staphyloferrin b biothesynthesis (see paper)
30% identity, 91% coverage: 36:404/407 of query aligns to 20:381/384 of 6knhC
6knkA Crystal structure of sbnh in complex with citryl-diaminoethane (see paper)
29% identity, 91% coverage: 36:404/407 of query aligns to 21:379/383 of 6knkA
6kniA Crystal structure of sbnh in complex with the cofactor plp, a plp- dependent decarboxylase in staphyloferrin b biothesynthesis (see paper)
29% identity, 91% coverage: 36:404/407 of query aligns to 20:377/381 of 6kniA
B4XMC6 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Helicobacter pylori (Campylobacter pylori) (see paper)
28% identity, 87% coverage: 33:388/407 of query aligns to 13:361/405 of B4XMC6
- K46 (= K65) modified: N6-(pyridoxal phosphate)lysine
- I148 (≠ M164) 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 (= G241) binding
- EPGR 259:262 (≠ ELGR 281:284) binding
- Y358 (= Y385) binding
3c5qA Crystal structure of diaminopimelate decarboxylase (i148l mutant) from helicobacter pylori complexed with l-lysine
28% identity, 87% coverage: 33:388/407 of query aligns to 11:354/394 of 3c5qA
- active site: K44 (= K65), H183 (≠ F200), E257 (= E281)
- binding lysine: L146 (≠ M164), R260 (= R284), R294 (≠ A320), Y298 (≠ V329), Y351 (= Y385)
- binding pyridoxal-5'-phosphate: K44 (= K65), D63 (= D84), H183 (≠ F200), S186 (= S203), G223 (= G241), E257 (= E281), P258 (≠ L282), G259 (= G283), R260 (= R284), Y351 (= Y385)
2yxxA Crystal structure analysis of diaminopimelate decarboxylate (lysa)
27% identity, 88% coverage: 32:390/407 of query aligns to 11:347/385 of 2yxxA
- active site: K45 (= K65), H178 (≠ F200), E245 (= E281)
- binding pyridoxal-5'-phosphate: K45 (= K65), D64 (= D84), H178 (≠ F200), S181 (= S203), G213 (= G241), E245 (= E281), G247 (= G283), R248 (= R284), Y342 (= Y385)
Q9X1K5 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
27% identity, 88% coverage: 32:390/407 of query aligns to 12:348/386 of Q9X1K5
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)
27% identity, 93% coverage: 12:388/407 of query aligns to 13:394/438 of Q58497
- K73 (= K65) modified: N6-(pyridoxal phosphate)lysine
- S217 (= S203) binding
- G254 (= G241) binding
- EPGR 294:297 (≠ ELGR 281:284) binding
- Y391 (= Y385) binding
1tufA Crystal structure of diaminopimelate decarboxylase from m. Jannaschi (see paper)
27% identity, 93% coverage: 12:388/407 of query aligns to 9:390/434 of 1tufA
1twiA Crystal structure of diaminopimelate decarboxylase from m. Jannaschii in co-complex with l-lysine (see paper)
27% identity, 93% coverage: 12:388/407 of query aligns to 9:390/434 of 1twiA
- active site: K69 (= K65), H210 (≠ F200), E290 (= E281)
- binding lysine: S213 (= S203), R293 (= R284), R329 (≠ A320), Y333 (≠ R330), Y387 (= Y385)
- binding pyridoxal-5'-phosphate: A67 (= A63), K69 (= K65), D88 (= D84), N111 (≠ A106), H210 (≠ F200), S213 (= S203), G250 (= G241), E290 (= E281), G292 (= G283), R293 (= R284), Y387 (= Y385)
4xg1B Psychromonas ingrahamii diaminopimelate decarboxylase with llp
25% identity, 93% coverage: 11:390/407 of query aligns to 5:378/418 of 4xg1B
- active site: K60 (= K65), H199 (≠ F200), E273 (= E281)
- binding (2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid: K60 (= K65), D79 (= D84), H199 (≠ F200), S202 (= S203), G239 (= G241), E273 (= E281), G275 (= G283), R276 (= R284), R310 (vs. gap), Y314 (≠ S322), C345 (= C356), E346 (≠ T357), Y373 (= Y385)
- binding propane: A35 (≠ G41), E38 (≠ H44), E206 (≠ D207), I207 (≠ T208), A208 (= A209)
4xg1A Psychromonas ingrahamii diaminopimelate decarboxylase with llp
25% identity, 94% coverage: 10:390/407 of query aligns to 2:353/393 of 4xg1A
- active site: K55 (= K65), H178 (= H198), E246 (= E281)
- binding (2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid: K55 (= K65), D74 (= D84), S97 (≠ A106), H178 (= H198), S181 (= S203), G216 (= G241), E246 (= E281), G248 (= G283), R249 (= R284), R285 (vs. gap), Y289 (≠ S322), C320 (= C356), E321 (≠ T357), Y348 (= Y385)
- binding propane: S121 (= S129), I122 (≠ E130)
P9WIU7 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
29% identity, 92% coverage: 15:390/407 of query aligns to 22:410/447 of P9WIU7
- K72 (= K65) modified: N6-(pyridoxal phosphate)lysine
- C93 (≠ A86) modified: Interchain (with C-375)
- G258 (= G241) binding
- EPGR 300:303 (≠ ELGR 281:284) binding
- C375 (= C356) modified: Interchain (with C-72)
- Y405 (= Y385) binding
1hkvA Mycobacterium diaminopimelate dicarboxylase (lysa) (see paper)
29% identity, 92% coverage: 15:390/407 of query aligns to 21:409/446 of 1hkvA
- binding lysine: E375 (≠ T357), S376 (≠ P358)
- binding pyridoxal-5'-phosphate: A69 (= A63), K71 (= K65), R160 (= R152), H210 (= H198), H212 (≠ F200), G256 (= G240), G257 (= G241), E299 (= E281), G301 (= G283), R302 (= R284), Y404 (= Y385)
6n2aA Meso-diaminopimelate decarboxylase from arabidopsis thaliana (isoform 1)
25% identity, 90% coverage: 34:399/407 of query aligns to 31:392/422 of 6n2aA
- binding lysine: K63 (= K65), R281 (= R284), R317 (≠ A320), Y321 (vs. gap), C349 (= C356), E350 (≠ T357), Y378 (= Y385)
- binding pyridoxal-5'-phosphate: K63 (= K65), H202 (≠ F200), S205 (= S203), G242 (= G241), E278 (= E281), G280 (= G283), R281 (= R284), Y378 (= Y385)
5gjoA Crystal structure of srldc mutant (a225c/t302c) in complex with plp (see paper)
28% identity, 91% coverage: 33:404/407 of query aligns to 21:371/385 of 5gjoA
- active site: K52 (= K65), H180 (≠ F200), E256 (= E281)
- binding pyridoxal-5'-phosphate: A50 (= A63), K52 (= K65), D71 (= D84), H180 (≠ F200), S183 (= S203), G219 (= G240), G220 (= G241), E256 (= E281), G258 (= G283), R259 (= R284), Y353 (= Y385)
O50657 Lysine/ornithine decarboxylase; LDC; EC 4.1.1.17; EC 4.1.1.18 from Selenomonas ruminantium (see paper)
28% identity, 91% coverage: 33:404/407 of query aligns to 20:370/393 of O50657
- AG-V 44:46 (≠ ACEI 57:60) mutation to VTP: 2-fold increase in substrate specificity towards ornithine. 5-fold increase in substrate specificity towards ornithine; when associated with D-54. 70-fold increase in substrate specificity towards ornithine; when associated with D-54 and A-322. 16-fold increase in substrate specificity towards ornithine; when associated with D-54; T-322 and L-326.
- P54 (= P68) mutation to D: 3-fold increase in substrate specificity towards ornithine. 5-fold increase in substrate specificity towards ornithine; when associated with 44-V--P-46. 70-fold increase in substrate specificity towards ornithine; when associated with 44-V--P-46 and A-322. 16-fold increase in substrate specificity towards ornithine; when associated with 44-V--P-46; T-322 and L-326.
- G319 (≠ V352) mutation to W: 7-fold increase in substrate specificity towards ornithine.
- S322 (≠ L355) mutation to A: 29-fold increase in substrate specificity towards ornithine. 70-fold increase in substrate specificity towards ornithine; when associated with 44-V--P-46 and D-54.; mutation to T: 16-fold increase in substrate specificity towards ornithine; when associated with L-326. 16-fold increase in substrate specificity towards ornithine; when associated with 44-V--P-46; D-54 and L-326.
- I326 (≠ L359) mutation to L: 16-fold increase in substrate specificity towards ornithine; when associated with T-322. 16-fold increase in substrate specificity towards ornithine; when associated with 44-V--P-46; D-54 and T-322.
- G350 (= G383) mutation to D: Loss of dimer formation and decarboxylase activity.
5gjpA Crystal structure of srldc in complex with plp and cadaverine (see paper)
27% identity, 91% coverage: 33:404/407 of query aligns to 20:362/381 of 5gjpA
- active site: K51 (= K65), H171 (≠ F200), E247 (= E281)
- binding pentane-1,5-diamine: Y290 (≠ R330), D291 (≠ R331), Y344 (= Y385)
- binding pyridoxal-5'-phosphate: A49 (= A63), K51 (= K65), H171 (≠ F200), S174 (= S203), G211 (= G241), E247 (= E281), G249 (= G283), R250 (= R284), Y344 (= Y385)
1knwA Crystal structure of diaminopimelate decarboxylase
26% identity, 89% coverage: 29:390/407 of query aligns to 21:382/421 of 1knwA
Query Sequence
>Ga0059261_4188 FitnessBrowser__Korea:Ga0059261_4188
MKPIGPIPPYFMRQGELTIAGRAAADWVAEAGSPLFVYDMGIVHERLRGLRAALPDACEI
HFAIKANPLPEFIAAVAPLVGGLDVASGGELAKALKVKDAAHISFAGPGKRDAELEAAIV
AGATLNLESEGEAERALTIGRVLGTTPRLAVRVNPDFELRGSGMKMGGRASPFGVDAARV
PALVNRLIAAGADWRGFHIFAGSQSLDTAAIIETQAATVALAARLAQEAGVSPPLVNLGG
GFGIPYFSGDMPIDIDAVGAALGKTLESRQEILAQSGFAIELGRWIAGECGVYLMRVIDR
KISGDETFLICDGGLHHQLAASGNFGTVVRRNYPVAVAEKMDAEPVETVSVVGPLCTPLD
RLADRVALPRTEPGDVIAVFLAGAYGASASPAAFLGHGPATEIVAGC
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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