SitesBLAST
Comparing WP_014149148.1 NCBI__GCF_000968535.2:WP_014149148.1 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)
7ru7A Crystal structure of btrk, a decarboxylase involved in butirosin biosynthesis
38% identity, 93% coverage: 27:410/411 of query aligns to 7:388/412 of 7ru7A
6knhC Crystal structure of sbnh in complex with citrate, a plp-dependent decarboxylase in staphyloferrin b biothesynthesis (see paper)
31% identity, 90% coverage: 41:411/411 of query aligns to 20:383/384 of 6knhC
6kniA Crystal structure of sbnh in complex with the cofactor plp, a plp- dependent decarboxylase in staphyloferrin b biothesynthesis (see paper)
31% identity, 90% coverage: 41:411/411 of query aligns to 20:379/381 of 6kniA
6knkA Crystal structure of sbnh in complex with citryl-diaminoethane (see paper)
30% identity, 90% coverage: 41:411/411 of query aligns to 21:381/383 of 6knkA
1tufA Crystal structure of diaminopimelate decarboxylase from m. Jannaschi (see paper)
29% identity, 93% coverage: 16:396/411 of query aligns to 9:392/434 of 1tufA
1twiA Crystal structure of diaminopimelate decarboxylase from m. Jannaschii in co-complex with l-lysine (see paper)
29% identity, 93% coverage: 16:396/411 of query aligns to 9:392/434 of 1twiA
- active site: K69 (= K70), H210 (≠ Y206), E290 (= E287)
- binding lysine: S213 (= S209), R293 (= R290), R329 (≠ A326), Y333 (≠ R336), Y387 (= Y391)
- binding pyridoxal-5'-phosphate: A67 (= A68), K69 (= K70), D88 (= D89), N111 (≠ A112), H210 (≠ Y206), S213 (= S209), G250 (= G247), E290 (= E287), G292 (= G289), R293 (= R290), Y387 (= Y391)
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)
29% identity, 93% coverage: 16:396/411 of query aligns to 13:396/438 of Q58497
- K73 (= K70) modified: N6-(pyridoxal phosphate)lysine
- S217 (= S209) binding
- G254 (= G247) binding
- EPGR 294:297 (≠ ELGR 287:290) binding
- Y391 (= Y391) binding
B4XMC6 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Helicobacter pylori (Campylobacter pylori) (see paper)
29% identity, 91% coverage: 37:409/411 of query aligns to 12:375/405 of B4XMC6
- K46 (= K70) modified: N6-(pyridoxal phosphate)lysine
- I148 (≠ M170) 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 (= G247) binding
- EPGR 259:262 (≠ ELGR 287:290) binding
- Y358 (= Y391) binding
3c5qA Crystal structure of diaminopimelate decarboxylase (i148l mutant) from helicobacter pylori complexed with l-lysine
30% identity, 91% coverage: 37:409/411 of query aligns to 10:368/394 of 3c5qA
- active site: K44 (= K70), H183 (≠ Y206), E257 (= E287)
- binding lysine: L146 (≠ M170), R260 (= R290), R294 (≠ A326), Y298 (≠ N330), Y351 (= Y391)
- binding pyridoxal-5'-phosphate: K44 (= K70), D63 (= D89), H183 (≠ Y206), S186 (= S209), G223 (= G247), E257 (= E287), P258 (≠ L288), G259 (= G289), R260 (= R290), Y351 (= Y391)
6n2aA Meso-diaminopimelate decarboxylase from arabidopsis thaliana (isoform 1)
27% identity, 93% coverage: 18:398/411 of query aligns to 10:385/422 of 6n2aA
- binding lysine: K63 (= K70), R281 (= R290), R317 (= R336), Y321 (≠ I343), C349 (= C362), E350 (≠ T363), Y378 (= Y391)
- binding pyridoxal-5'-phosphate: K63 (= K70), H202 (≠ Y206), S205 (= S209), G242 (= G247), E278 (= E287), G280 (= G289), R281 (= R290), Y378 (= Y391)
4xg1B Psychromonas ingrahamii diaminopimelate decarboxylase with llp
30% identity, 97% coverage: 14:411/411 of query aligns to 3:392/418 of 4xg1B
- active site: K60 (= K70), H199 (≠ Y206), E273 (= E287)
- binding (2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid: K60 (= K70), D79 (= D89), H199 (≠ Y206), S202 (= S209), G239 (= G247), E273 (= E287), G275 (= G289), R276 (= R290), R310 (vs. gap), Y314 (≠ S328), C345 (= C362), E346 (≠ T363), Y373 (= Y391)
- binding propane: A35 (≠ Q46), E38 (≠ N49), E206 (≠ K213), I207 (≠ A214), A208 (≠ E215)
Q9X1K5 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
25% identity, 93% coverage: 26:407/411 of query aligns to 1:359/386 of Q9X1K5
2yxxA Crystal structure analysis of diaminopimelate decarboxylate (lysa)
25% identity, 90% coverage: 38:407/411 of query aligns to 12:358/385 of 2yxxA
- active site: K45 (= K70), H178 (≠ Y206), E245 (= E287)
- binding pyridoxal-5'-phosphate: K45 (= K70), D64 (= D89), H178 (≠ Y206), S181 (= S209), G213 (= G247), E245 (= E287), G247 (= G289), R248 (= R290), Y342 (= Y391)
4xg1A Psychromonas ingrahamii diaminopimelate decarboxylase with llp
29% identity, 97% coverage: 14:411/411 of query aligns to 3:367/393 of 4xg1A
- active site: K55 (= K70), H178 (≠ Y206), E246 (= E287)
- binding (2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid: K55 (= K70), D74 (= D89), S97 (≠ A112), H178 (≠ Y206), S181 (= S209), G216 (= G247), E246 (= E287), G248 (= G289), R249 (= R290), R285 (vs. gap), Y289 (≠ S328), C320 (= C362), E321 (≠ T363), Y348 (= Y391)
- binding propane: S121 (= S135), I122 (≠ Q136)
2plkA Crystal structure of lysine/ornithine decarboxylase complexed with cadaverine from vibrio vulnificus (see paper)
26% identity, 84% coverage: 57:400/411 of query aligns to 43:356/370 of 2plkA
2pljA Crystal structure of lysine/ornithine decarboxylase complexed with putrescine from vibrio vulnificus (see paper)
26% identity, 84% coverage: 57:400/411 of query aligns to 47:361/376 of 2pljA
- active site: K60 (= K70), H179 (≠ Y206), E255 (= E287)
- binding (4-{[(4-aminobutyl)amino]methyl}-5-hydroxy-6-methylpyridin-3-yl)methyl dihydrogen phosphate: K60 (= K70), H179 (≠ Y206), S182 (= S209), G220 (= G247), E255 (= E287), G257 (= G289), R258 (= R290), D299 (≠ K337), Y353 (= Y391)
5gjoA Crystal structure of srldc mutant (a225c/t302c) in complex with plp (see paper)
27% identity, 91% coverage: 27:400/411 of query aligns to 11:361/385 of 5gjoA
- active site: K52 (= K70), H180 (≠ Y206), E256 (= E287)
- binding pyridoxal-5'-phosphate: A50 (= A68), K52 (= K70), D71 (= D89), H180 (≠ Y206), S183 (= S209), G219 (= G246), G220 (= G247), E256 (= E287), G258 (= G289), R259 (= R290), Y353 (= Y391)
O50657 Lysine/ornithine decarboxylase; LDC; EC 4.1.1.17; EC 4.1.1.18 from Selenomonas ruminantium (see paper)
27% identity, 91% coverage: 27:400/411 of query aligns to 10:360/393 of O50657
- AGV 44:46 (≠ LKI 63:65) 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 (= P73) 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 (≠ V358) mutation to W: 7-fold increase in substrate specificity towards ornithine.
- S322 (≠ L361) 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 (≠ L365) 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 (= G389) 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: 27:400/411 of query aligns to 10:352/381 of 5gjpA
- active site: K51 (= K70), H171 (≠ Y206), E247 (= E287)
- binding pentane-1,5-diamine: Y290 (≠ R336), D291 (≠ K337), Y344 (= Y391)
- binding pyridoxal-5'-phosphate: A49 (= A68), K51 (= K70), H171 (≠ Y206), S174 (= S209), G211 (= G247), E247 (= E287), G249 (= G289), R250 (= R290), Y344 (= Y391)
1hkvA Mycobacterium diaminopimelate dicarboxylase (lysa) (see paper)
25% identity, 94% coverage: 11:396/411 of query aligns to 10:409/446 of 1hkvA
- binding lysine: E375 (≠ T363), S376 (≠ P364)
- binding pyridoxal-5'-phosphate: A69 (= A68), K71 (= K70), R160 (= R158), H210 (= H204), H212 (≠ Y206), G256 (= G246), G257 (= G247), E299 (= E287), G301 (= G289), R302 (= R290), Y404 (= Y391)
Query Sequence
>WP_014149148.1 NCBI__GCF_000968535.2:WP_014149148.1
MNPTAPKHQFVNPFNIEDTELVIGGLKLSRLAQRVGQTPFYAYDRQLLNARIAELRQNMP
PELKIHYAMKANPMPAIVQHMATIVDGFDLASAGEMKVALDTVMPATQISMAGPGKRPAE
LGQAIAAGITINVESQQELNVIAALSEQTGIQANVALRINPAFELKASGMKMGGGPKQFG
IDEELIPTVLQHIKSLDLHFKGFHIYSGSQNLKAESIIDAQQKSIQLAVSLTEHCPSPIE
KLNIGGGFGIPYFPGDVPLDTRPIGDALAEAINQSKSQLPEAEIIIELGRYLVGEAGIYA
SQVIDKKISRGQIYLIVDGGLHHHLAASGNFGQVIRKNYPVAIGNKMGIEEMETVNIVGP
LCTPLDILADKVPLPKAEIGDYVVIFQSGAYGLTASPTAFLTQPNAEEILV
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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