SitesBLAST
Comparing WP_027485032.1 NCBI__GCF_021560695.1:WP_027485032.1 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)
2hmfA Structure of a threonine sensitive aspartokinase from methanococcus jannaschii complexed with mg-adp and aspartate (see paper)
32% identity, 53% coverage: 1:448/853 of query aligns to 4:462/464 of 2hmfA
- binding adenosine-5'-diphosphate: G7 (= G4), T229 (= T222), D230 (= D223), V231 (= V224), Y235 (≠ F228), T237 (≠ A230), D238 (≠ N231), P239 (= P232), R240 (= R233), K265 (= K258), V266 (= V259)
- binding aspartic acid: S39 (= S36), T45 (= T42), F192 (= F185), R206 (= R199), G207 (= G200), S209 (= S202)
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, 42% coverage: 497:852/853 of query aligns to 12:362/386 of Q9X1K5
- G214 (= G698) binding pyridoxal 5'-phosphate
- EIGR 246:249 (≠ EPGR 734:737) binding pyridoxal 5'-phosphate
- Y343 (= Y833) binding pyridoxal 5'-phosphate
2yxxA Crystal structure analysis of diaminopimelate decarboxylate (lysa)
36% identity, 42% coverage: 497:852/853 of query aligns to 11:361/385 of 2yxxA
- active site: K45 (= K529), H178 (= H662), E245 (= E734)
- binding pyridoxal-5'-phosphate: K45 (= K529), D64 (≠ E548), H178 (= H662), S181 (= S665), G213 (= G698), E245 (= E734), G247 (= G736), R248 (= R737), Y342 (= Y833)
3c1mC Cyrstal structure of threonine-sensitive aspartokinase from methanococcus jannaschii with mgamp-pnp and l-aspartate (see paper)
32% identity, 53% coverage: 1:448/853 of query aligns to 4:466/468 of 3c1mC
- binding phosphoaminophosphonic acid-adenylate ester: K5 (= K2), G7 (= G4), G8 (= G5), S39 (= S36), T229 (= T222), D230 (= D223), Y235 (≠ F228), D238 (≠ N231), P239 (= P232), R240 (= R233), K265 (= K258), V266 (= V259)
- binding aspartic acid: T45 (= T42), E129 (= E115), F192 (= F185), R206 (= R199), G207 (= G200), S209 (= S202)
3c1nA Crystal structure of allosteric inhibition threonine-sensitive aspartokinase from methanococcus jannaschii with l-threonine (see paper)
32% identity, 53% coverage: 1:448/853 of query aligns to 4:457/458 of 3c1nA
- binding threonine: G7 (= G4), G8 (= G5), T9 (= T6), S10 (= S7), W227 (= W221), T228 (= T222), D229 (= D223), A406 (vs. gap), I409 (≠ L399), A410 (≠ L400), N423 (≠ R414), I424 (≠ V415), Q429 (= Q420), E433 (≠ N424)
2j0xA Crystal structure of e. Coli aspartokinase iii in complex with lysine and aspartate (t-state) (see paper)
32% identity, 52% coverage: 2:448/853 of query aligns to 6:446/447 of 2j0xA
- binding aspartic acid: F182 (= F185), G197 (= G200), G198 (= G201), S199 (= S202), D200 (= D203)
- binding lysine: M316 (= M320), S319 (≠ Q323), F322 (= F326), L323 (= L327), S336 (= S340), V337 (= V341), D338 (= D342), S343 (≠ A347), E344 (= E348)
2j0wA Crystal structure of e. Coli aspartokinase iii in complex with aspartate and adp (r-state) (see paper)
32% identity, 52% coverage: 2:448/853 of query aligns to 6:446/447 of 2j0wA
- binding adenosine-5'-diphosphate: T219 (= T222), D220 (= D223), I224 (≠ M227), Y225 (≠ F228), D228 (≠ N231), R230 (= R233), K255 (= K258), V256 (= V259)
- binding aspartic acid: S37 (= S36), T43 (= T42), E117 (= E115), F182 (= F185), R196 (= R199), G197 (= G200), S199 (= S202)
P08660 Lysine-sensitive aspartokinase 3; Aspartate kinase III; AKIII; Lysine-sensitive aspartokinase III; EC 2.7.2.4 from Escherichia coli (strain K12) (see paper)
32% identity, 52% coverage: 2:448/853 of query aligns to 8:448/449 of P08660
- K8 (= K2) mutation to R: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition.
- E119 (= E115) mutation to D: Increases KM for aspartate about 3000-fold.
- R198 (= R199) mutation to K: Increases KM for aspartate about 200-fold.
- D202 (= D203) mutation to E: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition.
P00861 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Escherichia coli (strain K12)
36% identity, 43% coverage: 489:853/853 of query aligns to 16:398/420 of P00861
- K54 (= K529) modified: N6-(pyridoxal phosphate)lysine
- G227 (= G698) binding pyridoxal 5'-phosphate
- EPGR 268:271 (= EPGR 734:737) binding pyridoxal 5'-phosphate
- Y378 (= Y833) binding pyridoxal 5'-phosphate
1ko0A Crystal structure of a d,l-lysine complex of diaminopimelate decarboxylase
36% identity, 43% coverage: 489:853/853 of query aligns to 15:397/419 of 1ko0A
- binding d-lysine: K53 (= K529), T156 (= T628), H190 (= H662), Y310 (= Y777), Y377 (= Y833)
- binding lysine: K53 (= K529), R270 (= R737), R306 (= R773), Y310 (= Y777), Y377 (= Y833)
- binding pyridoxal-5'-phosphate: A51 (= A527), K53 (= K529), H190 (= H662), G226 (= G698), E267 (= E734), P268 (= P735), G269 (= G736), R270 (= R737), Y377 (= Y833)
1knwA Crystal structure of diaminopimelate decarboxylase
36% identity, 43% coverage: 489:853/853 of query aligns to 15:397/421 of 1knwA
O81852 Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic; AK-HD 2; AK-HSDH 2; Beta-aspartyl phosphate homoserine 2; EC 2.7.2.4; EC 1.1.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
32% identity, 51% coverage: 2:434/853 of query aligns to 93:538/916 of O81852
- I441 (= I344) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q443 (≠ S346) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- I522 (= I418) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q524 (= Q420) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
2cdqA Crystal structure of arabidopsis thaliana aspartate kinase complexed with lysine and s- adenosylmethionine (see paper)
28% identity, 53% coverage: 1:453/853 of query aligns to 7:464/470 of 2cdqA
- binding lysine: S40 (= S36), A41 (= A37), T46 (= T42), E124 (= E115), M327 (= M320), Q330 (= Q323), F333 (= F326), L334 (= L327), S347 (= S340), V348 (= V341), D349 (= D342)
- binding s-adenosylmethionine: G345 (= G338), I346 (≠ L339), S347 (= S340), W368 (vs. gap), S369 (vs. gap), R370 (≠ N360), L372 (= L362), E376 (≠ A366)
4xg1B Psychromonas ingrahamii diaminopimelate decarboxylase with llp
34% identity, 42% coverage: 498:853/853 of query aligns to 27:393/418 of 4xg1B
- active site: K60 (= K529), H199 (= H662), E273 (= E734)
- binding (2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid: K60 (= K529), D79 (≠ E548), H199 (= H662), S202 (= S665), G239 (= G698), E273 (= E734), G275 (= G736), R276 (= R737), R310 (= R773), Y314 (= Y777), C345 (= C804), E346 (= E805), Y373 (= Y833)
- binding propane: A35 (≠ P506), E38 (≠ R509), E206 (≠ D669), I207 (≠ A670), A208 (= A671)
1twiA Crystal structure of diaminopimelate decarboxylase from m. Jannaschii in co-complex with l-lysine (see paper)
32% identity, 37% coverage: 526:844/853 of query aligns to 66:398/434 of 1twiA
- active site: K69 (= K529), H210 (= H662), E290 (= E734)
- binding lysine: S213 (= S665), R293 (= R737), R329 (= R773), Y333 (= Y777), Y387 (= Y833)
- binding pyridoxal-5'-phosphate: A67 (= A527), K69 (= K529), D88 (≠ E548), N111 (≠ T571), H210 (= H662), S213 (= S665), G250 (= G698), E290 (= E734), G292 (= G736), R293 (= R737), Y387 (= Y833)
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)
32% identity, 37% coverage: 526:844/853 of query aligns to 70:402/438 of Q58497
- K73 (= K529) modified: N6-(pyridoxal phosphate)lysine
- S217 (= S665) binding pyridoxal 5'-phosphate
- G254 (= G698) binding pyridoxal 5'-phosphate
- EPGR 294:297 (= EPGR 734:737) binding pyridoxal 5'-phosphate
- Y391 (= Y833) binding pyridoxal 5'-phosphate
1tufA Crystal structure of diaminopimelate decarboxylase from m. Jannaschi (see paper)
32% identity, 37% coverage: 526:844/853 of query aligns to 66:398/434 of 1tufA
4xg1A Psychromonas ingrahamii diaminopimelate decarboxylase with llp
32% identity, 42% coverage: 498:853/853 of query aligns to 25:368/393 of 4xg1A
- active site: K55 (= K529), H178 (= H662), E246 (= E734)
- binding (2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid: K55 (= K529), D74 (≠ E548), S97 (≠ T571), H178 (= H662), S181 (= S665), G216 (= G698), E246 (= E734), G248 (= G736), R249 (= R737), R285 (= R773), Y289 (= Y777), C320 (= C804), E321 (= E805), Y348 (= Y833)
- binding propane: S121 (≠ H600), I122 (≠ W601)
6n2aA Meso-diaminopimelate decarboxylase from arabidopsis thaliana (isoform 1)
32% identity, 41% coverage: 499:844/853 of query aligns to 31:389/422 of 6n2aA
- binding lysine: K63 (= K529), R281 (= R737), R317 (= R773), Y321 (= Y777), C349 (= C804), E350 (= E805), Y378 (= Y833)
- binding pyridoxal-5'-phosphate: K63 (= K529), H202 (= H662), S205 (= S665), G242 (= G698), E278 (= E734), G280 (= G736), R281 (= R737), Y378 (= Y833)
O60163 Probable aspartokinase; Aspartate kinase; EC 2.7.2.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
29% identity, 40% coverage: 114:453/853 of query aligns to 145:500/519 of O60163
- S326 (vs. gap) modified: Phosphoserine
- T328 (vs. gap) modified: Phosphothreonine
Query Sequence
>WP_027485032.1 NCBI__GCF_021560695.1:WP_027485032.1
MKFGGTSVATLPRWQNIRELVASRRAEGARVLVVVSALTGITDALKQLCGEGEQDKRKAA
AGAVAQRHYDLLEHMQLALPDTLGSRLSDLAALAADGPAPRGELAWQAQVQAHGELMSSA
LGAAFLSHSGLPTQWLDARECLAAVALPNQNERTRLLSAMVEAKPDPALNARLAALGEVF
ITQGFIAREQHGRTVLLGRGGSDTSAAYFGALLKAQRVEIWTDVAGMFTANPRQVPGARL
LQRLDYEEAQEIASTGAKVLHPRCLSPLREPRVPLLIKDTNRPELDGTVIGPEVRAHAPS
VKAISARKGITLVSMESVGMWQQVGFLADVFAHFKTHGLSVDLIGSAETNVTVSLDPTEN
LLDSDAIAALASDLAKVCRVKVIAPCAAITLVGRGMRSLLHTLSGVLAEFGQLRVHLISQ
SSNNLNLTFVVDEEVVDALLPHLHDLLIGAGALRTDDSVLFGPSWQMLYGGGDIVPAVPA
WWRVAQRPRLLELAAAATPRYVYHLPTVRQQAHELKSLAAVDRLHYAVKANTHPAILRAL
AAEGFAFECVSPGELEAVSAVVPASVPLLFTPNFAPRRDYVRALATRASVTLDALHPLQH
WGELFRGREIVLRVDLGRGLGHHEKVRTGGSASKFGLPLDQLPTFLQLADAHGVAVRGLH
AHLGSGVLDAAHWGEVYAQLASLAERIASVVFLNIGGGLGVPAHPGEASLDIAALDRALR
EVKAAYPQYQLWMEPGRYLVADAGVLLTRVTQLKDKGGFRYLGVDTGMNSLIRPALYDAW
HKIVNLSRLGEPATALYQVVGPICESGDVLGTDRRLPEAAEGDVILIAQAGAYGKVMSSH
YNLRDEADEVIID
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