SitesBLAST
Comparing WP_057507033.1 NCBI__GCF_001431535.1:WP_057507033.1 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)
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: 498:860/864 of query aligns to 4:359/386 of Q9X1K5
2yxxA Crystal structure analysis of diaminopimelate decarboxylate (lysa)
36% identity, 42% coverage: 498:860/864 of query aligns to 3:358/385 of 2yxxA
- active site: K45 (= K537), H178 (= H672), E245 (= E744)
- binding pyridoxal-5'-phosphate: K45 (= K537), D64 (≠ E556), H178 (= H672), S181 (= S675), G213 (= G708), E245 (= E744), G247 (= G746), R248 (= R747), Y342 (= Y844)
2j0xA Crystal structure of e. Coli aspartokinase iii in complex with lysine and aspartate (t-state) (see paper)
31% identity, 52% coverage: 11:460/864 of query aligns to 3:447/447 of 2j0xA
- binding aspartic acid: F182 (= F197), G197 (= G212), G198 (= G213), S199 (= S214), D200 (= D215)
- binding lysine: M316 (= M331), S319 (≠ Q334), F322 (= F337), L323 (= L338), S336 (= S351), V337 (= V352), D338 (= D353), S343 (≠ A358), E344 (= E359)
2j0wA Crystal structure of e. Coli aspartokinase iii in complex with aspartate and adp (r-state) (see paper)
31% identity, 52% coverage: 11:460/864 of query aligns to 3:447/447 of 2j0wA
- binding adenosine-5'-diphosphate: T219 (= T234), D220 (= D235), I224 (≠ M239), Y225 (≠ F240), D228 (≠ N243), R230 (≠ K245), K255 (= K270), V256 (= V271)
- binding aspartic acid: S37 (= S49), T43 (= T55), E117 (= E125), F182 (= F197), R196 (= R211), G197 (= G212), S199 (= S214)
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)
31% identity, 52% coverage: 11:460/864 of query aligns to 5:449/449 of P08660
- K8 (= K14) mutation to R: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition.
- E119 (= E125) mutation to D: Increases KM for aspartate about 3000-fold.
- R198 (= R211) mutation to K: Increases KM for aspartate about 200-fold.
- D202 (= D215) mutation to E: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition.
1ko0A Crystal structure of a d,l-lysine complex of diaminopimelate decarboxylase
34% identity, 43% coverage: 497:864/864 of query aligns to 15:397/419 of 1ko0A
- binding d-lysine: K53 (= K537), T156 (= T638), H190 (= H672), Y310 (= Y787), Y377 (= Y844)
- binding lysine: K53 (= K537), R270 (= R747), R306 (= R783), Y310 (= Y787), Y377 (= Y844)
- binding pyridoxal-5'-phosphate: A51 (= A535), K53 (= K537), H190 (= H672), G226 (= G708), E267 (= E744), P268 (= P745), G269 (= G746), R270 (= R747), Y377 (= Y844)
P00861 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Escherichia coli (strain K12)
34% identity, 43% coverage: 497:864/864 of query aligns to 16:398/420 of P00861
- K54 (= K537) modified: N6-(pyridoxal phosphate)lysine
- G227 (= G708) binding
- EPGR 268:271 (= EPGR 744:747) binding
- Y378 (= Y844) binding
1knwA Crystal structure of diaminopimelate decarboxylase
34% identity, 42% coverage: 498:864/864 of query aligns to 16:397/421 of 1knwA
2cdqA Crystal structure of arabidopsis thaliana aspartate kinase complexed with lysine and s-adenosylmethionine (see paper)
29% identity, 52% coverage: 12:464/864 of query aligns to 6:464/470 of 2cdqA
- binding lysine: S40 (= S49), A41 (= A50), T46 (= T55), E124 (= E125), M327 (= M331), Q330 (= Q334), F333 (= F337), L334 (= L338), S347 (= S351), V348 (= V352), D349 (= D353)
- binding s-adenosylmethionine: G345 (= G349), I346 (≠ L350), S347 (= S351), W368 (vs. gap), S369 (vs. gap), R370 (vs. gap), L372 (= L372), E376 (≠ D376)
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)
31% identity, 52% coverage: 10:459/864 of query aligns to 89:552/916 of O81852
- I441 (= I355) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q443 (≠ S357) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- I522 (= I429) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q524 (= Q431) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
3c1nA Crystal structure of allosteric inhibition threonine-sensitive aspartokinase from methanococcus jannaschii with l-threonine (see paper)
33% identity, 52% coverage: 12:460/864 of query aligns to 3:458/458 of 3c1nA
- binding threonine: G7 (= G16), G8 (= G17), T9 (= T18), S10 (= S19), W227 (= W233), T228 (= T234), D229 (= D235), A406 (≠ L410), I409 (≠ K413), A410 (≠ L414), N423 (≠ R425), I424 (≠ V426), Q429 (= Q431), E433 (≠ D435)
2hmfA Structure of a threonine sensitive aspartokinase from methanococcus jannaschii complexed with mg-adp and aspartate (see paper)
31% identity, 52% coverage: 12:460/864 of query aligns to 3:463/464 of 2hmfA
- binding adenosine-5'-diphosphate: G7 (= G16), T229 (= T234), D230 (= D235), V231 (= V236), Y235 (≠ F240), T237 (≠ A242), D238 (≠ N243), P239 (= P244), R240 (≠ K245), K265 (= K270), V266 (= V271)
- binding aspartic acid: S39 (= S49), T45 (= T55), F192 (= F197), R206 (= R211), G207 (= G212), S209 (= S214)
3c1mC Cyrstal structure of threonine-sensitive aspartokinase from methanococcus jannaschii with mgamp-pnp and l-aspartate (see paper)
31% identity, 52% coverage: 12:460/864 of query aligns to 3:467/468 of 3c1mC
- binding phosphoaminophosphonic acid-adenylate ester: K5 (= K14), G7 (= G16), G8 (= G17), S39 (= S49), T229 (= T234), D230 (= D235), Y235 (≠ F240), D238 (≠ N243), P239 (= P244), R240 (≠ K245), K265 (= K270), V266 (= V271)
- binding aspartic acid: T45 (= T55), E129 (= E125), F192 (= F197), R206 (= R211), G207 (= G212), S209 (= S214)
4xg1B Psychromonas ingrahamii diaminopimelate decarboxylase with llp
31% identity, 42% coverage: 501:864/864 of query aligns to 22:393/418 of 4xg1B
- active site: K60 (= K537), H199 (= H672), E273 (= E744)
- binding (2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid: K60 (= K537), D79 (≠ E556), H199 (= H672), S202 (= S675), G239 (= G708), E273 (= E744), G275 (= G746), R276 (= R747), R310 (= R783), Y314 (= Y787), C345 (= C814), E346 (= E815), Y373 (= Y844)
- binding propane: A35 (≠ P514), E38 (≠ R517), E206 (= E678), I207 (≠ T679), A208 (= A680)
6n2aA Meso-diaminopimelate decarboxylase from arabidopsis thaliana (isoform 1)
33% identity, 43% coverage: 487:860/864 of query aligns to 11:394/422 of 6n2aA
- binding lysine: K63 (= K537), R281 (= R747), R317 (= R783), Y321 (= Y787), C349 (= C814), E350 (= E815), Y378 (= Y844)
- binding pyridoxal-5'-phosphate: K63 (= K537), H202 (= H672), S205 (= S675), G242 (= G708), E278 (= E744), G280 (= G746), R281 (= R747), Y378 (= Y844)
4xg1A Psychromonas ingrahamii diaminopimelate decarboxylase with llp
30% identity, 42% coverage: 501:864/864 of query aligns to 20:368/393 of 4xg1A
- active site: K55 (= K537), H178 (= H672), E246 (= E744)
- binding (2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid: K55 (= K537), D74 (≠ E556), S97 (= S583), H178 (= H672), S181 (= S675), G216 (= G708), E246 (= E744), G248 (= G746), R249 (= R747), R285 (= R783), Y289 (= Y787), C320 (= C814), E321 (= E815), Y348 (= Y844)
- binding propane: S121 (≠ A607), I122 (≠ L608)
B4XMC6 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Helicobacter pylori (Campylobacter pylori) (see paper)
33% identity, 38% coverage: 534:864/864 of query aligns to 43:378/405 of B4XMC6
- K46 (= K537) modified: N6-(pyridoxal phosphate)lysine
- I148 (≠ V636) 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 (= G708) binding
- EPGR 259:262 (= EPGR 744:747) binding
- Y358 (= Y844) binding
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)
30% identity, 42% coverage: 499:859/864 of query aligns to 26:406/438 of Q58497
- K73 (= K537) modified: N6-(pyridoxal phosphate)lysine
- S217 (= S675) binding
- G254 (= G708) binding
- EPGR 294:297 (= EPGR 744:747) binding
- Y391 (= Y844) binding
1twiA Crystal structure of diaminopimelate decarboxylase from m. Jannaschii in co-complex with l-lysine (see paper)
30% identity, 42% coverage: 499:859/864 of query aligns to 22:402/434 of 1twiA
- active site: K69 (= K537), H210 (= H672), E290 (= E744)
- binding lysine: S213 (= S675), R293 (= R747), R329 (= R783), Y333 (= Y787), Y387 (= Y844)
- binding pyridoxal-5'-phosphate: A67 (= A535), K69 (= K537), D88 (≠ E556), N111 (≠ T581), H210 (= H672), S213 (= S675), G250 (= G708), E290 (= E744), G292 (= G746), R293 (= R747), Y387 (= Y844)
1tufA Crystal structure of diaminopimelate decarboxylase from m. Jannaschi (see paper)
30% identity, 42% coverage: 499:859/864 of query aligns to 22:402/434 of 1tufA
Query Sequence
>WP_057507033.1 NCBI__GCF_001431535.1:WP_057507033.1
MPVSSPVDRWIVLKFGGTSVSRRHRWDTIGKLAKKRAEETGSRVLVVVSALSGVTNELTA
IADGAADSRARVAALVERHQAFLDELELPRAVLGERLAALQALLDDARAAARTLDWQAEV
LGQGELLSSSIGAAYLHQNGLDMGWMDARQWLDALPPLPNQSPWSQRLSVNCQWKSDEAW
AQRFRAQPTRLLITQGFIARHADGGTAILGRGGSDTSAAYFGALLGASRVEIWTDVPGMF
SANPKDVPDARLLTRLDYYEAQEIATTGAKVLHPRSIKPCRDAGVPMAILDTERPELPGT
SIDGSAAPVPGVKAISRRNGIVLVSMEGIGMWQQVGFLADVFGLFKKHGLSVDLIGSAET
NVTVSLDPSENLVNTDVLAALSADLSQICKVKIIVPCAAITLVGRGMRSLLHKLSDVWAT
FGRERVHMISQSSNDLNLTFVIDETDADGLLPILHAELIDSGAMPVEETAVFGPRWREIA
GTVRPRGTPWWRGQRAHLLQLAEAGTPRYVYHLPTVRARARALAAITPIDQRYYAIKANS
HPAILETLEAEGFGLECVSHGELKHVFNVLPGLSPRRVLFTPSFCPREEFEAAFALGVTV
TVDNVEALQRWPDLFRNRELWLRVDLGRGEGHHAKVRTGGKESKFGLPMARVDEFVRAAT
ELGTTIVGLHAHLGSGVETAQHWRLMCDELAGFARRIGTVQTIDIGGGMPIPYSEEDEPF
DLEAWAEGLAEVKAVHPAFRLAIEPGRYLVAESGVLLTRCTQVVEKEGVRRVGLDAGMNT
LIRPALYDAWHDIENLSRQGGYAEAAFDVVGPICESSDVFGKRRKLPASTAPDDVMVVAD
AGAYGYVMASTYNQRAMPREDILE
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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