SitesBLAST
Comparing WP_013519368.1 NCBI__GCF_000204645.1:WP_013519368.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
8u99A Crystal structure of cystathionine beta lyase from klebsiella aerogenes (plp-serine adduct)
35% identity, 97% coverage: 9:405/409 of query aligns to 2:389/391 of 8u99A
- binding pyridoxal-5'-phosphate: C81 (≠ S87), G82 (= G88), A83 (≠ L89), Y107 (= Y113), D181 (= D185), T205 (= T215), K206 (= K216), M215 (≠ L225), W336 (= W354)
- binding serine: Y107 (= Y113), K206 (= K216), Y334 (= Y352), S335 (= S353), W336 (= W354), R368 (= R384)
8u98A Crystal structure of cystathionine beta lyase from klebsiella aerogenes (plp-glycine adduct)
35% identity, 97% coverage: 9:405/409 of query aligns to 2:389/391 of 8u98A
- binding glycine: Y107 (= Y113), K206 (= K216), Y334 (= Y352), S335 (= S353), W336 (= W354), R368 (= R384)
- binding pyridoxal-5'-phosphate: Y52 (= Y58), R54 (≠ L60), C81 (≠ S87), G82 (= G88), A83 (≠ L89), Y107 (= Y113), D181 (= D185), A203 (= A213), T205 (= T215), K206 (= K216), M215 (≠ L225), W336 (= W354)
8sa9A Crystal structure of cystathionine beta lyase from klebsiella aerogenes, plp-oxamate adduct (c2 form)
35% identity, 97% coverage: 9:405/409 of query aligns to 2:389/391 of 8sa9A
- binding pyridoxal-5'-phosphate: C81 (≠ S87), G82 (= G88), A83 (≠ L89), Y107 (= Y113), D181 (= D185), A203 (= A213), T205 (= T215), K206 (= K216), M215 (≠ L225), W336 (= W354)
- binding [({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino](oxo)acetic acid: C81 (≠ S87), G82 (= G88), A83 (≠ L89), Y107 (= Y113), D181 (= D185), A203 (= A213), T205 (= T215), K206 (= K216), M215 (≠ L225), S335 (= S353), W336 (= W354), R368 (= R384)
8sabA Crystal structure of cystathionine beta lyase from klebsiella aerogenes, plp adduct with alanine (c2 form)
35% identity, 97% coverage: 9:405/409 of query aligns to 3:390/392 of 8sabA
- binding lysine: N9 (≠ H15), R12 (≠ Y18), R13 (= R19), K14 (≠ P20), T17 (≠ G23), L330 (= L347), E341 (≠ M358)
- binding pyridoxal-5'-phosphate: C82 (≠ S87), G83 (= G88), A84 (≠ L89), Y108 (= Y113), D182 (= D185), A204 (= A213), T206 (= T215), K207 (= K216), M216 (≠ L225), W337 (= W354)
- binding alanyl-pyridoxal-5'-phosphate: C82 (≠ S87), G83 (= G88), A84 (≠ L89), Y108 (= Y113), D182 (= D185), A204 (= A213), T206 (= T215), K207 (= K216), M216 (≠ L225), Y335 (= Y352), S336 (= S353), W337 (= W354), R369 (= R384)
8sadA Crystal structure of cystathionine beta lyase from klebsiella aerogenes, plp/malonate complex (c2 form)
35% identity, 97% coverage: 9:405/409 of query aligns to 9:396/398 of 8sadA
- binding magnesium ion: A359 (≠ P367), R362 (= R370), A365 (= A373)
- binding pyridoxal-5'-phosphate: C88 (≠ S87), G89 (= G88), A90 (≠ L89), Y114 (= Y113), D188 (= D185), A210 (= A213), T212 (= T215), K213 (= K216), M222 (≠ L225), W343 (= W354)
2gqnA Cystathionine beta-lyase (cbl) from escherichia coli in complex with n-hydrazinocarbonylmethyl-2-nitro-benzamide (see paper)
32% identity, 97% coverage: 9:405/409 of query aligns to 2:389/391 of 2gqnA
- active site: R54 (≠ L60), Y107 (= Y113), D181 (= D185), K206 (= K216)
- binding (5-hydroxy-6-methyl-4-((2-(2-(2-nitrobenzamido)acetyl)hydrazinyl)methyl)pyridin-3-yl)methyl dihydrogen phosphate: C81 (≠ S87), G82 (= G88), A83 (≠ L89), Y107 (= Y113), E108 (≠ G114), D181 (= D185), A203 (= A213), T205 (= T215), K206 (= K216), M215 (≠ L225), Y334 (= Y352), S335 (= S353), W336 (= W354), R368 (= R384)
2fq6A Cystathionine beta-lyase (cbl) from escherichia coli in complex with n-hydrazinocarbonylmethyl-2-trifluoromethyl-benzamide (see paper)
32% identity, 97% coverage: 9:405/409 of query aligns to 2:389/391 of 2fq6A
- active site: R54 (≠ L60), Y107 (= Y113), D181 (= D185), K206 (= K216)
- binding phosphoric acid mono-(5-hydroxy-6-methyl-4-{[2-(2-trifluoromethyl-benzoylamino)-acetyl]-hydrazonomethyl}-pyridin-3-ylmethyl)ester: C81 (≠ S87), G82 (= G88), A83 (≠ L89), Y107 (= Y113), P109 (= P115), D181 (= D185), A203 (= A213), T205 (= T215), K206 (= K216), M215 (≠ L225), Y334 (= Y352), S335 (= S353), W336 (= W354), R368 (= R384)
1cl2A Cystathionine beta-lyase (cbl) from escherichia coli in complex with aminoethoxyvinylglycine (see paper)
32% identity, 97% coverage: 9:405/409 of query aligns to 2:389/391 of 1cl2A
- active site: R54 (≠ L60), Y107 (= Y113), D181 (= D185), K206 (= K216)
- binding (2E,3E)-4-(2-aminoethoxy)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: C81 (≠ S87), G82 (= G88), A83 (≠ L89), Y107 (= Y113), D181 (= D185), A203 (= A213), T205 (= T215), K206 (= K216), M215 (≠ L225), Y334 (= Y352), S335 (= S353), W336 (= W354), R368 (= R384)
P06721 Cystathionine beta-lyase MetC; CBL; CL; Beta-cystathionase MetC; Cysteine desulfhydrase MetC; CD; Cysteine lyase MetC; Cysteine-S-conjugate beta-lyase MetC; EC 4.4.1.13; EC 4.4.1.28 from Escherichia coli (strain K12) (see 2 papers)
32% identity, 97% coverage: 9:405/409 of query aligns to 6:393/395 of P06721
- K210 (= K216) modified: N6-(pyridoxal phosphate)lysine
1cl1B Cystathionine beta-lyase (cbl) from escherichia coli (see paper)
32% identity, 97% coverage: 9:405/409 of query aligns to 3:390/392 of 1cl1B
4itxA P113s mutant of e. Coli cystathionine beta-lyase metc inhibited by reaction with l-ala-p (see paper)
32% identity, 97% coverage: 9:405/409 of query aligns to 2:389/391 of 4itxA
- active site: R54 (≠ L60), Y107 (= Y113), D181 (= D185), K206 (= K216)
- binding {1-[(3-hydroxy-methyl-5-phosphonooxy-methyl-pyridin-4-ylmethyl)-amino]-ethyl}-phosphonic acid: C81 (≠ S87), G82 (= G88), A83 (≠ L89), Y107 (= Y113), D181 (= D185), A203 (= A213), T205 (= T215), K206 (= K216), M215 (≠ L225), Y334 (= Y352), S335 (= S353), W336 (= W354), R368 (= R384)
7ba4A Structure of cystathionine gamma-lyase from pseudomonas aeruginosa
33% identity, 98% coverage: 5:405/409 of query aligns to 3:373/377 of 7ba4A
8j6nA Crystal structure of cystathionine gamma-lyase in complex with compound 1 (see paper)
31% identity, 86% coverage: 54:406/409 of query aligns to 47:388/390 of 8j6nA
- binding [6-methyl-4-[(~{E})-(oxamoylhydrazinylidene)methyl]-5-oxidanyl-pyridin-3-yl]methyl dihydrogen phosphate: Y51 (= Y58), R53 (≠ L60), G81 (= G88), L82 (= L89), Y105 (= Y113), E148 (= E156), N152 (≠ S160), D178 (= D185), S200 (≠ A213), T202 (= T215), K203 (= K216), E330 (≠ Y352), S331 (= S353), T346 (vs. gap), R366 (= R384)
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
30% identity, 97% coverage: 7:404/409 of query aligns to 8:395/398 of 1pg8A
- active site: R61 (≠ L60), Y114 (= Y113), D186 (= D185), K211 (= K216)
- binding pyridoxal-5'-phosphate: Y59 (= Y58), R61 (≠ L60), S88 (= S87), G89 (= G88), M90 (≠ L89), Y114 (= Y113), D186 (= D185), S208 (≠ A213), T210 (= T215), K211 (= K216)
P13254 L-methionine gamma-lyase; MGL; Homocysteine desulfhydrase; L-methioninase; EC 4.4.1.11; EC 4.4.1.2 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 3 papers)
30% identity, 97% coverage: 7:404/409 of query aligns to 8:395/398 of P13254
- YSR 59:61 (≠ YGL 58:60) binding
- R61 (≠ L60) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (≠ GL 88:89) binding in other chain
- Y114 (= Y113) binding
- C116 (≠ P115) mutation to H: Drastic decrease of the catalytic efficiency of the elimination reaction with L-methionine, by 6700-fold, and increases that with L-cysteine by 7-fold, mainly due to changes in kcat. Loss of ability to catalyze replacement reaction between L-methionine and 2-mercaptoethanol.; mutation to S: 9% of wild-type elimination activity against L-methionine.; mutation to T: 40% of wild-type elimination activity against L-methionine.
- SAT 208:210 (≠ ALT 213:215) binding in other chain
- K211 (= K216) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ R246) mutation K->D,E: Marked decrease in elimination activity against both L-methionine and DL-homocysteine.; mutation to M: 50% reduction in alpha,gamma-elimination activity against DL-homocysteine, while retaining elimination activity against L-methionine and L-cysteine.
- D241 (vs. gap) mutation D->H,R: 5 to 14-fold reduction in alpha,gamma-elimination activity against L-methionine, while no change in affinity for L-methionine.
- R375 (= R384) binding
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
30% identity, 97% coverage: 7:404/409 of query aligns to 7:394/397 of 3vk3A
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
30% identity, 97% coverage: 7:404/409 of query aligns to 2:389/392 of 5x2xA
- active site: R55 (≠ L60), Y108 (= Y113), D180 (= D185), K205 (= K216)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: Y53 (= Y58), R55 (≠ L60), G83 (= G88), M84 (≠ L89), Y108 (= Y113), N155 (≠ S160), D180 (= D185), S202 (≠ A213), T204 (= T215), K205 (= K216), V333 (≠ Y352), S334 (= S353), R369 (= R384)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
30% identity, 97% coverage: 7:404/409 of query aligns to 2:389/392 of 5x2wA
- active site: R55 (≠ L60), Y108 (= Y113), D180 (= D185), K205 (= K216)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y53 (= Y58), R55 (≠ L60), S82 (= S87), G83 (= G88), M84 (≠ L89), Y108 (= Y113), D180 (= D185), S202 (≠ A213), K205 (= K216), V333 (≠ Y352), S334 (= S353), R369 (= R384)
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
30% identity, 97% coverage: 7:404/409 of query aligns to 3:390/393 of 5x30C
4l0oH Structure determination of cystathionine gamma-synthase from helicobacter pylori
30% identity, 97% coverage: 9:405/409 of query aligns to 3:372/373 of 4l0oH
- active site: R40 (≠ L60), Y92 (= Y113), D164 (= D185), K189 (= K216)
- binding pyridoxal-5'-phosphate: Y38 (= Y58), R40 (≠ L60), S67 (= S87), G68 (= G88), L69 (= L89), Y92 (= Y113), D164 (= D185), S186 (≠ A213), T188 (= T215), K189 (= K216)
Query Sequence
>WP_013519368.1 NCBI__GCF_000204645.1:WP_013519368.1
MTQPPAPDLRTRLIHHDYRPPAGFEAPQPAVHKASTVIFPNVAAMRAREWKDKSSYTYGL
HGTPTTYQLEERLATLEGGRQCLLAPSGLAAIATVSLALLRHGDEVLIPDNAYGPNKALA
EVELRHYGIRHQVYDPLDPADLAARITDATRLVWLEAPGSVTLEFPDLPEQVRICRARGV
TTALDNTWGAGLAFAPFDLAGDGQLGVDISVHALTKYPSGGGDVLMGSITTRDEALHLRM
KLTHMRLGLGVGANDVEAVLRSLPSMALRYRAHDAAARALAQWMGTKAPVAQVLHPALPG
SPGHEHWRALCGSAGGPEGAAAGLFSVVIDARHTQAQVDAFCDGLRLFRLGYSWGGPMSL
VVPYDLPGMRERATPHLEAGTVVRFAVGLEAVEDLRQDLAQAMERAFAG
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