SitesBLAST
Comparing RR42_RS30610 FitnessBrowser__Cup4G11:RR42_RS30610 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)
43% identity, 94% coverage: 7:388/405 of query aligns to 4:390/391 of 8u99A
- binding pyridoxal-5'-phosphate: C81 (≠ S86), G82 (= G87), A83 (≠ L88), Y107 (= Y112), D181 (= D183), T205 (= T207), K206 (= K208), M215 (= M217), W336 (= W337)
- binding serine: Y107 (= Y112), K206 (= K208), Y334 (≠ A335), S335 (= S336), W336 (= W337), R368 (= R366)
8u98A Crystal structure of cystathionine beta lyase from klebsiella aerogenes (plp-glycine adduct)
43% identity, 94% coverage: 7:388/405 of query aligns to 4:390/391 of 8u98A
- binding glycine: Y107 (= Y112), K206 (= K208), Y334 (≠ A335), S335 (= S336), W336 (= W337), R368 (= R366)
- binding pyridoxal-5'-phosphate: Y52 (= Y57), R54 (≠ A59), C81 (≠ S86), G82 (= G87), A83 (≠ L88), Y107 (= Y112), D181 (= D183), A203 (= A205), T205 (= T207), K206 (= K208), M215 (= M217), W336 (= W337)
8sa9A Crystal structure of cystathionine beta lyase from klebsiella aerogenes, plp-oxamate adduct (c2 form)
43% identity, 94% coverage: 7:388/405 of query aligns to 4:390/391 of 8sa9A
- binding pyridoxal-5'-phosphate: C81 (≠ S86), G82 (= G87), A83 (≠ L88), Y107 (= Y112), D181 (= D183), A203 (= A205), T205 (= T207), K206 (= K208), M215 (= M217), W336 (= W337)
- binding [({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino](oxo)acetic acid: C81 (≠ S86), G82 (= G87), A83 (≠ L88), Y107 (= Y112), D181 (= D183), A203 (= A205), T205 (= T207), K206 (= K208), M215 (= M217), S335 (= S336), W336 (= W337), R368 (= R366)
8sabA Crystal structure of cystathionine beta lyase from klebsiella aerogenes, plp adduct with alanine (c2 form)
43% identity, 94% coverage: 7:388/405 of query aligns to 5:391/392 of 8sabA
- binding lysine: N9 (≠ H11), R12 (= R14), R13 (≠ A15), K14 (≠ S16), T17 (≠ D19), L330 (= L330), E341 (= E341)
- binding pyridoxal-5'-phosphate: C82 (≠ S86), G83 (= G87), A84 (≠ L88), Y108 (= Y112), D182 (= D183), A204 (= A205), T206 (= T207), K207 (= K208), M216 (= M217), W337 (= W337)
- binding alanyl-pyridoxal-5'-phosphate: C82 (≠ S86), G83 (= G87), A84 (≠ L88), Y108 (= Y112), D182 (= D183), A204 (= A205), T206 (= T207), K207 (= K208), M216 (= M217), Y335 (≠ A335), S336 (= S336), W337 (= W337), R369 (= R366)
8sadA Crystal structure of cystathionine beta lyase from klebsiella aerogenes, plp/malonate complex (c2 form)
43% identity, 94% coverage: 7:388/405 of query aligns to 11:397/398 of 8sadA
- binding magnesium ion: A359 (= A347), R362 (= R350), A365 (≠ R353)
- binding pyridoxal-5'-phosphate: C88 (≠ S86), G89 (= G87), A90 (≠ L88), Y114 (= Y112), D188 (= D183), A210 (= A205), T212 (= T207), K213 (= K208), M222 (= M217), W343 (= W337)
1cl1B Cystathionine beta-lyase (cbl) from escherichia coli (see paper)
42% identity, 94% coverage: 7:385/405 of query aligns to 5:388/392 of 1cl1B
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)
42% identity, 94% coverage: 7:385/405 of query aligns to 8:391/395 of P06721
- K210 (= K208) modified: N6-(pyridoxal phosphate)lysine
2gqnA Cystathionine beta-lyase (cbl) from escherichia coli in complex with n-hydrazinocarbonylmethyl-2-nitro-benzamide (see paper)
42% identity, 94% coverage: 7:385/405 of query aligns to 4:387/391 of 2gqnA
- active site: R54 (≠ A59), Y107 (= Y112), D181 (= D183), K206 (= K208)
- binding (5-hydroxy-6-methyl-4-((2-(2-(2-nitrobenzamido)acetyl)hydrazinyl)methyl)pyridin-3-yl)methyl dihydrogen phosphate: C81 (≠ S86), G82 (= G87), A83 (≠ L88), Y107 (= Y112), E108 (= E113), D181 (= D183), A203 (= A205), T205 (= T207), K206 (= K208), M215 (= M217), Y334 (≠ A335), S335 (= S336), W336 (= W337), R368 (= R366)
2fq6A Cystathionine beta-lyase (cbl) from escherichia coli in complex with n-hydrazinocarbonylmethyl-2-trifluoromethyl-benzamide (see paper)
42% identity, 94% coverage: 7:385/405 of query aligns to 4:387/391 of 2fq6A
- active site: R54 (≠ A59), Y107 (= Y112), D181 (= D183), K206 (= K208)
- binding phosphoric acid mono-(5-hydroxy-6-methyl-4-{[2-(2-trifluoromethyl-benzoylamino)-acetyl]-hydrazonomethyl}-pyridin-3-ylmethyl)ester: C81 (≠ S86), G82 (= G87), A83 (≠ L88), Y107 (= Y112), P109 (= P114), D181 (= D183), A203 (= A205), T205 (= T207), K206 (= K208), M215 (= M217), Y334 (≠ A335), S335 (= S336), W336 (= W337), R368 (= R366)
1cl2A Cystathionine beta-lyase (cbl) from escherichia coli in complex with aminoethoxyvinylglycine (see paper)
42% identity, 94% coverage: 7:385/405 of query aligns to 4:387/391 of 1cl2A
- active site: R54 (≠ A59), Y107 (= Y112), D181 (= D183), K206 (= K208)
- binding (2E,3E)-4-(2-aminoethoxy)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: C81 (≠ S86), G82 (= G87), A83 (≠ L88), Y107 (= Y112), D181 (= D183), A203 (= A205), T205 (= T207), K206 (= K208), M215 (= M217), Y334 (≠ A335), S335 (= S336), W336 (= W337), R368 (= R366)
4itxA P113s mutant of e. Coli cystathionine beta-lyase metc inhibited by reaction with l-ala-p (see paper)
42% identity, 94% coverage: 7:385/405 of query aligns to 4:387/391 of 4itxA
- active site: R54 (≠ A59), Y107 (= Y112), D181 (= D183), K206 (= K208)
- binding {1-[(3-hydroxy-methyl-5-phosphonooxy-methyl-pyridin-4-ylmethyl)-amino]-ethyl}-phosphonic acid: C81 (≠ S86), G82 (= G87), A83 (≠ L88), Y107 (= Y112), D181 (= D183), A203 (= A205), T205 (= T207), K206 (= K208), M215 (= M217), Y334 (≠ A335), S335 (= S336), W336 (= W337), R368 (= R366)
4l0oH Structure determination of cystathionine gamma-synthase from helicobacter pylori
35% identity, 94% coverage: 7:388/405 of query aligns to 5:373/373 of 4l0oH
- active site: R40 (≠ A59), Y92 (= Y112), D164 (= D183), K189 (= K208)
- binding pyridoxal-5'-phosphate: Y38 (= Y57), R40 (≠ A59), S67 (= S86), G68 (= G87), L69 (= L88), Y92 (= Y112), D164 (= D183), S186 (≠ A205), T188 (= T207), K189 (= K208)
8j6nA Crystal structure of cystathionine gamma-lyase in complex with compound 1 (see paper)
34% identity, 94% coverage: 7:386/405 of query aligns to 11:386/390 of 8j6nA
- binding [6-methyl-4-[(~{E})-(oxamoylhydrazinylidene)methyl]-5-oxidanyl-pyridin-3-yl]methyl dihydrogen phosphate: Y51 (= Y57), R53 (≠ A59), G81 (= G87), L82 (= L88), Y105 (= Y112), E148 (= E154), N152 (≠ S158), D178 (= D183), S200 (≠ A205), T202 (= T207), K203 (= K208), E330 (≠ A335), S331 (= S336), T346 (≠ G351), R366 (= R366)
P55217 Cystathionine gamma-synthase 1, chloroplastic; AtCGS1; METHIONINE OVERACCUMULATION 1; O-succinylhomoserine (thiol)-lyase; EC 2.5.1.48 from Arabidopsis thaliana (Mouse-ear cress) (see 4 papers)
31% identity, 93% coverage: 13:388/405 of query aligns to 187:563/563 of P55217
- T412 (≠ S241) natural variant: T -> P
- G459 (≠ A288) natural variant: G -> A
Sites not aligning to the query:
- 8 natural variant: C -> S
- 55 natural variant: A -> G
- 77 R→H: In mto1-4; over-accumulation of soluble methionine.
- 78 R→K: In mto1-7; over-accumulation of soluble methionine.
- 81 S→N: In mto1-2; over-accumulation of soluble methionine.
- 84 G→D: In mto1-3 and mto1-5; over-accumulation of soluble methionine.; G→S: In mto1-1; over-accumulation of soluble methionine.
- 86 A→V: In mto1-6; over-accumulation of soluble methionine.
- 91 natural variant: A -> G
5eigC Engineered human cystathionine gamma lyase (e59t, e339v) to deplet cysteine
36% identity, 78% coverage: 55:370/405 of query aligns to 47:368/388 of 5eigC
1e5eA Methionine gamma-lyase (mgl) from trichomonas vaginalis in complex with propargylglycine
30% identity, 90% coverage: 26:388/405 of query aligns to 24:392/394 of 1e5eA
- active site: R55 (≠ A59), Y108 (= Y112), D181 (= D183), K206 (= K208)
- binding n-(hydroxy{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)norvaline: Y53 (= Y57), R55 (≠ A59), G83 (= G87), M84 (≠ L88), Y108 (= Y112), N155 (≠ S158), D181 (= D183), S203 (≠ A205), T205 (= T207), K206 (= K208), S335 (= S336), T350 (vs. gap), R370 (= R366)
1e5fA Methionine gamma-lyase (mgl) from trichomonas vaginalis
30% identity, 90% coverage: 26:388/405 of query aligns to 24:392/393 of 1e5fA
- active site: R55 (≠ A59), Y108 (= Y112), D181 (= D183), K206 (= K208)
- binding pyridoxal-5'-phosphate: Y53 (= Y57), R55 (≠ A59), G83 (= G87), M84 (≠ L88), Y108 (= Y112), D181 (= D183), S203 (≠ A205), K206 (= K208)
P32929 Cystathionine gamma-lyase; CGL; CSE; Cysteine desulfhydrase; Cysteine-protein sulfhydrase; Gamma-cystathionase; Homocysteine desulfhydrase; EC 4.4.1.1; EC 4.4.1.2 from Homo sapiens (Human) (see 5 papers)
35% identity, 79% coverage: 50:370/405 of query aligns to 53:379/405 of P32929
- T67 (= T64) to I: in CSTNU; reduces catalytic activity and affinity for pyridoxal phosphate; dbSNP:rs28941785
- K212 (= K208) modified: N6-(pyridoxal phosphate)lysine
- Q240 (≠ A235) to E: in CSTNU; strongly reduces catalytic activity and affinity for pyridoxal phosphate; dbSNP:rs28941786
Sites not aligning to the query:
- 403 S → I: in dbSNP:rs1021737
6nbaA Crystal structure of human cystathionine gamma lyase with s-3- carboxpropyl-l-cysteine (see paper)
35% identity, 79% coverage: 50:370/405 of query aligns to 44:370/389 of 6nbaA
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: Y51 (= Y57), R53 (≠ A59), G81 (= G87), L82 (= L88), Y105 (= Y112), E148 (= E154), N152 (≠ S158), D178 (= D183), S200 (≠ A205), K203 (= K208), S331 (= S336), T346 (vs. gap), R366 (= R366)
5tsuA Active conformation for engineered human cystathionine gamma lyase (e59n, r119l, e339v) to depleting methionine (see paper)
36% identity, 78% coverage: 55:370/405 of query aligns to 43:363/384 of 5tsuA
Query Sequence
>RR42_RS30610 FitnessBrowser__Cup4G11:RR42_RS30610
MKPSILTHLAHAGRASAVDGGQPVNPPVVRASTVLFDSVAQMREMRSRRGSERLFTYGAR
GNPTAFALEDMVTELEAGYRTRLFPSGLAAAAMTLLAYLRPGQHVLLPDCVYEPVRKLAE
GFLAQHGIAASFYAADGHDLQARLRRETRLVYVEAPGSLAYEMCDLPAIADIAHRHGALV
AADNTWGSGLLYQPLALGADISLMAATKYLSGHSDVMMGTVCTLEAAWPALAAVADAFGI
SVSPDDAYLVQRGMRSLGARLSQHERSALAVAHWLRTRPEVAEVFCPALPGDPGHALWQR
DCHGTNGLLSFALRAVAPDAAERFIDSLALFGIGASWGGFESLAVIADMRGARSVTDWSG
RGQVIRLHIGLEDVDDLLADLARGFEVIGGGRVAGRALEARLDTA
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