SitesBLAST
Comparing PfGW456L13_3549 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_3549 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)
4d8uH Crystal structure of d-cysteine desulfhydrase from salmonella typhimurium at 3.3 a in monoclinic space group with 8 subunits in the asymmetric unit (see paper)
42% identity, 96% coverage: 9:338/343 of query aligns to 9:328/331 of 4d8uH
4d9fA D-cysteine desulfhydrase from salmonella typhimurium complexed with d- cycloserine (dcs) (see paper)
42% identity, 96% coverage: 9:338/343 of query aligns to 6:325/328 of 4d9fA
- active site: K51 (= K59), Y261 (= Y274), Y287 (= Y300)
- binding d-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-n,o-cycloserylamide: N50 (= N58), K51 (= K59), K54 (= K62), N79 (= N87), G194 (= G203), S195 (= S204), A196 (= A205), T198 (= T207), Y287 (= Y300), T315 (= T328), G316 (= G329), G317 (= G330)
4d9eA D-cysteine desulfhydrase from salmonella typhimurium complexed with l- cycloserine (lcs) (see paper)
42% identity, 96% coverage: 9:338/343 of query aligns to 6:325/328 of 4d9eA
- active site: K51 (= K59), Y261 (= Y274), Y287 (= Y300)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: N50 (= N58), K51 (= K59), N79 (= N87), G194 (= G203), S195 (= S204), A196 (= A205), T198 (= T207), Y287 (= Y300), T315 (= T328), G316 (= G329), G317 (= G330)
4d9bA Pyridoxamine 5' phosphate (pmp) bound form of salmonella typhimurium d-cysteine desulfhydrase obtained after co-crystallization with d- cycloserine (see paper)
42% identity, 96% coverage: 9:338/343 of query aligns to 6:325/328 of 4d9bA
- active site: K51 (= K59), Y261 (= Y274), Y287 (= Y300)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: N50 (= N58), K51 (= K59), N79 (= N87), G194 (= G203), S195 (= S204), A196 (= A205), T198 (= T207), Y287 (= Y300), T315 (= T328), G316 (= G329), G317 (= G330)
4d99A Salmonella typhimurium d-cysteine desulfhydrase with l-ser bound non- covalently at the active site (see paper)
42% identity, 96% coverage: 9:338/343 of query aligns to 6:325/328 of 4d99A
4d97A Salmonella typhimurium d-cysteine desulfhydrase with d-ser bound at active site (see paper)
42% identity, 96% coverage: 9:338/343 of query aligns to 6:325/328 of 4d97A
4d96A D-cysteine desulfhydrase from salmonella typhimurium complexed with 1- amino-1-carboxycyclopropane (acc) (see paper)
42% identity, 96% coverage: 9:338/343 of query aligns to 6:325/328 of 4d96A
- active site: K51 (= K59), Y261 (= Y274), Y287 (= Y300)
- binding n-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-y-lmethyl]-1-amino-cyclopropanecarboxylic acid: N50 (= N58), K51 (= K59), S78 (= S86), N79 (= N87), H80 (= H88), G194 (= G203), S195 (= S204), A196 (= A205), T198 (= T207), Y287 (= Y300), T315 (= T328), G316 (= G329), G317 (= G330)
4d8wA Salmonella typhimurium d-cysteine desulfhydrase soaked with d-cys shows pyruvate bound 4 a away from active site (see paper)
42% identity, 96% coverage: 9:338/343 of query aligns to 6:325/328 of 4d8wA
1rqxC Crystal structure of acc deaminase complexed with inhibitor (see paper)
38% identity, 98% coverage: 8:342/343 of query aligns to 2:336/338 of 1rqxC
- active site: K51 (= K59), Y268 (= Y274), Y294 (= Y300)
- binding 1-aminocyclopropylphosphonate: K51 (= K59), S78 (= S86), N79 (= N87), Q80 (≠ H88), T199 (≠ S204), Y294 (= Y300)
- binding pyridoxal-5'-phosphate: N50 (= N58), K51 (= K59), K54 (= K62), N79 (= N87), S197 (≠ N202), V198 (≠ G203), T199 (≠ S204), G200 (≠ A205), T202 (= T207), Y294 (= Y300), E295 (≠ S301), L322 (≠ T328), G323 (= G329), G324 (= G330)
Q5PWZ8 1-aminocyclopropane-1-carboxylate deaminase; ACC deaminase; ACCD; EC 3.5.99.7 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see paper)
35% identity, 98% coverage: 8:342/343 of query aligns to 2:336/338 of Q5PWZ8
- G44 (≠ L52) mutation to D: Loss of activity.
1tzmA Crystal structure of acc deaminase complexed with substrate analog b- chloro-d-alanine (see paper)
38% identity, 98% coverage: 8:342/343 of query aligns to 2:329/331 of 1tzmA
- active site: K51 (= K59), Y261 (= Y274), Y287 (= Y300)
- binding 3-chloro-D-alanine: G74 (= G82), S78 (= S86), N79 (= N87), Q80 (≠ H88), W102 (≠ A110), A153 (≠ T166), G154 (= G167), Y287 (= Y300)
- binding amino-acrylate: K51 (= K59), S78 (= S86), Q80 (≠ H88), Y287 (= Y300)
- binding pyridoxal-5'-phosphate: N50 (= N58), K51 (= K59), K54 (= K62), N79 (= N87), C189 (≠ P201), S190 (≠ N202), V191 (≠ G203), T192 (≠ S204), G193 (≠ A205), T195 (= T207), Y287 (= Y300), E288 (≠ S301), L315 (≠ T328), G316 (= G329), G317 (= G330)
1tzkA Crystal structure of 1-aminocyclopropane-1-carboxylate-deaminase complexed with alpha-keto-butyrate (see paper)
38% identity, 98% coverage: 8:342/343 of query aligns to 2:329/331 of 1tzkA
- active site: K51 (= K59), Y261 (= Y274), Y287 (= Y300)
- binding 2-ketobutyric acid: K51 (= K59), G74 (= G82), S78 (= S86), N79 (= N87), Q80 (≠ H88), A153 (≠ T166), G154 (= G167), Y287 (= Y300)
- binding pyridoxal-5'-phosphate: N50 (= N58), K51 (= K59), K54 (= K62), N79 (= N87), C189 (≠ P201), S190 (≠ N202), V191 (≠ G203), T192 (≠ S204), G193 (≠ A205), T195 (= T207), Y287 (= Y300), E288 (≠ S301), L315 (≠ T328), G316 (= G329), G317 (= G330)
1tzjA Crystal structure of 1-aminocyclopropane-1-carboxylate deaminase complexed with d-vinyl glycine (see paper)
38% identity, 98% coverage: 8:342/343 of query aligns to 2:329/331 of 1tzjA
- active site: K51 (= K59), Y261 (= Y274), Y287 (= Y300)
- binding d-vinylglycine: G74 (= G82), S78 (= S86), N79 (= N87), Q80 (≠ H88), A153 (≠ T166), G154 (= G167), Y287 (= Y300)
- binding pyridoxal-5'-phosphate: N50 (= N58), K51 (= K59), K54 (= K62), N79 (= N87), C189 (≠ P201), S190 (≠ N202), V191 (≠ G203), T192 (≠ S204), G193 (≠ A205), T195 (= T207), Y287 (= Y300), E288 (≠ S301), L315 (≠ T328), G316 (= G329), G317 (= G330)
1tz2A Crystal structure of 1-aminocyclopropane-1-carboyxlate deaminase complexed with acc (see paper)
38% identity, 98% coverage: 8:342/343 of query aligns to 2:329/331 of 1tz2A
- active site: K51 (= K59), Y261 (= Y274), Y287 (= Y300)
- binding 1-aminocyclopropanecarboxylic acid: K51 (= K59), S78 (= S86), Y287 (= Y300)
- binding pyridoxal-5'-phosphate: N50 (= N58), K51 (= K59), K54 (= K62), N79 (= N87), C189 (≠ P201), S190 (≠ N202), V191 (≠ G203), T192 (≠ S204), G193 (≠ A205), T195 (= T207), Y287 (= Y300), E288 (≠ S301), L315 (≠ T328), G316 (= G329), G317 (= G330)
1j0bA Crystal structure analysis of the acc deaminase homologue complexed with inhibitor (see paper)
37% identity, 98% coverage: 1:337/343 of query aligns to 1:317/325 of 1j0bA
- active site: K54 (= K59), Y256 (= Y274), Y282 (= Y300)
- binding n-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-y-lmethyl]-1-amino-cyclopropanecarboxylic acid: N53 (= N58), K54 (= K59), S81 (= S86), N82 (= N87), H83 (= H88), A189 (≠ N202), G190 (= G203), S191 (= S204), G192 (≠ A205), G193 (= G206), T194 (= T207), Y282 (= Y300), T308 (= T328), G309 (= G329), G310 (= G330)
1j0aA Crystal structure analysis of the acc deaminase homologue (see paper)
37% identity, 98% coverage: 1:337/343 of query aligns to 1:317/325 of 1j0aA
- active site: K54 (= K59), Y256 (= Y274), Y282 (= Y300)
- binding pyridoxal-5'-phosphate: N53 (= N58), K54 (= K59), K57 (= K62), N82 (= N87), G190 (= G203), S191 (= S204), G192 (≠ A205), G193 (= G206), T194 (= T207), Y282 (= Y300), T308 (= T328), G309 (= G329), G310 (= G330)
Q7M523 1-aminocyclopropane-1-carboxylate deaminase; ACC deaminase; ACCD; EC 3.5.99.7 from Cyberlindnera saturnus (Yeast) (Williopsis saturnus) (see paper)
35% identity, 96% coverage: 12:341/343 of query aligns to 6:336/341 of Q7M523
Sites not aligning to the query:
- 1 modified: N-acetylserine
1f2dA 1-aminocyclopropane-1-carboxylate deaminase (see paper)
35% identity, 96% coverage: 12:341/343 of query aligns to 6:336/341 of 1f2dA
- active site: K51 (= K59), Y269 (= Y274), Y295 (= Y300)
- binding pyridoxal-5'-phosphate: N50 (= N58), K51 (= K59), K54 (= K62), N79 (= N87), C200 (≠ N202), T202 (≠ S204), G203 (≠ A205), S204 (≠ G206), T205 (= T207), Y295 (= Y300), E296 (≠ S301), L323 (≠ T328), G324 (= G329), G325 (= G330)
1j0eA Acc deaminase mutant reacton intermediate (see paper)
34% identity, 96% coverage: 12:341/343 of query aligns to 6:336/341 of 1j0eA
- binding 1-aminocyclopropanecarboxylic acid: S78 (= S86), N79 (= N87), Q80 (≠ H88), F295 (≠ Y300)
- binding pyridoxal-5'-phosphate: N50 (= N58), K51 (= K59), K54 (= K62), N79 (= N87), C199 (≠ P201), T202 (≠ S204), G203 (≠ A205), T205 (= T207), F295 (≠ Y300), E296 (≠ S301)
1j0dA Acc deaminase mutant complexed with acc (see paper)
34% identity, 96% coverage: 12:341/343 of query aligns to 6:336/341 of 1j0dA
- binding n-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-y-lmethyl]-1-amino-cyclopropanecarboxylic acid: S78 (= S86), N79 (= N87), Q80 (≠ H88), A163 (≠ T166), G164 (= G167), C200 (≠ N202), V201 (≠ G203), T202 (≠ S204), G203 (≠ A205), S204 (≠ G206), T205 (= T207), Y295 (= Y300), E296 (≠ S301)
Query Sequence
>PfGW456L13_3549 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_3549
MQTQLDKSLSVFARADLLQGPTPIQRAARLEQLLGLDKQGIGLFLKRDDHMLIGAGGNKL
RKLEFHIGAALQAGIDTIITVGGIQSNHARLTAAVCARLGIACELLLTRAVAKAEVDYEL
NGNVLLDQLFGAQMQVFAGGTDSLAKAEARAALLRDSGHKVMVLPTGGSTPLGSLGYARC
AAEIAQQEAELQLTFNQVVVPNGSAGTHAGLAAGFRLLGRGTSMVKSFSVLSDQESSIAR
TLQLTRETLALLDSNAQVRADELVVDGSQLGTGYGLPTAAMQDAVRLMARAEGLLVDPVY
SGKAFAGLLADLQQGRFVPGDNVLFIMTGGTPGLYAYRETFQA
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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