SitesBLAST
Comparing 3608032 Dshi_1439 pyridoxal phosphate-dependent enzyme, D-cysteine desulfhydrase family (RefSeq) 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)
46% identity, 94% coverage: 16:342/347 of query aligns to 9:331/331 of 4d8uH
4d9fA D-cysteine desulfhydrase from salmonella typhimurium complexed with d- cycloserine (dcs) (see paper)
46% identity, 94% coverage: 16:342/347 of query aligns to 6:328/328 of 4d9fA
- active site: K51 (= K62), Y261 (= Y275), Y287 (= Y301)
- binding d-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-n,o-cycloserylamide: N50 (= N61), K51 (= K62), K54 (= K65), N79 (= N90), G194 (= G206), S195 (= S207), A196 (≠ T208), T198 (= T210), Y287 (= Y301), T315 (= T329), G316 (= G330), G317 (= G331)
4d9eA D-cysteine desulfhydrase from salmonella typhimurium complexed with l- cycloserine (lcs) (see paper)
46% identity, 94% coverage: 16:342/347 of query aligns to 6:328/328 of 4d9eA
- active site: K51 (= K62), Y261 (= Y275), Y287 (= Y301)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: N50 (= N61), K51 (= K62), N79 (= N90), G194 (= G206), S195 (= S207), A196 (≠ T208), T198 (= T210), Y287 (= Y301), T315 (= T329), G316 (= G330), G317 (= G331)
4d9bA Pyridoxamine 5' phosphate (pmp) bound form of salmonella typhimurium d-cysteine desulfhydrase obtained after co-crystallization with d- cycloserine (see paper)
46% identity, 94% coverage: 16:342/347 of query aligns to 6:328/328 of 4d9bA
- active site: K51 (= K62), Y261 (= Y275), Y287 (= Y301)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: N50 (= N61), K51 (= K62), N79 (= N90), G194 (= G206), S195 (= S207), A196 (≠ T208), T198 (= T210), Y287 (= Y301), T315 (= T329), G316 (= G330), G317 (= G331)
4d99A Salmonella typhimurium d-cysteine desulfhydrase with l-ser bound non- covalently at the active site (see paper)
46% identity, 94% coverage: 16:342/347 of query aligns to 6:328/328 of 4d99A
4d97A Salmonella typhimurium d-cysteine desulfhydrase with d-ser bound at active site (see paper)
46% identity, 94% coverage: 16:342/347 of query aligns to 6:328/328 of 4d97A
4d96A D-cysteine desulfhydrase from salmonella typhimurium complexed with 1- amino-1-carboxycyclopropane (acc) (see paper)
46% identity, 94% coverage: 16:342/347 of query aligns to 6:328/328 of 4d96A
- active site: K51 (= K62), Y261 (= Y275), Y287 (= Y301)
- binding n-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-y-lmethyl]-1-amino-cyclopropanecarboxylic acid: N50 (= N61), K51 (= K62), S78 (= S89), N79 (= N90), H80 (= H91), G194 (= G206), S195 (= S207), A196 (≠ T208), T198 (= T210), Y287 (= Y301), T315 (= T329), G316 (= G330), G317 (= G331)
4d8wA Salmonella typhimurium d-cysteine desulfhydrase soaked with d-cys shows pyruvate bound 4 a away from active site (see paper)
46% identity, 94% coverage: 16:342/347 of query aligns to 6:328/328 of 4d8wA
1rqxC Crystal structure of acc deaminase complexed with inhibitor (see paper)
42% identity, 94% coverage: 14:338/347 of query aligns to 1:331/338 of 1rqxC
- active site: K51 (= K62), Y268 (= Y275), Y294 (= Y301)
- binding 1-aminocyclopropylphosphonate: K51 (= K62), S78 (= S89), N79 (= N90), Q80 (≠ H91), T199 (≠ S207), Y294 (= Y301)
- binding pyridoxal-5'-phosphate: N50 (= N61), K51 (= K62), K54 (= K65), N79 (= N90), S197 (≠ T205), V198 (≠ G206), T199 (≠ S207), G200 (≠ T208), T202 (= T210), Y294 (= Y301), E295 (≠ S302), L322 (≠ T329), G323 (= G330), G324 (= G331)
1tzmA Crystal structure of acc deaminase complexed with substrate analog b- chloro-d-alanine (see paper)
42% identity, 94% coverage: 14:338/347 of query aligns to 1:324/331 of 1tzmA
- active site: K51 (= K62), Y261 (= Y275), Y287 (= Y301)
- binding 3-chloro-D-alanine: G74 (= G85), S78 (= S89), N79 (= N90), Q80 (≠ H91), W102 (≠ R113), A153 (≠ G169), G154 (= G170), Y287 (= Y301)
- binding amino-acrylate: K51 (= K62), S78 (= S89), Q80 (≠ H91), Y287 (= Y301)
- binding pyridoxal-5'-phosphate: N50 (= N61), K51 (= K62), K54 (= K65), N79 (= N90), C189 (≠ S204), S190 (≠ T205), V191 (≠ G206), T192 (≠ S207), G193 (≠ T208), T195 (= T210), Y287 (= Y301), E288 (≠ S302), L315 (≠ T329), G316 (= G330), G317 (= G331)
1tzkA Crystal structure of 1-aminocyclopropane-1-carboxylate-deaminase complexed with alpha-keto-butyrate (see paper)
42% identity, 94% coverage: 14:338/347 of query aligns to 1:324/331 of 1tzkA
- active site: K51 (= K62), Y261 (= Y275), Y287 (= Y301)
- binding 2-ketobutyric acid: K51 (= K62), G74 (= G85), S78 (= S89), N79 (= N90), Q80 (≠ H91), A153 (≠ G169), G154 (= G170), Y287 (= Y301)
- binding pyridoxal-5'-phosphate: N50 (= N61), K51 (= K62), K54 (= K65), N79 (= N90), C189 (≠ S204), S190 (≠ T205), V191 (≠ G206), T192 (≠ S207), G193 (≠ T208), T195 (= T210), Y287 (= Y301), E288 (≠ S302), L315 (≠ T329), G316 (= G330), G317 (= G331)
1tzjA Crystal structure of 1-aminocyclopropane-1-carboxylate deaminase complexed with d-vinyl glycine (see paper)
42% identity, 94% coverage: 14:338/347 of query aligns to 1:324/331 of 1tzjA
- active site: K51 (= K62), Y261 (= Y275), Y287 (= Y301)
- binding d-vinylglycine: G74 (= G85), S78 (= S89), N79 (= N90), Q80 (≠ H91), A153 (≠ G169), G154 (= G170), Y287 (= Y301)
- binding pyridoxal-5'-phosphate: N50 (= N61), K51 (= K62), K54 (= K65), N79 (= N90), C189 (≠ S204), S190 (≠ T205), V191 (≠ G206), T192 (≠ S207), G193 (≠ T208), T195 (= T210), Y287 (= Y301), E288 (≠ S302), L315 (≠ T329), G316 (= G330), G317 (= G331)
1tz2A Crystal structure of 1-aminocyclopropane-1-carboyxlate deaminase complexed with acc (see paper)
42% identity, 94% coverage: 14:338/347 of query aligns to 1:324/331 of 1tz2A
- active site: K51 (= K62), Y261 (= Y275), Y287 (= Y301)
- binding 1-aminocyclopropanecarboxylic acid: K51 (= K62), S78 (= S89), Y287 (= Y301)
- binding pyridoxal-5'-phosphate: N50 (= N61), K51 (= K62), K54 (= K65), N79 (= N90), C189 (≠ S204), S190 (≠ T205), V191 (≠ G206), T192 (≠ S207), G193 (≠ T208), T195 (= T210), Y287 (= Y301), E288 (≠ S302), L315 (≠ T329), G316 (= G330), G317 (= G331)
Q5PWZ8 1-aminocyclopropane-1-carboxylate deaminase; ACC deaminase; ACCD; EC 3.5.99.7 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see paper)
42% identity, 94% coverage: 14:338/347 of query aligns to 1:331/338 of Q5PWZ8
- G44 (= G55) mutation to D: Loss of activity.
Q7M523 1-aminocyclopropane-1-carboxylate deaminase; ACC deaminase; ACCD; EC 3.5.99.7 from Cyberlindnera saturnus (Yeast) (Williopsis saturnus) (see paper)
37% identity, 93% coverage: 18:338/347 of query aligns to 5:332/341 of Q7M523
Sites not aligning to the query:
- 1 modified: N-acetylserine
1f2dA 1-aminocyclopropane-1-carboxylate deaminase (see paper)
37% identity, 93% coverage: 18:338/347 of query aligns to 5:332/341 of 1f2dA
- active site: K51 (= K62), Y269 (= Y275), Y295 (= Y301)
- binding pyridoxal-5'-phosphate: N50 (= N61), K51 (= K62), K54 (= K65), N79 (= N90), C200 (≠ T205), T202 (≠ S207), G203 (≠ T208), S204 (≠ G209), T205 (= T210), Y295 (= Y301), E296 (≠ S302), L323 (≠ T329), G324 (= G330), G325 (= G331)
1j0bA Crystal structure analysis of the acc deaminase homologue complexed with inhibitor (see paper)
37% identity, 95% coverage: 16:345/347 of query aligns to 9:324/325 of 1j0bA
- active site: K54 (= K62), Y256 (= Y275), Y282 (= Y301)
- binding n-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-y-lmethyl]-1-amino-cyclopropanecarboxylic acid: N53 (= N61), K54 (= K62), S81 (= S89), N82 (= N90), H83 (= H91), A189 (≠ T205), G190 (= G206), S191 (= S207), G192 (≠ T208), G193 (= G209), T194 (= T210), Y282 (= Y301), T308 (= T329), G309 (= G330), G310 (= G331)
1j0aA Crystal structure analysis of the acc deaminase homologue (see paper)
37% identity, 95% coverage: 16:345/347 of query aligns to 9:324/325 of 1j0aA
- active site: K54 (= K62), Y256 (= Y275), Y282 (= Y301)
- binding pyridoxal-5'-phosphate: N53 (= N61), K54 (= K62), K57 (= K65), N82 (= N90), G190 (= G206), S191 (= S207), G192 (≠ T208), G193 (= G209), T194 (= T210), Y282 (= Y301), T308 (= T329), G309 (= G330), G310 (= G331)
1j0eA Acc deaminase mutant reacton intermediate (see paper)
37% identity, 93% coverage: 18:338/347 of query aligns to 5:332/341 of 1j0eA
- binding 1-aminocyclopropanecarboxylic acid: S78 (= S89), N79 (= N90), Q80 (≠ H91), F295 (≠ Y301)
- binding pyridoxal-5'-phosphate: N50 (= N61), K51 (= K62), K54 (= K65), N79 (= N90), C199 (≠ S204), T202 (≠ S207), G203 (≠ T208), T205 (= T210), F295 (≠ Y301), E296 (≠ S302)
1j0dA Acc deaminase mutant complexed with acc (see paper)
37% identity, 93% coverage: 18:338/347 of query aligns to 5:332/341 of 1j0dA
- binding n-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-y-lmethyl]-1-amino-cyclopropanecarboxylic acid: S78 (= S89), N79 (= N90), Q80 (≠ H91), A163 (≠ G169), G164 (= G170), C200 (≠ T205), V201 (≠ G206), T202 (≠ S207), G203 (≠ T208), S204 (≠ G209), T205 (= T210), Y295 (= Y301), E296 (≠ S302)
Query Sequence
>3608032 Dshi_1439 pyridoxal phosphate-dependent enzyme, D-cysteine desulfhydrase family (RefSeq)
MSSTETLDRQHAQIDLDRFPRTPLCHQPTPIEAMPRLSAALGGPSLFVKRDDCTGLAMGG
NKTRKLEFLVGEAMEEKADMLVTQGAVQSNHVRQTAAAACKLGMKCHVLLERRVPGRDAS
YESTGNVLLDNLFGATHEFRPAGLDMNAEARTVTERLQAEGHRPYFIPGGGSNPTGALGY
VACAREIAEHSRATGQSFDWLVMSTGSTGTHAGLVAGFHAMGHELPVMGVSVRQPRERQM
QAVHALTQATLEKLGHDGVPLKKIIVDDGYVGEGYGIPAPSTLEAIRLTARQEGLLLDPV
YSAKGMAGLIGMVRSGFFKPSDSVLFLHTGGASALFAYEDQITALAD
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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