SitesBLAST
Comparing Pf6N2E2_1819 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1819 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)
Q5PWZ8 1-aminocyclopropane-1-carboxylate deaminase; ACC deaminase; ACCD; EC 3.5.99.7 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see paper)
97% identity, 100% coverage: 1:338/338 of query aligns to 1:338/338 of Q5PWZ8
- G44 (= G44) mutation to D: Loss of activity.
1rqxC Crystal structure of acc deaminase complexed with inhibitor (see paper)
82% identity, 100% coverage: 1:338/338 of query aligns to 1:338/338 of 1rqxC
- active site: K51 (= K51), Y268 (= Y268), Y294 (= Y294)
- binding 1-aminocyclopropylphosphonate: K51 (= K51), S78 (= S78), N79 (= N79), Q80 (= Q80), T199 (= T199), Y294 (= Y294)
- binding pyridoxal-5'-phosphate: N50 (= N50), K51 (= K51), K54 (= K54), N79 (= N79), S197 (= S197), V198 (= V198), T199 (= T199), G200 (= G200), T202 (= T202), Y294 (= Y294), E295 (= E295), L322 (= L322), G323 (= G323), G324 (= G324)
1tzmA Crystal structure of acc deaminase complexed with substrate analog b- chloro-d-alanine (see paper)
80% identity, 100% coverage: 1:338/338 of query aligns to 1:331/331 of 1tzmA
- active site: K51 (= K51), Y261 (= Y268), Y287 (= Y294)
- binding 3-chloro-D-alanine: G74 (= G74), S78 (= S78), N79 (= N79), Q80 (= Q80), W102 (= W102), A153 (= A160), G154 (= G161), Y287 (= Y294)
- binding amino-acrylate: K51 (= K51), S78 (= S78), Q80 (= Q80), Y287 (= Y294)
- binding pyridoxal-5'-phosphate: N50 (= N50), K51 (= K51), K54 (= K54), N79 (= N79), C189 (= C196), S190 (= S197), V191 (= V198), T192 (= T199), G193 (= G200), T195 (= T202), Y287 (= Y294), E288 (= E295), L315 (= L322), G316 (= G323), G317 (= G324)
1tzkA Crystal structure of 1-aminocyclopropane-1-carboxylate-deaminase complexed with alpha-keto-butyrate (see paper)
80% identity, 100% coverage: 1:338/338 of query aligns to 1:331/331 of 1tzkA
- active site: K51 (= K51), Y261 (= Y268), Y287 (= Y294)
- binding 2-ketobutyric acid: K51 (= K51), G74 (= G74), S78 (= S78), N79 (= N79), Q80 (= Q80), A153 (= A160), G154 (= G161), Y287 (= Y294)
- binding pyridoxal-5'-phosphate: N50 (= N50), K51 (= K51), K54 (= K54), N79 (= N79), C189 (= C196), S190 (= S197), V191 (= V198), T192 (= T199), G193 (= G200), T195 (= T202), Y287 (= Y294), E288 (= E295), L315 (= L322), G316 (= G323), G317 (= G324)
1tzjA Crystal structure of 1-aminocyclopropane-1-carboxylate deaminase complexed with d-vinyl glycine (see paper)
80% identity, 100% coverage: 1:338/338 of query aligns to 1:331/331 of 1tzjA
- active site: K51 (= K51), Y261 (= Y268), Y287 (= Y294)
- binding d-vinylglycine: G74 (= G74), S78 (= S78), N79 (= N79), Q80 (= Q80), A153 (= A160), G154 (= G161), Y287 (= Y294)
- binding pyridoxal-5'-phosphate: N50 (= N50), K51 (= K51), K54 (= K54), N79 (= N79), C189 (= C196), S190 (= S197), V191 (= V198), T192 (= T199), G193 (= G200), T195 (= T202), Y287 (= Y294), E288 (= E295), L315 (= L322), G316 (= G323), G317 (= G324)
1tz2A Crystal structure of 1-aminocyclopropane-1-carboyxlate deaminase complexed with acc (see paper)
80% identity, 100% coverage: 1:338/338 of query aligns to 1:331/331 of 1tz2A
- active site: K51 (= K51), Y261 (= Y268), Y287 (= Y294)
- binding 1-aminocyclopropanecarboxylic acid: K51 (= K51), S78 (= S78), Y287 (= Y294)
- binding pyridoxal-5'-phosphate: N50 (= N50), K51 (= K51), K54 (= K54), N79 (= N79), C189 (= C196), S190 (= S197), V191 (= V198), T192 (= T199), G193 (= G200), T195 (= T202), Y287 (= Y294), E288 (= E295), L315 (= L322), G316 (= G323), G317 (= G324)
1f2dA 1-aminocyclopropane-1-carboxylate deaminase (see paper)
64% identity, 98% coverage: 5:335/338 of query aligns to 5:336/341 of 1f2dA
- active site: K51 (= K51), Y269 (= Y268), Y295 (= Y294)
- binding pyridoxal-5'-phosphate: N50 (= N50), K51 (= K51), K54 (= K54), N79 (= N79), C200 (≠ S197), T202 (= T199), G203 (= G200), S204 (= S201), T205 (= T202), Y295 (= Y294), E296 (= E295), L323 (= L322), G324 (= G323), G325 (= G324)
Q7M523 1-aminocyclopropane-1-carboxylate deaminase; ACC deaminase; ACCD; EC 3.5.99.7 from Cyberlindnera saturnus (Yeast) (Williopsis saturnus) (see paper)
64% identity, 98% coverage: 5:335/338 of query aligns to 5:336/341 of Q7M523
Sites not aligning to the query:
- 1 modified: N-acetylserine
1j0eA Acc deaminase mutant reacton intermediate (see paper)
64% identity, 98% coverage: 5:335/338 of query aligns to 5:336/341 of 1j0eA
- binding 1-aminocyclopropanecarboxylic acid: S78 (= S78), N79 (= N79), Q80 (= Q80), F295 (≠ Y294)
- binding pyridoxal-5'-phosphate: N50 (= N50), K51 (= K51), K54 (= K54), N79 (= N79), C199 (= C196), T202 (= T199), G203 (= G200), T205 (= T202), F295 (≠ Y294), E296 (= E295)
1j0dA Acc deaminase mutant complexed with acc (see paper)
64% identity, 98% coverage: 5:335/338 of query aligns to 5:336/341 of 1j0dA
- binding n-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-y-lmethyl]-1-amino-cyclopropanecarboxylic acid: S78 (= S78), N79 (= N79), Q80 (= Q80), A163 (= A160), G164 (= G161), C200 (≠ S197), V201 (= V198), T202 (= T199), G203 (= G200), S204 (= S201), T205 (= T202), Y295 (= Y294), E296 (= E295)
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)
37% identity, 98% coverage: 2:331/338 of query aligns to 8:327/331 of 4d8uH
4d9fA D-cysteine desulfhydrase from salmonella typhimurium complexed with d- cycloserine (dcs) (see paper)
37% identity, 98% coverage: 2:331/338 of query aligns to 5:324/328 of 4d9fA
- active site: K51 (= K51), Y261 (= Y268), Y287 (= Y294)
- binding d-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-n,o-cycloserylamide: N50 (= N50), K51 (= K51), K54 (= K54), N79 (= N79), G194 (≠ V198), S195 (≠ T199), A196 (≠ G200), T198 (= T202), Y287 (= Y294), T315 (≠ L322), G316 (= G323), G317 (= G324)
4d9eA D-cysteine desulfhydrase from salmonella typhimurium complexed with l- cycloserine (lcs) (see paper)
37% identity, 98% coverage: 2:331/338 of query aligns to 5:324/328 of 4d9eA
- active site: K51 (= K51), Y261 (= Y268), Y287 (= Y294)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: N50 (= N50), K51 (= K51), N79 (= N79), G194 (≠ V198), S195 (≠ T199), A196 (≠ G200), T198 (= T202), Y287 (= Y294), T315 (≠ L322), G316 (= G323), G317 (= G324)
4d9bA Pyridoxamine 5' phosphate (pmp) bound form of salmonella typhimurium d-cysteine desulfhydrase obtained after co-crystallization with d- cycloserine (see paper)
37% identity, 98% coverage: 2:331/338 of query aligns to 5:324/328 of 4d9bA
- active site: K51 (= K51), Y261 (= Y268), Y287 (= Y294)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: N50 (= N50), K51 (= K51), N79 (= N79), G194 (≠ V198), S195 (≠ T199), A196 (≠ G200), T198 (= T202), Y287 (= Y294), T315 (≠ L322), G316 (= G323), G317 (= G324)
4d99A Salmonella typhimurium d-cysteine desulfhydrase with l-ser bound non- covalently at the active site (see paper)
37% identity, 98% coverage: 2:331/338 of query aligns to 5:324/328 of 4d99A
4d97A Salmonella typhimurium d-cysteine desulfhydrase with d-ser bound at active site (see paper)
37% identity, 98% coverage: 2:331/338 of query aligns to 5:324/328 of 4d97A
4d96A D-cysteine desulfhydrase from salmonella typhimurium complexed with 1- amino-1-carboxycyclopropane (acc) (see paper)
37% identity, 98% coverage: 2:331/338 of query aligns to 5:324/328 of 4d96A
- active site: K51 (= K51), Y261 (= Y268), Y287 (= Y294)
- binding n-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-y-lmethyl]-1-amino-cyclopropanecarboxylic acid: N50 (= N50), K51 (= K51), S78 (= S78), N79 (= N79), H80 (≠ Q80), G194 (≠ V198), S195 (≠ T199), A196 (≠ G200), T198 (= T202), Y287 (= Y294), T315 (≠ L322), G316 (= G323), G317 (= G324)
4d8wA Salmonella typhimurium d-cysteine desulfhydrase soaked with d-cys shows pyruvate bound 4 a away from active site (see paper)
37% identity, 98% coverage: 2:331/338 of query aligns to 5:324/328 of 4d8wA
1j0bA Crystal structure analysis of the acc deaminase homologue complexed with inhibitor (see paper)
31% identity, 95% coverage: 3:324/338 of query aligns to 9:310/325 of 1j0bA
- active site: K54 (= K51), Y256 (= Y268), Y282 (= Y294)
- binding n-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-y-lmethyl]-1-amino-cyclopropanecarboxylic acid: N53 (= N50), K54 (= K51), S81 (= S78), N82 (= N79), H83 (≠ Q80), A189 (≠ S197), G190 (≠ V198), S191 (≠ T199), G192 (= G200), G193 (≠ S201), T194 (= T202), Y282 (= Y294), T308 (≠ L322), G309 (= G323), G310 (= G324)
1j0aA Crystal structure analysis of the acc deaminase homologue (see paper)
31% identity, 95% coverage: 3:324/338 of query aligns to 9:310/325 of 1j0aA
- active site: K54 (= K51), Y256 (= Y268), Y282 (= Y294)
- binding pyridoxal-5'-phosphate: N53 (= N50), K54 (= K51), K57 (= K54), N82 (= N79), G190 (≠ V198), S191 (≠ T199), G192 (= G200), G193 (≠ S201), T194 (= T202), Y282 (= Y294), T308 (≠ L322), G309 (= G323), G310 (= G324)
Query Sequence
>Pf6N2E2_1819 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1819
MNLNRFKRYPLTFGPSPITPLKRLSAHLGGKVELYAKREDCNSGLAFGGNKTRKLEYLIP
EAIEQGCDTLVSIGGIQSNQTRQVAAVAAHLGMKCVLVQENWVNYSDAVYDRVGNIEMSR
IMGADVRLDAAGFDIGIRPSWEKAMSDVVEQGGKPFPIPAGCSEHPYGGLGFVGFAEEVR
EQEKQLGFTFDYIVVCSVTGSTQAGMVVGFAADGRSKNVIGIDASAKPEKTKAQILRIAR
HTAELVELGREITEEDVVLDTRFAYPEYGLPNDGTLEAIRLCGSLEGVLTDPVYEGKSMH
GMIEMVRRGEFPEGSKVLYAHLGGAPALNAYSFLFRNG
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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