SitesBLAST
Comparing WP_011989078.1 NCBI__GCF_000016505.1:WP_011989078.1 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)
38% identity, 96% coverage: 7:321/329 of query aligns to 14:325/331 of 4d8uH
4d9fA D-cysteine desulfhydrase from salmonella typhimurium complexed with d- cycloserine (dcs) (see paper)
38% identity, 96% coverage: 7:321/329 of query aligns to 11:322/328 of 4d9fA
- active site: K51 (= K48), Y261 (= Y260), Y287 (= Y286)
- binding d-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-n,o-cycloserylamide: N50 (= N47), K51 (= K48), K54 (= K51), N79 (= N76), G194 (= G190), S195 (= S191), A196 (≠ G192), T198 (= T194), Y287 (= Y286), T315 (= T314), G316 (= G315), G317 (= G316)
4d9eA D-cysteine desulfhydrase from salmonella typhimurium complexed with l- cycloserine (lcs) (see paper)
38% identity, 96% coverage: 7:321/329 of query aligns to 11:322/328 of 4d9eA
- active site: K51 (= K48), Y261 (= Y260), Y287 (= Y286)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: N50 (= N47), K51 (= K48), N79 (= N76), G194 (= G190), S195 (= S191), A196 (≠ G192), T198 (= T194), Y287 (= Y286), T315 (= T314), G316 (= G315), G317 (= G316)
4d9bA Pyridoxamine 5' phosphate (pmp) bound form of salmonella typhimurium d-cysteine desulfhydrase obtained after co-crystallization with d- cycloserine (see paper)
38% identity, 96% coverage: 7:321/329 of query aligns to 11:322/328 of 4d9bA
- active site: K51 (= K48), Y261 (= Y260), Y287 (= Y286)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: N50 (= N47), K51 (= K48), N79 (= N76), G194 (= G190), S195 (= S191), A196 (≠ G192), T198 (= T194), Y287 (= Y286), T315 (= T314), G316 (= G315), G317 (= G316)
4d99A Salmonella typhimurium d-cysteine desulfhydrase with l-ser bound non- covalently at the active site (see paper)
38% identity, 96% coverage: 7:321/329 of query aligns to 11:322/328 of 4d99A
4d97A Salmonella typhimurium d-cysteine desulfhydrase with d-ser bound at active site (see paper)
38% identity, 96% coverage: 7:321/329 of query aligns to 11:322/328 of 4d97A
4d96A D-cysteine desulfhydrase from salmonella typhimurium complexed with 1- amino-1-carboxycyclopropane (acc) (see paper)
38% identity, 96% coverage: 7:321/329 of query aligns to 11:322/328 of 4d96A
- active site: K51 (= K48), Y261 (= Y260), Y287 (= Y286)
- binding n-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-y-lmethyl]-1-amino-cyclopropanecarboxylic acid: N50 (= N47), K51 (= K48), S78 (= S75), N79 (= N76), H80 (= H77), G194 (= G190), S195 (= S191), A196 (≠ G192), T198 (= T194), Y287 (= Y286), T315 (= T314), G316 (= G315), G317 (= G316)
4d8wA Salmonella typhimurium d-cysteine desulfhydrase soaked with d-cys shows pyruvate bound 4 a away from active site (see paper)
38% identity, 96% coverage: 7:321/329 of query aligns to 11:322/328 of 4d8wA
1j0bA Crystal structure analysis of the acc deaminase homologue complexed with inhibitor (see paper)
40% identity, 98% coverage: 1:321/329 of query aligns to 9:315/325 of 1j0bA
- active site: K54 (= K48), Y256 (≠ V256), Y282 (= Y286)
- binding n-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-y-lmethyl]-1-amino-cyclopropanecarboxylic acid: N53 (= N47), K54 (= K48), S81 (= S75), N82 (= N76), H83 (= H77), A189 (≠ T189), G190 (= G190), S191 (= S191), G192 (= G192), G193 (= G193), T194 (= T194), Y282 (= Y286), T308 (= T314), G309 (= G315), G310 (= G316)
1j0aA Crystal structure analysis of the acc deaminase homologue (see paper)
40% identity, 98% coverage: 1:321/329 of query aligns to 9:315/325 of 1j0aA
- active site: K54 (= K48), Y256 (≠ V256), Y282 (= Y286)
- binding pyridoxal-5'-phosphate: N53 (= N47), K54 (= K48), K57 (= K51), N82 (= N76), G190 (= G190), S191 (= S191), G192 (= G192), G193 (= G193), T194 (= T194), Y282 (= Y286), T308 (= T314), G309 (= G315), G310 (= G316)
1tzmA Crystal structure of acc deaminase complexed with substrate analog b- chloro-d-alanine (see paper)
33% identity, 92% coverage: 14:317/329 of query aligns to 15:318/331 of 1tzmA
- active site: K51 (= K48), Y261 (= Y260), Y287 (= Y286)
- binding 3-chloro-D-alanine: G74 (= G71), S78 (= S75), N79 (= N76), Q80 (≠ H77), W102 (≠ S99), A153 (≠ E153), G154 (= G154), Y287 (= Y286)
- binding amino-acrylate: K51 (= K48), S78 (= S75), Q80 (≠ H77), Y287 (= Y286)
- binding pyridoxal-5'-phosphate: N50 (= N47), K51 (= K48), K54 (= K51), N79 (= N76), C189 (≠ A188), S190 (≠ T189), V191 (≠ G190), T192 (≠ S191), G193 (= G192), T195 (= T194), Y287 (= Y286), E288 (≠ T287), L315 (≠ T314), G316 (= G315), G317 (= G316)
1tzkA Crystal structure of 1-aminocyclopropane-1-carboxylate-deaminase complexed with alpha-keto-butyrate (see paper)
33% identity, 92% coverage: 14:317/329 of query aligns to 15:318/331 of 1tzkA
- active site: K51 (= K48), Y261 (= Y260), Y287 (= Y286)
- binding 2-ketobutyric acid: K51 (= K48), G74 (= G71), S78 (= S75), N79 (= N76), Q80 (≠ H77), A153 (≠ E153), G154 (= G154), Y287 (= Y286)
- binding pyridoxal-5'-phosphate: N50 (= N47), K51 (= K48), K54 (= K51), N79 (= N76), C189 (≠ A188), S190 (≠ T189), V191 (≠ G190), T192 (≠ S191), G193 (= G192), T195 (= T194), Y287 (= Y286), E288 (≠ T287), L315 (≠ T314), G316 (= G315), G317 (= G316)
1tzjA Crystal structure of 1-aminocyclopropane-1-carboxylate deaminase complexed with d-vinyl glycine (see paper)
33% identity, 92% coverage: 14:317/329 of query aligns to 15:318/331 of 1tzjA
- active site: K51 (= K48), Y261 (= Y260), Y287 (= Y286)
- binding d-vinylglycine: G74 (= G71), S78 (= S75), N79 (= N76), Q80 (≠ H77), A153 (≠ E153), G154 (= G154), Y287 (= Y286)
- binding pyridoxal-5'-phosphate: N50 (= N47), K51 (= K48), K54 (= K51), N79 (= N76), C189 (≠ A188), S190 (≠ T189), V191 (≠ G190), T192 (≠ S191), G193 (= G192), T195 (= T194), Y287 (= Y286), E288 (≠ T287), L315 (≠ T314), G316 (= G315), G317 (= G316)
1tz2A Crystal structure of 1-aminocyclopropane-1-carboyxlate deaminase complexed with acc (see paper)
33% identity, 92% coverage: 14:317/329 of query aligns to 15:318/331 of 1tz2A
- active site: K51 (= K48), Y261 (= Y260), Y287 (= Y286)
- binding 1-aminocyclopropanecarboxylic acid: K51 (= K48), S78 (= S75), Y287 (= Y286)
- binding pyridoxal-5'-phosphate: N50 (= N47), K51 (= K48), K54 (= K51), N79 (= N76), C189 (≠ A188), S190 (≠ T189), V191 (≠ G190), T192 (≠ S191), G193 (= G192), T195 (= T194), Y287 (= Y286), E288 (≠ T287), L315 (≠ T314), G316 (= G315), G317 (= G316)
1rqxC Crystal structure of acc deaminase complexed with inhibitor (see paper)
33% identity, 92% coverage: 14:317/329 of query aligns to 15:325/338 of 1rqxC
- active site: K51 (= K48), Y268 (= Y260), Y294 (= Y286)
- binding 1-aminocyclopropylphosphonate: K51 (= K48), S78 (= S75), N79 (= N76), Q80 (≠ H77), T199 (≠ S191), Y294 (= Y286)
- binding pyridoxal-5'-phosphate: N50 (= N47), K51 (= K48), K54 (= K51), N79 (= N76), S197 (≠ T189), V198 (≠ G190), T199 (≠ S191), G200 (= G192), T202 (= T194), Y294 (= Y286), E295 (≠ T287), L322 (≠ T314), G323 (= G315), G324 (= G316)
Q5PWZ8 1-aminocyclopropane-1-carboxylate deaminase; ACC deaminase; ACCD; EC 3.5.99.7 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see paper)
33% identity, 95% coverage: 6:316/329 of query aligns to 7:324/338 of Q5PWZ8
- G44 (= G41) mutation to D: Loss of activity.
1f2dA 1-aminocyclopropane-1-carboxylate deaminase (see paper)
32% identity, 95% coverage: 14:325/329 of query aligns to 15:340/341 of 1f2dA
- active site: K51 (= K48), Y269 (= Y260), Y295 (= Y286)
- binding pyridoxal-5'-phosphate: N50 (= N47), K51 (= K48), K54 (= K51), N79 (= N76), C200 (≠ T189), T202 (≠ S191), G203 (= G192), S204 (≠ G193), T205 (= T194), Y295 (= Y286), E296 (≠ T287), L323 (≠ T314), G324 (= G315), G325 (= G316)
Q7M523 1-aminocyclopropane-1-carboxylate deaminase; ACC deaminase; ACCD; EC 3.5.99.7 from Cyberlindnera saturnus (Yeast) (Williopsis saturnus) (see paper)
32% identity, 95% coverage: 14:325/329 of query aligns to 15:340/341 of Q7M523
Sites not aligning to the query:
- 1 modified: N-acetylserine
1j0eA Acc deaminase mutant reacton intermediate (see paper)
31% identity, 95% coverage: 14:325/329 of query aligns to 15:340/341 of 1j0eA
- binding 1-aminocyclopropanecarboxylic acid: S78 (= S75), N79 (= N76), Q80 (≠ H77), F295 (≠ Y286)
- binding pyridoxal-5'-phosphate: N50 (= N47), K51 (= K48), K54 (= K51), N79 (= N76), C199 (≠ A188), T202 (≠ S191), G203 (= G192), T205 (= T194), F295 (≠ Y286), E296 (≠ T287)
1j0dA Acc deaminase mutant complexed with acc (see paper)
31% identity, 95% coverage: 14:325/329 of query aligns to 15:340/341 of 1j0dA
- binding n-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-y-lmethyl]-1-amino-cyclopropanecarboxylic acid: S78 (= S75), N79 (= N76), Q80 (≠ H77), A163 (≠ E153), G164 (= G154), C200 (≠ T189), V201 (≠ G190), T202 (≠ S191), G203 (= G192), S204 (≠ G193), T205 (= T194), Y295 (= Y286), E296 (≠ T287)
Query Sequence
>WP_011989078.1 NCBI__GCF_000016505.1:WP_011989078.1
MIKIPERMNMANLPTKIEKMERLSQKLGGPDIYIKRDDQTGTEISGNKIRKLEFSAAEAL
NKGCNTLITCGGIQSNHCRATAAVAVKLGFKCCLVLNGSNDTEVDGNLLLDKLLGAEIYF
VSQKEYENRRMEIMKEIKTNMENKGLKPYIIPEGASNGIGGFGYYKAVQEIMLQEREMKV
HFDGIVIATGSGGTYSGLLLGSRILNYDAKIYGVNVCQNEKYFKDRIYEILHDSMKYIDV
NLNFSKDEINIIDGYVGRGYALSREEELEFIKELAELEGIILDPVYTGKAMYGLTQEIKK
GKFSKYKNLLFIHTGGIFGIFPQKSQFRV
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