SitesBLAST
Comparing WP_044051560.1 NCBI__GCF_000738435.1:WP_044051560.1 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)
4d9fA D-cysteine desulfhydrase from salmonella typhimurium complexed with d- cycloserine (dcs) (see paper)
44% identity, 96% coverage: 2:324/337 of query aligns to 5:324/328 of 4d9fA
- active site: K51 (= K48), Y261 (= Y262), Y287 (= Y288)
- binding d-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-n,o-cycloserylamide: N50 (= N47), K51 (= K48), K54 (= K51), N79 (= N76), G194 (= G192), S195 (= S193), A196 (≠ S194), T198 (= T196), Y287 (= Y288), T315 (= T315), G316 (= G316), G317 (= G317)
4d9eA D-cysteine desulfhydrase from salmonella typhimurium complexed with l- cycloserine (lcs) (see paper)
44% identity, 96% coverage: 2:324/337 of query aligns to 5:324/328 of 4d9eA
- active site: K51 (= K48), Y261 (= Y262), Y287 (= Y288)
- 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 (= G192), S195 (= S193), A196 (≠ S194), T198 (= T196), Y287 (= Y288), T315 (= T315), G316 (= G316), G317 (= G317)
4d9bA Pyridoxamine 5' phosphate (pmp) bound form of salmonella typhimurium d-cysteine desulfhydrase obtained after co-crystallization with d- cycloserine (see paper)
44% identity, 96% coverage: 2:324/337 of query aligns to 5:324/328 of 4d9bA
- active site: K51 (= K48), Y261 (= Y262), Y287 (= Y288)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: N50 (= N47), K51 (= K48), N79 (= N76), G194 (= G192), S195 (= S193), A196 (≠ S194), T198 (= T196), Y287 (= Y288), T315 (= T315), G316 (= G316), G317 (= G317)
4d99A Salmonella typhimurium d-cysteine desulfhydrase with l-ser bound non- covalently at the active site (see paper)
44% identity, 96% coverage: 2:324/337 of query aligns to 5:324/328 of 4d99A
4d97A Salmonella typhimurium d-cysteine desulfhydrase with d-ser bound at active site (see paper)
44% identity, 96% coverage: 2:324/337 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)
44% identity, 96% coverage: 2:324/337 of query aligns to 5:324/328 of 4d96A
- active site: K51 (= K48), Y261 (= Y262), Y287 (= Y288)
- binding n-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-y-lmethyl]-1-amino-cyclopropanecarboxylic acid: N50 (= N47), K51 (= K48), S78 (≠ T75), N79 (= N76), H80 (= H77), G194 (= G192), S195 (= S193), A196 (≠ S194), T198 (= T196), Y287 (= Y288), T315 (= T315), G316 (= G316), G317 (= G317)
4d8wA Salmonella typhimurium d-cysteine desulfhydrase soaked with d-cys shows pyruvate bound 4 a away from active site (see paper)
44% identity, 96% coverage: 2:324/337 of query aligns to 5:324/328 of 4d8wA
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)
44% identity, 96% coverage: 2:324/337 of query aligns to 8:327/331 of 4d8uH
1rqxC Crystal structure of acc deaminase complexed with inhibitor (see paper)
41% identity, 97% coverage: 1:328/337 of query aligns to 1:335/338 of 1rqxC
- active site: K51 (= K48), Y268 (= Y262), Y294 (= Y288)
- binding 1-aminocyclopropylphosphonate: K51 (= K48), S78 (≠ T75), N79 (= N76), Q80 (≠ H77), T199 (≠ S193), Y294 (= Y288)
- binding pyridoxal-5'-phosphate: N50 (= N47), K51 (= K48), K54 (= K51), N79 (= N76), S197 (≠ T191), V198 (≠ G192), T199 (≠ S193), G200 (≠ S194), T202 (= T196), Y294 (= Y288), E295 (≠ S289), L322 (≠ T315), G323 (= G316), G324 (= G317)
1tzmA Crystal structure of acc deaminase complexed with substrate analog b- chloro-d-alanine (see paper)
41% identity, 97% coverage: 1:328/337 of query aligns to 1:328/331 of 1tzmA
- active site: K51 (= K48), Y261 (= Y262), Y287 (= Y288)
- binding 3-chloro-D-alanine: G74 (= G71), S78 (≠ T75), N79 (= N76), Q80 (≠ H77), W102 (≠ R99), A153 (≠ G155), G154 (= G156), Y287 (= Y288)
- binding amino-acrylate: K51 (= K48), S78 (≠ T75), Q80 (≠ H77), Y287 (= Y288)
- binding pyridoxal-5'-phosphate: N50 (= N47), K51 (= K48), K54 (= K51), N79 (= N76), C189 (≠ A190), S190 (≠ T191), V191 (≠ G192), T192 (≠ S193), G193 (≠ S194), T195 (= T196), Y287 (= Y288), E288 (≠ S289), L315 (≠ T315), G316 (= G316), G317 (= G317)
1tzkA Crystal structure of 1-aminocyclopropane-1-carboxylate-deaminase complexed with alpha-keto-butyrate (see paper)
41% identity, 97% coverage: 1:328/337 of query aligns to 1:328/331 of 1tzkA
- active site: K51 (= K48), Y261 (= Y262), Y287 (= Y288)
- binding 2-ketobutyric acid: K51 (= K48), G74 (= G71), S78 (≠ T75), N79 (= N76), Q80 (≠ H77), A153 (≠ G155), G154 (= G156), Y287 (= Y288)
- binding pyridoxal-5'-phosphate: N50 (= N47), K51 (= K48), K54 (= K51), N79 (= N76), C189 (≠ A190), S190 (≠ T191), V191 (≠ G192), T192 (≠ S193), G193 (≠ S194), T195 (= T196), Y287 (= Y288), E288 (≠ S289), L315 (≠ T315), G316 (= G316), G317 (= G317)
1tzjA Crystal structure of 1-aminocyclopropane-1-carboxylate deaminase complexed with d-vinyl glycine (see paper)
41% identity, 97% coverage: 1:328/337 of query aligns to 1:328/331 of 1tzjA
- active site: K51 (= K48), Y261 (= Y262), Y287 (= Y288)
- binding d-vinylglycine: G74 (= G71), S78 (≠ T75), N79 (= N76), Q80 (≠ H77), A153 (≠ G155), G154 (= G156), Y287 (= Y288)
- binding pyridoxal-5'-phosphate: N50 (= N47), K51 (= K48), K54 (= K51), N79 (= N76), C189 (≠ A190), S190 (≠ T191), V191 (≠ G192), T192 (≠ S193), G193 (≠ S194), T195 (= T196), Y287 (= Y288), E288 (≠ S289), L315 (≠ T315), G316 (= G316), G317 (= G317)
1tz2A Crystal structure of 1-aminocyclopropane-1-carboyxlate deaminase complexed with acc (see paper)
41% identity, 97% coverage: 1:328/337 of query aligns to 1:328/331 of 1tz2A
- active site: K51 (= K48), Y261 (= Y262), Y287 (= Y288)
- binding 1-aminocyclopropanecarboxylic acid: K51 (= K48), S78 (≠ T75), Y287 (= Y288)
- binding pyridoxal-5'-phosphate: N50 (= N47), K51 (= K48), K54 (= K51), N79 (= N76), C189 (≠ A190), S190 (≠ T191), V191 (≠ G192), T192 (≠ S193), G193 (≠ S194), T195 (= T196), Y287 (= Y288), E288 (≠ S289), L315 (≠ T315), G316 (= G316), G317 (= G317)
Q5PWZ8 1-aminocyclopropane-1-carboxylate deaminase; ACC deaminase; ACCD; EC 3.5.99.7 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see paper)
39% identity, 97% coverage: 1:328/337 of query aligns to 1:335/338 of Q5PWZ8
- G44 (= G41) mutation to D: Loss of activity.
1j0bA Crystal structure analysis of the acc deaminase homologue complexed with inhibitor (see paper)
41% identity, 94% coverage: 3:319/337 of query aligns to 9:312/325 of 1j0bA
- active site: K54 (= K48), Y256 (= Y262), Y282 (= Y288)
- binding n-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-y-lmethyl]-1-amino-cyclopropanecarboxylic acid: N53 (= N47), K54 (= K48), S81 (≠ T75), N82 (= N76), H83 (= H77), A189 (≠ T191), G190 (= G192), S191 (= S193), G192 (≠ S194), G193 (= G195), T194 (= T196), Y282 (= Y288), T308 (= T315), G309 (= G316), G310 (= G317)
1j0aA Crystal structure analysis of the acc deaminase homologue (see paper)
41% identity, 94% coverage: 3:319/337 of query aligns to 9:312/325 of 1j0aA
- active site: K54 (= K48), Y256 (= Y262), Y282 (= Y288)
- binding pyridoxal-5'-phosphate: N53 (= N47), K54 (= K48), K57 (= K51), N82 (= N76), G190 (= G192), S191 (= S193), G192 (≠ S194), G193 (= G195), T194 (= T196), Y282 (= Y288), T308 (= T315), G309 (= G316), G310 (= G317)
Q7M523 1-aminocyclopropane-1-carboxylate deaminase; ACC deaminase; ACCD; EC 3.5.99.7 from Cyberlindnera saturnus (Yeast) (Williopsis saturnus) (see paper)
34% identity, 97% coverage: 3:328/337 of query aligns to 3:336/341 of Q7M523
Sites not aligning to the query:
- 1 modified: N-acetylserine
1f2dA 1-aminocyclopropane-1-carboxylate deaminase (see paper)
34% identity, 97% coverage: 3:328/337 of query aligns to 3:336/341 of 1f2dA
- active site: K51 (= K48), Y269 (= Y262), Y295 (= Y288)
- binding pyridoxal-5'-phosphate: N50 (= N47), K51 (= K48), K54 (= K51), N79 (= N76), C200 (≠ T191), T202 (≠ S193), G203 (≠ S194), S204 (≠ G195), T205 (= T196), Y295 (= Y288), E296 (≠ S289), L323 (≠ T315), G324 (= G316), G325 (= G317)
1j0eA Acc deaminase mutant reacton intermediate (see paper)
33% identity, 97% coverage: 3:328/337 of query aligns to 3:336/341 of 1j0eA
- binding 1-aminocyclopropanecarboxylic acid: S78 (≠ T75), N79 (= N76), Q80 (≠ H77), F295 (≠ Y288)
- binding pyridoxal-5'-phosphate: N50 (= N47), K51 (= K48), K54 (= K51), N79 (= N76), C199 (≠ A190), T202 (≠ S193), G203 (≠ S194), T205 (= T196), F295 (≠ Y288), E296 (≠ S289)
1j0dA Acc deaminase mutant complexed with acc (see paper)
33% identity, 97% coverage: 3:328/337 of query aligns to 3:336/341 of 1j0dA
- binding n-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-y-lmethyl]-1-amino-cyclopropanecarboxylic acid: S78 (≠ T75), N79 (= N76), Q80 (≠ H77), A163 (≠ G155), G164 (= G156), C200 (≠ T191), V201 (≠ G192), T202 (≠ S193), G203 (≠ S194), S204 (≠ G195), T205 (= T196), Y295 (= Y288), E296 (≠ S289)
Query Sequence
>WP_044051560.1 NCBI__GCF_000738435.1:WP_044051560.1
MHLARFPRVFLAHLSTPLEPMERLSKELGVEIWIKRDDCTGMSTGGNKTRKLEFLMAEAL
DQGADMVMTQGATQTNHGRQTAAFAAKLGLKCHILLEDRTGYQDGNYNTNGNVLLDHLHG
ATTQKFPAGHDMPGEMERAAEAKRAEGHKVYVIPGGGSNPTGALGYVNAAFELLGQANDR
GLKFDRLVHATGSSGTQAGLVTGLCAMNAQLPVLGIGTRAPMEKQENMVFDLACRTAEKL
GCPGVVQRSDVMANTDYVGEGYGLPTKSGLEAIKMFAELEGILLDPCYSAKGAAGLIDLA
RKGAFYGERIVFLHTGGAAALGGYDFAFDFSRNWVTL
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