SitesBLAST
Comparing WP_012710112.1 NCBI__GCF_000018545.1:WP_012710112.1 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)
2ay9A Aromatic amino acid aminotransferase with 5-phenylvaleric acid (see paper)
47% identity, 96% coverage: 1:375/389 of query aligns to 1:378/394 of 2ay9A
- active site: W127 (= W126), D208 (= D207), A210 (= A209), K243 (= K242)
- binding 5-phenylvaleric acid: Y65 (= Y65), W127 (= W126), N129 (= N128), N180 (= N179), S281 (= S280), F282 (≠ M281), R371 (= R368)
- binding pyridoxal-5'-phosphate: G99 (= G99), G100 (= G100), T101 (≠ S101), W127 (= W126), N180 (= N179), D208 (= D207), A210 (= A209), Y211 (= Y210), S240 (= S239), S242 (= S241), K243 (= K242), R251 (= R250)
2ay8A Aromatic amino acid aminotransferase with 4-(2-thienyl)butyric acid (see paper)
47% identity, 96% coverage: 1:375/389 of query aligns to 1:378/394 of 2ay8A
- active site: W127 (= W126), D208 (= D207), A210 (= A209), K243 (= K242)
- binding 4-(2-thienyl)butyric acid: G34 (= G34), Y65 (= Y65), W127 (= W126), N180 (= N179), S281 (= S280), F282 (≠ M281), F345 (= F342), R371 (= R368)
- binding pyridoxal-5'-phosphate: G100 (= G100), T101 (≠ S101), W127 (= W126), N180 (= N179), D208 (= D207), A210 (= A209), Y211 (= Y210), S240 (= S239), S242 (= S241), K243 (= K242), R251 (= R250)
2ay7A Aromatic amino acid aminotransferase with 4-phenylbutyric acid (see paper)
47% identity, 96% coverage: 1:375/389 of query aligns to 1:378/394 of 2ay7A
- active site: W127 (= W126), D208 (= D207), A210 (= A209), K243 (= K242)
- binding 4-phenyl-butanoic acid: Y65 (= Y65), S281 (= S280)
- binding pyridoxal-5'-phosphate: G99 (= G99), G100 (= G100), T101 (≠ S101), W127 (= W126), D208 (= D207), A210 (= A209), Y211 (= Y210), S240 (= S239), S242 (= S241), K243 (= K242), R251 (= R250)
2ay6A Aromatic amino acid aminotransferase with 3-indolebutyric acid (see paper)
47% identity, 96% coverage: 1:375/389 of query aligns to 1:378/394 of 2ay6A
- active site: W127 (= W126), D208 (= D207), A210 (= A209), K243 (= K242)
- binding 3-indolebutyric acid: Y65 (= Y65), S281 (= S280)
- binding pyridoxal-5'-phosphate: G99 (= G99), G100 (= G100), T101 (≠ S101), W127 (= W126), N180 (= N179), D208 (= D207), A210 (= A209), Y211 (= Y210), S240 (= S239), S242 (= S241), K243 (= K242), R251 (= R250)
2ay5A Aromatic amino acid aminotransferase with 3-indolepropionic acid (see paper)
47% identity, 96% coverage: 1:375/389 of query aligns to 1:378/394 of 2ay5A
- active site: W127 (= W126), D208 (= D207), A210 (= A209), K243 (= K242)
- binding indolylpropionic acid: Y65 (= Y65), S281 (= S280)
- binding pyridoxal-5'-phosphate: G99 (= G99), G100 (= G100), T101 (≠ S101), W127 (= W126), N180 (= N179), D208 (= D207), A210 (= A209), Y211 (= Y210), S240 (= S239), S242 (= S241), K243 (= K242), R251 (= R250)
2ay3A Aromatic amino acid aminotransferase with 3-(3,4-dimethoxyphenyl) propionic acid (see paper)
47% identity, 96% coverage: 1:375/389 of query aligns to 1:378/394 of 2ay3A
- active site: W127 (= W126), D208 (= D207), A210 (= A209), K243 (= K242)
- binding 3-(3,4-dimethoxyphenyl)propionic acid: G34 (= G34), W127 (= W126), N129 (= N128), N180 (= N179), R371 (= R368)
- binding pyridoxal-5'-phosphate: G99 (= G99), G100 (= G100), T101 (≠ S101), W127 (= W126), N180 (= N179), D208 (= D207), A210 (= A209), Y211 (= Y210), S240 (= S239), S242 (= S241), K243 (= K242), R251 (= R250)
2ay1A Aromatic amino acid aminotransferase with 4-aminohydrocinnamic acid (see paper)
47% identity, 96% coverage: 1:375/389 of query aligns to 1:378/394 of 2ay1A
- active site: W127 (= W126), D208 (= D207), A210 (= A209), K243 (= K242)
- binding 4-aminohydrocinnamic acid: Y65 (= Y65), S281 (= S280)
- binding pyridoxal-5'-phosphate: G100 (= G100), T101 (≠ S101), W127 (= W126), N180 (= N179), D208 (= D207), A210 (= A209), Y211 (= Y210), S240 (= S239), S242 (= S241), K243 (= K242), R251 (= R250)
1ay4A Aromatic amino acid aminotransferase without substrate (see paper)
47% identity, 96% coverage: 1:375/389 of query aligns to 1:378/394 of 1ay4A
- active site: W127 (= W126), D208 (= D207), A210 (= A209), K243 (= K242)
- binding pyridoxal-5'-phosphate: G100 (= G100), T101 (≠ S101), W127 (= W126), D208 (= D207), A210 (= A209), Y211 (= Y210), S240 (= S239), S242 (= S241), K243 (= K242), R251 (= R250)
5vwrA E.Coli aspartate aminotransferase-(1r,3s,4s)-3-amino-4- fluorocyclopentane-1-carboxylic acid (fcp)-alpha-ketoglutarate (see paper)
43% identity, 100% coverage: 1:389/389 of query aligns to 1:395/396 of 5vwrA
- active site: W130 (= W126), D211 (= D207), A213 (= A209), K246 (= K242)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-glutamic acid: I13 (≠ L13), G34 (= G34), G102 (= G99), G103 (= G100), T104 (≠ S101), W130 (= W126), N183 (= N179), D211 (= D207), Y214 (= Y210), S243 (= S239), S245 (= S241), K246 (= K242), R254 (= R250), R374 (= R368)
5t4lA Plp and gaba trigger gabr-mediated transcription regulation in bacillus subsidies via external aldimine formation (see paper)
43% identity, 100% coverage: 1:389/389 of query aligns to 1:395/396 of 5t4lA
- active site: W130 (= W126), D211 (= D207), A213 (= A209), K246 (= K242)
- binding (4R)-4-amino-6-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}hexanoic acid: G102 (= G99), G103 (= G100), T104 (≠ S101), W130 (= W126), D211 (= D207), Y214 (= Y210), S243 (= S239), S245 (= S241), K246 (= K242), R254 (= R250)
3qpgA Crystal structures of escherichia coli aspartate aminotransferase reconstituted with 1-deaza-pyridoxal 5'-phosphate: internal aldimine and stable l-aspartate external aldimine (see paper)
43% identity, 100% coverage: 1:389/389 of query aligns to 1:395/396 of 3qpgA
- active site: W130 (= W126), D211 (= D207), A213 (= A209), K246 (= K242)
- binding (E)-N-{2-hydroxy-3-methyl-6-[(phosphonooxy)methyl]benzylidene}-L-aspartic acid: I13 (≠ L13), G34 (= G34), G102 (= G99), G103 (= G100), T104 (≠ S101), W130 (= W126), N183 (= N179), D211 (= D207), Y214 (= Y210), S243 (= S239), S245 (= S241), K246 (= K242), R254 (= R250), R374 (= R368)
3pa9A Mechanism of inactivation of e. Coli aspartate aminotransferase by (s)-4-amino-4,5-dihydro-2-furancarboxylic acid (s-adfa) ph 7.5 (see paper)
43% identity, 100% coverage: 1:389/389 of query aligns to 1:395/396 of 3pa9A
- active site: W130 (= W126), D211 (= D207), A213 (= A209), K246 (= K242)
- binding 4-aminofuran-2-carboxylic acid: G34 (= G34), W130 (= W126), K246 (= K242), F348 (= F342), R374 (= R368)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G103 (= G100), T104 (≠ S101), W130 (= W126), D211 (= D207), A213 (= A209), Y214 (= Y210), S243 (= S239), S245 (= S241), K246 (= K242), R254 (= R250)
1x2aA Crystal structure of e.Coli aspat complexed with n-phosphopyridoxyl-d- glutamic acid (see paper)
43% identity, 100% coverage: 1:389/389 of query aligns to 1:395/396 of 1x2aA
- active site: W130 (= W126), D211 (= D207), A213 (= A209), K246 (= K242)
- binding n-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-d-glutamic acid: I33 (≠ V33), G34 (= G34), Y65 (= Y65), G102 (= G99), G103 (= G100), T104 (≠ S101), W130 (= W126), N183 (= N179), D211 (= D207), Y214 (= Y210), S243 (= S239), S245 (= S241), K246 (= K242), R254 (= R250), R280 (= R276), F348 (= F342), R374 (= R368)
1x29A Crystal structure of e.Coli aspat complexed with n-phosphopyridoxyl-2- methyl-l-glutamic acid (see paper)
43% identity, 100% coverage: 1:389/389 of query aligns to 1:395/396 of 1x29A
- active site: W130 (= W126), D211 (= D207), A213 (= A209), K246 (= K242)
- binding n-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-2-methyl-l-glutamic acid: I13 (≠ L13), G34 (= G34), Y65 (= Y65), G103 (= G100), T104 (≠ S101), W130 (= W126), N183 (= N179), D211 (= D207), Y214 (= Y210), S243 (= S239), S245 (= S241), K246 (= K242), R254 (= R250), R280 (= R276), F348 (= F342), R374 (= R368)
1x28A Crystal structure of e.Coli aspat complexed with n-phosphopyridoxyl-l- glutamic acid (see paper)
43% identity, 100% coverage: 1:389/389 of query aligns to 1:395/396 of 1x28A
- active site: W130 (= W126), D211 (= D207), A213 (= A209), K246 (= K242)
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I13 (≠ L13), Y65 (= Y65), G103 (= G100), T104 (≠ S101), W130 (= W126), N183 (= N179), D211 (= D207), Y214 (= Y210), S243 (= S239), S245 (= S241), K246 (= K242), R254 (= R250), R280 (= R276), F348 (= F342), R374 (= R368)
1cq8A Aspartate aminotransferase (E.C. 2.6.1.1) complexed with c6-pyridoxal- 5p-phosphate (see paper)
43% identity, 100% coverage: 1:389/389 of query aligns to 1:395/396 of 1cq8A
- active site: W130 (= W126), D211 (= D207), A213 (= A209), K246 (= K242)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: I33 (≠ V33), G34 (= G34), G103 (= G100), T104 (≠ S101), W130 (= W126), N183 (= N179), D211 (= D207), A213 (= A209), Y214 (= Y210), S243 (= S239), S245 (= S241), K246 (= K242), R254 (= R250), R374 (= R368)
1cq7A Aspartate aminotransferase (E.C. 2.6.1.1) complexed with c5-pyridoxal- 5p-phosphate (see paper)
43% identity, 100% coverage: 1:389/389 of query aligns to 1:395/396 of 1cq7A
- active site: W130 (= W126), D211 (= D207), A213 (= A209), K246 (= K242)
- binding 2-[o-phosphonopyridoxyl]-amino-pentanoic acid: I13 (≠ L13), I33 (≠ V33), G34 (= G34), G103 (= G100), T104 (≠ S101), W130 (= W126), N183 (= N179), D211 (= D207), Y214 (= Y210), S243 (= S239), S245 (= S241), K246 (= K242), R254 (= R250), R374 (= R368)
1cq6A Aspartate aminotransferase complex with c4-pyridoxal-5p-phosphate (see paper)
43% identity, 100% coverage: 1:389/389 of query aligns to 1:395/396 of 1cq6A
- active site: W130 (= W126), D211 (= D207), A213 (= A209), K246 (= K242)
- binding 2-[o-phosphonopyridoxyl]-amino- butyric acid: G103 (= G100), T104 (≠ S101), W130 (= W126), N183 (= N179), D211 (= D207), Y214 (= Y210), S243 (= S239), S245 (= S241), R254 (= R250)
1c9cA Aspartate aminotransferase complexed with c3-pyridoxal-5'-phosphate (see paper)
43% identity, 100% coverage: 1:389/389 of query aligns to 1:395/396 of 1c9cA
- active site: W130 (= W126), D211 (= D207), A213 (= A209), K246 (= K242)
- binding alanyl-pyridoxal-5'-phosphate: G103 (= G100), T104 (≠ S101), W130 (= W126), N183 (= N179), D211 (= D207), A213 (= A209), Y214 (= Y210), S243 (= S239), S245 (= S241), K246 (= K242), R254 (= R250)
1aslA Crystal structures of escherichia coli aspartate aminotransferase in two conformations: comparison of an unliganded open and two liganded closed forms (see paper)
43% identity, 100% coverage: 1:389/389 of query aligns to 1:395/396 of 1aslA
- active site: W130 (= W126), D211 (= D207), A213 (= A209), K246 (= K242)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-2-methyl-succinic acid: I13 (≠ L13), G34 (= G34), Y65 (= Y65), G102 (= G99), G103 (= G100), T104 (≠ S101), W130 (= W126), N183 (= N179), D211 (= D207), Y214 (= Y210), S243 (= S239), K246 (= K242), R254 (= R250), R280 (= R276), R374 (= R368)
Query Sequence
>WP_012710112.1 NCBI__GCF_000018545.1:WP_012710112.1
MFDALARQPDDPLLALIGLFRKDERPGKVDLGVGVYRDETGRTPIFRAVKEAEKRLLETQ
ETKAYVGPEGDLVFLDHLWRLVGGDTVERSHVAGVQTPGGSGALRLAADLIYRMGGRKIW
LGLPSWPNHAPIFKAAGLEIATYDFFDMPSQSVIFDNVVSALEGAAPGDAVLLHASCHNP
TGGVLTEAQWMEIAALVAERGLLPLVDLAYQGFGRGLEQDVAGLRHLLTVVPEALVAVSC
SKSFGLYRERTGAIFGVTPSTSSADTVRSNLAGLARTSYSMPPDHGAAVVRTILADPDLA
RDWAEELEGMRLRMTGIRQALAEGLRSRWQSLGAVADQEGMFSMLPLTEAEVMRLRTEHG
LYMPGSGRINIAGLKTAEVADVIQKFTSL
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