SitesBLAST
Comparing WP_072909529.1 NCBI__GCF_900142125.1:WP_072909529.1 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)
5vwrA E.Coli aspartate aminotransferase-(1r,3s,4s)-3-amino-4- fluorocyclopentane-1-carboxylic acid (fcp)-alpha-ketoglutarate (see paper)
58% identity, 100% coverage: 1:396/396 of query aligns to 1:396/396 of 5vwrA
- active site: W130 (= W130), D211 (= D211), A213 (= A213), K246 (= K246)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-glutamic acid: I13 (= I13), G34 (= G34), G102 (= G102), G103 (= G103), T104 (= T104), W130 (= W130), N183 (= N183), D211 (= D211), Y214 (= Y214), S243 (= S243), S245 (= S245), K246 (= K246), R254 (= R254), R374 (= R374)
5t4lA Plp and gaba trigger gabr-mediated transcription regulation in bacillus subsidies via external aldimine formation (see paper)
58% identity, 100% coverage: 1:396/396 of query aligns to 1:396/396 of 5t4lA
- active site: W130 (= W130), D211 (= D211), A213 (= A213), K246 (= K246)
- binding (4R)-4-amino-6-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}hexanoic acid: G102 (= G102), G103 (= G103), T104 (= T104), W130 (= W130), D211 (= D211), Y214 (= Y214), S243 (= S243), S245 (= S245), K246 (= K246), R254 (= R254)
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)
58% identity, 100% coverage: 1:396/396 of query aligns to 1:396/396 of 3qpgA
- active site: W130 (= W130), D211 (= D211), A213 (= A213), K246 (= K246)
- binding (E)-N-{2-hydroxy-3-methyl-6-[(phosphonooxy)methyl]benzylidene}-L-aspartic acid: I13 (= I13), G34 (= G34), G102 (= G102), G103 (= G103), T104 (= T104), W130 (= W130), N183 (= N183), D211 (= D211), Y214 (= Y214), S243 (= S243), S245 (= S245), K246 (= K246), R254 (= R254), R374 (= R374)
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)
58% identity, 100% coverage: 1:396/396 of query aligns to 1:396/396 of 3pa9A
- active site: W130 (= W130), D211 (= D211), A213 (= A213), K246 (= K246)
- binding 4-aminofuran-2-carboxylic acid: G34 (= G34), W130 (= W130), K246 (= K246), F348 (= F348), R374 (= R374)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G103 (= G103), T104 (= T104), W130 (= W130), D211 (= D211), A213 (= A213), Y214 (= Y214), S243 (= S243), S245 (= S245), K246 (= K246), R254 (= R254)
1x2aA Crystal structure of e.Coli aspat complexed with n-phosphopyridoxyl-d- glutamic acid (see paper)
58% identity, 100% coverage: 1:396/396 of query aligns to 1:396/396 of 1x2aA
- active site: W130 (= W130), D211 (= D211), A213 (= A213), K246 (= K246)
- binding n-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-d-glutamic acid: I33 (≠ V33), G34 (= G34), Y65 (= Y65), G102 (= G102), G103 (= G103), T104 (= T104), W130 (= W130), N183 (= N183), D211 (= D211), Y214 (= Y214), S243 (= S243), S245 (= S245), K246 (= K246), R254 (= R254), R280 (= R280), F348 (= F348), R374 (= R374)
1x29A Crystal structure of e.Coli aspat complexed with n-phosphopyridoxyl-2- methyl-l-glutamic acid (see paper)
58% identity, 100% coverage: 1:396/396 of query aligns to 1:396/396 of 1x29A
- active site: W130 (= W130), D211 (= D211), A213 (= A213), K246 (= K246)
- binding n-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-2-methyl-l-glutamic acid: I13 (= I13), G34 (= G34), Y65 (= Y65), G103 (= G103), T104 (= T104), W130 (= W130), N183 (= N183), D211 (= D211), Y214 (= Y214), S243 (= S243), S245 (= S245), K246 (= K246), R254 (= R254), R280 (= R280), F348 (= F348), R374 (= R374)
1x28A Crystal structure of e.Coli aspat complexed with n-phosphopyridoxyl-l- glutamic acid (see paper)
58% identity, 100% coverage: 1:396/396 of query aligns to 1:396/396 of 1x28A
- active site: W130 (= W130), D211 (= D211), A213 (= A213), K246 (= K246)
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I13 (= I13), Y65 (= Y65), G103 (= G103), T104 (= T104), W130 (= W130), N183 (= N183), D211 (= D211), Y214 (= Y214), S243 (= S243), S245 (= S245), K246 (= K246), R254 (= R254), R280 (= R280), F348 (= F348), R374 (= R374)
1cq8A Aspartate aminotransferase (E.C. 2.6.1.1) complexed with c6-pyridoxal- 5p-phosphate (see paper)
58% identity, 100% coverage: 1:396/396 of query aligns to 1:396/396 of 1cq8A
- active site: W130 (= W130), D211 (= D211), A213 (= A213), K246 (= K246)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: I33 (≠ V33), G34 (= G34), G103 (= G103), T104 (= T104), W130 (= W130), N183 (= N183), D211 (= D211), A213 (= A213), Y214 (= Y214), S243 (= S243), S245 (= S245), K246 (= K246), R254 (= R254), R374 (= R374)
1cq7A Aspartate aminotransferase (E.C. 2.6.1.1) complexed with c5-pyridoxal- 5p-phosphate (see paper)
58% identity, 100% coverage: 1:396/396 of query aligns to 1:396/396 of 1cq7A
- active site: W130 (= W130), D211 (= D211), A213 (= A213), K246 (= K246)
- binding 2-[o-phosphonopyridoxyl]-amino-pentanoic acid: I13 (= I13), I33 (≠ V33), G34 (= G34), G103 (= G103), T104 (= T104), W130 (= W130), N183 (= N183), D211 (= D211), Y214 (= Y214), S243 (= S243), S245 (= S245), K246 (= K246), R254 (= R254), R374 (= R374)
1cq6A Aspartate aminotransferase complex with c4-pyridoxal-5p-phosphate (see paper)
58% identity, 100% coverage: 1:396/396 of query aligns to 1:396/396 of 1cq6A
- active site: W130 (= W130), D211 (= D211), A213 (= A213), K246 (= K246)
- binding 2-[o-phosphonopyridoxyl]-amino- butyric acid: G103 (= G103), T104 (= T104), W130 (= W130), N183 (= N183), D211 (= D211), Y214 (= Y214), S243 (= S243), S245 (= S245), R254 (= R254)
1c9cA Aspartate aminotransferase complexed with c3-pyridoxal-5'-phosphate (see paper)
58% identity, 100% coverage: 1:396/396 of query aligns to 1:396/396 of 1c9cA
- active site: W130 (= W130), D211 (= D211), A213 (= A213), K246 (= K246)
- binding alanyl-pyridoxal-5'-phosphate: G103 (= G103), T104 (= T104), W130 (= W130), N183 (= N183), D211 (= D211), A213 (= A213), Y214 (= Y214), S243 (= S243), S245 (= S245), K246 (= K246), R254 (= R254)
1aslA Crystal structures of escherichia coli aspartate aminotransferase in two conformations: comparison of an unliganded open and two liganded closed forms (see paper)
58% identity, 100% coverage: 1:396/396 of query aligns to 1:396/396 of 1aslA
- active site: W130 (= W130), D211 (= D211), A213 (= A213), K246 (= K246)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-2-methyl-succinic acid: I13 (= I13), G34 (= G34), Y65 (= Y65), G102 (= G102), G103 (= G103), T104 (= T104), W130 (= W130), N183 (= N183), D211 (= D211), Y214 (= Y214), S243 (= S243), K246 (= K246), R254 (= R254), R280 (= R280), R374 (= R374)
1aseA The structure of wild type e. Coli aspartate aminotransferase reconstituted with plp-n-oxide
58% identity, 100% coverage: 1:396/396 of query aligns to 1:396/396 of 1aseA
- active site: W130 (= W130), D211 (= D211), A213 (= A213), K246 (= K246)
- binding pyridoxal-5'-phosphate-n-oxide: G102 (= G102), G103 (= G103), T104 (= T104), W130 (= W130), N183 (= N183), D211 (= D211), A213 (= A213), Y214 (= Y214), S243 (= S243), S245 (= S245), K246 (= K246), R254 (= R254)
1asdA The structure of wild type e. Coli aspartate aminotransferase reconstituted with n-meplp
58% identity, 100% coverage: 1:396/396 of query aligns to 1:396/396 of 1asdA
- active site: W130 (= W130), D211 (= D211), A213 (= A213), K246 (= K246)
- binding n-methyl-pyridoxal-5'-phosphate: G102 (= G102), G103 (= G103), T104 (= T104), W130 (= W130), N183 (= N183), D211 (= D211), A213 (= A213), Y214 (= Y214), S243 (= S243), S245 (= S245), K246 (= K246), R254 (= R254)
1artA X-ray crystallographic study of pyridoxal 5'-phosphate-type aspartate aminotransferases from escherichia coli in open and closed form (see paper)
58% identity, 100% coverage: 1:396/396 of query aligns to 1:396/396 of 1artA
- active site: W130 (= W130), D211 (= D211), A213 (= A213), K246 (= K246)
- binding 2-methyl-L-aspartic acid: I33 (≠ V33), G34 (= G34), W130 (= W130), Y214 (= Y214), R374 (= R374)
- binding pyridoxal-5'-phosphate: G102 (= G102), G103 (= G103), T104 (= T104), W130 (= W130), N183 (= N183), D211 (= D211), Y214 (= Y214), S243 (= S243), S245 (= S245), K246 (= K246), R254 (= R254)
1argA Aspartate aminotransferase, phospho-5'-pyridoxyl aspartate complex (see paper)
58% identity, 100% coverage: 1:396/396 of query aligns to 1:396/396 of 1argA
- active site: W130 (= W130), D211 (= D211), A213 (= A213), K246 (= K246)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethylene)-amino]-succinic acid: I13 (= I13), G34 (= G34), Y65 (= Y65), G103 (= G103), T104 (= T104), W130 (= W130), N183 (= N183), D211 (= D211), Y214 (= Y214), S243 (= S243), S245 (= S245), K246 (= K246), R254 (= R254), R280 (= R280), R374 (= R374)
1amsA X-ray crystallographic study of pyridoxamine 5'-phosphate-type aspartate aminotransferases from escherichia coli in three forms (see paper)
58% identity, 100% coverage: 1:396/396 of query aligns to 1:396/396 of 1amsA
- active site: W130 (= W130), D211 (= D211), A213 (= A213), K246 (= K246)
- binding glutaric acid: W130 (= W130), R374 (= R374)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G103 (= G103), T104 (= T104), W130 (= W130), N183 (= N183), D211 (= D211), Y214 (= Y214), S243 (= S243), S245 (= S245), R254 (= R254)
P00509 Aspartate aminotransferase; AspAT; Transaminase A; EC 2.6.1.1 from Escherichia coli (strain K12) (see 7 papers)
58% identity, 100% coverage: 1:396/396 of query aligns to 1:396/396 of P00509
- Y65 (= Y65) mutation Y->F,S: Slight changes in activity.
- H133 (= H133) mutation to A: Slight increase in maximum velocity of the overall transamination reaction between aspartate and 2-oxoglutarate.; mutation to N: Decreases to 60% in maximum rate of the overall reactions in both directions.
- K246 (= K246) modified: N6-(pyridoxal phosphate)lysine
- R280 (= R280) mutation to V: Reduces first-order rate constant over 25000-fold.
- R374 (= R374) mutation to A: Reduces first-order rate constant about 10000-fold.; mutation R->F,Y: Second-order rate constants are reduced by >5 orders of magnitude.
1aibA Structural basis for the catalytic activity of aspartate aminotransferase k258h lacking the pyridoxal-5'-phosphate binding lysine residue (see paper)
58% identity, 100% coverage: 1:396/396 of query aligns to 1:396/396 of 1aibA
- active site: W130 (= W130), D211 (= D211), A213 (= A213), H246 (≠ K246)
- binding 2-oxoglutaric acid: I13 (= I13), R374 (= R374)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G103 (= G103), T104 (= T104), W130 (= W130), H178 (= H178), D211 (= D211), A213 (= A213), Y214 (= Y214), S243 (= S243), S245 (= S245), R254 (= R254)
1aiaA Structural basis for the catalytic activity of aspartate aminotransferase k258h lacking the pyridoxal-5'-phosphate binding lysine residue (see paper)
58% identity, 100% coverage: 1:396/396 of query aligns to 1:396/396 of 1aiaA
- active site: W130 (= W130), D211 (= D211), A213 (= A213), H246 (≠ K246)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G102 (= G102), G103 (= G103), T104 (= T104), W130 (= W130), D211 (= D211), Y214 (= Y214), S243 (= S243), S245 (= S245), H246 (≠ K246), R254 (= R254)
Query Sequence
>WP_072909529.1 NCBI__GCF_900142125.1:WP_072909529.1
MFENVQTAPADPILGLTELFKADPNPEKINLSVGVYQDATGKTPVLETVKEAEKRILEQE
NSKGYLPMTGEPAYCAEVQKLLFGEGHEIITSKRAATAQCPGGTGALRVAGDYLNIVHPG
AKIWLSNPTWANHNTIFEAAGVECKQYAYRDAATNGLDFDAMCASIKTIPAGDVILLHGC
CHNPTGIDPTPEQWAIIGDLLAAQGVTPLVDFAYHGLADGLEQDRLGLLELVKKVKQMFI
CSSFSKNFGLYRERTGALTLVADNAEQAGTVMSQVKLRIRYNYSNPPSHGGQIVATVLSD
PELKAKWIEEVADIRNRINEMRHLFVKTLKDKGVTQDFSTIIEQRGMFSFSGLTKDQVDR
LREEFSIYIVGSGRINVAGMTPDNMDRLCDAIKAVL
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