SitesBLAST
Comparing 5209529 FitnessBrowser__PV4:5209529 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)
5vwrA E.Coli aspartate aminotransferase-(1r,3s,4s)-3-amino-4- fluorocyclopentane-1-carboxylic acid (fcp)-alpha-ketoglutarate (see paper)
62% identity, 100% coverage: 2:397/397 of query aligns to 1:396/396 of 5vwrA
- active site: W130 (= W131), D211 (= D212), A213 (= A214), K246 (= K247)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-glutamic acid: I13 (= I14), G34 (= G35), G102 (= G103), G103 (= G104), T104 (= T105), W130 (= W131), N183 (= N184), D211 (= D212), Y214 (= Y215), S243 (= S244), S245 (= S246), K246 (= K247), R254 (= R255), R374 (= R375)
5t4lA Plp and gaba trigger gabr-mediated transcription regulation in bacillus subsidies via external aldimine formation (see paper)
62% identity, 100% coverage: 2:397/397 of query aligns to 1:396/396 of 5t4lA
- active site: W130 (= W131), D211 (= D212), A213 (= A214), K246 (= K247)
- binding (4R)-4-amino-6-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}hexanoic acid: G102 (= G103), G103 (= G104), T104 (= T105), W130 (= W131), D211 (= D212), Y214 (= Y215), S243 (= S244), S245 (= S246), K246 (= K247), R254 (= R255)
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)
62% identity, 100% coverage: 2:397/397 of query aligns to 1:396/396 of 3qpgA
- active site: W130 (= W131), D211 (= D212), A213 (= A214), K246 (= K247)
- binding (E)-N-{2-hydroxy-3-methyl-6-[(phosphonooxy)methyl]benzylidene}-L-aspartic acid: I13 (= I14), G34 (= G35), G102 (= G103), G103 (= G104), T104 (= T105), W130 (= W131), N183 (= N184), D211 (= D212), Y214 (= Y215), S243 (= S244), S245 (= S246), K246 (= K247), R254 (= R255), R374 (= R375)
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)
62% identity, 100% coverage: 2:397/397 of query aligns to 1:396/396 of 3pa9A
- active site: W130 (= W131), D211 (= D212), A213 (= A214), K246 (= K247)
- binding 4-aminofuran-2-carboxylic acid: G34 (= G35), W130 (= W131), K246 (= K247), F348 (= F349), R374 (= R375)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G103 (= G104), T104 (= T105), W130 (= W131), D211 (= D212), A213 (= A214), Y214 (= Y215), S243 (= S244), S245 (= S246), K246 (= K247), R254 (= R255)
1x2aA Crystal structure of e.Coli aspat complexed with n-phosphopyridoxyl-d- glutamic acid (see paper)
62% identity, 100% coverage: 2:397/397 of query aligns to 1:396/396 of 1x2aA
- active site: W130 (= W131), D211 (= D212), A213 (= A214), K246 (= K247)
- binding n-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-d-glutamic acid: I33 (≠ V34), G34 (= G35), Y65 (= Y66), G102 (= G103), G103 (= G104), T104 (= T105), W130 (= W131), N183 (= N184), D211 (= D212), Y214 (= Y215), S243 (= S244), S245 (= S246), K246 (= K247), R254 (= R255), R280 (= R281), F348 (= F349), R374 (= R375)
1x29A Crystal structure of e.Coli aspat complexed with n-phosphopyridoxyl-2- methyl-l-glutamic acid (see paper)
62% identity, 100% coverage: 2:397/397 of query aligns to 1:396/396 of 1x29A
- active site: W130 (= W131), D211 (= D212), A213 (= A214), K246 (= K247)
- binding n-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-2-methyl-l-glutamic acid: I13 (= I14), G34 (= G35), Y65 (= Y66), G103 (= G104), T104 (= T105), W130 (= W131), N183 (= N184), D211 (= D212), Y214 (= Y215), S243 (= S244), S245 (= S246), K246 (= K247), R254 (= R255), R280 (= R281), F348 (= F349), R374 (= R375)
1x28A Crystal structure of e.Coli aspat complexed with n-phosphopyridoxyl-l- glutamic acid (see paper)
62% identity, 100% coverage: 2:397/397 of query aligns to 1:396/396 of 1x28A
- active site: W130 (= W131), D211 (= D212), A213 (= A214), K246 (= K247)
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I13 (= I14), Y65 (= Y66), G103 (= G104), T104 (= T105), W130 (= W131), N183 (= N184), D211 (= D212), Y214 (= Y215), S243 (= S244), S245 (= S246), K246 (= K247), R254 (= R255), R280 (= R281), F348 (= F349), R374 (= R375)
1cq8A Aspartate aminotransferase (E.C. 2.6.1.1) complexed with c6-pyridoxal- 5p-phosphate (see paper)
62% identity, 100% coverage: 2:397/397 of query aligns to 1:396/396 of 1cq8A
- active site: W130 (= W131), D211 (= D212), A213 (= A214), K246 (= K247)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: I33 (≠ V34), G34 (= G35), G103 (= G104), T104 (= T105), W130 (= W131), N183 (= N184), D211 (= D212), A213 (= A214), Y214 (= Y215), S243 (= S244), S245 (= S246), K246 (= K247), R254 (= R255), R374 (= R375)
1cq7A Aspartate aminotransferase (E.C. 2.6.1.1) complexed with c5-pyridoxal- 5p-phosphate (see paper)
62% identity, 100% coverage: 2:397/397 of query aligns to 1:396/396 of 1cq7A
- active site: W130 (= W131), D211 (= D212), A213 (= A214), K246 (= K247)
- binding 2-[o-phosphonopyridoxyl]-amino-pentanoic acid: I13 (= I14), I33 (≠ V34), G34 (= G35), G103 (= G104), T104 (= T105), W130 (= W131), N183 (= N184), D211 (= D212), Y214 (= Y215), S243 (= S244), S245 (= S246), K246 (= K247), R254 (= R255), R374 (= R375)
1cq6A Aspartate aminotransferase complex with c4-pyridoxal-5p-phosphate (see paper)
62% identity, 100% coverage: 2:397/397 of query aligns to 1:396/396 of 1cq6A
- active site: W130 (= W131), D211 (= D212), A213 (= A214), K246 (= K247)
- binding 2-[o-phosphonopyridoxyl]-amino- butyric acid: G103 (= G104), T104 (= T105), W130 (= W131), N183 (= N184), D211 (= D212), Y214 (= Y215), S243 (= S244), S245 (= S246), R254 (= R255)
1c9cA Aspartate aminotransferase complexed with c3-pyridoxal-5'-phosphate (see paper)
62% identity, 100% coverage: 2:397/397 of query aligns to 1:396/396 of 1c9cA
- active site: W130 (= W131), D211 (= D212), A213 (= A214), K246 (= K247)
- binding alanyl-pyridoxal-5'-phosphate: G103 (= G104), T104 (= T105), W130 (= W131), N183 (= N184), D211 (= D212), A213 (= A214), Y214 (= Y215), S243 (= S244), S245 (= S246), K246 (= K247), R254 (= R255)
1aslA Crystal structures of escherichia coli aspartate aminotransferase in two conformations: comparison of an unliganded open and two liganded closed forms (see paper)
62% identity, 100% coverage: 2:397/397 of query aligns to 1:396/396 of 1aslA
- active site: W130 (= W131), D211 (= D212), A213 (= A214), K246 (= K247)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-2-methyl-succinic acid: I13 (= I14), G34 (= G35), Y65 (= Y66), G102 (= G103), G103 (= G104), T104 (= T105), W130 (= W131), N183 (= N184), D211 (= D212), Y214 (= Y215), S243 (= S244), K246 (= K247), R254 (= R255), R280 (= R281), R374 (= R375)
1aseA The structure of wild type e. Coli aspartate aminotransferase reconstituted with plp-n-oxide
62% identity, 100% coverage: 2:397/397 of query aligns to 1:396/396 of 1aseA
- active site: W130 (= W131), D211 (= D212), A213 (= A214), K246 (= K247)
- binding pyridoxal-5'-phosphate-n-oxide: G102 (= G103), G103 (= G104), T104 (= T105), W130 (= W131), N183 (= N184), D211 (= D212), A213 (= A214), Y214 (= Y215), S243 (= S244), S245 (= S246), K246 (= K247), R254 (= R255)
1asdA The structure of wild type e. Coli aspartate aminotransferase reconstituted with n-meplp
62% identity, 100% coverage: 2:397/397 of query aligns to 1:396/396 of 1asdA
- active site: W130 (= W131), D211 (= D212), A213 (= A214), K246 (= K247)
- binding n-methyl-pyridoxal-5'-phosphate: G102 (= G103), G103 (= G104), T104 (= T105), W130 (= W131), N183 (= N184), D211 (= D212), A213 (= A214), Y214 (= Y215), S243 (= S244), S245 (= S246), K246 (= K247), R254 (= R255)
1artA X-ray crystallographic study of pyridoxal 5'-phosphate-type aspartate aminotransferases from escherichia coli in open and closed form (see paper)
62% identity, 100% coverage: 2:397/397 of query aligns to 1:396/396 of 1artA
- active site: W130 (= W131), D211 (= D212), A213 (= A214), K246 (= K247)
- binding 2-methyl-L-aspartic acid: I33 (≠ V34), G34 (= G35), W130 (= W131), Y214 (= Y215), R374 (= R375)
- binding pyridoxal-5'-phosphate: G102 (= G103), G103 (= G104), T104 (= T105), W130 (= W131), N183 (= N184), D211 (= D212), Y214 (= Y215), S243 (= S244), S245 (= S246), K246 (= K247), R254 (= R255)
1argA Aspartate aminotransferase, phospho-5'-pyridoxyl aspartate complex (see paper)
62% identity, 100% coverage: 2:397/397 of query aligns to 1:396/396 of 1argA
- active site: W130 (= W131), D211 (= D212), A213 (= A214), K246 (= K247)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethylene)-amino]-succinic acid: I13 (= I14), G34 (= G35), Y65 (= Y66), G103 (= G104), T104 (= T105), W130 (= W131), N183 (= N184), D211 (= D212), Y214 (= Y215), S243 (= S244), S245 (= S246), K246 (= K247), R254 (= R255), R280 (= R281), R374 (= R375)
1amsA X-ray crystallographic study of pyridoxamine 5'-phosphate-type aspartate aminotransferases from escherichia coli in three forms (see paper)
62% identity, 100% coverage: 2:397/397 of query aligns to 1:396/396 of 1amsA
- active site: W130 (= W131), D211 (= D212), A213 (= A214), K246 (= K247)
- binding glutaric acid: W130 (= W131), R374 (= R375)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G103 (= G104), T104 (= T105), W130 (= W131), N183 (= N184), D211 (= D212), Y214 (= Y215), S243 (= S244), S245 (= S246), R254 (= R255)
P00509 Aspartate aminotransferase; AspAT; Transaminase A; EC 2.6.1.1 from Escherichia coli (strain K12) (see 7 papers)
62% identity, 100% coverage: 2:397/397 of query aligns to 1:396/396 of P00509
- Y65 (= Y66) mutation Y->F,S: Slight changes in activity.
- H133 (= H134) 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 (= K247) modified: N6-(pyridoxal phosphate)lysine
- R280 (= R281) mutation to V: Reduces first-order rate constant over 25000-fold.
- R374 (= R375) 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)
62% identity, 100% coverage: 2:397/397 of query aligns to 1:396/396 of 1aibA
- active site: W130 (= W131), D211 (= D212), A213 (= A214), H246 (≠ K247)
- binding 2-oxoglutaric acid: I13 (= I14), R374 (= R375)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G103 (= G104), T104 (= T105), W130 (= W131), H178 (= H179), D211 (= D212), A213 (= A214), Y214 (= Y215), S243 (= S244), S245 (= S246), R254 (= R255)
1aiaA Structural basis for the catalytic activity of aspartate aminotransferase k258h lacking the pyridoxal-5'-phosphate binding lysine residue (see paper)
62% identity, 100% coverage: 2:397/397 of query aligns to 1:396/396 of 1aiaA
- active site: W130 (= W131), D211 (= D212), A213 (= A214), H246 (≠ K247)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G102 (= G103), G103 (= G104), T104 (= T105), W130 (= W131), D211 (= D212), Y214 (= Y215), S243 (= S244), S245 (= S246), H246 (≠ K247), R254 (= R255)
Query Sequence
>5209529 FitnessBrowser__PV4:5209529
MIFNQVVLAPADPILGLTDAFKADPRADKVNLGVGIYKDESGQTPILKSVKLAEQKLLET
ETSKSYLGIDGVIAYNQAVQGLLFGTDHAVMSEKRAVTAQAPGGTGSLRMAAEFVVRNTA
SRTVWVSNLTWANHNNIFQSAGLTVKQYGYYDAASHDIDFDAMLTSLEQANSGDLLLLHG
CCHNPTGIDLNICQWEVIAQLCVDKGLIPLFDFAYQGFGAGVEEDAQGLRLVASKVPELL
VANSFSKNFGLYNERIGAVTLVAEDEETAKRAFSQIKSTIRSSYSNPPAHGALIVATILG
DAELRKLWEEELTQMRERIAEMRVLFVKTLSEQGVEQDFSFISAQNGMFSFSGLNKDQVA
RLKEEFGVYIVGSGRISVAGMTRANMDTICRAIAQVL
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