SitesBLAST
Comparing H281DRAFT_01578 FitnessBrowser__Burk376:H281DRAFT_01578 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)
Q9A3Q9 Omega-aminotransferase; Beta-alanine--pyruvate aminotransferase; EC 2.6.1.-; EC 2.6.1.18 from Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus) (see paper)
66% identity, 98% coverage: 8:442/442 of query aligns to 7:439/439 of Q9A3Q9
- V227 (= V229) mutation to G: Decreases activity toward 3-aminobutanoate by 2-fold. Increases activity toward the aromatic beta-amino acid 3-amino-3-phenylpropanoate by 2-fold.
- R260 (= R262) mutation to L: Decreases activity toward 3-aminobutanoate by 30-fold.
- N285 (= N287) mutation to A: Decreases activity toward 3-aminobutanoate by 4-fold. Increases activity toward the aromatic beta-amino acid 3-amino-3-phenylpropanoate by 3-fold.
Q9I700 Beta-alanine--pyruvate aminotransferase; Beta-A--Py AT; Beta-alanine--pyruvate transaminase; Omega-amino acid aminotransferase; Omega-amino acid AT; Omega-amino acid--pyruvate aminotransferase; Omega-APT; EC 2.6.1.18 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see paper)
52% identity, 98% coverage: 9:441/442 of query aligns to 16:447/448 of Q9I700
- W61 (= W54) binding
- T327 (= T321) binding
- R414 (= R408) binding
- Q421 (≠ A415) binding
4b98A The structure of the omega aminotransferase from pseudomonas aeruginosa (see paper)
53% identity, 97% coverage: 9:438/442 of query aligns to 9:437/441 of 4b98A
- active site: F17 (= F17), Y146 (= Y146), E219 (= E221), D252 (= D254), I255 (= I257), K281 (= K283), Q414 (≠ A415)
- binding pyridoxal-5'-phosphate: G233 (= G235), Q236 (= Q238), F270 (= F272), G271 (= G273)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: L53 (= L53), W54 (= W54), F82 (= F82), S112 (= S112), G113 (= G113), S114 (= S114), Y146 (= Y146), H147 (= H147), G148 (= G148), E219 (= E221), S224 (= S226), D252 (= D254), V254 (= V256), I255 (= I257), K281 (= K283), Y319 (= Y320), T320 (= T321), R407 (= R408), Q414 (≠ A415)
4uhmA Characterization of a novel transaminase from pseudomonas sp. Strain aac (see paper)
52% identity, 98% coverage: 9:441/442 of query aligns to 3:434/435 of 4uhmA
- active site: F11 (= F17), Y140 (= Y146), E213 (= E221), D246 (= D254), I249 (= I257), K275 (= K283), Q408 (≠ A415)
- binding magnesium ion: A91 (= A97), D99 (= D105)
- binding pyridoxal-5'-phosphate: G107 (= G113), S108 (= S114), Y140 (= Y146), H141 (= H147), G142 (= G148), E213 (= E221), D246 (= D254), V248 (= V256), I249 (= I257), K275 (= K283)
3a8uX Crystal structure of omega-amino acid:pyruvate aminotransferase
51% identity, 97% coverage: 10:438/442 of query aligns to 9:437/441 of 3a8uX
- active site: Y145 (= Y146), D252 (= D254), K281 (= K283), Q414 (≠ A415)
- binding pyridoxal-5'-phosphate: S111 (= S112), G112 (= G113), S113 (= S114), Y145 (= Y146), H146 (= H147), G147 (= G148), E219 (= E221), D252 (= D254), V254 (= V256), I255 (= I257), K281 (= K283)
3i5tA Crystal structure of aminotransferase prk07036 from rhodobacter sphaeroides kd131
39% identity, 91% coverage: 24:427/442 of query aligns to 22:423/444 of 3i5tA
- active site: Y144 (= Y146), E216 (= E221), D249 (= D254), V252 (≠ I257), K279 (= K283), V411 (≠ A415)
- binding pyridoxal-5'-phosphate: G111 (= G113), S112 (= S114), Y144 (= Y146), H145 (= H147), E216 (= E221), D249 (= D254), V251 (= V256), K279 (= K283), Y315 (= Y320), T316 (= T321)
Sites not aligning to the query:
6gwiB The crystal structure of halomonas elongata amino-transferase (see paper)
36% identity, 94% coverage: 16:432/442 of query aligns to 17:436/450 of 6gwiB
- active site: F18 (= F17), Y149 (= Y146), D255 (= D254), K284 (= K283)
- binding pyridoxal-5'-phosphate: S115 (= S112), G116 (= G113), S117 (= S114), Y149 (= Y146), H150 (= H147), G151 (= G148), E222 (= E221), D255 (= D254), V257 (= V256), I258 (= I257), K284 (= K283)
5lhaA Amine transaminase crystal structure from an uncultivated pseudomonas species in the pmp-bound form
39% identity, 94% coverage: 11:426/442 of query aligns to 8:431/447 of 5lhaA
- active site: Y146 (= Y146), D253 (= D254), K282 (= K283), T319 (= T321)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G113 (= G113), S114 (= S114), Y146 (= Y146), H147 (= H147), G148 (= G148), E220 (= E221), D253 (= D254), K282 (= K283), Y318 (= Y320), T319 (= T321)
5lh9D Amine transaminase crystal structure from an uncultivated pseudomonas species in the plp-bound (internal aldimine) form
39% identity, 94% coverage: 11:426/442 of query aligns to 10:433/449 of 5lh9D
- active site: Y148 (= Y146), D255 (= D254), K284 (= K283), T321 (= T321)
- binding pyridoxal-5'-phosphate: G115 (= G113), S116 (= S114), Y148 (= Y146), H149 (= H147), G150 (= G148), E222 (= E221), D255 (= D254), V257 (= V256), K284 (= K283)
7qx3A Structure of the transaminase tr2e2 with eos (see paper)
35% identity, 91% coverage: 28:431/442 of query aligns to 2:407/422 of 7qx3A
6fyqA The crystal structure of a new transaminase from the marine bacterium virgibacillus (see paper)
33% identity, 98% coverage: 9:442/442 of query aligns to 7:439/443 of 6fyqA
- active site: F15 (= F17), Y147 (= Y146), D243 (= D254), K272 (= K283)
- binding pyridoxal-5'-phosphate: G114 (= G113), S115 (= S114), Y147 (= Y146), H148 (= H147), G149 (= G148), E210 (= E221), D243 (= D254), V245 (= V256), I246 (= I257), K272 (= K283)
5kr5A Directed evolution of transaminases by ancestral reconstruction. Using old proteins for new chemistries
36% identity, 91% coverage: 28:430/442 of query aligns to 31:441/455 of 5kr5A
- binding calcium ion: E66 (≠ D63), D70 (≠ A67), D412 (≠ A403)
- binding pyridoxal-5'-phosphate: S117 (= S112), G118 (= G113), S119 (= S114), Y151 (= Y146), H152 (= H147), G153 (= G148), E224 (= E221), D257 (= D254), V259 (= V256), K286 (= K283), W322 (≠ Y320), T323 (= T321)
Sites not aligning to the query:
6io1B Crystal structure of a novel thermostable (s)-enantioselective omega- transaminase from thermomicrobium roseum (see paper)
34% identity, 99% coverage: 6:441/442 of query aligns to 9:446/448 of 6io1B
- active site: L20 (≠ F17), Y151 (= Y146), D257 (= D254), K286 (= K283)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G117 (≠ S112), G118 (= G113), A119 (≠ S114), N122 (≠ V117), Y151 (= Y146), H152 (= H147), D257 (= D254), V259 (= V256), I260 (= I257), K286 (= K283)
7q9xAAA Probable aminotransferase
33% identity, 94% coverage: 16:431/442 of query aligns to 17:435/455 of 7q9xAAA
- binding (3E)-4-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}-2-oxobut-3-enoic acid: L55 (= L53), W56 (= W54), S115 (= S112), G116 (= G113), S117 (= S114), Y149 (= Y146), G151 (= G148), E222 (= E221), D255 (= D254), V257 (= V256), I258 (= I257), K284 (= K283), F316 (≠ Y320), T317 (= T321), R412 (= R408)
- binding pyridoxal-5'-phosphate: F316 (≠ Y320), T317 (= T321)
4a6tC Crystal structure of the omega transaminase from chromobacterium violaceum in complex with plp (see paper)
33% identity, 94% coverage: 16:431/442 of query aligns to 17:435/455 of 4a6tC
- active site: F18 (= F17), Y149 (= Y146), E222 (= E221), D255 (= D254), I258 (= I257), K284 (= K283), V419 (≠ A415)
- binding pyridoxal-5'-phosphate: G116 (= G113), S117 (= S114), Y149 (= Y146), H150 (= H147), G151 (= G148), E222 (= E221), D255 (= D254), V257 (= V256), I258 (= I257), K284 (= K283)
6s4gA Crystal structure of the omega transaminase from chromobacterium violaceum in complex with pmp (see paper)
33% identity, 94% coverage: 16:431/442 of query aligns to 16:434/453 of 6s4gA
- active site: F17 (= F17), Y148 (= Y146), D254 (= D254), K283 (= K283)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: S114 (= S112), G115 (= G113), S116 (= S114), Y148 (= Y146), H149 (= H147), G150 (= G148), E221 (= E221), D254 (= D254), V256 (= V256), I257 (= I257), K283 (= K283), F315 (≠ Y320), T316 (= T321)
7qx0B Transaminase structure of plurienzyme (tr2e2) in complex with plp (see paper)
33% identity, 94% coverage: 16:431/442 of query aligns to 16:428/443 of 7qx0B
4a6rA Crystal structure of the omega transaminase from chromobacterium violaceum in the apo form, crystallised from polyacrylic acid (see paper)
33% identity, 91% coverage: 28:431/442 of query aligns to 1:403/423 of 4a6rA
- active site: Y120 (= Y146), E190 (= E221), D223 (= D254), I226 (= I257), K252 (= K283), V387 (≠ A415)
- binding polyacrylic acid: T84 (= T110), N85 (= N111), S86 (= S112), S88 (= S114), E89 (= E115), T93 (= T119), R96 (≠ K122), Y120 (= Y146), S123 (≠ V149), T124 (≠ G150)
7ypmA Crystal structure of transaminase cc1012 complexed with plp and l- alanine (see paper)
34% identity, 93% coverage: 24:434/442 of query aligns to 27:440/454 of 7ypmA
- binding alanine: W57 (= W54), Y150 (= Y146)
- binding pyridoxal-5'-phosphate: S116 (= S112), G117 (= G113), S118 (= S114), Y150 (= Y146), G152 (= G148), E223 (= E221), D256 (= D254), V258 (= V256), I259 (= I257), K285 (= K283)
4ba5A Crystal structure of omega-transaminase from chromobacterium violaceum (see paper)
33% identity, 91% coverage: 28:431/442 of query aligns to 2:407/427 of 4ba5A
- active site: Y121 (= Y146), E194 (= E221), D227 (= D254), I230 (= I257), K256 (= K283), V391 (≠ A415)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: L27 (= L53), W28 (= W54), G88 (= G113), S89 (= S114), Y121 (= Y146), H122 (= H147), G123 (= G148), E194 (= E221), A199 (≠ S226), D227 (= D254), V229 (= V256), R384 (= R408)
Query Sequence
>H281DRAFT_01578 FitnessBrowser__Burk376:H281DRAFT_01578
MTSRPVIDDLSSFWMPFTANRQFKAAPRLLESAKGMYYRSTDGREVLDGCAGLWCVNAGH
SRDEIVAAITQQLSTLDFAPTFQMGHPLAFEAATKVAELMPEGLDRIFFTNSGSESVDTA
LKIALAYHRSRGEGQRTRLIGRERGYHGVGFGGISVGGIAPNRKTFSGALLPAVDHLPHT
HNLEHNAFSKGQPAWGAHLAEELERIVTLHDASTIAAVIVEPVAGSTGVLIPPQGYLQKL
REICTKHGILLIFDEVITGFGRVGKATASEYFGVTPDLITMAKAINNASIPMGAVAASRT
VHDTIVNAGAQGAIELFHGYTYSAHPAAVAAAIATLDLYRREGLFERAASLAPTFEAAAH
SLRGAKHVKDIRNLGMIAGIELEPRDGAPGARAYEAFVKCFEAGVLVRFTGDILAFSPPL
IINEEQIAHIFKTVGDVLATVQ
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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