SitesBLAST
Comparing WP_066918533.1 NCBI__GCF_001579945.1:WP_066918533.1 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)
67% identity, 97% coverage: 12:438/442 of query aligns to 9:435/439 of Q9A3Q9
- V227 (= V230) 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 (= R263) mutation to L: Decreases activity toward 3-aminobutanoate by 30-fold.
- N285 (= N288) 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, 99% coverage: 4:440/442 of query aligns to 9:446/448 of Q9I700
- W61 (= W56) binding
- T327 (= T321) binding
- R414 (= R408) binding
- Q421 (≠ A415) binding
4b98A The structure of the omega aminotransferase from pseudomonas aeruginosa (see paper)
52% identity, 99% coverage: 4:440/442 of query aligns to 2:439/441 of 4b98A
- active site: F17 (= F19), Y146 (= Y148), E219 (= E222), D252 (= D255), I255 (= I258), K281 (= K284), Q414 (≠ A415)
- binding pyridoxal-5'-phosphate: G233 (= G236), Q236 (= Q239), F270 (= F273), G271 (≠ D274)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: L53 (= L55), W54 (= W56), F82 (= F84), S112 (= S114), G113 (= G115), S114 (= S116), Y146 (= Y148), H147 (= H149), G148 (= G150), E219 (= E222), S224 (= S227), D252 (= D255), V254 (= V257), I255 (= I258), K281 (= K284), Y319 (= Y320), T320 (= T321), R407 (= R408), Q414 (≠ A415)
4uhmA Characterization of a novel transaminase from pseudomonas sp. Strain aac (see paper)
51% identity, 97% coverage: 11:439/442 of query aligns to 3:432/435 of 4uhmA
- active site: F11 (= F19), Y140 (= Y148), E213 (= E222), D246 (= D255), I249 (= I258), K275 (= K284), Q408 (≠ A415)
- binding magnesium ion: A91 (≠ V99), D99 (= D107)
- binding pyridoxal-5'-phosphate: G107 (= G115), S108 (= S116), Y140 (= Y148), H141 (= H149), G142 (= G150), E213 (= E222), D246 (= D255), V248 (= V257), I249 (= I258), K275 (= K284)
3a8uX Crystal structure of omega-amino acid:pyruvate aminotransferase
51% identity, 97% coverage: 12:439/442 of query aligns to 9:438/441 of 3a8uX
- active site: Y145 (= Y148), D252 (= D255), K281 (= K284), Q414 (≠ A415)
- binding pyridoxal-5'-phosphate: S111 (= S114), G112 (= G115), S113 (= S116), Y145 (= Y148), H146 (= H149), G147 (= G150), E219 (= E222), D252 (= D255), V254 (= V257), I255 (= I258), K281 (= K284)
7qx3A Structure of the transaminase tr2e2 with eos (see paper)
39% identity, 93% coverage: 30:441/442 of query aligns to 2:417/422 of 7qx3A
3i5tA Crystal structure of aminotransferase prk07036 from rhodobacter sphaeroides kd131
38% identity, 93% coverage: 26:434/442 of query aligns to 22:430/444 of 3i5tA
- active site: Y144 (= Y148), E216 (= E222), D249 (= D255), V252 (≠ I258), K279 (= K284), V411 (≠ A415)
- binding pyridoxal-5'-phosphate: G111 (= G115), S112 (= S116), Y144 (= Y148), H145 (= H149), E216 (= E222), D249 (= D255), V251 (= V257), K279 (= K284), Y315 (= Y320), T316 (= T321)
Sites not aligning to the query:
5lhaA Amine transaminase crystal structure from an uncultivated pseudomonas species in the pmp-bound form
40% identity, 95% coverage: 15:434/442 of query aligns to 10:439/447 of 5lhaA
- active site: Y146 (= Y148), D253 (= D255), K282 (= K284), T319 (= T321)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G113 (= G115), S114 (= S116), Y146 (= Y148), H147 (= H149), G148 (= G150), E220 (= E222), D253 (= D255), K282 (= K284), Y318 (= Y320), T319 (= T321)
5lh9D Amine transaminase crystal structure from an uncultivated pseudomonas species in the plp-bound (internal aldimine) form
40% identity, 95% coverage: 15:434/442 of query aligns to 12:441/449 of 5lh9D
- active site: Y148 (= Y148), D255 (= D255), K284 (= K284), T321 (= T321)
- binding pyridoxal-5'-phosphate: G115 (= G115), S116 (= S116), Y148 (= Y148), H149 (= H149), G150 (= G150), E222 (= E222), D255 (= D255), V257 (= V257), K284 (= K284)
6io1B Crystal structure of a novel thermostable (s)-enantioselective omega- transaminase from thermomicrobium roseum (see paper)
39% identity, 93% coverage: 29:438/442 of query aligns to 31:443/448 of 6io1B
- active site: Y151 (= Y148), D257 (= D255), K286 (= K284)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G117 (≠ S114), G118 (= G115), A119 (≠ S116), N122 (≠ V119), Y151 (= Y148), H152 (= H149), D257 (= D255), V259 (= V257), I260 (= I258), K286 (= K284)
Sites not aligning to the query:
7qx0B Transaminase structure of plurienzyme (tr2e2) in complex with plp (see paper)
37% identity, 96% coverage: 18:441/442 of query aligns to 16:438/443 of 7qx0B
7q9xAAA Probable aminotransferase
36% identity, 95% coverage: 18:438/442 of query aligns to 17:442/455 of 7q9xAAA
- binding (3E)-4-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}-2-oxobut-3-enoic acid: L55 (= L55), W56 (= W56), S115 (= S114), G116 (= G115), S117 (= S116), Y149 (= Y148), G151 (= G150), E222 (= E222), D255 (= D255), V257 (= V257), I258 (= I258), K284 (= K284), 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)
36% identity, 95% coverage: 18:438/442 of query aligns to 17:442/455 of 4a6tC
- active site: F18 (= F19), Y149 (= Y148), E222 (= E222), D255 (= D255), I258 (= I258), K284 (= K284), V419 (≠ A415)
- binding pyridoxal-5'-phosphate: G116 (= G115), S117 (= S116), Y149 (= Y148), H150 (= H149), G151 (= G150), E222 (= E222), D255 (= D255), V257 (= V257), I258 (= I258), K284 (= K284)
6s4gA Crystal structure of the omega transaminase from chromobacterium violaceum in complex with pmp (see paper)
36% identity, 95% coverage: 18:438/442 of query aligns to 16:441/453 of 6s4gA
- active site: F17 (= F19), Y148 (= Y148), D254 (= D255), K283 (= K284)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: S114 (= S114), G115 (= G115), S116 (= S116), Y148 (= Y148), H149 (= H149), G150 (= G150), E221 (= E222), D254 (= D255), V256 (= V257), I257 (= I258), K283 (= K284), F315 (≠ Y320), T316 (= T321)
4a6rA Crystal structure of the omega transaminase from chromobacterium violaceum in the apo form, crystallised from polyacrylic acid (see paper)
37% identity, 93% coverage: 30:438/442 of query aligns to 1:410/423 of 4a6rA
- active site: Y120 (= Y148), E190 (= E222), D223 (= D255), I226 (= I258), K252 (= K284), V387 (≠ A415)
- binding polyacrylic acid: T84 (= T112), N85 (= N113), S86 (= S114), S88 (= S116), E89 (= E117), T93 (= T121), R96 (≠ K124), Y120 (= Y148), S123 (≠ V151), T124 (≠ G152)
4ba5A Crystal structure of omega-transaminase from chromobacterium violaceum (see paper)
36% identity, 93% coverage: 30:438/442 of query aligns to 2:414/427 of 4ba5A
- active site: Y121 (= Y148), E194 (= E222), D227 (= D255), I230 (= I258), K256 (= K284), V391 (≠ A415)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: L27 (= L55), W28 (= W56), G88 (= G115), S89 (= S116), Y121 (= Y148), H122 (= H149), G123 (= G150), E194 (= E222), A199 (≠ S227), D227 (= D255), V229 (= V257), R384 (= R408)
6gwiB The crystal structure of halomonas elongata amino-transferase (see paper)
36% identity, 94% coverage: 18:431/442 of query aligns to 17:435/450 of 6gwiB
- active site: F18 (= F19), Y149 (= Y148), D255 (= D255), K284 (= K284)
- binding pyridoxal-5'-phosphate: S115 (= S114), G116 (= G115), S117 (= S116), Y149 (= Y148), H150 (= H149), G151 (= G150), E222 (= E222), D255 (= D255), V257 (= V257), I258 (= I258), K284 (= K284)
7ypmA Crystal structure of transaminase cc1012 complexed with plp and l- alanine (see paper)
36% identity, 95% coverage: 14:434/442 of query aligns to 12:440/454 of 7ypmA
- binding alanine: W57 (= W56), Y150 (= Y148)
- binding pyridoxal-5'-phosphate: S116 (= S114), G117 (= G115), S118 (= S116), Y150 (= Y148), G152 (= G150), E223 (= E222), D256 (= D255), V258 (= V257), I259 (= I258), K285 (= K284)
5kr5A Directed evolution of transaminases by ancestral reconstruction. Using old proteins for new chemistries
35% identity, 91% coverage: 30:431/442 of query aligns to 31:442/455 of 5kr5A
- binding calcium ion: E66 (≠ P65), D70 (≠ E69), D412 (≠ K403)
- binding pyridoxal-5'-phosphate: S117 (= S114), G118 (= G115), S119 (= S116), Y151 (= Y148), H152 (= H149), G153 (= G150), E224 (= E222), D257 (= D255), V259 (= V257), K286 (= K284), W322 (≠ Y320), T323 (= T321)
Sites not aligning to the query:
D6R3B6 Vanillin aminotransferase; Putative aminotransferase; pAMT; EC 2.6.1.119 from Capsicum frutescens (Cayenne pepper) (Tabasco pepper) (see paper)
31% identity, 96% coverage: 18:441/442 of query aligns to 16:447/459 of D6R3B6
- SAGL 155:158 (≠ GISV 155:158) mutation Missing: Low pungency phenotype, characterized by low levels of capsaicinoids, and accumulation of high levels of capsinoids, which are non-pungent capsaicinoid analogs.
Query Sequence
>WP_066918533.1 NCBI__GCF_001579945.1:WP_066918533.1
MTIPTVPTPATLDAFWMPFTANRRFKAHPRLLARAQGMHYWTDDGRQILDGIAGLWCVNA
GHARPEITEAVSRQLATLDYAPTFQMGHPQAFELANRLVELVPGDLDHVFFTNSGSESVD
TALKIAIAYHRSRGEAARTRLIGREKGYHGVGFGGISVGGIVNNRKFFGSLLPGVDHLSH
TLDIEHNAYSRGQPEWGVHLADELERLVALHDASTIAAVIVEPIAGSAGVILPPKGYLQR
LRSICDRHGILLIFDEVITGFGRLGTPFGAHYFDVVPDMITSAKGLTNGAVPMGAVFVRK
SIYDAFMHAPEDAIELFHGYTYSAHPAACAAALATLEIYRREGLLTRAADLSRIWEDAVH
SLRGLPHVIDVRNLGLVAGIELQPRSSAPGTRAYDVFVAAFEKGVLIRTTGDIIALSPPL
IIEPVQIDQLVTTLADILRATP
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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