SitesBLAST
Comparing 17768 FitnessBrowser__Keio:17768 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)
P0A853 Tryptophanase; L-tryptophan indole-lyase; TNase; EC 4.1.99.1 from Escherichia coli (strain K12) (see 2 papers)
100% identity, 100% coverage: 1:471/471 of query aligns to 1:471/471 of P0A853
- K5 (= K5) modified: N6-acetyllysine
- K115 (= K115) modified: N6-acetyllysine
- K156 (= K156) modified: N6-acetyllysine
- C294 (= C294) mutation to S: Identical to wild-type.
- C298 (= C298) mutation to S: Alters activity.
- K450 (= K450) modified: N6-acetyllysine
2c44C Crystal structure of e. Coli tryptophanase (see paper)
100% identity, 99% coverage: 4:471/471 of query aligns to 1:468/468 of 2c44C
- active site: Y71 (= Y74), F133 (= F136), D134 (= D137), D224 (= D227), A226 (= A229), K267 (= K270), I393 (= I396), H460 (= H463)
- binding sulfate ion: T49 (= T52), Q98 (= Q101), G99 (= G102), R100 (= R103), S264 (= S267), K267 (= K270), R416 (= R419)
5d8gA A structural view on the dissociation of e. Coli tryptophanase (see paper)
99% identity, 99% coverage: 5:471/471 of query aligns to 1:465/465 of 5d8gA
- active site: Y70 (= Y74), F130 (= F136), D131 (= D137), D221 (= D227), A223 (= A229), K264 (= K270), I390 (= I396), H457 (= H463)
- binding calcium ion: R65 (= R69), E310 (= E316)
- binding magnesium ion: D49 (= D53), H352 (= H358), T415 (= T421), I416 (= I422)
4w1yB Crystal structure of escherichia coli tryptophanase in 'semi-holo' form (see paper)
93% identity, 99% coverage: 5:471/471 of query aligns to 1:433/433 of 4w1yB
8v9pA Proteus vulgaris tryptophan indole-lyase complexed with (3s)- dioxindolyl-l-alanine
52% identity, 99% coverage: 5:471/471 of query aligns to 2:465/466 of 8v9pA
- binding (2~{E})-2-[(~{Z})-[2-methyl-3-oxidanyl-5-[[oxidanyl-bis(oxidanylidene)-$l^{6}-phosphanyl]oxymethyl]-1~{H}-pyridin-4-ylidene]methyl]imino-3-[(3~{S})-3-oxidanyl-2-oxidanylidene-1~{H}-indol-3-yl]propanoic acid: T49 (= T52), Q98 (= Q101), G99 (= G102), R100 (= R103), F131 (= F136), D132 (= D137), T133 (= T138), N193 (= N198), D222 (= D227), R225 (= R230), S262 (= S267), K265 (= K270), V388 (= V394), R413 (= R419), F458 (= F464)
8v6pB Tryptophanase
52% identity, 99% coverage: 5:471/471 of query aligns to 2:465/466 of 8v6pB
- binding (2E)-2-{[(Z)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4(1H)-ylidene}methyl]imino}-3-(1H-pyrrolo[2,3-b]pyridin-3-yl)propanoic acid: T49 (= T52), Q98 (= Q101), G99 (= G102), R100 (= R103), F131 (= F136), D132 (= D137), N193 (= N198), D222 (= D227), R225 (= R230), S262 (= S267), K265 (= K270), R413 (= R419), H457 (= H463), F458 (= F464)
8v4aB Proteus vulgaris tryptophan indole-lyase complexed with l-ethionine
52% identity, 99% coverage: 5:471/471 of query aligns to 2:465/466 of 8v4aB
- binding (2E)-4-(ethylsulfanyl)-2-{[(Z)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4(1H)-ylidene}methyl]imino}butanoic acid: T49 (= T52), Q98 (= Q101), G99 (= G102), R100 (= R103), F131 (= F136), N193 (= N198), D222 (= D227), R225 (= R230), S262 (= S267), K265 (= K270), R413 (= R419)
8v4aA Proteus vulgaris tryptophan indole-lyase complexed with l-ethionine
52% identity, 99% coverage: 5:471/471 of query aligns to 2:465/466 of 8v4aA
- binding (E)-S-ethyl-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-homocysteine: F36 (= F39), T49 (= T52), Q98 (= Q101), G99 (= G102), R100 (= R103), F131 (= F136), T133 (= T138), N193 (= N198), D222 (= D227), R225 (= R230), S262 (= S267), K265 (= K270), R413 (= R419), F458 (= F464)
5w19A Tryptophan indole-lyase complex with oxindolyl-l-alanine (see paper)
52% identity, 99% coverage: 5:471/471 of query aligns to 2:465/466 of 5w19A
- active site: Y71 (= Y74), F131 (= F136), D132 (= D137), D222 (= D227), A224 (= A229), K265 (= K270), I390 (= I396), H457 (= H463)
- binding 1-carboxy-1-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]azaniumyl}-2-[(3R)-2-oxo-2,3-dihydro-1H-indol-3-yl]ethan-1-ide: F36 (= F39), T49 (= T52), Q98 (= Q101), G99 (= G102), R100 (= R103), F131 (= F136), D132 (= D137), T133 (= T138), N193 (= N198), D222 (= D227), R225 (= R230), S262 (= S267), K265 (= K270), R413 (= R419), F458 (= F464)
8v6pA Tryptophanase
52% identity, 99% coverage: 5:471/471 of query aligns to 2:465/465 of 8v6pA
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-3-(1H-pyrrolo[2,3-b]pyridin-3-yl)-L-alanine: T49 (= T52), S51 (= S54), Q98 (= Q101), G99 (= G102), R100 (= R103), F131 (= F136), D132 (= D137), T133 (= T138), N193 (= N198), D222 (= D227), R225 (= R230), S262 (= S267), K265 (= K270), L394 (= L400), R413 (= R419), H457 (= H463), F458 (= F464)
8v2kA Proteus vulgaris tryptophan indole-lyase complexed with l-alanine
52% identity, 99% coverage: 5:471/471 of query aligns to 2:460/460 of 8v2kA
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-alanine: T49 (= T52), Q98 (= Q101), G99 (= G102), R100 (= R103), F131 (= F136), N193 (= N198), D222 (= D227), R225 (= R230), S262 (= S267), K265 (= K270), R408 (= R419)
8v2kB Proteus vulgaris tryptophan indole-lyase complexed with l-alanine
51% identity, 99% coverage: 5:471/471 of query aligns to 2:458/458 of 8v2kB
- binding (2e)-2-{[(z)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4(1h)-ylidene}methyl]imino}propanoic acid: T49 (= T52), Q98 (= Q101), G99 (= G102), R100 (= R103), F131 (= F136), N193 (= N198), D222 (= D227), R225 (= R230), S262 (= S267), K265 (= K270), R406 (= R419)
8sijA Crystal structure of f. Varium tryptophanase (see paper)
46% identity, 99% coverage: 5:471/471 of query aligns to 3:445/445 of 8sijA
8sijB Crystal structure of f. Varium tryptophanase (see paper)
46% identity, 99% coverage: 5:471/471 of query aligns to 3:441/441 of 8sijB
1c7gA Tyrosine phenol-lyase from erwinia herbicola
44% identity, 98% coverage: 9:468/471 of query aligns to 6:453/456 of 1c7gA
- active site: Y71 (= Y74), F123 (= F136), T124 (≠ D137), D214 (= D227), T216 (≠ A229), K257 (= K270), R381 (≠ I396), F448 (≠ H463)
- binding pyridoxal-5'-phosphate: Q98 (= Q101), G99 (= G102), R100 (= R103), F123 (= F136), D214 (= D227), T216 (≠ A229), R217 (= R230), S254 (= S267), K257 (= K270)
6nv8B Perdeuterated tyrosine phenol-lyase from citrobacter freundii complexed with an aminoacrylate intermediate formed from s-ethyl-l- cysteine and 4-hydroxypyridine
42% identity, 98% coverage: 9:468/471 of query aligns to 5:452/455 of 6nv8B
- active site: Y70 (= Y74), F122 (= F136), T123 (≠ D137), D213 (= D227), T215 (≠ A229), K256 (= K270), R380 (≠ I396), F447 (≠ H463)
- binding pyridin-4-ol: S39 (= S43), K40 (≠ E44)
- binding 2-amino-acrylic acid: F122 (= F136), K256 (= K270), R403 (= R419)
2yctA Tyrosine phenol-lyase from citrobacter freundii in complex with pyridine n-oxide and the quinonoid intermediate formed with l-alanine (see paper)
42% identity, 98% coverage: 9:468/471 of query aligns to 5:452/455 of 2yctA
- active site: Y70 (= Y74), F122 (= F136), T123 (≠ D137), D213 (= D227), T215 (≠ A229), K256 (= K270), R380 (≠ I396), F447 (≠ H463)
- binding pyridine-n-oxide: S11 (≠ V15), W60 (≠ Q64), R99 (= R103), F122 (= F136), T123 (≠ D137), M378 (≠ V394), R380 (≠ I396), F447 (≠ H463), F448 (= F464)
- binding (2e)-2-{[(z)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4(1h)-ylidene}methyl]imino}propanoic acid: T48 (= T52), S50 (= S54), Q97 (= Q101), G98 (= G102), R99 (= R103), F122 (= F136), N184 (= N198), D213 (= D227), R216 (= R230), S253 (= S267), K256 (= K270), R403 (= R419)
- binding pyridoxal-5'-phosphate: Q97 (= Q101), G98 (= G102), R99 (= R103), F122 (= F136), D213 (= D227), R216 (= R230), S253 (= S267), K256 (= K270)
- binding phosphate ion: T48 (= T52), F122 (= F136), N184 (= N198), R403 (= R419)
2vlhA Quinonoid intermediate of citrobacter freundii tyrosine phenol-lyase formed with methionine (see paper)
42% identity, 98% coverage: 9:468/471 of query aligns to 6:453/456 of 2vlhA
- active site: Y71 (= Y74), F123 (= F136), T124 (≠ D137), D214 (= D227), T216 (≠ A229), K257 (= K270), R381 (≠ I396), F448 (≠ H463)
- binding (2e)-2-{[(z)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4(1h)-ylidene}methyl]imino}-4-(methylsulfanyl)butanoic acid: T49 (= T52), Q98 (= Q101), G99 (= G102), R100 (= R103), F123 (= F136), N185 (= N198), D214 (= D227), R217 (= R230), S254 (= S267), K257 (= K270), R404 (= R419), F449 (= F464)
2vlfA Quinonoid intermediate of citrobacter freundii tyrosine phenol-lyase formed with alanine (see paper)
42% identity, 98% coverage: 9:468/471 of query aligns to 6:453/456 of 2vlfA
- active site: Y71 (= Y74), F123 (= F136), T124 (≠ D137), D214 (= D227), T216 (≠ A229), K257 (= K270), R381 (≠ I396), F448 (≠ H463)
- binding (2e)-2-{[(z)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4(1h)-ylidene}methyl]imino}propanoic acid: T49 (= T52), Q98 (= Q101), G99 (= G102), R100 (= R103), F123 (= F136), N185 (= N198), D214 (= D227), T216 (≠ A229), R217 (= R230), S254 (= S267), K257 (= K270), R404 (= R419)
2ez2A Apo tyrosine phenol-lyase from citrobacter freundii at ph 8.0 (see paper)
42% identity, 98% coverage: 9:468/471 of query aligns to 6:453/456 of 2ez2A
- active site: Y71 (= Y74), F123 (= F136), T124 (≠ D137), D214 (= D227), T216 (≠ A229), K257 (= K270), R381 (≠ I396), F448 (≠ H463)
- binding phosphate ion: Q98 (= Q101), G99 (= G102), R100 (= R103), S254 (= S267), K257 (= K270)
Query Sequence
>17768 FitnessBrowser__Keio:17768
MENFKHLPEPFRIRVIEPVKRTTRAYREEAIIKSGMNPFLLDSEDVFIDLLTDSGTGAVT
QSMQAAMMRGDEAYSGSRSYYALAESVKNIFGYQYTIPTHQGRGAEQIYIPVLIKKREQE
KGLDRSKMVAFSNYFFDTTQGHSQINGCTVRNVYIKEAFDTGVRYDFKGNFDLEGLERGI
EEVGPNNVPYIVATITSNSAGGQPVSLANLKAMYSIAKKYDIPVVMDSARFAENAYFIKQ
REAEYKDWTIEQITRETYKYADMLAMSAKKDAMVPMGGLLCMKDDSFFDVYTECRTLCVV
QEGFPTYGGLEGGAMERLAVGLYDGMNLDWLAYRIAQVQYLVDGLEEIGVVCQQAGGHAA
FVDAGKLLPHIPADQFPAQALACELYKVAGIRAVEIGSFLLGRDPKTGKQLPCPAELLRL
TIPRATYTQTHMDFIIEAFKHVKENAANIKGLTFTYEPKVLRHFTAKLKEV
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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