SitesBLAST
Comparing BWI76_RS03535 FitnessBrowser__Koxy:BWI76_RS03535 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)
8v9pA Proteus vulgaris tryptophan indole-lyase complexed with (3s)- dioxindolyl-l-alanine
69% identity, 100% coverage: 2:462/462 of query aligns to 2:466/466 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 (= T49), Q98 (= Q98), G99 (= G99), R100 (= R100), F131 (= F127), D132 (= D128), T133 (= T129), N193 (= N189), D222 (= D218), R225 (= R221), S262 (= S258), K265 (= K261), V388 (= V384), R413 (= R409), F458 (= F454)
8v6pB Tryptophanase
69% identity, 100% coverage: 2:462/462 of query aligns to 2:466/466 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 (= T49), Q98 (= Q98), G99 (= G99), R100 (= R100), F131 (= F127), D132 (= D128), N193 (= N189), D222 (= D218), R225 (= R221), S262 (= S258), K265 (= K261), R413 (= R409), H457 (= H453), F458 (= F454)
8v4aB Proteus vulgaris tryptophan indole-lyase complexed with l-ethionine
69% identity, 100% coverage: 2:462/462 of query aligns to 2:466/466 of 8v4aB
- binding (2E)-4-(ethylsulfanyl)-2-{[(Z)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4(1H)-ylidene}methyl]imino}butanoic acid: T49 (= T49), Q98 (= Q98), G99 (= G99), R100 (= R100), F131 (= F127), N193 (= N189), D222 (= D218), R225 (= R221), S262 (= S258), K265 (= K261), R413 (= R409)
8v4aA Proteus vulgaris tryptophan indole-lyase complexed with l-ethionine
69% identity, 100% coverage: 2:462/462 of query aligns to 2:466/466 of 8v4aA
- binding (E)-S-ethyl-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-homocysteine: F36 (= F36), T49 (= T49), Q98 (= Q98), G99 (= G99), R100 (= R100), F131 (= F127), T133 (= T129), N193 (= N189), D222 (= D218), R225 (= R221), S262 (= S258), K265 (= K261), R413 (= R409), F458 (= F454)
5w19A Tryptophan indole-lyase complex with oxindolyl-l-alanine (see paper)
69% identity, 100% coverage: 2:462/462 of query aligns to 2:466/466 of 5w19A
- active site: Y71 (= Y71), F131 (= F127), D132 (= D128), D222 (= D218), A224 (= A220), K265 (= K261), I390 (= I386), H457 (= H453)
- 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 (= F36), T49 (= T49), Q98 (= Q98), G99 (= G99), R100 (= R100), F131 (= F127), D132 (= D128), T133 (= T129), N193 (= N189), D222 (= D218), R225 (= R221), S262 (= S258), K265 (= K261), R413 (= R409), F458 (= F454)
8v6pA Tryptophanase
69% identity, 100% coverage: 2:461/462 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 (= T49), S51 (= S51), Q98 (= Q98), G99 (= G99), R100 (= R100), F131 (= F127), D132 (= D128), T133 (= T129), N193 (= N189), D222 (= D218), R225 (= R221), S262 (= S258), K265 (= K261), L394 (= L390), R413 (= R409), H457 (= H453), F458 (= F454)
8v2kA Proteus vulgaris tryptophan indole-lyase complexed with l-alanine
68% identity, 100% coverage: 2:461/462 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 (= T49), Q98 (= Q98), G99 (= G99), R100 (= R100), F131 (= F127), N193 (= N189), D222 (= D218), R225 (= R221), S262 (= S258), K265 (= K261), R408 (= R409)
8v2kB Proteus vulgaris tryptophan indole-lyase complexed with l-alanine
68% identity, 100% coverage: 2:461/462 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 (= T49), Q98 (= Q98), G99 (= G99), R100 (= R100), F131 (= F127), N193 (= N189), D222 (= D218), R225 (= R221), S262 (= S258), K265 (= K261), R406 (= R409)
P0A853 Tryptophanase; L-tryptophan indole-lyase; TNase; EC 4.1.99.1 from Escherichia coli (strain K12) (see 2 papers)
58% identity, 100% coverage: 1:461/462 of query aligns to 4:471/471 of P0A853
- K5 (= K2) modified: N6-acetyllysine
- K115 (≠ A112) modified: N6-acetyllysine
- K156 (≠ P147) modified: N6-acetyllysine
- C294 (≠ V283) mutation to S: Identical to wild-type.
- C298 (= C287) mutation to S: Alters activity.
- K450 (= K440) modified: N6-acetyllysine
2c44C Crystal structure of e. Coli tryptophanase (see paper)
58% identity, 100% coverage: 1:461/462 of query aligns to 1:468/468 of 2c44C
- active site: Y71 (= Y71), F133 (= F127), D134 (= D128), D224 (= D218), A226 (= A220), K267 (= K261), I393 (= I386), H460 (= H453)
- binding sulfate ion: T49 (= T49), Q98 (= Q98), G99 (= G99), R100 (= R100), S264 (= S258), K267 (= K261), R416 (= R409)
5d8gA A structural view on the dissociation of e. Coli tryptophanase (see paper)
58% identity, 100% coverage: 2:461/462 of query aligns to 1:465/465 of 5d8gA
- active site: Y70 (= Y71), F130 (= F127), D131 (= D128), D221 (= D218), A223 (= A220), K264 (= K261), I390 (= I386), H457 (= H453)
- binding calcium ion: R65 (≠ M66), E310 (= E305)
- binding magnesium ion: D49 (= D50), H352 (= H348), T415 (= T411), I416 (= I412)
1c7gA Tyrosine phenol-lyase from erwinia herbicola
51% identity, 98% coverage: 6:458/462 of query aligns to 6:453/456 of 1c7gA
- active site: Y71 (= Y71), F123 (= F127), T124 (≠ D128), D214 (= D218), T216 (≠ A220), K257 (= K261), R381 (≠ I386), F448 (≠ H453)
- binding pyridoxal-5'-phosphate: Q98 (= Q98), G99 (= G99), R100 (= R100), F123 (= F127), D214 (= D218), T216 (≠ A220), R217 (= R221), S254 (= S258), K257 (= K261)
8sijA Crystal structure of f. Varium tryptophanase (see paper)
52% identity, 100% coverage: 1:461/462 of query aligns to 2:445/445 of 8sijA
8sijB Crystal structure of f. Varium tryptophanase (see paper)
51% identity, 100% coverage: 1:461/462 of query aligns to 2:441/441 of 8sijB
4w1yB Crystal structure of escherichia coli tryptophanase in 'semi-holo' form (see paper)
54% identity, 100% coverage: 2:461/462 of query aligns to 1:433/433 of 4w1yB
6nv8B Perdeuterated tyrosine phenol-lyase from citrobacter freundii complexed with an aminoacrylate intermediate formed from s-ethyl-l- cysteine and 4-hydroxypyridine
50% identity, 98% coverage: 6:458/462 of query aligns to 5:452/455 of 6nv8B
- active site: Y70 (= Y71), F122 (= F127), T123 (≠ D128), D213 (= D218), T215 (≠ A220), K256 (= K261), R380 (≠ I386), F447 (≠ H453)
- binding pyridin-4-ol: S39 (= S40), K40 (≠ Q41)
- binding 2-amino-acrylic acid: F122 (= F127), K256 (= K261), R403 (= R409)
2yctA Tyrosine phenol-lyase from citrobacter freundii in complex with pyridine n-oxide and the quinonoid intermediate formed with l-alanine (see paper)
50% identity, 98% coverage: 6:458/462 of query aligns to 5:452/455 of 2yctA
- active site: Y70 (= Y71), F122 (= F127), T123 (≠ D128), D213 (= D218), T215 (≠ A220), K256 (= K261), R380 (≠ I386), F447 (≠ H453)
- binding pyridine-n-oxide: S11 (≠ M12), W60 (= W61), R99 (= R100), F122 (= F127), T123 (≠ D128), M378 (≠ V384), R380 (≠ I386), F447 (≠ H453), F448 (= F454)
- binding (2e)-2-{[(z)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4(1h)-ylidene}methyl]imino}propanoic acid: T48 (= T49), S50 (= S51), Q97 (= Q98), G98 (= G99), R99 (= R100), F122 (= F127), N184 (= N189), D213 (= D218), R216 (= R221), S253 (= S258), K256 (= K261), R403 (= R409)
- binding pyridoxal-5'-phosphate: Q97 (= Q98), G98 (= G99), R99 (= R100), F122 (= F127), D213 (= D218), R216 (= R221), S253 (= S258), K256 (= K261)
- binding phosphate ion: T48 (= T49), F122 (= F127), N184 (= N189), R403 (= R409)
2vlhA Quinonoid intermediate of citrobacter freundii tyrosine phenol-lyase formed with methionine (see paper)
50% identity, 98% coverage: 6:458/462 of query aligns to 6:453/456 of 2vlhA
- active site: Y71 (= Y71), F123 (= F127), T124 (≠ D128), D214 (= D218), T216 (≠ A220), K257 (= K261), R381 (≠ I386), F448 (≠ H453)
- binding (2e)-2-{[(z)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4(1h)-ylidene}methyl]imino}-4-(methylsulfanyl)butanoic acid: T49 (= T49), Q98 (= Q98), G99 (= G99), R100 (= R100), F123 (= F127), N185 (= N189), D214 (= D218), R217 (= R221), S254 (= S258), K257 (= K261), R404 (= R409), F449 (= F454)
2vlfA Quinonoid intermediate of citrobacter freundii tyrosine phenol-lyase formed with alanine (see paper)
50% identity, 98% coverage: 6:458/462 of query aligns to 6:453/456 of 2vlfA
- active site: Y71 (= Y71), F123 (= F127), T124 (≠ D128), D214 (= D218), T216 (≠ A220), K257 (= K261), R381 (≠ I386), F448 (≠ H453)
- binding (2e)-2-{[(z)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4(1h)-ylidene}methyl]imino}propanoic acid: T49 (= T49), Q98 (= Q98), G99 (= G99), R100 (= R100), F123 (= F127), N185 (= N189), D214 (= D218), T216 (≠ A220), R217 (= R221), S254 (= S258), K257 (= K261), R404 (= R409)
2ez2A Apo tyrosine phenol-lyase from citrobacter freundii at ph 8.0 (see paper)
50% identity, 98% coverage: 6:458/462 of query aligns to 6:453/456 of 2ez2A
- active site: Y71 (= Y71), F123 (= F127), T124 (≠ D128), D214 (= D218), T216 (≠ A220), K257 (= K261), R381 (≠ I386), F448 (≠ H453)
- binding phosphate ion: Q98 (= Q98), G99 (= G99), R100 (= R100), S254 (= S258), K257 (= K261)
Query Sequence
>BWI76_RS03535 FitnessBrowser__Koxy:BWI76_RS03535
MKRIPEPFRIKMVENIRMTTFDDRVKALEEAGYNPFLLNSQDVYIDLLTDSGTGAMSDHQ
WAGLMMGDEAYAGSRNYQHLCEKVKEIIGYPYTIPTHQGRGAEQILFPSLIARRKSAHPV
FISNFHFDTTAAHVELNGAKAINVVTPKAFDTTSWYDWKGNFDIVLLKATIAEHGAENVA
AIITTVTCNSSGGQPVSLANMREVYQIARQNNIPVVIDSARFCENAWFIKQREEGYADKS
VKEIILEMYQYGDMLTMSAKKDPMVNIGGLCCFRDDEDLFNEVRIRCVPMEGFVTYGGLA
GRDMEALAIGLEEGTNEDYLAYRINQVEYLGERLREGGIPIQYPTGGHAVFVDAKLLLPH
IPPEQFPAHALNNELYLEAGIRSVEIGSLLLGRDPQTGKQKASPMELLRLTIPRRVYTND
HMDYIADALIAVKARAATIKGLTFTYEPPVLRHFVARLKPVK
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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