SitesBLAST
Comparing AO356_16855 FitnessBrowser__pseudo5_N2C3_1:AO356_16855 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)
6cgqA Threonine synthase from bacillus subtilis atcc 6633 with plp and plp- ala (see paper)
34% identity, 82% coverage: 63:405/417 of query aligns to 3:327/339 of 6cgqA
- active site: K56 (= K117), T80 (= T141), E206 (≠ Q275), S210 (= S279), A228 (≠ S306), T305 (= T382)
- binding pyridoxal-5'-phosphate: F55 (≠ L116), K56 (= K117), N82 (= N143), V175 (= V243), G176 (= G244), N177 (= N245), A178 (≠ G246), G179 (≠ C247), N180 (≠ I248), A228 (≠ S306), E275 (= E353), T305 (= T382), G306 (= G383)
6cgqB Threonine synthase from bacillus subtilis atcc 6633 with plp and plp- ala (see paper)
34% identity, 82% coverage: 65:407/417 of query aligns to 7:337/345 of 6cgqB
- active site: K58 (= K117), T82 (= T141), E214 (≠ Q275), S218 (= S279), A236 (≠ S306), T313 (= T382)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-alanine: K58 (= K117), S81 (= S140), T82 (= T141), N84 (= N143), T85 (≠ A144), V183 (= V243), G184 (= G244), N185 (= N245), A186 (≠ G246), N188 (≠ I248), A236 (≠ S306), I237 (= I307), E283 (= E353), T313 (= T382)
- binding phosphate ion: K58 (= K117), T85 (≠ A144), N151 (≠ T210), S152 (≠ G211), R157 (≠ M216), N185 (= N245)
6nmxA Threonine synthase from bacillus subtilis atcc 6633 with plp and appa (see paper)
34% identity, 82% coverage: 65:407/417 of query aligns to 9:339/350 of 6nmxA
- active site: K60 (= K117), T84 (= T141), E216 (≠ Q275), S220 (= S279), A238 (≠ S306), T315 (= T382)
- binding (2E,3Z)-2-{[(Z)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4(1H)-ylidene}methyl]imino}-5-phosphonopent-3-enoic acid: K60 (= K117), S83 (= S140), T84 (= T141), N86 (= N143), T87 (≠ A144), F133 (≠ Y189), N153 (≠ T210), S154 (≠ G211), R159 (≠ M216), V185 (= V243), G186 (= G244), N187 (= N245), A188 (≠ G246), G189 (≠ C247), N190 (≠ I248), A238 (≠ S306), I239 (= I307), E285 (= E353), T315 (= T382)
2zsjA Crystal structure of threonine synthase from aquifex aeolicus vf5
33% identity, 83% coverage: 65:412/417 of query aligns to 8:339/350 of 2zsjA
- active site: K61 (= K117), T85 (= T141), Q218 (= Q275), A222 (≠ S279), A240 (≠ S306), T317 (= T382)
- binding pyridoxal-5'-phosphate: F60 (≠ L116), K61 (= K117), N87 (= N143), V186 (= V243), G187 (= G244), N188 (= N245), A189 (≠ G246), G190 (≠ C247), N191 (≠ I248), A240 (≠ S306), T317 (= T382), G318 (= G383)
P9WG59 Threonine synthase; TS; EC 4.2.3.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
33% identity, 79% coverage: 67:395/417 of query aligns to 21:339/360 of P9WG59
- K69 (= K117) modified: N6-(pyridoxal phosphate)lysine
- N95 (= N143) binding
- K151 (≠ N198) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
- GNAGN 196:200 (≠ GNGCI 244:248) binding
- T326 (= T382) binding
2d1fA Structure of mycobacterium tuberculosis threonine synthase (see paper)
33% identity, 79% coverage: 67:395/417 of query aligns to 12:330/349 of 2d1fA
- active site: K60 (= K117), T84 (= T141), D209 (≠ E266), R213 (= R270), L215 (≠ I272), A240 (≠ S306), T317 (= T382)
- binding pyridoxal-5'-phosphate: F59 (≠ L116), K60 (= K117), N86 (= N143), V186 (= V243), G187 (= G244), N188 (= N245), A189 (≠ G246), G190 (≠ C247), N191 (≠ I248), A240 (≠ S306), T317 (= T382)
1uimA Crystal structure of threonine synthase from thermus thermophilus hb8, orthorhombic crystal form (see paper)
34% identity, 78% coverage: 65:388/417 of query aligns to 8:323/350 of 1uimA
- active site: K61 (= K117), T85 (= T141), P212 (= P269), G216 (= G273), Q218 (= Q275), A240 (≠ S306), T317 (= T382)
- binding pyridoxal-5'-phosphate: F60 (≠ L116), K61 (= K117), N87 (= N143), G187 (= G244), N188 (= N245), A189 (≠ G246), G190 (≠ C247), N191 (≠ I248), A240 (≠ S306), E287 (= E353), T317 (= T382), G318 (= G383)
3aexA Catalytic intermediate analogue of threonine synthase from thermus thermophilus hb8 (see paper)
34% identity, 78% coverage: 65:388/417 of query aligns to 8:323/351 of 3aexA
- active site: K61 (= K117), T85 (= T141), P212 (= P269), G216 (= G273), Q218 (= Q275), A240 (≠ S306), T317 (= T382)
- binding (3E)-4-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}-2-oxobut-3-enoic acid: K61 (= K117), S84 (= S140), T85 (= T141), N87 (= N143), T88 (≠ A144), V186 (= V243), G187 (= G244), N188 (= N245), A189 (≠ G246), G190 (≠ C247), N191 (≠ I248), A240 (≠ S306), I241 (= I307), E287 (= E353), T317 (= T382)
- binding phosphate ion: K61 (= K117), T88 (≠ A144), N154 (≠ T210), S155 (≠ G211), R160 (≠ M216), N188 (= N245)
1v7cA Crystal structure of threonine synthase from thermus thermophilus hb8 in complex with a substrate analogue (see paper)
34% identity, 78% coverage: 65:388/417 of query aligns to 8:323/351 of 1v7cA
- active site: K61 (= K117), T85 (= T141), P212 (= P269), G216 (= G273), Q218 (= Q275), A240 (≠ S306), T317 (= T382)
- binding (2e)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-5-phosphonopent-2-enoic acid: K61 (= K117), S84 (= S140), T85 (= T141), N87 (= N143), T88 (≠ A144), F134 (≠ Y189), N154 (≠ T210), S155 (≠ G211), R160 (≠ M216), V186 (= V243), G187 (= G244), N188 (= N245), A189 (≠ G246), G190 (≠ C247), N191 (≠ I248), A240 (≠ S306), I241 (= I307), E287 (= E353), T317 (= T382)
3aeyA Apo form of threonine synthase from thermus thermophilus hb8 (see paper)
34% identity, 78% coverage: 63:388/417 of query aligns to 5:322/350 of 3aeyA
- active site: K60 (= K117), T84 (= T141), P211 (= P269), G215 (= G273), Q217 (= Q275), A239 (≠ S306), T316 (= T382)
- binding sulfate ion: K60 (= K117), K60 (= K117), G85 (= G142), N86 (= N143), T87 (≠ A144), T87 (≠ A144), S154 (≠ G211), R159 (≠ M216), N187 (= N245), R228 (≠ W286), V230 (≠ H288), E231 (≠ D289), R232 (= R290), A239 (≠ S306)
A0R220 Threonine synthase; TS; EC 4.2.3.1 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
33% identity, 81% coverage: 67:405/417 of query aligns to 21:345/360 of A0R220
- K151 (≠ N198) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
2c2bA Crystallographic structure of arabidopsis thaliana threonine synthase complexed with pyridoxal phosphate and s-adenosylmethionine (see paper)
27% identity, 95% coverage: 17:414/417 of query aligns to 19:428/444 of 2c2bA
- binding pyridoxal-5'-phosphate: F127 (≠ L116), K128 (= K117), D159 (≠ N143), G259 (≠ V243), G260 (= G244), N261 (= N245), L262 (≠ G246), G263 (≠ C247), N264 (≠ I248), A321 (≠ S306), H369 (≠ G355), T397 (= T382)
- binding s-adenosylmethionine: S64 (≠ G62), T65 (≠ M63), W66 (= W64), P67 (≠ R65), G69 (vs. gap), S90 (≠ P80), F92 (≠ L82), N97 (≠ P87), L98 (= L88), W100 (≠ R91), W115 (≠ F104), W115 (≠ F104), Q246 (= Q230), F247 (≠ L231)
Q9S7B5 Threonine synthase 1, chloroplastic; Protein METHIONINE OVER-ACCUMULATOR 2; EC 4.2.3.1 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
27% identity, 95% coverage: 18:414/417 of query aligns to 95:503/526 of Q9S7B5
- N172 (≠ P87) binding
- L173 (= L88) binding
- K181 (= K97) binding in monomer B; binding in monomer A
- N187 (≠ I101) binding in monomer B
- L205 (≠ R119) mutation to R: In mto2-1; causes a strong decrease in the concentration of soluble threonine and over-accumulation of methionine.
2c2gA Crystal structure of threonine synthase from arabidopsis thaliana in complex with its cofactor pyridoxal phosphate (see paper)
28% identity, 76% coverage: 17:331/417 of query aligns to 37:369/448 of 2c2gA
1tdjA Threonine deaminase (biosynthetic) from e. Coli (see paper)
27% identity, 72% coverage: 86:387/417 of query aligns to 28:316/494 of 1tdjA
- active site: K58 (= K117), A83 (≠ T141), E209 (≠ Q275), S213 (= S279), C215 (≠ F281), G237 (≠ N308), L310 (≠ I381), S311 (≠ T382)
- binding pyridoxal-5'-phosphate: F57 (≠ L116), K58 (= K117), N85 (= N143), G184 (= G244), G185 (≠ N245), G186 (= G246), G187 (≠ C247), G237 (≠ N308), E282 (= E353), S311 (≠ T382), G312 (= G383)
P04968 L-threonine dehydratase biosynthetic IlvA; Threonine deaminase; EC 4.3.1.19 from Escherichia coli (strain K12) (see paper)
27% identity, 72% coverage: 86:387/417 of query aligns to 32:320/514 of P04968
- K62 (= K117) modified: N6-(pyridoxal phosphate)lysine
- N89 (= N143) binding
- GGGGL 188:192 (≠ GNGCI 244:248) binding
- S315 (≠ T382) binding
4d9kA Crystal structure of escherichia coli diaminopropionate ammonia lyase in apo form (see paper)
26% identity, 42% coverage: 86:259/417 of query aligns to 45:246/366 of 4d9kA
Sites not aligning to the query:
4d9mA Crystal structure of diaminopropionate ammonia lyase from escherichia coli in complex with aminoacrylate-plp azomethine reaction intermediate (see paper)
26% identity, 42% coverage: 86:259/417 of query aligns to 44:236/378 of 4d9mA
Sites not aligning to the query:
5ygrB Crystal structure of plp bound diaminopropionate ammonia lyase from salmonella typhimurium (see paper)
25% identity, 48% coverage: 86:285/417 of query aligns to 35:252/365 of 5ygrB
P16703 Cysteine synthase B; CSase B; O-acetylserine (thiol)-lyase B; OAS-TL B; O-acetylserine sulfhydrylase B; EC 2.5.1.47 from Escherichia coli (strain K12) (see paper)
26% identity, 74% coverage: 83:392/417 of query aligns to 8:292/303 of P16703
- N71 (= N143) binding
- S255 (= S333) binding
Query Sequence
>AO356_16855 FitnessBrowser__pseudo5_N2C3_1:AO356_16855
MKNSYREYVLQCLVCDRSYQPHEVSYYCPHCNIDGALDALYDYPTLKREWSRDSLAHDHA
RGMWRYDRLMPLSSTQFIPPLLVGNTPLYSRPELLGKGARIKVFVKDESRQPTGSLKDRA
SALAVAHAMQSGARTVAVASTGNAASALAGMSASLGLHNVIYLPKSAPREKLAQMQGYGA
EIVLVDGQYDEAFEQCLNACEKHGWYNRTTGINSYMSEGKKTVAFEMCEQLNWQVPDLVF
VPVGNGCILGSVYKGFFDLLQLGWIERIPRLIGVQAEHSNFMYRAWRHDRSMQQTERLPP
TSLASSINVALPRDRLKAMRAVTASDGEFICVSDPSIVAAASRLAASTGVFPEAGAASAF
AGLLKYAETHPDTPQTAVILITGSGLKDTSIFLSDSSKSQPRVLPHHVTAPPAEALI
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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