SitesBLAST
Comparing WP_018869600.1 NCBI__GCF_001995255.1:WP_018869600.1 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)
2zsjA Crystal structure of threonine synthase from aquifex aeolicus vf5
53% identity, 97% coverage: 6:375/380 of query aligns to 1:348/350 of 2zsjA
- active site: K61 (= K66), T85 (= T90), Q218 (= Q244), A222 (≠ S248), A240 (= A266), T317 (= T343)
- binding pyridoxal-5'-phosphate: F60 (= F65), K61 (= K66), N87 (= N92), V186 (= V191), G187 (= G192), N188 (= N193), A189 (= A194), G190 (= G195), N191 (= N196), A240 (= A266), T317 (= T343), G318 (= G344)
6nmxA Threonine synthase from bacillus subtilis atcc 6633 with plp and appa (see paper)
52% identity, 97% coverage: 7:376/380 of query aligns to 3:348/350 of 6nmxA
- active site: K60 (= K66), T84 (= T90), E216 (≠ Q244), S220 (= S248), A238 (= A266), T315 (= T343)
- binding (2E,3Z)-2-{[(Z)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4(1H)-ylidene}methyl]imino}-5-phosphonopent-3-enoic acid: K60 (= K66), S83 (= S89), T84 (= T90), N86 (= N92), T87 (= T93), F133 (= F139), N153 (= N159), S154 (= S160), R159 (= R165), V185 (= V191), G186 (= G192), N187 (= N193), A188 (= A194), G189 (= G195), N190 (= N196), A238 (= A266), I239 (= I267), E285 (= E313), T315 (= T343)
6cgqB Threonine synthase from bacillus subtilis atcc 6633 with plp and plp- ala (see paper)
52% identity, 97% coverage: 7:375/380 of query aligns to 1:345/345 of 6cgqB
- active site: K58 (= K66), T82 (= T90), E214 (≠ Q244), S218 (= S248), A236 (= A266), T313 (= T343)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-alanine: K58 (= K66), S81 (= S89), T82 (= T90), N84 (= N92), T85 (= T93), V183 (= V191), G184 (= G192), N185 (= N193), A186 (= A194), N188 (= N196), A236 (= A266), I237 (= I267), E283 (= E313), T313 (= T343)
- binding phosphate ion: K58 (= K66), T85 (= T93), N151 (= N159), S152 (= S160), R157 (= R165), N185 (= N193)
3aeyA Apo form of threonine synthase from thermus thermophilus hb8 (see paper)
54% identity, 95% coverage: 10:369/380 of query aligns to 4:341/350 of 3aeyA
- active site: K60 (= K66), T84 (= T90), P211 (= P238), G215 (= G242), Q217 (= Q244), A239 (= A266), T316 (= T343)
- binding sulfate ion: K60 (= K66), K60 (= K66), G85 (= G91), N86 (= N92), T87 (= T93), T87 (= T93), S154 (= S160), R159 (= R165), N187 (= N193), R228 (≠ A255), V230 (= V257), E231 (≠ D258), R232 (≠ D259), A239 (= A266)
1uimA Crystal structure of threonine synthase from thermus thermophilus hb8, orthorhombic crystal form (see paper)
54% identity, 95% coverage: 10:369/380 of query aligns to 5:342/350 of 1uimA
- active site: K61 (= K66), T85 (= T90), P212 (= P238), G216 (= G242), Q218 (= Q244), A240 (= A266), T317 (= T343)
- binding pyridoxal-5'-phosphate: F60 (= F65), K61 (= K66), N87 (= N92), G187 (= G192), N188 (= N193), A189 (= A194), G190 (= G195), N191 (= N196), A240 (= A266), E287 (= E313), T317 (= T343), G318 (= G344)
3aexA Catalytic intermediate analogue of threonine synthase from thermus thermophilus hb8 (see paper)
54% identity, 95% coverage: 10:369/380 of query aligns to 5:342/351 of 3aexA
- active site: K61 (= K66), T85 (= T90), P212 (= P238), G216 (= G242), Q218 (= Q244), A240 (= A266), T317 (= T343)
- binding (3E)-4-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}-2-oxobut-3-enoic acid: K61 (= K66), S84 (= S89), T85 (= T90), N87 (= N92), T88 (= T93), V186 (= V191), G187 (= G192), N188 (= N193), A189 (= A194), G190 (= G195), N191 (= N196), A240 (= A266), I241 (= I267), E287 (= E313), T317 (= T343)
- binding phosphate ion: K61 (= K66), T88 (= T93), N154 (= N159), S155 (= S160), R160 (= R165), N188 (= N193)
1v7cA Crystal structure of threonine synthase from thermus thermophilus hb8 in complex with a substrate analogue (see paper)
54% identity, 95% coverage: 10:369/380 of query aligns to 5:342/351 of 1v7cA
- active site: K61 (= K66), T85 (= T90), P212 (= P238), G216 (= G242), Q218 (= Q244), A240 (= A266), T317 (= T343)
- binding (2e)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-5-phosphonopent-2-enoic acid: K61 (= K66), S84 (= S89), T85 (= T90), N87 (= N92), T88 (= T93), F134 (= F139), N154 (= N159), S155 (= S160), R160 (= R165), V186 (= V191), G187 (= G192), N188 (= N193), A189 (= A194), G190 (= G195), N191 (= N196), A240 (= A266), I241 (= I267), E287 (= E313), T317 (= T343)
A0R220 Threonine synthase; TS; EC 4.2.3.1 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
56% identity, 96% coverage: 7:371/380 of query aligns to 12:353/360 of A0R220
- K151 (≠ E148) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
P9WG59 Threonine synthase; TS; EC 4.2.3.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
58% identity, 92% coverage: 7:354/380 of query aligns to 12:337/360 of P9WG59
- K69 (= K66) modified: N6-(pyridoxal phosphate)lysine
- N95 (= N92) binding pyridoxal 5'-phosphate
- K151 (≠ E148) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
- GNAGN 196:200 (= GNAGN 192:196) binding pyridoxal 5'-phosphate
- T326 (= T343) binding pyridoxal 5'-phosphate
2d1fA Structure of mycobacterium tuberculosis threonine synthase (see paper)
58% identity, 92% coverage: 7:354/380 of query aligns to 3:328/349 of 2d1fA
- active site: K60 (= K66), T84 (= T90), D209 (≠ G235), R213 (≠ H239), L215 (≠ V241), A240 (= A266), T317 (= T343)
- binding pyridoxal-5'-phosphate: F59 (= F65), K60 (= K66), N86 (= N92), V186 (= V191), G187 (= G192), N188 (= N193), A189 (= A194), G190 (= G195), N191 (= N196), A240 (= A266), T317 (= T343)
6cgqA Threonine synthase from bacillus subtilis atcc 6633 with plp and plp- ala (see paper)
51% identity, 97% coverage: 9:376/380 of query aligns to 1:338/339 of 6cgqA
- active site: K56 (= K66), T80 (= T90), E206 (≠ Q244), S210 (= S248), A228 (= A266), T305 (= T343)
- binding pyridoxal-5'-phosphate: F55 (= F65), K56 (= K66), N82 (= N92), V175 (= V191), G176 (= G192), N177 (= N193), A178 (= A194), G179 (= G195), N180 (= N196), A228 (= A266), E275 (= E313), T305 (= T343), G306 (= G344)
2c2bA Crystallographic structure of arabidopsis thaliana threonine synthase complexed with pyridoxal phosphate and s-adenosylmethionine (see paper)
34% identity, 91% coverage: 8:354/380 of query aligns to 70:408/444 of 2c2bA
- binding pyridoxal-5'-phosphate: F127 (= F65), K128 (= K66), D159 (≠ N92), G259 (≠ V191), G260 (= G192), N261 (= N193), L262 (≠ A194), G263 (= G195), N264 (= N196), A321 (= A266), H369 (≠ A315), T397 (= T343)
- binding s-adenosylmethionine: S90 (= S28), F92 (≠ G30), N97 (≠ P35), L98 (= L36), W100 (≠ R38), W115 (≠ Y53), W115 (≠ Y53), Q246 (≠ E179), F247 (≠ L180)
Sites not aligning to the query:
Q9S7B5 Threonine synthase 1, chloroplastic; Protein METHIONINE OVER-ACCUMULATOR 2; EC 4.2.3.1 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
34% identity, 89% coverage: 18:354/380 of query aligns to 155:483/526 of Q9S7B5
- N172 (≠ P35) binding S-adenosyl-L-methionine
- L173 (= L36) binding S-adenosyl-L-methionine
- K181 (≠ R44) binding in monomer B; binding in monomer A
- N187 (≠ V50) binding in monomer B
- L205 (≠ R68) 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)
32% identity, 91% coverage: 8:354/380 of query aligns to 88:410/448 of 2c2gA
3pc2A Full length structure of cystathionine beta-synthase from drosophila (see paper)
32% identity, 44% coverage: 32:198/380 of query aligns to 46:223/500 of 3pc2A
Sites not aligning to the query:
- active site: 310
- binding protoporphyrin ix containing fe: 12, 13, 14, 15, 16, 24, 25, 26, 227
- binding pyridoxal-5'-phosphate: 266, 310, 336, 337
3pc4A Full length structure of cystathionine beta-synthase from drosophila in complex with serine (see paper)
32% identity, 44% coverage: 32:198/380 of query aligns to 48:225/504 of 3pc4A
- active site: K82 (= K66)
- binding protoporphyrin ix containing fe: A189 (≠ Q167), P192 (≠ K170), L193 (≠ T171), Y196 (≠ F174)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: K82 (= K66), T109 (≠ S89), S110 (≠ T90), N112 (= N92), T113 (= T93), Q185 (≠ P163), A218 (≠ V191), G219 (= G192), T220 (≠ N193), A221 (= A194), T223 (≠ N196)
Sites not aligning to the query:
- active site: 312
- binding protoporphyrin ix containing fe: 14, 15, 16, 17, 18, 26, 27, 28, 229, 276
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: 268, 269, 271, 312, 338, 339
3pc3A Full length structure of cystathionine beta-synthase from drosophila in complex with aminoacrylate (see paper)
32% identity, 44% coverage: 32:198/380 of query aligns to 48:225/504 of 3pc3A
- active site: K82 (= K66)
- binding protoporphyrin ix containing fe: A189 (≠ Q167), P192 (≠ K170), L193 (≠ T171), Y196 (≠ F174)
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K82 (= K66), T109 (≠ S89), S110 (≠ T90), N112 (= N92), T113 (= T93), Q185 (≠ P163), A218 (≠ V191), G219 (= G192), T220 (≠ N193), A221 (= A194), T223 (≠ N196)
Sites not aligning to the query:
- active site: 312
- binding protoporphyrin ix containing fe: 14, 15, 16, 17, 18, 26, 27, 28, 229
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: 268, 269, 312, 338, 339
O59791 Serine racemase; D-serine ammonia-lyase; D-serine dehydratase; L-serine ammonia-lyase; L-serine dehydratase; EC 5.1.1.18; EC 4.3.1.18; EC 4.3.1.17 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
26% identity, 84% coverage: 18:338/380 of query aligns to 7:312/323 of O59791
- K57 (= K66) active site, Proton acceptor; modified: Lysino-D-alanine (Lys); alternate; modified: N6-(pyridoxal phosphate)lysine; alternate
- S82 (≠ T90) active site, Proton acceptor; mutation to A: Loss of racemase activity. Reduces D-serine dehydratase activity by 99%. Slightly reduced L-serine dehydratase activity.
- N84 (= N92) binding pyridoxal 5'-phosphate
- G183 (≠ H200) binding pyridoxal 5'-phosphate
- G184 (≠ W201) binding pyridoxal 5'-phosphate
- G185 (≠ I202) binding pyridoxal 5'-phosphate
- G186 (= G203) binding pyridoxal 5'-phosphate
- L187 (≠ Y204) binding pyridoxal 5'-phosphate
- E208 (≠ G231) binding Mg(2+)
- G212 (= G235) binding Mg(2+)
- D214 (≠ S246) binding Mg(2+)
- S308 (≠ A334) binding pyridoxal 5'-phosphate
1wtcA Crystal structure of s.Pombe serine racemase complex with amppcp (see paper)
26% identity, 84% coverage: 18:338/380 of query aligns to 2:307/318 of 1wtcA
- active site: K52 (= K66), S77 (≠ T90), E203 (≠ G231), G207 (= G235), D209 (≠ S246), G231 (≠ A266), I302 (≠ P333), S303 (≠ A334)
- binding phosphomethylphosphonic acid adenylate ester: N20 (≠ G32), K47 (≠ P61), M48 (≠ T62), A109 (= A123), A110 (≠ Q124), Y114 (≠ H128)
- binding magnesium ion: E203 (≠ G231), G207 (= G235), D209 (≠ S246)
- binding pyridoxal-5'-phosphate: F51 (= F65), K52 (= K66), N79 (= N92), G178 (≠ H200), G179 (≠ W201), G180 (≠ I202), G181 (= G203), G231 (≠ A266), E276 (= E313), T278 (≠ A315), S303 (≠ A334)
1v71A Crystal structure of s.Pombe serine racemase
26% identity, 84% coverage: 18:338/380 of query aligns to 2:307/318 of 1v71A
- active site: K52 (= K66), S77 (≠ T90), E203 (≠ G231), G207 (= G235), D209 (≠ S246), G231 (≠ A266), I302 (≠ P333), S303 (≠ A334)
- binding magnesium ion: E203 (≠ G231), G207 (= G235), D209 (≠ S246)
- binding pyridoxal-5'-phosphate: F51 (= F65), K52 (= K66), N79 (= N92), G178 (≠ H200), G179 (≠ W201), G180 (≠ I202), G181 (= G203), G231 (≠ A266), E276 (= E313), T278 (≠ A315), S303 (≠ A334), G304 (= G335)
Query Sequence
>WP_018869600.1 NCBI__GCF_001995255.1:WP_018869600.1
MAHGHRYTGLIDRYRDRLPVHDDTRVISLGEGATPLIRLNNIPRELDSEVEIYVKYEGLN
PTGSFKDRGMTMAVTRAVEEGSRAIVCASTGNTSAAAAAYAARAGITAFVVIPDGKIAMG
KLAQAMMHGATVIQIAGNFDDGMRLVKEVASNTPVTLVNSVNPYRLQGQKTAAFEIIEEL
GRAPDYHCLPVGNAGNITAHWIGYSEMAARSSEDVTDACAYCQGHCKYAGGGMVGNRPHM
VGYQASGSAPFMRGAMVDDPDTVATAIRIGHPQSWDMAWKVREESGGWFDECADDEILAA
QKLLAEKEGVFCEPASAASLAGALRDIRSGRIPAGSTVVCTLTGNGLKDPDTAISQSVVQ
PTRVPAELDAVSQAIRDNLA
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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