SitesBLAST
Comparing WP_018231340.1 NCBI__GCF_000378965.1:WP_018231340.1 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
54% identity, 98% coverage: 6:375/379 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)
53% identity, 97% coverage: 7:374/379 of query aligns to 3:350/350 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)
1uimA Crystal structure of threonine synthase from thermus thermophilus hb8, orthorhombic crystal form (see paper)
54% identity, 91% coverage: 10:353/379 of query aligns to 5:327/350 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)
3aeyA Apo form of threonine synthase from thermus thermophilus hb8 (see paper)
54% identity, 91% coverage: 10:353/379 of query aligns to 4:326/350 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 (≠ E255), V230 (= V257), E231 (≠ D258), R232 (≠ N259), A239 (= A266)
3aexA Catalytic intermediate analogue of threonine synthase from thermus thermophilus hb8 (see paper)
54% identity, 91% coverage: 10:353/379 of query aligns to 5:327/351 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, 91% coverage: 10:353/379 of query aligns to 5:327/351 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)
6cgqB Threonine synthase from bacillus subtilis atcc 6633 with plp and plp- ala (see paper)
55% identity, 92% coverage: 7:354/379 of query aligns to 1:324/345 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)
A0R220 Threonine synthase; TS; EC 4.2.3.1 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
55% identity, 92% coverage: 7:354/379 of query aligns to 12:337/360 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)
56% identity, 92% coverage: 7:354/379 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)
56% identity, 92% coverage: 7:354/379 of query aligns to 3:328/349 of 2d1fA
- active site: K60 (= K66), T84 (= T90), D209 (≠ G235), R213 (≠ K239), 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)
52% identity, 96% coverage: 9:372/379 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)
33% identity, 92% coverage: 8:354/379 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, 87% coverage: 18:348/379 of query aligns to 155:477/526 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, 89% coverage: 18:354/379 of query aligns to 98:410/448 of 2c2gA
3pc4A Full length structure of cystathionine beta-synthase from drosophila in complex with serine (see paper)
31% identity, 44% coverage: 32:198/379 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)
31% identity, 44% coverage: 32:198/379 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
3pc2A Full length structure of cystathionine beta-synthase from drosophila (see paper)
31% identity, 44% coverage: 32:198/379 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
Q9GZT4 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 Homo sapiens (Human) (see 4 papers)
24% identity, 86% coverage: 34:360/379 of query aligns to 26:332/340 of Q9GZT4
- S31 (≠ L39) binding ATP
- S32 (≠ N40) binding ATP
- I33 (≠ N41) binding ATP
- K51 (≠ P61) binding ATP
- T52 (= T62) binding ATP
- K56 (= K66) modified: N6-(pyridoxal phosphate)lysine
- P69 (vs. gap) binding Ca(2+)
- T81 (≠ C87) binding Ca(2+)
- N86 (= N92) binding pyridoxal 5'-phosphate
- Q89 (≠ A95) binding ATP
- Y121 (≠ H128) binding ATP
- D178 (= D185) binding Mg(2+)
- G185 (= G192) binding pyridoxal 5'-phosphate
- G186 (≠ N193) binding pyridoxal 5'-phosphate
- G187 (≠ A194) binding pyridoxal 5'-phosphate
- G188 (= G195) binding pyridoxal 5'-phosphate
- M189 (≠ N196) binding pyridoxal 5'-phosphate
- E210 (= E217) binding Ca(2+); binding Mg(2+); binding Mn(2+)
- A214 (≠ K223) binding Ca(2+); binding Mg(2+); binding Mn(2+)
- D216 (≠ H225) binding Ca(2+); binding Mg(2+); binding Mn(2+)
- N247 (≠ S277) binding Ca(2+); binding Mg(2+)
- K279 (≠ G309) binding ATP
- S313 (≠ T343) binding pyridoxal 5'-phosphate
- N316 (≠ G346) binding ATP
Sites not aligning to the query:
Q2V0C9 Cystathionine beta-synthase; EC 4.2.1.22 from Apis mellifera (Honeybee) (see paper)
36% identity, 27% coverage: 32:134/379 of query aligns to 44:149/504 of Q2V0C9
- K78 (= K66) modified: N6-(pyridoxal phosphate)lysine
- N108 (= N92) binding pyridoxal 5'-phosphate
Sites not aligning to the query:
- 12 binding axial binding residue
- 23 binding axial binding residue
- 215:219 binding pyridoxal 5'-phosphate
- 307 binding pyridoxal 5'-phosphate
5ohxA Structure of active cystathionine b-synthase from apis mellifera (see paper)
36% identity, 27% coverage: 32:134/379 of query aligns to 40:145/488 of 5ohxA
Sites not aligning to the query:
- binding protoporphyrin ix containing fe: 4, 7, 8, 9, 10, 14, 16, 17, 18, 19, 181, 184, 188, 221
- binding pyridoxal-5'-phosphate: 209, 211, 212, 213, 214, 215, 256, 300, 326, 327
Query Sequence
>WP_018231340.1 NCBI__GCF_000378965.1:WP_018231340.1
MPFRTRYTGLIDRYRDRLPVHDDTRIISLGEGNTPLIRLNNIPRIVGREVDIYVKYEGLN
PTGSFKDRGMTMAVTKAVEEGSKAIICASTGNTSAAAAAYAARAGIAAFVIIPDGKIAMG
KLAQAMMHGSVVIQIKGNFDDGMRLVKEVASEAPVTIVNSINPYRLQGQKTAAFEITEEL
GRAPDYHCLPVGNAGNITAHWIGYCEYSSASGDHVTEACTFCKGHCAYAGGAIVGNRPKM
VGYQAAGSAPFMRGEMVDNPDTVATAIRIGHPQSWDSAWKVKEESGGWFDECTDAEILAA
QKLLAEKEGVFCEPASAASLAGALRDVQNDRIPEGSSIVCTLTGHGLKDPDTAIAQSTRP
LINVEATLDQVKRAILDNM
Or try a new SitesBLAST search
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