SitesBLAST
Comparing WP_012854251.1 NCBI__GCF_000024385.1:WP_012854251.1 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)
A0R220 Threonine synthase; TS; EC 4.2.3.1 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
67% identity, 100% coverage: 1:352/352 of query aligns to 8:360/360 of A0R220
- K151 (= K144) 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)
68% identity, 93% coverage: 2:329/352 of query aligns to 9:337/360 of P9WG59
- K69 (= K62) modified: N6-(pyridoxal phosphate)lysine
- N95 (= N88) binding
- K151 (= K144) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
- GNAGN 196:200 (= GNAGN 188:192) binding
- T326 (= T318) binding
2d1fA Structure of mycobacterium tuberculosis threonine synthase (see paper)
68% identity, 93% coverage: 3:329/352 of query aligns to 1:328/349 of 2d1fA
- active site: K60 (= K62), T84 (= T86), D209 (≠ T210), R213 (= R214), L215 (= L216), A240 (= A241), T317 (= T318)
- binding pyridoxal-5'-phosphate: F59 (= F61), K60 (= K62), N86 (= N88), V186 (= V187), G187 (= G188), N188 (= N189), A189 (= A190), G190 (= G191), N191 (= N192), A240 (= A241), T317 (= T318)
2zsjA Crystal structure of threonine synthase from aquifex aeolicus vf5
59% identity, 99% coverage: 5:351/352 of query aligns to 2:350/350 of 2zsjA
- active site: K61 (= K62), T85 (= T86), Q218 (= Q219), A222 (= A223), A240 (= A241), T317 (= T318)
- binding pyridoxal-5'-phosphate: F60 (= F61), K61 (= K62), N87 (= N88), V186 (= V187), G187 (= G188), N188 (= N189), A189 (= A190), G190 (= G191), N191 (= N192), A240 (= A241), T317 (= T318), G318 (= G319)
1uimA Crystal structure of threonine synthase from thermus thermophilus hb8, orthorhombic crystal form (see paper)
61% identity, 95% coverage: 8:341/352 of query aligns to 5:342/350 of 1uimA
- active site: K61 (= K62), T85 (= T86), P212 (= P213), G216 (= G217), Q218 (= Q219), A240 (= A241), T317 (= T318)
- binding pyridoxal-5'-phosphate: F60 (= F61), K61 (= K62), N87 (= N88), G187 (= G188), N188 (= N189), A189 (= A190), G190 (= G191), N191 (= N192), A240 (= A241), E287 (= E288), T317 (= T318), G318 (= G319)
3aeyA Apo form of threonine synthase from thermus thermophilus hb8 (see paper)
61% identity, 95% coverage: 8:341/352 of query aligns to 4:341/350 of 3aeyA
- active site: K60 (= K62), T84 (= T86), P211 (= P213), G215 (= G217), Q217 (= Q219), A239 (= A241), T316 (= T318)
- binding sulfate ion: K60 (= K62), K60 (= K62), G85 (= G87), N86 (= N88), T87 (= T89), T87 (= T89), S154 (= S156), R159 (= R161), N187 (= N189), R228 (≠ E230), V230 (= V232), E231 (≠ R233), R232 (≠ S234), A239 (= A241)
3aexA Catalytic intermediate analogue of threonine synthase from thermus thermophilus hb8 (see paper)
61% identity, 95% coverage: 8:341/352 of query aligns to 5:342/351 of 3aexA
- active site: K61 (= K62), T85 (= T86), P212 (= P213), G216 (= G217), Q218 (= Q219), A240 (= A241), T317 (= T318)
- binding (3E)-4-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}-2-oxobut-3-enoic acid: K61 (= K62), S84 (= S85), T85 (= T86), N87 (= N88), T88 (= T89), V186 (= V187), G187 (= G188), N188 (= N189), A189 (= A190), G190 (= G191), N191 (= N192), A240 (= A241), I241 (= I242), E287 (= E288), T317 (= T318)
- binding phosphate ion: K61 (= K62), T88 (= T89), N154 (= N155), S155 (= S156), R160 (= R161), N188 (= N189)
1v7cA Crystal structure of threonine synthase from thermus thermophilus hb8 in complex with a substrate analogue (see paper)
61% identity, 95% coverage: 8:341/352 of query aligns to 5:342/351 of 1v7cA
- active site: K61 (= K62), T85 (= T86), P212 (= P213), G216 (= G217), Q218 (= Q219), A240 (= A241), T317 (= T318)
- binding (2e)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-5-phosphonopent-2-enoic acid: K61 (= K62), S84 (= S85), T85 (= T86), N87 (= N88), T88 (= T89), F134 (= F135), N154 (= N155), S155 (= S156), R160 (= R161), V186 (= V187), G187 (= G188), N188 (= N189), A189 (= A190), G190 (= G191), N191 (= N192), A240 (= A241), I241 (= I242), E287 (= E288), T317 (= T318)
6nmxA Threonine synthase from bacillus subtilis atcc 6633 with plp and appa (see paper)
59% identity, 93% coverage: 4:329/352 of query aligns to 2:326/350 of 6nmxA
- active site: K60 (= K62), T84 (= T86), E216 (≠ Q219), S220 (≠ A223), A238 (= A241), T315 (= T318)
- binding (2E,3Z)-2-{[(Z)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4(1H)-ylidene}methyl]imino}-5-phosphonopent-3-enoic acid: K60 (= K62), S83 (= S85), T84 (= T86), N86 (= N88), T87 (= T89), F133 (= F135), N153 (= N155), S154 (= S156), R159 (= R161), V185 (= V187), G186 (= G188), N187 (= N189), A188 (= A190), G189 (= G191), N190 (= N192), A238 (= A241), I239 (= I242), E285 (= E288), T315 (= T318)
6cgqB Threonine synthase from bacillus subtilis atcc 6633 with plp and plp- ala (see paper)
59% identity, 92% coverage: 5:329/352 of query aligns to 1:324/345 of 6cgqB
- active site: K58 (= K62), T82 (= T86), E214 (≠ Q219), S218 (≠ A223), A236 (= A241), T313 (= T318)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-alanine: K58 (= K62), S81 (= S85), T82 (= T86), N84 (= N88), T85 (= T89), V183 (= V187), G184 (= G188), N185 (= N189), A186 (= A190), N188 (= N192), A236 (= A241), I237 (= I242), E283 (= E288), T313 (= T318)
- binding phosphate ion: K58 (= K62), T85 (= T89), N151 (= N155), S152 (= S156), R157 (= R161), N185 (= N189)
6cgqA Threonine synthase from bacillus subtilis atcc 6633 with plp and plp- ala (see paper)
57% identity, 92% coverage: 7:329/352 of query aligns to 1:316/339 of 6cgqA
- active site: K56 (= K62), T80 (= T86), E206 (≠ Q219), S210 (≠ A223), A228 (= A241), T305 (= T318)
- binding pyridoxal-5'-phosphate: F55 (= F61), K56 (= K62), N82 (= N88), V175 (= V187), G176 (= G188), N177 (= N189), A178 (= A190), G179 (= G191), N180 (= N192), A228 (= A241), E275 (= E288), T305 (= T318), G306 (= G319)
2c2bA Crystallographic structure of arabidopsis thaliana threonine synthase complexed with pyridoxal phosphate and s-adenosylmethionine (see paper)
34% identity, 95% coverage: 16:349/352 of query aligns to 80:440/444 of 2c2bA
- binding pyridoxal-5'-phosphate: F127 (= F61), K128 (= K62), D159 (≠ N88), G259 (≠ V187), G260 (= G188), N261 (= N189), L262 (≠ A190), G263 (= G191), N264 (= N192), A321 (= A241), H369 (≠ A290), T397 (= T318)
- binding s-adenosylmethionine: S90 (≠ T26), F92 (≠ L28), N97 (≠ P33), L98 (= L34), W100 (≠ P36), W115 (≠ Y49), W115 (≠ Y49), Q246 (≠ A175), F247 (≠ L176)
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, 95% coverage: 16:349/352 of query aligns to 155:515/526 of Q9S7B5
- N172 (≠ P33) binding
- L173 (= L34) binding
- K181 (≠ S41) binding in monomer B; binding in monomer A
- N187 (vs. gap) binding in monomer B
- L205 (≠ R64) 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, 95% coverage: 16:349/352 of query aligns to 98:442/448 of 2c2gA
Q8VBT2 L-serine dehydratase/L-threonine deaminase; SDH; L-serine deaminase; L-threonine dehydratase; TDH; EC 4.3.1.17; EC 4.3.1.19 from Mus musculus (Mouse)
25% identity, 85% coverage: 28:325/352 of query aligns to 7:294/327 of Q8VBT2
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
1pwhA Rat liver l-serine dehydratase- complex with pyridoxyl-(o-methyl- serine)-5-monophosphate (see paper)
25% identity, 77% coverage: 28:298/352 of query aligns to 7:277/327 of 1pwhA
- active site: K41 (= K62), A65 (≠ T86), E194 (≠ R214), A198 (≠ F218), S200 (≠ A220), A222 (≠ R243), A269 (= A290)
- binding n-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-o-methyl-l-serine: F40 (= F61), K41 (= K62), S64 (= S85), A65 (≠ T86), N67 (= N88), A68 (≠ T89), F136 (≠ S156), G168 (= G188), G169 (≠ N189), G170 (≠ A190), G171 (= G191), A222 (≠ R243), G224 (= G245)
Sites not aligning to the query:
P20132 L-serine dehydratase/L-threonine deaminase; SDH; L-serine deaminase; L-threonine dehydratase; TDH; EC 4.3.1.17; EC 4.3.1.19 from Homo sapiens (Human) (see paper)
27% identity, 79% coverage: 28:306/352 of query aligns to 7:285/328 of P20132
Sites not aligning to the query:
- 303 C→A: Loss of enzyme activity.
1p5jA Crystal structure analysis of human serine dehydratase (see paper)
27% identity, 79% coverage: 28:306/352 of query aligns to 4:282/319 of 1p5jA
- active site: K38 (= K62), A62 (≠ T86), E191 (≠ R214), A195 (≠ F218), S197 (≠ A220), A219 (≠ R243)
- binding pyridoxal-5'-phosphate: F37 (= F61), K38 (= K62), N64 (= N88), V164 (= V187), G165 (= G188), G166 (≠ N189), G167 (≠ A190), G168 (= G191), A219 (≠ R243)
Sites not aligning to the query:
A4F2N8 L-threo-3-hydroxyaspartate ammonia-lyase; L-threo-3-hydroxyaspartate dehydratase; L-THA DH; EC 4.3.1.16 from Pseudomonas sp. (see paper)
26% identity, 84% coverage: 32:328/352 of query aligns to 23:314/319 of A4F2N8
- K53 (= K62) mutation to A: Loss of enzymatic activity.
5c3uA Crystal structure of a fungal l-serine ammonia-lyase from rhizomucor miehei (see paper)
28% identity, 76% coverage: 28:296/352 of query aligns to 3:272/315 of 5c3uA
- active site: K37 (= K62), G63 (≠ T86), E191 (≠ K211), S195 (≠ M215), A197 (≠ G217), S219 (≠ A241)
- binding pyridoxal-5'-phosphate: K37 (= K62), N65 (= N88), S132 (= S156), P163 (= P186), G165 (= G188), G166 (≠ N189), G167 (≠ A190), G168 (= G191), S219 (≠ A241)
Sites not aligning to the query:
Query Sequence
>WP_012854251.1 NCBI__GCF_000024385.1:WP_012854251.1
MNRAWRGLIAEYRDRLPVTEATPVVTLLEGGTPLLPAQRISQLTGCEVYLKVEGANPTGS
FKDRGMTVAISKAAEEGAKAVICASTGNTSASAAAYAVRAGMTCAVLVPKGKIAMGKLAQ
ALVHGARLLQVDGNFDDCLELARKLAVDYPVALVNSVNKFRLQGQKTAAFEIVDALGDAP
DVHCLPVGNAGNISAYWMGYTEYAADKVATKTPRMLGFQASGAAPFVKGEPVRSPQTIAT
AIRIGNPASWDLAIAARDESGGAISAVTDRQILAAYRLLAREEGVFVEPASAASVAGVLQ
AREQGLIEAGERVVCTVTGNGLKDPDWAISGAPAPITVKVDAHAAASALGLT
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