SitesBLAST
Comparing WP_012568920.1 NCBI__GCF_000016185.1:WP_012568920.1 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)
4iqdA Crystal structure of carboxyvinyl-carboxyphosphonate phosphorylmutase from bacillus anthracis
57% identity, 94% coverage: 16:296/300 of query aligns to 11:290/290 of 4iqdA
- active site: Y46 (= Y51), S48 (= S53), G49 (= G54), A50 (= A55), D60 (= D65), D87 (= D92), D89 (= D94), Q114 (≠ H119), E116 (= E121), K122 (= K127), C124 (= C129), G125 (= G130), H126 (= H131), R157 (= R162), E187 (= E192), N209 (= N215)
- binding pyruvic acid: E71 (≠ F76), R72 (≠ F77), D75 (≠ Q80), G165 (= G170), L166 (= L171), Y218 (≠ V224), Y219 (≠ F225)
Q56062 2-methylisocitrate lyase; 2-MIC; MICL; (2R,3S)-2-methylisocitrate lyase; EC 4.1.3.30 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
46% identity, 93% coverage: 14:292/300 of query aligns to 6:288/295 of Q56062
- SGG 45:47 (≠ SGA 53:55) binding substrate
- D58 (= D65) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- D85 (= D92) binding Mg(2+)
- K121 (= K127) mutation to A: 1000-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R122 (≠ K128) mutation to K: 2-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- C123 (= C129) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- H125 (= H131) mutation to A: 750-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R158 (= R162) binding substrate
P77541 2-methylisocitrate lyase; 2-MIC; MICL; (2R,3S)-2-methylisocitrate lyase; EC 4.1.3.30 from Escherichia coli (strain K12) (see 3 papers)
44% identity, 95% coverage: 14:297/300 of query aligns to 6:293/296 of P77541
- SGG 45:47 (≠ SGA 53:55) binding substrate
- D85 (= D92) binding Mg(2+)
- D87 (= D94) binding Mg(2+)
- C123 (= C129) mutation to S: Inactive.
- CG 123:124 (= CG 129:130) binding substrate
- R158 (= R162) binding substrate
- E188 (= E192) binding substrate
- NIT 210:212 (≠ NMT 215:217) binding substrate
- R241 (= R246) binding substrate
- R270 (= R275) binding substrate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1mumA Structure of the 2-methylisocitrate lyase (prpb) from escherichia coli (see paper)
44% identity, 92% coverage: 14:288/300 of query aligns to 4:281/289 of 1mumA
- active site: Y41 (= Y51), S43 (= S53), G44 (= G54), G45 (≠ A55), D56 (= D65), D83 (= D92), D85 (= D94), H111 (= H119), E113 (= E121), K119 (= K127), C121 (= C129), G122 (= G130), H123 (= H131), R156 (= R162), E186 (= E192), N208 (= N215), T215 (= T222), L217 (≠ V224)
- binding magnesium ion: D56 (= D65), D85 (= D94)
1o5qA Crystal structure of pyruvate and mg2+ bound 2-methylisocitrate lyase (prpb) from salmonella typhimurium (see paper)
44% identity, 92% coverage: 14:288/300 of query aligns to 2:268/271 of 1o5qA
- active site: Y39 (= Y51), S41 (= S53), G42 (= G54), G43 (≠ A55), D54 (= D65), D81 (= D92), D83 (= D94), H109 (= H119), E111 (= E121), R143 (= R162), E173 (= E192), N195 (= N215), T202 (= T222), L204 (≠ V224)
- binding pyruvic acid: Y39 (= Y51), S41 (= S53), G43 (≠ A55), D81 (= D92), R143 (= R162)
6t4vC Crystal structure of 2-methylisocitrate lyase (prpb) from pseudomonas aeruginosa in apo form.
44% identity, 93% coverage: 14:292/300 of query aligns to 4:275/277 of 6t4vC
- active site: Y41 (= Y51), S43 (= S53), G44 (= G54), G45 (≠ A55), D56 (= D65), D83 (= D92), D85 (= D94), H111 (= H119), E113 (= E121), R145 (= R162), E175 (= E192), N197 (= N215), T204 (= T222), L206 (≠ V224)
- binding pyruvic acid: F88 (≠ Y97), N94 (= N102)
3fa3B Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
39% identity, 82% coverage: 19:263/300 of query aligns to 11:261/302 of 3fa3B
- active site: Y43 (= Y51), T45 (≠ S53), G46 (= G54), A47 (= A55), D58 (= D65), D86 (= D92), D88 (= D94), H113 (= H119), E115 (= E121), K121 (= K127), C123 (= C129), G124 (= G130), H125 (= H131), R160 (= R162), E190 (= E192), N213 (= N215), T220 (= T222), S222 (≠ V224)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y43 (= Y51), T45 (≠ S53), G46 (= G54), A47 (= A55), D86 (= D92), G124 (= G130), R160 (= R162), E190 (= E192), N213 (= N215), P239 (= P241)
Q05957 Petal death protein; (R)-2-methylmalate lyase; D-citramalate lyase; Oxalacetic hydrolase; PSR132; EC 3.7.1.1; EC 4.1.3.- from Dianthus caryophyllus (Carnation) (Clove pink) (see 2 papers)
39% identity, 91% coverage: 21:294/300 of query aligns to 34:310/318 of Q05957
- D79 (= D65) mutation to A: Reduces catalytic efficiency 1000-fold.
- D107 (= D92) binding Mg(2+)
- D109 (= D94) binding Mg(2+)
- K142 (= K127) binding Mg(2+)
- C144 (= C129) mutation to A: Loss of catalytic activity.
Sites not aligning to the query:
- 1:3 modified: propeptide, Removed in mature form
1zlpA Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
39% identity, 91% coverage: 21:294/300 of query aligns to 7:283/284 of 1zlpA
- active site: F37 (≠ Y51), S39 (= S53), G40 (= G54), Y41 (≠ A55), D52 (= D65), D80 (= D92), D82 (= D94), F107 (≠ H119), E109 (= E121), K115 (= K127), C117 (= C129), G118 (= G130), H119 (= H131), R152 (= R162), E182 (= E192), N204 (= N215), T211 (= T222), L213 (≠ V224)
- binding 5-hydroxypentanal: C117 (= C129), G118 (= G130), R152 (= R162), I206 (≠ T217)
- binding magnesium ion: D80 (= D92), K115 (= K127)
1zlpB Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
39% identity, 91% coverage: 21:294/300 of query aligns to 7:283/285 of 1zlpB
- active site: F37 (≠ Y51), S39 (= S53), G40 (= G54), Y41 (≠ A55), D52 (= D65), D80 (= D92), D82 (= D94), F107 (≠ H119), E109 (= E121), K115 (= K127), C117 (= C129), G118 (= G130), H119 (= H131), R152 (= R162), E182 (= E192), N204 (= N215), T211 (= T222), L213 (≠ V224)
- binding 5-hydroxypentanal: Y41 (≠ A55), C117 (= C129), R152 (= R162), I206 (≠ T217)
3fa4A Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, triclinic crystal form (see paper)
37% identity, 82% coverage: 19:263/300 of query aligns to 11:254/284 of 3fa4A
- active site: Y43 (= Y51), T45 (≠ S53), G46 (= G54), A47 (= A55), D58 (= D65), D86 (= D92), D88 (= D94), H113 (= H119), E115 (= E121), R153 (= R162), E183 (= E192), N206 (= N215), T213 (= T222), S215 (≠ V224)
- binding magnesium ion: D86 (= D92), D88 (= D94)
3fa3J Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
37% identity, 82% coverage: 19:263/300 of query aligns to 10:252/292 of 3fa3J
- active site: Y42 (= Y51), T44 (≠ S53), G45 (= G54), A46 (= A55), D57 (= D65), D85 (= D92), D87 (= D94), H112 (= H119), E114 (= E121), R151 (= R162), E181 (= E192), N204 (= N215), T211 (= T222), S213 (≠ V224)
- binding manganese (ii) ion: D85 (= D92), D87 (= D94)
3m0jA Structure of oxaloacetate acetylhydrolase in complex with the inhibitor 3,3-difluorooxalacetate (see paper)
34% identity, 95% coverage: 11:295/300 of query aligns to 3:293/297 of 3m0jA
- binding calcium ion: E218 (= E218), N219 (≠ F219)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y44 (= Y51), T46 (≠ S53), G47 (= G54), A48 (= A55), D88 (= D92), G126 (= G130), R162 (= R162), E192 (= E192), N215 (= N215), S241 (≠ P241)
3m0kA Structure of oxaloacetate acetylhydrolase in complex with the product oxalate (see paper)
33% identity, 95% coverage: 11:295/300 of query aligns to 3:288/289 of 3m0kA
5uncA The crystal structure of phosphoenolpyruvate phosphomutase from streptomyces platensis subsp. Rosaceus
36% identity, 84% coverage: 17:268/300 of query aligns to 5:259/289 of 5uncA
- active site: W39 (≠ Y51), S41 (= S53), G42 (= G54), L43 (≠ A55), D53 (= D65), D80 (= D92), D82 (= D94), T107 (≠ H119), E109 (= E121), K115 (= K127), N117 (≠ C129), S118 (≠ G130), R153 (= R162), H184 (≠ E192), V209 (≠ N215)
- binding alpha-D-xylopyranose: H22 (= H34), N23 (= N35), G26 (≠ A38), L29 (≠ Q41), G239 (≠ A248), V243 (≠ Q252)
P56839 Phosphoenolpyruvate phosphomutase; PEP mutase; PEP phosphomutase; Phosphoenolpyruvate mutase; EC 5.4.2.9 from Mytilus edulis (Blue mussel) (see 2 papers)
33% identity, 77% coverage: 17:248/300 of query aligns to 10:245/295 of P56839
- D58 (= D65) mutation D->A,S: Abolishes enzyme activity.; mutation to N: Strongly reduces enzyme activity.
- D85 (= D92) mutation to A: Strongly reduces enzyme activity and increases KM.
- D87 (= D94) mutation to A: Strongly reduces enzyme activity.
- E114 (= E121) mutation to A: Strongly reduces enzyme activity.
- N122 (≠ G130) mutation N->A,D: Strongly reduces enzyme activity.
- R159 (= R162) mutation to A: Strongly reduces enzyme activity.
- H190 (≠ E192) mutation to A: Strongly reduces enzyme activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1pymA Phosphoenolpyruvate mutase from mollusk in with bound mg2-oxalate (see paper)
33% identity, 77% coverage: 17:248/300 of query aligns to 6:241/291 of 1pymA
- active site: W40 (≠ Y51), S42 (= S53), G43 (= G54), L44 (≠ A55), D54 (= D65), D81 (= D92), D83 (= D94), C108 (≠ H119), E110 (= E121), K116 (= K128), N118 (≠ G130), S119 (≠ H131), R155 (= R162), H186 (≠ E192), V211 (≠ N215)
- binding oxalate ion: W40 (≠ Y51), S42 (= S53), G43 (= G54), L44 (≠ A55), D81 (= D92), R155 (= R162)
1m1bA Crystal structure of phosphoenolpyruvate mutase complexed with sulfopyruvate (see paper)
33% identity, 77% coverage: 17:248/300 of query aligns to 6:241/291 of 1m1bA
- active site: W40 (≠ Y51), S42 (= S53), G43 (= G54), L44 (≠ A55), D54 (= D65), D81 (= D92), D83 (= D94), C108 (≠ H119), E110 (= E121), K116 (= K128), N118 (≠ G130), S119 (≠ H131), R155 (= R162), H186 (≠ E192), V211 (≠ N215)
- binding magnesium ion: D81 (= D92), R155 (= R162)
- binding sulfopyruvate: S42 (= S53), G43 (= G54), L44 (≠ A55), D81 (= D92), N118 (≠ G130), S119 (≠ H131), L120 (= L132), R155 (= R162)
Q84G06 Phosphonopyruvate hydrolase; PPH; EC 3.11.1.3 from Variovorax sp. (strain Pal2) (see paper)
33% identity, 82% coverage: 33:278/300 of query aligns to 22:275/290 of Q84G06
- D81 (= D92) binding Mg(2+)
- R188 (vs. gap) mutation to A: Reduced affinity for substrate.
2hjpA Crystal structure of phosphonopyruvate hydrolase complex with phosphonopyruvate and mg++ (see paper)
33% identity, 82% coverage: 33:278/300 of query aligns to 22:268/283 of 2hjpA
- active site: W40 (≠ Y51), S42 (= S53), G43 (= G54), F44 (≠ A55), D54 (= D65), D81 (= D92), D83 (= D94), V108 (≠ H119), E110 (= E121), K116 (= K127), T118 (≠ D134), R148 (= R162), H179 (≠ E192), V204 (≠ N215)
- binding phosphonopyruvate: W40 (≠ Y51), S42 (= S53), F44 (≠ A55), D81 (= D92), R148 (= R162), H179 (≠ E192), R181 (vs. gap)
- binding alpha-D-xylopyranose: E32 (≠ M43), S75 (≠ G86)
Query Sequence
>WP_012568920.1 NCBI__GCF_000016185.1:WP_012568920.1
MPYLIATDLPPTPPGDRFRALLARPGILRLPGAHNGMAALQAMAAGFDGLYLSGAAMTAS
MGLPDLGLITLEEVAFFIRQVARASGLPVLVDGDTGYGEVLNVMRMVRVFEEAGAAAVHL
EDQVLPKKCGHLNDKRLVPPAEMAAKVAAAAKARRHLYLIARTDAAASEGLEGAVARAKL
YLEAGADAIFPEALTSAEMFREFARRMPGVPLLANMTEFGRTPVFTAGEFEAMGYRMVIW
PVSSLRVANKAQERLYATLARTGSTEAMLPDMQTRAELYATIAYHDYEALDASIGRTVLP
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