SitesBLAST
Comparing WP_013840426.1 NCBI__GCF_000215085.1:WP_013840426.1 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)
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
49% identity, 98% coverage: 8:456/459 of query aligns to 1:450/451 of 1tj7B
2e9fB Crystal structure of t.Th.Hb8 argininosuccinate lyase complexed with l-arginine
50% identity, 96% coverage: 14:453/459 of query aligns to 3:444/450 of 2e9fB
- active site: E71 (= E82), T146 (= T155), H147 (= H156), S268 (= S277), S269 (= S278), K274 (= K283), E281 (= E290)
- binding arginine: R98 (= R109), N99 (= N110), V102 (= V113), Y308 (= Y317), Q313 (= Q322), K316 (= K325)
P24058 Argininosuccinate lyase; ASAL; Arginosuccinase; Delta crystallin II; Delta-2 crystallin; EC 4.3.2.1 from Anas platyrhynchos (Mallard) (Anas boschas) (see 4 papers)
44% identity, 100% coverage: 3:459/459 of query aligns to 9:460/468 of P24058
- W11 (= W5) mutation to A: 98% decrease in catalytic efficiency.; mutation to F: 90% decrease in catalytic efficiency.; mutation to M: 99% decrease in catalytic efficiency.; mutation to R: 97% decrease in catalytic efficiency.; mutation to Y: 50% decrease in catalytic efficiency.
- S29 (= S23) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
- D33 (= D27) mutation to N: 99% decrease in catalytic efficiency.
- D89 (= D83) mutation to N: Loss of activity.
- N116 (= N110) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (= D111) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T155) binding in chain C; mutation to A: Loss of activity.; mutation to D: Loss of activity.; mutation to S: 30% decrease in catalytic efficiency.; mutation to V: Loss of activity.
- H162 (= H156) mutation to E: Loss of activity.
- R238 (= R232) mutation to Q: Loss of activity.
- T281 (= T275) mutation to V: 80% decrease in catalytic efficiency.
- S283 (= S277) mutation to A: Loss of activity.; mutation to C: Loss of activity.; mutation to D: Loss of activity.; mutation to H: Loss of activity.; mutation to T: Loss of activity.
- N291 (= N285) binding in chain B; mutation to L: Loss of activity.
- D293 (= D287) mutation to N: 99% decrease in catalytic efficiency.
- E296 (= E290) mutation to D: Loss of activity.
- Y323 (= Y317) binding in chain A
- K325 (= K319) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (= Q322) binding in chain A
- D330 (= D324) mutation to N: Loss of activity.
- K331 (= K325) binding in chain A; mutation to Q: Loss of activity.
P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
45% identity, 99% coverage: 3:457/459 of query aligns to 7:460/464 of P04424
- R12 (= R8) to Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
- D31 (= D27) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
- K51 (≠ R47) mutation to N: 2-fold reduction in activity.
- K69 (≠ E65) modified: N6-acetyllysine
- E73 (= E69) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
- D87 (= D83) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
- H89 (= H85) mutation to Q: 10-fold reduction in activity.
- R94 (≠ Q90) to C: in ARGINSA; severe; dbSNP:rs374304304
- R95 (≠ L91) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
- R113 (= R109) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (= D116) to E: in ARGINSA; severe
- V178 (≠ Q174) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ L177) to S: in a breast cancer sample; somatic mutation
- R182 (= R178) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (= R182) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (= G196) to V: in a breast cancer sample; somatic mutation
- R236 (= R232) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (= D233) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (= Q282) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (= K284) modified: N6-acetyllysine; mutation to R: Refractory to inhibition by TSA and NAM and by addition of extra amino acids. No effect on protein structure.
- R297 (= R293) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
- R306 (≠ D302) to W: in ARGINSA; severe; dbSNP:rs868834862
- Q326 (= Q322) to L: in ARGINSA; severe
- V335 (≠ A331) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- M360 (= M356) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- M382 (≠ V379) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- R385 (= R382) to L: in ARGINSA; severe
- H388 (= H385) to Q: in ARGINSA; severe
- A398 (≠ C395) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
- R456 (≠ K453) to W: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs759396688
1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
44% identity, 98% coverage: 12:459/459 of query aligns to 1:443/450 of 1k7wD
- active site: E71 (= E82), T144 (= T155), H145 (= H156), A266 (≠ S277), S267 (= S278), K272 (= K283), E279 (= E290)
- binding argininosuccinate: R98 (= R109), N99 (= N110), V102 (= V113), T144 (= T155), H145 (= H156), Y306 (= Y317), Q311 (= Q322), K314 (= K325)
1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
42% identity, 97% coverage: 14:459/459 of query aligns to 1:441/447 of 1hy0A
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
42% identity, 100% coverage: 3:459/459 of query aligns to 7:458/466 of P02521
Sites not aligning to the query:
- 2 modified: Blocked amino end (Ala)
6ienB Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
43% identity, 95% coverage: 20:457/459 of query aligns to 8:449/454 of 6ienB
- binding argininosuccinate: S97 (= S108), R98 (= R109), N99 (= N110), T144 (= T155), H145 (= H156), S266 (= S277), S267 (= S278), M269 (= M280), K272 (= K283), Y306 (= Y317), Q311 (= Q322), K314 (= K325)
6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
43% identity, 95% coverage: 20:457/459 of query aligns to 8:447/452 of 6ienA
- binding argininosuccinate: R98 (= R109), N99 (= N110), V102 (= V113), T144 (= T155), H145 (= H156), Y304 (= Y317), Q309 (= Q322), K312 (= K325)
- binding fumaric acid: S266 (= S277), S267 (= S278), K270 (= K283), N272 (= N285)
6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
41% identity, 95% coverage: 20:457/459 of query aligns to 8:413/418 of 6ienC
- binding arginine: R98 (= R109), N99 (= N110), V102 (= V113), Y306 (= Y317), Q311 (= Q322), K314 (= K325)
- binding argininosuccinate: T144 (= T155), H145 (= H156), S266 (= S277), S267 (= S278), M269 (= M280), K272 (= K283)
- binding fumaric acid: S97 (= S108), R98 (= R109), N99 (= N110)
6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
32% identity, 96% coverage: 19:458/459 of query aligns to 23:463/496 of 6g3iA
Sites not aligning to the query:
6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
32% identity, 96% coverage: 19:458/459 of query aligns to 23:463/497 of 6g3hA
Sites not aligning to the query:
6g3gA Crystal structure of edds lyase in complex with succinate (see paper)
32% identity, 96% coverage: 19:458/459 of query aligns to 23:463/497 of 6g3gA
6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
32% identity, 96% coverage: 19:458/459 of query aligns to 23:463/497 of 6g3fA
3r6qA A triclinic-lattice structure of aspartase from bacillus sp. Ym55-1 (see paper)
29% identity, 39% coverage: 128:308/459 of query aligns to 149:345/462 of 3r6qA
Sites not aligning to the query:
3r6vG Crystal structure of aspartase from bacillus sp. Ym55-1 with bound l- aspartate (see paper)
29% identity, 39% coverage: 128:308/459 of query aligns to 150:346/463 of 3r6vG
Q9LCC6 Aspartate ammonia-lyase; Aspartase; EC 4.3.1.1 from Bacillus sp. (see 3 papers)
29% identity, 39% coverage: 128:308/459 of query aligns to 153:349/468 of Q9LCC6
- K183 (≠ M151) mutation to A: Loss of activity. Does not affect tertiary structure.
- T187 (= T155) binding L-aspartate; mutation to A: 6280-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation to S: 2.3-fold decrease in catalytic efficiency.
- H188 (= H156) binding L-aspartate; mutation to A: 100-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation H->K,Q,R: Loss of activity.
- S318 (= S277) mutation to A: Loss of activity.
- S319 (= S278) binding L-aspartate; mutation to A: Almost no change in catalytic efficiency.
- I320 (= I279) mutation to A: 50-fold decrease in catalytic efficiency.
- M321 (= M280) mutation to A: 338-fold decrease in catalytic efficiency.
- P322 (= P281) mutation to A: Almost no change in catalytic efficiency.
- K324 (= K283) binding L-aspartate; mutation to A: Loss of activity. Does not result in any major conformational changes.; mutation K->D,H,R,S,V: Loss of activity.
- N326 (= N285) mutation to A: 22500-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation to Q: 168750-fold decrease in catalytic efficiency.
Sites not aligning to the query:
- 101 binding L-aspartate; T→A: 7100-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; T→S: 80-fold decrease in catalytic efficiency.
- 134 H→A: Retains full activity. Shows a slightly stronger affinity for L-aspartate. Does not affect tertiary structure.
- 140 binding L-aspartate; S→A: 27-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation S->K,R: Loss of activity.
- 141 binding L-aspartate; T→A: 15-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; T→K: 40000-fold decrease in catalytic efficiency.; mutation T->V,R: Loss of activity.
- 142 binding L-aspartate; N→A: Loss of activity. Does not result in any major conformational changes.; N→Q: 3000-fold decrease in catalytic efficiency.
P12047 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; Glutamyl--tRNA ligase regulatory factor; EC 4.3.2.2 from Bacillus subtilis (strain 168) (see paper)
25% identity, 73% coverage: 22:356/459 of query aligns to 11:341/431 of P12047
- H89 (= H104) mutation to Q: Abolishes enzyme activity.
- H141 (= H156) mutation to Q: Abolishes enzyme activity.
- Q212 (≠ N224) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N285) mutation N->D,L: Abolishes enzyme activity.
- R301 (≠ K319) mutation R->K,Q: Abolishes enzyme activity.
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
24% identity, 73% coverage: 22:356/459 of query aligns to 10:340/427 of 2x75A
Sites not aligning to the query:
4adlA Crystal structures of rv1098c in complex with malate (see paper)
25% identity, 47% coverage: 85:302/459 of query aligns to 101:335/459 of 4adlA
Sites not aligning to the query:
Query Sequence
>WP_013840426.1 NCBI__GCF_000215085.1:WP_013840426.1
MTKLWGGRFQKTTDHLVEDFHSSISFDQRLYKQDIQGSIAHATMLGRVGVISPEEAGQIV
EGLREILKEIEEGNVEFDVAAEDIHMNVEQLLTAKIGAVGKKLHTARSRNDQVAVDIRMY
LKDEIKEIRSQLRELVETLLNLAEQHLSTVMPGYTHMQRAQPITLSHHLMAYVQMFLRDM
DRLADCYRRTDVMPLGSGALAGTTFPLDREYTAELLGFAAVSDNSLDAVSDRDFAVEFCA
ASSLIMMHLSRFCEEIILWATGEFAFIELDDAYSTGSSIMPQKKNPDVAELIRGKTGRVY
GDLLGLLTMLKGLPMAYNKDMQEDKEALFDAIDTVKGCLLVFRPMVATMTVRKENMAGAA
RGGFTNATDVADYLAKKGVPFREAHEVVGKAVFYCLQHQKNLEALTLEEYQALSPAFAED
IYAAIGVEYCAAARKVRGGPAPEAVQQAIGVAKARLREI
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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