SitesBLAST
Comparing WP_092998813.1 NCBI__GCF_900102855.1:WP_092998813.1 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)
2e9fB Crystal structure of t.Th.Hb8 argininosuccinate lyase complexed with l-arginine
51% identity, 95% coverage: 20:460/463 of query aligns to 3:444/450 of 2e9fB
- active site: E71 (= E88), T146 (= T162), H147 (= H163), S268 (= S284), S269 (= S285), K274 (= K290), E281 (= E297)
- binding arginine: R98 (= R115), N99 (= N116), V102 (= V119), Y308 (= Y324), Q313 (= Q329), K316 (= K332)
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
49% identity, 97% coverage: 14:463/463 of query aligns to 1:450/451 of 1tj7B
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)
46% identity, 100% coverage: 1:463/463 of query aligns to 1:461/468 of P24058
- W11 (= W11) 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 (= S29) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
- D33 (= D33) mutation to N: 99% decrease in catalytic efficiency.
- D89 (= D89) mutation to N: Loss of activity.
- N116 (= N116) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (= D117) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T162) 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 (= H163) mutation to E: Loss of activity.
- R238 (= R239) mutation to Q: Loss of activity.
- T281 (= T282) mutation to V: 80% decrease in catalytic efficiency.
- S283 (= S284) 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 (= N292) binding in chain B; mutation to L: Loss of activity.
- D293 (= D294) mutation to N: 99% decrease in catalytic efficiency.
- E296 (= E297) mutation to D: Loss of activity.
- Y323 (= Y324) binding in chain A
- K325 (= K326) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (= Q329) binding in chain A
- D330 (= D331) mutation to N: Loss of activity.
- K331 (= K332) binding in chain A; mutation to Q: Loss of activity.
1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
46% identity, 96% coverage: 19:463/463 of query aligns to 2:444/450 of 1k7wD
- active site: E71 (= E88), T144 (= T162), H145 (= H163), A266 (≠ S284), S267 (= S285), K272 (= K290), E279 (= E297)
- binding argininosuccinate: R98 (= R115), N99 (= N116), V102 (= V119), T144 (= T162), H145 (= H163), Y306 (= Y324), Q311 (= Q329), K314 (= K332)
P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
46% identity, 98% coverage: 9:463/463 of query aligns to 7:459/464 of P04424
- R12 (= R14) to Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
- D31 (= D33) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
- K51 (≠ H53) mutation to N: 2-fold reduction in activity.
- K69 (= K71) modified: N6-acetyllysine
- E73 (= E75) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
- D87 (= D89) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
- H89 (= H91) mutation to Q: 10-fold reduction in activity.
- R94 (≠ K96) to C: in ARGINSA; severe; dbSNP:rs374304304
- R95 (= R97) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
- R113 (= R115) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (= D122) to E: in ARGINSA; severe
- V178 (≠ E181) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ Q184) to S: in a breast cancer sample; somatic mutation
- R182 (= R185) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (= R189) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (= G203) to V: in a breast cancer sample; somatic mutation
- R236 (= R239) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (= D240) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (= Q289) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (= K291) 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 (= R300) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
- R306 (≠ H309) to W: in ARGINSA; severe; dbSNP:rs868834862
- Q326 (= Q329) to L: in ARGINSA; severe
- V335 (≠ T338) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- M360 (= M363) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- M382 (≠ V386) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- R385 (= R389) to L: in ARGINSA; severe
- H388 (= H392) to Q: in ARGINSA; severe
- A398 (≠ G402) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
- R456 (= R460) to W: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs759396688
1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
45% identity, 96% coverage: 20:463/463 of query aligns to 1:442/447 of 1hy0A
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
43% identity, 98% coverage: 8:463/463 of query aligns to 6:459/466 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)
45% identity, 95% coverage: 18:458/463 of query aligns to 1:440/454 of 6ienB
- binding argininosuccinate: S97 (= S114), R98 (= R115), N99 (= N116), T144 (= T162), H145 (= H163), S266 (= S284), S267 (= S285), M269 (= M287), K272 (= K290), Y306 (= Y324), Q311 (= Q329), K314 (= K332)
6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
44% identity, 95% coverage: 18:458/463 of query aligns to 1:438/452 of 6ienA
- binding argininosuccinate: R98 (= R115), N99 (= N116), V102 (= V119), T144 (= T162), H145 (= H163), Y304 (= Y324), Q309 (= Q329), K312 (= K332)
- binding fumaric acid: S266 (= S284), S267 (= S285), K270 (= K290), N272 (= N292)
6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
42% identity, 95% coverage: 18:458/463 of query aligns to 1:404/418 of 6ienC
- binding arginine: R98 (= R115), N99 (= N116), V102 (= V119), Y306 (= Y324), Q311 (= Q329), K314 (= K332)
- binding argininosuccinate: T144 (= T162), H145 (= H163), S266 (= S284), S267 (= S285), M269 (= M287), K272 (= K290)
- binding fumaric acid: S97 (= S114), R98 (= R115), N99 (= N116)
6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
31% identity, 94% coverage: 27:463/463 of query aligns to 26:461/497 of 6g3hA