SitesBLAST

Comparing WP_068174499.1 NCBI__GCF_001592305.1:WP_068174499.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Found 20 (the maximum) hits to proteins with known functional sites

1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
47% identity, 96% coverage: 17:482/483 of query aligns to 2:450/451 of 1tj7B

• active site: H150 (= H164), S271 (= S291), K277 (= K297), E284 (= E304)
• binding phosphate ion: S271 (= S291), M274 (= M294), K277 (= K297)

2e9fB Crystal structure of t.Th.Hb8 argininosuccinate lyase complexed with l-arginine
48% identity, 94% coverage: 24:475/483 of query aligns to 5:440/450 of 2e9fB

• active site: E71 (= E90), T146 (= T163), H147 (= H164), S268 (= S291), S269 (= S292), K274 (= K297), E281 (= E304)
• binding arginine: R98 (= R117), N99 (= N118), V102 (= V121), Y308 (= Y331), Q313 (= Q336), K316 (= K339)

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)
40% identity, 97% coverage: 13:479/483 of query aligns to 11:458/468 of P24058

• W11 (= W13) 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 (= S31) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
• D33 (= D35) mutation to N: 99% decrease in catalytic efficiency.
• D89 (= D91) mutation to N: Loss of activity.
• N116 (= N118) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
• D117 (= D119) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
• T161 (= T163) 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 (= H164) mutation to E: Loss of activity.
• R238 (= R246) mutation to Q: Loss of activity.
• T281 (= T289) mutation to V: 80% decrease in catalytic efficiency.
• S283 (= S291) 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 (= N299) binding in chain B; mutation to L: Loss of activity.
• D293 (= D301) mutation to N: 99% decrease in catalytic efficiency.
• E296 (= E304) mutation to D: Loss of activity.
• Y323 (= Y331) binding in chain A
• K325 (= K333) mutation to N: 99% decrease in catalytic efficiency.
• Q328 (= Q336) binding in chain A
• D330 (= D338) mutation to N: Loss of activity.
• K331 (= K339) binding in chain A; mutation to Q: Loss of activity.

1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
40% identity, 94% coverage: 24:479/483 of query aligns to 5:441/450 of 1k7wD

• active site: E71 (= E90), T144 (= T163), H145 (= H164), A266 (≠ S291), S267 (= S292), K272 (= K297), E279 (= E304)
• binding argininosuccinate: R98 (= R117), N99 (= N118), V102 (= V121), T144 (= T163), H145 (= H164), Y306 (= Y331), Q311 (= Q336), K314 (= K339)

P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
40% identity, 97% coverage: 13:482/483 of query aligns to 9:459/464 of P04424

• R12 (≠ L16) to Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
• D31 (= D35) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
• K51 (≠ A55) mutation to N: 2-fold reduction in activity.
• K69 (≠ Q73) modified: N6-acetyllysine
• E73 (= E77) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
• D87 (= D91) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
• H89 (= H93) mutation to Q: 10-fold reduction in activity.
• R94 (≠ A98) to C: in ARGINSA; severe; dbSNP:rs374304304
• R95 (= R99) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
• R113 (= R117) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
• D120 (= D124) to E: in ARGINSA; severe
• V178 (≠ E182) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
• T181 (≠ A185) to S: in a breast cancer sample; somatic mutation
• R182 (= R186) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
• R186 (= R190) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
• G200 (= G204) to V: in a breast cancer sample; somatic mutation
• R236 (= R246) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
• D237 (= D247) to N: in ARGINSA; severe; dbSNP:rs552951774
• Q286 (= Q296) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
• K288 (= K298) 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 (= R307) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
• R306 (≠ H316) to W: in ARGINSA; severe; dbSNP:rs868834862
• Q326 (= Q336) to L: in ARGINSA; severe
• V335 (≠ T345) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
• M360 (= M382) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
• M382 (≠ L405) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
• R385 (= R408) to L: in ARGINSA; severe
• H388 (= H411) to Q: in ARGINSA; severe
• A398 (= A421) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
• R456 (= R479) 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)
39% identity, 94% coverage: 24:479/483 of query aligns to 3:439/447 of 1hy0A

• active site: E69 (= E90), T142 (= T163), H143 (= H164), S264 (= S291), S265 (= S292), K270 (= K297), E277 (= E304)
• binding sulfate ion: S264 (= S291), M267 (= M294), N272 (= N299)

P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
37% identity, 96% coverage: 18:482/483 of query aligns to 17:459/466 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)
41% identity, 94% coverage: 22:475/483 of query aligns to 2:438/454 of 6ienB

• binding argininosuccinate: S97 (= S116), R98 (= R117), N99 (= N118), T144 (= T163), H145 (= H164), S266 (= S291), S267 (= S292), M269 (= M294), K272 (= K297), Y306 (= Y331), Q311 (= Q336), K314 (= K339)

6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
40% identity, 94% coverage: 22:475/483 of query aligns to 2:436/452 of 6ienA

• binding argininosuccinate: R98 (= R117), N99 (= N118), V102 (= V121), T144 (= T163), H145 (= H164), Y304 (= Y331), Q309 (= Q336), K312 (= K339)
• binding fumaric acid: S266 (= S291), S267 (= S292), K270 (= K297), N272 (= N299)

6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
39% identity, 94% coverage: 22:475/483 of query aligns to 2:402/418 of 6ienC