SitesBLAST

Comparing WP_022949997.1 NCBI__GCF_000421465.1:WP_022949997.1 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)
50% identity, 94% coverage: 18:466/477 of query aligns to 1:450/451 of 1tj7B

• active site: H150 (= H166), S271 (= S287), K277 (= K293), E284 (= E300)
• binding phosphate ion: S271 (= S287), M274 (= M290), K277 (= K293)

2e9fB Crystal structure of t.Th.Hb8 argininosuccinate lyase complexed with l-arginine
50% identity, 92% coverage: 24:463/477 of query aligns to 3:444/450 of 2e9fB

• active site: E71 (= E92), T146 (= T165), H147 (= H166), S268 (= S287), S269 (= S288), K274 (= K293), E281 (= E300)
• binding arginine: R98 (= R119), N99 (= N120), V102 (= V123), Y308 (= Y327), Q313 (= Q332), K316 (= K335)

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, 96% coverage: 12:470/477 of query aligns to 8:465/468 of P24058

• W11 (= W15) 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 (= S33) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
• D33 (= D37) mutation to N: 99% decrease in catalytic efficiency.
• D89 (= D93) mutation to N: Loss of activity.
• N116 (= N120) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
• D117 (= D121) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
• T161 (= T165) 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 (= H166) mutation to E: Loss of activity.
• R238 (= R242) mutation to Q: Loss of activity.
• T281 (= T285) mutation to V: 80% decrease in catalytic efficiency.
• S283 (= S287) 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 (= N295) binding in chain B; mutation to L: Loss of activity.
• D293 (= D297) mutation to N: 99% decrease in catalytic efficiency.
• E296 (= E300) mutation to D: Loss of activity.
• Y323 (= Y327) binding in chain A
• K325 (= K329) mutation to N: 99% decrease in catalytic efficiency.
• Q328 (= Q332) binding in chain A
• D330 (= D334) mutation to N: Loss of activity.
• K331 (= K335) 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)
46% identity, 96% coverage: 13:470/477 of query aligns to 7:463/464 of P04424

• R12 (= R18) to Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
• D31 (= D37) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
• K51 (= K57) mutation to N: 2-fold reduction in activity.
• K69 (≠ Q75) modified: N6-acetyllysine
• E73 (= E79) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
• D87 (= D93) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
• H89 (= H95) mutation to Q: 10-fold reduction in activity.
• R94 (≠ A100) to C: in ARGINSA; severe; dbSNP:rs374304304
• R95 (= R101) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
• R113 (= R119) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
• D120 (= D126) to E: in ARGINSA; severe
• V178 (≠ E184) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
• T181 (≠ Q187) to S: in a breast cancer sample; somatic mutation
• R182 (= R188) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
• R186 (= R192) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
• G200 (= G206) to V: in a breast cancer sample; somatic mutation
• R236 (= R242) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
• D237 (= D243) to N: in ARGINSA; severe; dbSNP:rs552951774
• Q286 (= Q292) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
• K288 (= K294) 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 (= R303) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
• R306 (≠ H312) to W: in ARGINSA; severe; dbSNP:rs868834862
• Q326 (= Q332) to L: in ARGINSA; severe
• V335 (≠ T341) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
• M360 (= M366) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
• M382 (≠ V389) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
• R385 (= R392) to L: in ARGINSA; severe
• H388 (= H395) to Q: in ARGINSA; severe
• A398 (= A405) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
• R456 (= R463) 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, 94% coverage: 23:470/477 of query aligns to 2:448/450 of 1k7wD

• active site: E71 (= E92), T144 (= T165), H145 (= H166), A266 (≠ S287), S267 (= S288), K272 (= K293), E279 (= E300)
• binding argininosuccinate: R98 (= R119), N99 (= N120), V102 (= V123), T144 (= T165), H145 (= H166), Y306 (= Y327), Q311 (= Q332), K314 (= K335)

1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
42% identity, 94% coverage: 24:470/477 of query aligns to 1:446/447 of 1hy0A

• active site: E69 (= E92), T142 (= T165), H143 (= H166), S264 (= S287), S265 (= S288), K270 (= K293), E277 (= E300)
• binding sulfate ion: S264 (= S287), M267 (= M290), N272 (= N295)

P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
41% identity, 96% coverage: 12:470/477 of query aligns to 6:463/466 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)
46% identity, 94% coverage: 22:467/477 of query aligns to 1:449/454 of 6ienB

• binding argininosuccinate: S97 (= S118), R98 (= R119), N99 (= N120), T144 (= T165), H145 (= H166), S266 (= S287), S267 (= S288), M269 (= M290), K272 (= K293), Y306 (= Y327), Q311 (= Q332), K314 (= K335)

6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
46% identity, 94% coverage: 22:467/477 of query aligns to 1:447/452 of 6ienA

• binding argininosuccinate: R98 (= R119), N99 (= N120), V102 (= V123), T144 (= T165), H145 (= H166), Y304 (= Y327), Q309 (= Q332), K312 (= K335)
• binding fumaric acid: S266 (= S287), S267 (= S288), K270 (= K293), N272 (= N295)

6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
43% identity, 94% coverage: 22:467/477 of query aligns to 1:413/418 of 6ienC