SitesBLAST

Comparing WP_028487461.1 NCBI__GCF_000483485.1:WP_028487461.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

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

2e9fB Crystal structure of t.Th.Hb8 argininosuccinate lyase complexed with l-arginine
50% identity, 94% coverage: 23:462/466 of query aligns to 3:444/450 of 2e9fB

• active site: E71 (= E91), T146 (= T164), H147 (= H165), S268 (= S286), S269 (= S287), K274 (= K292), E281 (= E299)
• binding arginine: R98 (= R118), N99 (= N119), V102 (= V122), Y308 (= Y326), Q313 (= Q331), K316 (= K334)

1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
46% identity, 96% coverage: 17:465/466 of query aligns to 1:450/451 of 1tj7B

• active site: H150 (= H165), S271 (= S286), K277 (= K292), E284 (= E299)
• binding phosphate ion: S271 (= S286), M274 (= M289), K277 (= K292)

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)
45% identity, 95% coverage: 11:454/466 of query aligns to 8:450/468 of P24058

• W11 (≠ S14) 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 (= S32) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
• D33 (= D36) mutation to N: 99% decrease in catalytic efficiency.
• D89 (= D92) mutation to N: Loss of activity.
• N116 (= N119) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
• D117 (= D120) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
• T161 (= T164) 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 (= H165) mutation to E: Loss of activity.
• R238 (= R241) mutation to Q: Loss of activity.
• T281 (= T284) mutation to V: 80% decrease in catalytic efficiency.
• S283 (= S286) 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 (= N294) binding in chain B; mutation to L: Loss of activity.
• D293 (= D296) mutation to N: 99% decrease in catalytic efficiency.
• E296 (= E299) mutation to D: Loss of activity.
• Y323 (= Y326) binding in chain A
• K325 (= K328) mutation to N: 99% decrease in catalytic efficiency.
• Q328 (= Q331) binding in chain A
• D330 (= D333) mutation to N: Loss of activity.
• K331 (= K334) binding in chain A; mutation to Q: Loss of activity.

1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
44% identity, 96% coverage: 21:466/466 of query aligns to 1:445/450 of 1k7wD

• active site: E71 (= E91), T144 (= T164), H145 (= H165), A266 (≠ S286), S267 (= S287), K272 (= K292), E279 (= E299)
• binding argininosuccinate: R98 (= R118), N99 (= N119), V102 (= V122), T144 (= T164), H145 (= H165), Y306 (= Y326), Q311 (= Q331), K314 (= K334)

P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
43% identity, 95% coverage: 12:454/466 of query aligns to 7:448/464 of P04424

• R12 (= R17) to Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
• D31 (= D36) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
• K51 (= K56) mutation to N: 2-fold reduction in activity.
• K69 (≠ Q74) modified: N6-acetyllysine
• E73 (≠ D78) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
• D87 (= D92) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
• H89 (= H94) mutation to Q: 10-fold reduction in activity.
• R94 (≠ S99) to C: in ARGINSA; severe; dbSNP:rs374304304
• R95 (= R100) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
• R113 (= R118) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
• D120 (= D125) to E: in ARGINSA; severe
• V178 (≠ E183) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
• T181 (≠ K186) to S: in a breast cancer sample; somatic mutation
• R182 (= R187) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
• R186 (= R191) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
• G200 (= G205) to V: in a breast cancer sample; somatic mutation
• R236 (= R241) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
• D237 (= D242) to N: in ARGINSA; severe; dbSNP:rs552951774
• Q286 (= Q291) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
• K288 (= K293) 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 (= R302) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
• R306 (≠ H311) to W: in ARGINSA; severe; dbSNP:rs868834862
• Q326 (= Q331) to L: in ARGINSA; severe
• V335 (≠ T340) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
• M360 (≠ T365) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
• M382 (≠ L388) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
• R385 (= R391) to L: in ARGINSA; severe
• H388 (= H394) to Q: in ARGINSA; severe
• A398 (≠ G404) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity

Sites not aligning to the query:

• 456 R → 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)
42% identity, 95% coverage: 23:466/466 of query aligns to 1:443/447 of 1hy0A

• active site: E69 (= E91), T142 (= T164), H143 (= H165), S264 (= S286), S265 (= S287), K270 (= K292), E277 (= E299)
• binding sulfate ion: S264 (= S286), M267 (= M289), N272 (= N294)

P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
41% identity, 98% coverage: 11:466/466 of query aligns to 6:460/466 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)
42% identity, 91% coverage: 29:454/466 of query aligns to 8:434/454 of 6ienB

• binding argininosuccinate: S97 (= S117), R98 (= R118), N99 (= N119), T144 (= T164), H145 (= H165), S266 (= S286), S267 (= S287), M269 (= M289), K272 (= K292), Y306 (= Y326), Q311 (= Q331), K314 (= K334)

6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
41% identity, 91% coverage: 29:454/466 of query aligns to 8:432/452 of 6ienA

• binding argininosuccinate: R98 (= R118), N99 (= N119), V102 (= V122), T144 (= T164), H145 (= H165), Y304 (= Y326), Q309 (= Q331), K312 (= K334)
• binding fumaric acid: S266 (= S286), S267 (= S287), K270 (= K292), N272 (= N294)

6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
39% identity, 91% coverage: 29:454/466 of query aligns to 8:398/418 of 6ienC

• binding arginine: R98 (= R118), N99 (= N119), V102 (= V122), Y306 (= Y326), Q311 (= Q331), K314 (= K334)
• binding argininosuccinate: T144 (= T164), H145 (= H165), S266 (= S286), S267 (= S287), M269 (= M289), K272 (= K292)
• binding fumaric acid: S97 (= S117), R98 (= R118), N99 (= N119)

6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
31% identity, 95% coverage: 15:457/466 of query aligns to 4:453/497 of 6g3hA