SitesBLAST

Comparing WP_022949749.1 NCBI__GCF_000421465.1:WP_022949749.1 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)
30% identity, 74% coverage: 99:472/504 of query aligns to 80:450/451 of 1tj7B

• active site: H150 (≠ Y164), S271 (= S285), K277 (= K291), E284 (≠ S298)
• binding phosphate ion: S271 (= S285), M274 (= M288), K277 (= K291)

2e9fB Crystal structure of t.Th.Hb8 argininosuccinate lyase complexed with l-arginine
33% identity, 76% coverage: 90:472/504 of query aligns to 70:447/450 of 2e9fB

• active site: E71 (≠ G91), T146 (= T163), H147 (≠ Y164), S268 (= S285), S269 (≠ K286), K274 (= K291), E281 (≠ S298)
• binding arginine: R98 (= R117), N99 (≠ R118), V102 (≠ I121), Y308 (≠ Q324), Q313 (≠ M329), K316 (≠ Y332)

6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
30% identity, 77% coverage: 98:486/504 of query aligns to 88:475/497 of 6g3hA

• binding (2~{S})-2-[2-[[(2~{S})-1,4-bis(oxidanyl)-1,4-bis(oxidanylidene)butan-2-yl]amino]ethylamino]butanedioic acid: S276 (= S285), S277 (≠ K286), M279 (= M288), K282 (= K291), N284 (= N293), D286 (≠ F295), R290 (≠ Y299)

Sites not aligning to the query:

• binding (2~{S})-2-[2-[[(2~{S})-1,4-bis(oxidanyl)-1,4-bis(oxidanylidene)butan-2-yl]amino]ethylamino]butanedioic acid: 22

6g3gA Crystal structure of edds lyase in complex with succinate (see paper)
30% identity, 77% coverage: 98:486/504 of query aligns to 88:475/497 of 6g3gA

• binding succinic acid: S276 (= S285), S277 (≠ K286), M279 (= M288), K282 (= K291), N284 (= N293)

6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
30% identity, 77% coverage: 98:486/504 of query aligns to 88:475/497 of 6g3fA

• binding fumaric acid: S276 (= S285), S277 (≠ K286), M279 (= M288), K282 (= K291), N284 (= N293)

6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
30% identity, 77% coverage: 98:486/504 of query aligns to 88:475/496 of 6g3iA

• binding (2~{S})-2-(2-azanylethylamino)butanedioic acid: S276 (= S285), S277 (≠ K286), M279 (= M288), K282 (= K291), N284 (= N293), D286 (≠ F295)
• binding fumaric acid: R290 (≠ Y299)

Sites not aligning to the query:

• binding fumaric acid: 22

1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
28% identity, 75% coverage: 92:469/504 of query aligns to 70:439/447 of 1hy0A

• active site: T142 (= T163), H143 (≠ Y164), S264 (= S285), S265 (≠ K286), K270 (= K291), E277 (≠ S298)
• binding sulfate ion: S264 (= S285), M267 (= M288), N272 (= N293)

Sites not aligning to the query:

• active site: 69

1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
28% identity, 75% coverage: 92:469/504 of query aligns to 72:441/450 of 1k7wD

• active site: T144 (= T163), H145 (≠ Y164), A266 (≠ S285), S267 (≠ K286), K272 (= K291), E279 (≠ S298)
• binding argininosuccinate: R98 (= R117), N99 (≠ R118), V102 (≠ I121), T144 (= T163), H145 (≠ Y164), Y306 (≠ Q324), Q311 (≠ M329), K314 (≠ Y332)

Sites not aligning to the query:

• active site: 71

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)
30% identity, 66% coverage: 92:426/504 of query aligns to 89:415/468 of P24058

• D89 (= D92) mutation to N: Loss of activity.
• N116 (≠ R118) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
• D117 (≠ E119) 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 (≠ Y164) mutation to E: Loss of activity.
• R238 (≠ A240) mutation to Q: Loss of activity.
• T281 (≠ R283) mutation to V: 80% decrease in catalytic efficiency.
• S283 (= S285) 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 (= N293) binding in chain B; mutation to L: Loss of activity.
• D293 (≠ F295) mutation to N: 99% decrease in catalytic efficiency.
• E296 (≠ S298) mutation to D: Loss of activity.
• Y323 (≠ Q324) binding in chain A
• K325 (≠ D326) mutation to N: 99% decrease in catalytic efficiency.
• Q328 (≠ M329) binding in chain A
• D330 (≠ A331) mutation to N: Loss of activity.
• K331 (≠ Y332) binding in chain A; mutation to Q: Loss of activity.

Sites not aligning to the query:

• 11 W→A: 98% decrease in catalytic efficiency.; W→F: 90% decrease in catalytic efficiency.; W→M: 99% decrease in catalytic efficiency.; W→R: 97% decrease in catalytic efficiency.; W→Y: 50% decrease in catalytic efficiency.
• 29 binding in chain A; S→A: 10% decrease in catalytic efficiency.
• 33 D→N: 99% decrease in catalytic efficiency.

P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
28% identity, 75% coverage: 92:469/504 of query aligns to 87:456/466 of P02521

Sites not aligning to the query:

• 2 modified: Blocked amino end (Ala)

P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
31% identity, 63% coverage: 92:407/504 of query aligns to 87:402/464 of P04424

• D87 (= D92) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
• H89 (≠ V94) mutation to Q: 10-fold reduction in activity.
• R94 (≠ A99) to C: in ARGINSA; severe; dbSNP:rs374304304
• R95 (≠ W100) 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 (≠ G124) to E: in ARGINSA; severe
• V178 (≠ F182) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
• T181 (≠ E185) 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 (≠ A240) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
• D237 (= D241) to N: in ARGINSA; severe; dbSNP:rs552951774
• Q286 (= Q290) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
• K288 (= K292) 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 (= R301) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
• R306 (≠ A310) to W: in ARGINSA; severe; dbSNP:rs868834862
• Q326 (≠ M329) to L: in ARGINSA; severe
• V335 (≠ S338) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
• M360 (≠ C363) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
• M382 (≠ A386) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
• R385 (= R390) to L: in ARGINSA; severe
• H388 (= H393) to Q: in ARGINSA; severe
• A398 (≠ L403) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity

Sites not aligning to the query:

• 12 R → Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
• 31 D → N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
• 51 K→N: 2-fold reduction in activity.
• 69 modified: N6-acetyllysine
• 73 E → K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
• 456 R → W: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs759396688

6ienB Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
32% identity, 76% coverage: 87:468/504 of query aligns to 60:441/454 of 6ienB