SitesBLAST
Comparing WP_090214906.1 NCBI__GCF_002796795.1:WP_090214906.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
9ggjF Crystal structure of argininosuccinate lyase from arabidopsis thaliana (atasl) in complex with biological substrate and products - argininosuccinate, argnine and fumarate (see paper)
49% identity, 97% coverage: 11:458/464 of query aligns to 1:447/454 of 9ggjF
9ggjA Crystal structure of argininosuccinate lyase from arabidopsis thaliana (atasl) in complex with biological substrate and products - argininosuccinate, argnine and fumarate (see paper)
49% identity, 94% coverage: 22:458/464 of query aligns to 7:442/451 of 9ggjA
2e9fB Crystal structure of t.Th.Hb8 argininosuccinate lyase complexed with l-arginine
51% identity, 95% coverage: 17:459/464 of query aligns to 1:444/450 of 2e9fB
- active site: E71 (= E87), T146 (= T160), H147 (= H161), S268 (= S282), S269 (= S283), K274 (= K288), E281 (= E295)
- binding arginine: R98 (= R114), N99 (= N115), V102 (= V118), Y308 (= Y322), Q313 (= Q327), K316 (= K330)
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, 99% coverage: 7:464/464 of query aligns to 8:463/468 of P24058
- W11 (= W10) 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 (= S28) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
- D33 (= D32) mutation to N: 99% decrease in catalytic efficiency.
- D89 (= D88) mutation to N: Loss of activity.
- N116 (= N115) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (= D116) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T160) 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 (= H161) mutation to E: Loss of activity.
- R238 (= R237) mutation to Q: Loss of activity.
- T281 (= T280) mutation to V: 80% decrease in catalytic efficiency.
- S283 (= S282) 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 (= N290) binding in chain B; mutation to L: Loss of activity.
- D293 (= D292) mutation to N: 99% decrease in catalytic efficiency.
- E296 (= E295) mutation to D: Loss of activity.
- Y323 (= Y322) binding in chain A
- K325 (= K324) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (= Q327) binding in chain A
- D330 (= D329) mutation to N: Loss of activity.
- K331 (= K330) binding in chain A; mutation to Q: Loss of activity.
1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
45% identity, 96% coverage: 19:464/464 of query aligns to 3:446/450 of 1k7wD
- active site: E71 (= E87), T144 (= T160), H145 (= H161), A266 (≠ S282), S267 (= S283), K272 (= K288), E279 (= E295)
- binding argininosuccinate: R98 (= R114), N99 (= N115), V102 (= V118), T144 (= T160), H145 (= H161), Y306 (= Y322), Q311 (= Q327), K314 (= K330)
P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
44% identity, 98% coverage: 6:462/464 of query aligns to 5:459/464 of P04424
- R12 (= R13) to Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
- D31 (= D32) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
- K51 (≠ A52) mutation to N: 2-fold reduction in activity.
- K69 (≠ T70) modified: N6-acetyllysine
- E73 (= E74) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
- D87 (= D88) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
- H89 (= H90) mutation to Q: 10-fold reduction in activity.
- R94 (≠ A95) to C: in ARGINSA; severe; dbSNP:rs374304304
- R95 (= R96) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
- R113 (= R114) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (= D121) to E: in ARGINSA; severe
- V178 (≠ E179) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ G182) to S: in a breast cancer sample; somatic mutation
- R182 (= R183) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (= R187) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (= G201) to V: in a breast cancer sample; somatic mutation
- R236 (= R237) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (= D238) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (= Q287) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (= K289) 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 (= R298) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
- R306 (≠ A307) to W: in ARGINSA; severe; dbSNP:rs868834862
- Q326 (= Q327) to L: in ARGINSA; severe
- V335 (≠ A336) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- M360 (≠ L361) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- M382 (≠ V385) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- R385 (= R388) to L: in ARGINSA; severe
- H388 (= H391) to Q: in ARGINSA; severe
- A398 (= A401) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
- R456 (≠ K459) to W: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs759396688
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
47% identity, 95% coverage: 13:451/464 of query aligns to 1:439/451 of 1tj7B
1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
43% identity, 96% coverage: 19:464/464 of query aligns to 1:444/447 of 1hy0A
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
41% identity, 99% coverage: 7:464/464 of query aligns to 6:461/466 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)
43% identity, 95% coverage: 18:456/464 of query aligns to 1:439/454 of 6ienB
- binding argininosuccinate: S97 (= S113), R98 (= R114), N99 (= N115), T144 (= T160), H145 (= H161), S266 (= S282), S267 (= S283), M269 (= M285), K272 (= K288), Y306 (= Y322), Q311 (= Q327), K314 (= K330)
6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
43% identity, 95% coverage: 18:456/464 of query aligns to 1:437/452 of 6ienA
- binding argininosuccinate: R98 (= R114), N99 (= N115), V102 (= V118), T144 (= T160), H145 (= H161), Y304 (= Y322), Q309 (= Q327), K312 (= K330)
- binding fumaric acid: S266 (= S282), S267 (= S283), K270 (= K288), N272 (= N290)
6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
44% identity, 84% coverage: 18:406/464 of query aligns to 1:389/418 of 6ienC
- binding arginine: R98 (= R114), N99 (= N115), V102 (= V118), Y306 (= Y322), Q311 (= Q327), K314 (= K330)
- binding argininosuccinate: T144 (= T160), H145 (= H161), S266 (= S282), S267 (= S283), M269 (= M285), K272 (= K288)
- binding fumaric acid: S97 (= S113), R98 (= R114), N99 (= N115)
6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
34% identity, 90% coverage: 39:455/464 of query aligns to 39:454/496 of 6g3iA
Sites not aligning to the query:
6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
34% identity, 90% coverage: 39:455/464 of query aligns to 39:454/497 of 6g3hA
Sites not aligning to the query:
6g3gA Crystal structure of edds lyase in complex with succinate (see paper)
34% identity, 90% coverage: 39:455/464 of query aligns to 39:454/497 of 6g3gA
6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
34% identity, 90% coverage: 39:455/464 of query aligns to 39:454/497 of 6g3fA
3r6vG Crystal structure of aspartase from bacillus sp. Ym55-1 with bound l- aspartate (see paper)
27% identity, 58% coverage: 40:306/464 of query aligns to 33:339/463 of 3r6vG
Q9LCC6 Aspartate ammonia-lyase; Aspartase; EC 4.3.1.1 from Bacillus sp. (see 3 papers)
27% identity, 58% coverage: 40:306/464 of query aligns to 36:342/468 of Q9LCC6
- T101 (vs. gap) binding L-aspartate; mutation to A: 7100-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation to S: 80-fold decrease in catalytic efficiency.
- H134 (≠ R107) mutation to A: Retains full activity. Shows a slightly stronger affinity for L-aspartate. Does not affect tertiary structure.
- S140 (= S113) binding L-aspartate; mutation to A: 27-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation S->K,R: Loss of activity.
- T141 (≠ R114) binding L-aspartate; mutation to A: 15-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation to K: 40000-fold decrease in catalytic efficiency.; mutation T->V,R: Loss of activity.
- N142 (= N115) binding L-aspartate; mutation to A: Loss of activity. Does not result in any major conformational changes.; mutation to Q: 3000-fold decrease in catalytic efficiency.
- K183 (≠ M156) mutation to A: Loss of activity. Does not affect tertiary structure.
- T187 (= T160) binding L-aspartate; mutation to A: 6280-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation to S: 2.3-fold decrease in catalytic efficiency.
- H188 (= H161) binding L-aspartate; mutation to A: 100-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation H->K,Q,R: Loss of activity.
- S318 (= S282) mutation to A: Loss of activity.
- S319 (= S283) binding L-aspartate; mutation to A: Almost no change in catalytic efficiency.
- I320 (= I284) mutation to A: 50-fold decrease in catalytic efficiency.
- M321 (= M285) mutation to A: 338-fold decrease in catalytic efficiency.
- P322 (= P286) mutation to A: Almost no change in catalytic efficiency.
- K324 (= K288) binding L-aspartate; mutation to A: Loss of activity. Does not result in any major conformational changes.; mutation K->D,H,R,S,V: Loss of activity.
- N326 (= N290) mutation to A: 22500-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation to Q: 168750-fold decrease in catalytic efficiency.
3r6qA A triclinic-lattice structure of aspartase from bacillus sp. Ym55-1 (see paper)
27% identity, 58% coverage: 40:306/464 of query aligns to 32:338/462 of 3r6qA
Sites not aligning to the query:
P9WN93 Fumarate hydratase class II; Fumarase C; Aerobic fumarase; Iron-independent fumarase; EC 4.2.1.2 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
28% identity, 48% coverage: 90:311/464 of query aligns to 109:347/474 of P9WN93
- SSN 138:140 (≠ ATD 119:121) binding substrate
- T186 (= T160) binding substrate
- S318 (= S282) active site; mutation S->A,C: Absence of fumarase activity.
- S319 (= S283) binding substrate
- KVN 324:326 (≠ KKN 288:290) binding substrate
Sites not aligning to the query:
- 104:106 binding substrate
Query Sequence
>WP_090214906.1 NCBI__GCF_002796795.1:WP_090214906.1
MTDQTSNQMWGGRFAAGPDAIMEAINASIGFDKRMAAQDIQGSRAHAAMLAASGVITDSD
AEAIREGLLTILSEIEAGNFQFSTALEDIHMNVEARLKEIIGEPAGRLHTGRSRNDQVAT
DFKLWVRDQLDAAETGLLALIAALLDQAEAGADWVMPGFTHLQTAQPVTWGHHMMAYVEM
FGRDLSRVRDARTRMNECPLGAAALAGTSFPIDRSMTAEALGFERPAANSLDAVSDRDFA
LEFLSVASICAVHLSRFAEELVIWSSAQFRFVTLSDRFSTGSSIMPQKKNPDAAELIRAK
VGRIFGANTALMMVMKGLPLAYSKDMQEDKEQVFDAADNLMLALAAMEGMVKDMSANRES
LAAAAGSGFSTATDLADWLVRVLKVPFRDAHHVTGTLVGMAEARGCDLPDLSLDDMQGVH
SGITEDIFTVLGVENSVNSRTSYGGTAPEQVRAQVTRWKALLAQ
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory