SitesBLAST
Comparing WP_005808617.1 NCBI__GCF_000021925.1:WP_005808617.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
50% identity, 97% coverage: 7:452/461 of query aligns to 1:447/451 of 1tj7B
2e9fB Crystal structure of t.Th.Hb8 argininosuccinate lyase complexed with l-arginine
51% identity, 95% coverage: 13:448/461 of query aligns to 3:440/450 of 2e9fB
- active site: E71 (= E81), T146 (= T154), H147 (= H155), S268 (= S276), S269 (= S277), K274 (= K282), E281 (= E289)
- binding arginine: R98 (= R108), N99 (= N109), V102 (= V112), Y308 (= Y316), Q313 (= Q321), K316 (= K324)
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, 97% coverage: 2:448/461 of query aligns to 9:454/468 of P24058
- W11 (= W4) 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 (= S22) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
- D33 (= D26) mutation to N: 99% decrease in catalytic efficiency.
- D89 (= D82) mutation to N: Loss of activity.
- N116 (= N109) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (= D110) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T154) 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 (= H155) mutation to E: Loss of activity.
- R238 (= R231) mutation to Q: Loss of activity.
- T281 (= T274) mutation to V: 80% decrease in catalytic efficiency.
- S283 (= S276) 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 (= N284) binding in chain B; mutation to L: Loss of activity.
- D293 (= D286) mutation to N: 99% decrease in catalytic efficiency.
- E296 (= E289) mutation to D: Loss of activity.
- Y323 (= Y316) binding in chain A
- K325 (= K318) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (= Q321) binding in chain A
- D330 (= D323) mutation to N: Loss of activity.
- K331 (= K324) 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)
45% identity, 96% coverage: 2:444/461 of query aligns to 7:448/464 of P04424
- R12 (= R7) to Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
- D31 (= D26) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
- K51 (≠ E46) mutation to N: 2-fold reduction in activity.
- K69 (≠ G64) modified: N6-acetyllysine
- E73 (≠ D68) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
- D87 (= D82) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
- H89 (= H84) mutation to Q: 10-fold reduction in activity.
- R94 (≠ K89) to C: in ARGINSA; severe; dbSNP:rs374304304
- R95 (≠ L90) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
- R113 (= R108) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (= D115) to E: in ARGINSA; severe
- V178 (≠ Q173) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ L176) to S: in a breast cancer sample; somatic mutation
- R182 (= R177) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (= R181) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (= G195) to V: in a breast cancer sample; somatic mutation
- R236 (= R231) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (= D232) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (= Q281) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (= K283) 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 (= R292) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
- R306 (≠ D301) to W: in ARGINSA; severe; dbSNP:rs868834862
- Q326 (= Q321) to L: in ARGINSA; severe
- V335 (≠ A330) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- M360 (= M355) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- M382 (≠ V378) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- R385 (= R381) to L: in ARGINSA; severe
- H388 (= H384) to Q: in ARGINSA; severe
- A398 (≠ C394) 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
1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
45% identity, 95% coverage: 11:448/461 of query aligns to 1:437/450 of 1k7wD
- active site: E71 (= E81), T144 (= T154), H145 (= H155), A266 (≠ S276), S267 (= S277), K272 (= K282), E279 (= E289)
- binding argininosuccinate: R98 (= R108), N99 (= N109), V102 (= V112), T144 (= T154), H145 (= H155), Y306 (= Y316), Q311 (= Q321), K314 (= K324)
1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
43% identity, 95% coverage: 13:448/461 of query aligns to 1:435/447 of 1hy0A
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
43% identity, 97% coverage: 2:448/461 of query aligns to 7:452/466 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, 94% coverage: 12:446/461 of query aligns to 2:436/454 of 6ienB
- binding argininosuccinate: S97 (= S107), R98 (= R108), N99 (= N109), T144 (= T154), H145 (= H155), S266 (= S276), S267 (= S277), M269 (= M279), K272 (= K282), Y306 (= Y316), Q311 (= Q321), K314 (= K324)
6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
41% identity, 94% coverage: 12:446/461 of query aligns to 2:434/452 of 6ienA
- binding argininosuccinate: R98 (= R108), N99 (= N109), V102 (= V112), T144 (= T154), H145 (= H155), Y304 (= Y316), Q309 (= Q321), K312 (= K324)
- binding fumaric acid: S266 (= S276), S267 (= S277), K270 (= K282), N272 (= N284)
6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
42% identity, 84% coverage: 12:399/461 of query aligns to 2:389/418 of 6ienC
- binding arginine: R98 (= R108), N99 (= N109), V102 (= V112), Y306 (= Y316), Q311 (= Q321), K314 (= K324)
- binding argininosuccinate: T144 (= T154), H145 (= H155), S266 (= S276), S267 (= S277), M269 (= M279), K272 (= K282)
- binding fumaric acid: S97 (= S107), R98 (= R108), N99 (= N109)
6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
32% identity, 96% coverage: 7:448/461 of query aligns to 6:454/496 of 6g3iA
6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
32% identity, 96% coverage: 7:448/461 of query aligns to 6:454/497 of 6g3hA
6g3gA Crystal structure of edds lyase in complex with succinate (see paper)
32% identity, 96% coverage: 7:448/461 of query aligns to 6:454/497 of 6g3gA
6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
32% identity, 96% coverage: 7:448/461 of query aligns to 6:454/497 of 6g3fA
3r6vG Crystal structure of aspartase from bacillus sp. Ym55-1 with bound l- aspartate (see paper)
29% identity, 37% coverage: 131:301/461 of query aligns to 150:340/463 of 3r6vG
3r6qA A triclinic-lattice structure of aspartase from bacillus sp. Ym55-1 (see paper)
29% identity, 37% coverage: 131:301/461 of query aligns to 149:339/462 of 3r6qA
Sites not aligning to the query:
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
24% identity, 65% coverage: 21:320/461 of query aligns to 10:302/427 of 2x75A
Sites not aligning to the query:
P12047 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; Glutamyl--tRNA ligase regulatory factor; EC 4.3.2.2 from Bacillus subtilis (strain 168) (see paper)
23% identity, 65% coverage: 21:320/461 of query aligns to 11:303/431 of P12047
- H89 (= H103) mutation to Q: Abolishes enzyme activity.
- H141 (= H155) mutation to Q: Abolishes enzyme activity.
- Q212 (≠ N223) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N284) mutation N->D,L: Abolishes enzyme activity.
- R301 (≠ K318) mutation R->K,Q: Abolishes enzyme activity.
6wngA Crystal structure of an aspartate ammonia-lyase from elizabethkingia anophelis nuhp1
24% identity, 43% coverage: 102:301/461 of query aligns to 135:343/466 of 6wngA
Sites not aligning to the query:
Q9X0I0 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see paper)
22% identity, 87% coverage: 30:432/461 of query aligns to 20:420/431 of Q9X0I0
- H141 (= H155) active site, Proton donor/acceptor
Query Sequence
>WP_005808617.1 NCBI__GCF_000021925.1:WP_005808617.1
MKLWGGRFEKSTDALVEDFHSSISFDQRLYKQDIQGSIAHARMLGEIGVLTSAEAQQIIE
GLKGILTDIREGKIQFEIGAEDIHMNVEKLLTERVGTVGKKVHTGRSRNDQVALDLRLFL
REEIDHTQELLIALLRTVLDLAKEHQETYMPGYTHLQKAQPISFAHHMMAYAQMFLRDLG
RLKDTRQRLNVSPLGSGALAGTTFPLEREMVAQELGFDGITWNSLDGVSDRDFALEFLSA
ASILMMHLSRLCEELVLWSTGEFQFVIMDDGYSTGSSIMPQKKNPDVAELVRGKTGRVYG
DLVALLTVMKGLPLAYNKDMQEDKEQVFDAVDTIQKSLLVVEPMLRTMKVNKKAMAEGAK
GGFTNATDLADYLAKKNVPFREAHEIVGKLVLYCSKRGCGLEDLTLKEFQEHSDVFAEDL
FESIGIEYCVRQRHIPGGPSPESVAQAILWTEHILEQFTGG
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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