SitesBLAST
Comparing Ac3H11_3293 Argininosuccinate lyase (EC 4.3.2.1) to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 17 hits to proteins with known functional sites (download)
6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
29% identity, 89% coverage: 52:535/546 of query aligns to 13:482/496 of 6g3iA
6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
29% identity, 89% coverage: 52:535/546 of query aligns to 13:482/497 of 6g3hA
6g3gA Crystal structure of edds lyase in complex with succinate (see paper)
29% identity, 89% coverage: 52:535/546 of query aligns to 13:482/497 of 6g3gA
6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
29% identity, 89% coverage: 52:535/546 of query aligns to 13:482/497 of 6g3fA
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
27% identity, 71% coverage: 122:511/546 of query aligns to 66:447/451 of 1tj7B
2e9fB Crystal structure of t.Th.Hb8 argininosuccinate lyase complexed with l-arginine
28% identity, 63% coverage: 94:436/546 of query aligns to 38:383/450 of 2e9fB
- active site: E71 (≠ T124), T146 (= T196), H147 (≠ N197), S268 (= S320), S269 (= S321), K274 (= K326), E281 (≠ Q333)
- binding arginine: R98 (= R150), N99 (≠ Q151), V102 (≠ H154), Y308 (≠ S371), Q313 (≠ V376), K316 (≠ T379)
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)
28% identity, 64% coverage: 94:444/546 of query aligns to 55:405/468 of P24058
- D89 (≠ V126) mutation to N: Loss of activity.
- N116 (≠ Q151) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (= D152) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T196) 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 (≠ N197) mutation to E: Loss of activity.
- R238 (≠ Y275) mutation to Q: Loss of activity.
- T281 (≠ Y318) mutation to V: 80% decrease in catalytic efficiency.
- S283 (= S320) 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 (= N328) binding in chain B; mutation to L: Loss of activity.
- D293 (≠ G330) mutation to N: 99% decrease in catalytic efficiency.
- E296 (≠ Q333) mutation to D: Loss of activity.
- Y323 (≠ I361) binding in chain A
- K325 (≠ Y363) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (≠ T366) binding in chain A
- D330 (≠ S368) mutation to N: Loss of activity.
- K331 (≠ P369) 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.
1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
28% identity, 64% coverage: 94:444/546 of query aligns to 38:388/450 of 1k7wD
- active site: E71 (≠ D125), T144 (= T196), H145 (≠ N197), A266 (≠ S320), S267 (= S321), K272 (= K326), E279 (≠ Q333)
- binding argininosuccinate: R98 (= R150), N99 (≠ Q151), V102 (≠ H154), T144 (= T196), H145 (≠ N197), Y306 (≠ I361), Q311 (≠ T366), K314 (≠ P369)
1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
28% identity, 64% coverage: 94:444/546 of query aligns to 36:386/447 of 1hy0A
P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
28% identity, 64% coverage: 94:444/546 of query aligns to 53:403/464 of P04424
- K69 (≠ L110) modified: N6-acetyllysine
- E73 (≠ S111) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
- D87 (= D125) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
- H89 (≠ L127) mutation to Q: 10-fold reduction in activity.
- R94 (≠ K131) to C: in ARGINSA; severe; dbSNP:rs374304304
- R95 (≠ I132) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
- R113 (= R150) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (≠ Q161) to E: in ARGINSA; severe
- V178 (≠ D215) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ A218) to S: in a breast cancer sample; somatic mutation
- R182 (= R219) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (= R223) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (= G237) to V: in a breast cancer sample; somatic mutation
- R236 (≠ Y275) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (= D276) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (= Q325) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (≠ A327) 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 (= R336) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
- R306 (≠ S345) to W: in ARGINSA; severe; dbSNP:rs868834862
- Q326 (≠ W367) to L: in ARGINSA; severe
- V335 (= V376) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- M360 (≠ A399) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- M382 (≠ V423) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- R385 (= R426) to L: in ARGINSA; severe
- H388 (= H429) to Q: in ARGINSA; severe
- A398 (= A439) 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.
- 456 R → W: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs759396688
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
24% identity, 78% coverage: 95:518/546 of query aligns to 54:463/466 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)
28% identity, 70% coverage: 64:444/546 of query aligns to 3:389/454 of 6ienB
- binding argininosuccinate: S97 (= S149), R98 (= R150), N99 (≠ Q151), T144 (= T196), H145 (≠ N197), S266 (= S320), S267 (= S321), M269 (= M323), K272 (= K326), Y306 (= Y363), Q311 (≠ S368), K314 (≠ S371)
6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
28% identity, 67% coverage: 64:429/546 of query aligns to 3:374/418 of 6ienC
- binding arginine: R98 (= R150), N99 (≠ Q151), V102 (≠ H154), Y306 (= Y363), Q311 (≠ S368), K314 (≠ S371)
- binding argininosuccinate: T144 (= T196), H145 (≠ N197), S266 (= S320), S267 (= S321), M269 (= M323), K272 (= K326)
- binding fumaric acid: S97 (= S149), R98 (= R150), N99 (≠ Q151)
6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
27% identity, 70% coverage: 64:444/546 of query aligns to 3:387/452 of 6ienA
- binding argininosuccinate: R98 (= R150), N99 (≠ Q151), V102 (≠ H154), T144 (= T196), H145 (≠ N197), Y304 (= Y363), Q309 (≠ S368), K312 (≠ S371)
- binding fumaric acid: S266 (≠ A322), S267 (≠ M323), K270 (= K326), N272 (= N328)
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)
25% identity, 45% coverage: 82:329/546 of query aligns to 26:271/431 of Q9X0I0
- H141 (≠ N197) active site, Proton donor/acceptor
P12047 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; Glutamyl--tRNA ligase regulatory factor; EC 4.3.2.2 from Bacillus subtilis (strain 168) (see paper)
21% identity, 60% coverage: 67:396/546 of query aligns to 11:338/431 of P12047
- H89 (= H145) mutation to Q: Abolishes enzyme activity.
- H141 (≠ N197) mutation to Q: Abolishes enzyme activity.
- Q212 (≠ Y275) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N328) mutation N->D,L: Abolishes enzyme activity.
- R301 (≠ H354) mutation R->K,Q: Abolishes enzyme activity.
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
23% identity, 27% coverage: 92:240/546 of query aligns to 35:183/427 of 2x75A
Sites not aligning to the query:
Query Sequence
>Ac3H11_3293 Argininosuccinate lyase (EC 4.3.2.1)
MPSPQRHPARTITLRPTRFLLAPVVGAILAMGQAQAADTLDTACKTTAECQAQVAKIQGV
VKGDATSALAKSQDTFYWFGRINMASTVVNVEQGIIPKAQAGRIARGVELSITQATTPGG
KRPTDVLQVEKIITDAVGPEATLIHTGRSRQDIHSTLNAAQLRLEMLDFADALDQVRARL
INTAQAHTATYVPAYTNGVQAMPISYGHYLMAWADSFARDSARVREAYARINLSPMGTAV
LSNSSWGINRERLAQLLGFDGLIVNSLDAGQISTYDIPIEATSIASSTAIRVGAFMQDVH
TQYHQTRPWLLLASGKTYTSSAMPQKANPGIIQNTRAKASDVVASAQASLWRAHNVTPGM
IDYKNTWSPASAKTFVQGTEMLQQFADVLDSLRIDPARALDELESEWTTSMELAEALQRS
HGVPFRVGHHFASDVVVFAKERSIRPKDFPYAEAVRIYREAGKKYDLKDQRLPLGEAAFR
RALSPADMVTTRTGTGGPQPQEVTRMATVAKDTLAKDRVWSGEARQRLLAAEAALNAAFE
GVKSLP
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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