SitesBLAST
Comparing Ac3H11_1632 Argininosuccinate lyase (EC 4.3.2.1) 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)
2e9fB Crystal structure of t.Th.Hb8 argininosuccinate lyase complexed with l-arginine
48% identity, 93% coverage: 36:489/489 of query aligns to 5:448/450 of 2e9fB
- active site: E71 (= E102), T146 (= T175), H147 (= H176), S268 (= S297), S269 (= S298), K274 (= K303), E281 (= E310)
- binding arginine: R98 (= R129), N99 (= N130), V102 (= V133), Y308 (= Y337), Q313 (= Q342), K316 (= K345)
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
46% identity, 94% coverage: 29:489/489 of query aligns to 2:451/451 of 1tj7B
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)
41% identity, 94% coverage: 25:485/489 of query aligns to 11:458/468 of P24058
- W11 (= W25) 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 (= S43) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
- D33 (= D47) mutation to N: 99% decrease in catalytic efficiency.
- D89 (= D103) mutation to N: Loss of activity.
- N116 (= N130) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (= D131) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T175) 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 (= H176) mutation to E: Loss of activity.
- R238 (= R252) mutation to Q: Loss of activity.
- T281 (= T295) mutation to V: 80% decrease in catalytic efficiency.
- S283 (= S297) 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 (= N305) binding in chain B; mutation to L: Loss of activity.
- D293 (= D307) mutation to N: 99% decrease in catalytic efficiency.
- E296 (= E310) mutation to D: Loss of activity.
- Y323 (= Y337) binding in chain A
- K325 (= K339) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (= Q342) binding in chain A
- D330 (= D344) mutation to N: Loss of activity.
- K331 (= K345) binding in chain A; mutation to Q: Loss of activity.
1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
42% identity, 92% coverage: 36:485/489 of query aligns to 5:441/450 of 1k7wD
- active site: E71 (= E102), T144 (= T175), H145 (= H176), A266 (≠ S297), S267 (= S298), K272 (= K303), E279 (= E310)
- binding argininosuccinate: R98 (= R129), N99 (= N130), V102 (= V133), T144 (= T175), H145 (= H176), Y306 (= Y337), Q311 (= Q342), K314 (= K345)
P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
41% identity, 95% coverage: 25:488/489 of query aligns to 9:459/464 of P04424
- R12 (≠ L28) to Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
- D31 (= D47) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
- K51 (≠ A67) mutation to N: 2-fold reduction in activity.
- K69 (≠ Q85) modified: N6-acetyllysine
- E73 (= E89) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
- D87 (= D103) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
- H89 (= H105) mutation to Q: 10-fold reduction in activity.
- R94 (≠ A110) to C: in ARGINSA; severe; dbSNP:rs374304304
- R95 (= R111) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
- R113 (= R129) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (= D136) to E: in ARGINSA; severe
- V178 (≠ E194) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ K197) to S: in a breast cancer sample; somatic mutation
- R182 (= R198) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (= R202) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (= G216) to V: in a breast cancer sample; somatic mutation
- R236 (= R252) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (= D253) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (= Q302) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (= K304) 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 (= R313) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
- R306 (≠ H322) to W: in ARGINSA; severe; dbSNP:rs868834862
- Q326 (= Q342) to L: in ARGINSA; severe
- V335 (≠ T351) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- M360 (= M388) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- M382 (≠ L411) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- R385 (= R414) to L: in ARGINSA; severe
- H388 (= H417) to Q: in ARGINSA; severe
- A398 (= A427) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
- R456 (= R485) to 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)
40% identity, 92% coverage: 36:485/489 of query aligns to 3:439/447 of 1hy0A
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
38% identity, 94% coverage: 30:488/489 of query aligns to 17:459/466 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)
41% identity, 92% coverage: 34:481/489 of query aligns to 2:438/454 of 6ienB
- binding argininosuccinate: S97 (= S128), R98 (= R129), N99 (= N130), T144 (= T175), H145 (= H176), S266 (= S297), S267 (= S298), M269 (= M300), K272 (= K303), Y306 (= Y337), Q311 (= Q342), K314 (= K345)
6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
41% identity, 92% coverage: 34:481/489 of query aligns to 2:436/452 of 6ienA
- binding argininosuccinate: R98 (= R129), N99 (= N130), V102 (= V133), T144 (= T175), H145 (= H176), Y304 (= Y337), Q309 (= Q342), K312 (= K345)
- binding fumaric acid: S266 (= S297), S267 (= S298), K270 (= K303), N272 (= N305)
6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
39% identity, 92% coverage: 34:481/489 of query aligns to 2:402/418 of 6ienC
- binding arginine: R98 (= R129), N99 (= N130), V102 (= V133), Y306 (= Y337), Q311 (= Q342), K314 (= K345)
- binding argininosuccinate: T144 (= T175), H145 (= H176), S266 (= S297), S267 (= S298), M269 (= M300), K272 (= K303)
- binding fumaric acid: S97 (= S128), R98 (= R129), N99 (= N130)
6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
31% identity, 82% coverage: 41:443/489 of query aligns to 32:408/497 of 6g3hA
Sites not aligning to the query:
6g3gA Crystal structure of edds lyase in complex with succinate (see paper)
31% identity, 82% coverage: 41:443/489 of query aligns to 32:408/497 of 6g3gA
6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
31% identity, 82% coverage: 41:443/489 of query aligns to 32:408/497 of 6g3fA
6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
31% identity, 82% coverage: 41:443/489 of query aligns to 32:408/496 of 6g3iA
Sites not aligning to the query:
3r6vG Crystal structure of aspartase from bacillus sp. Ym55-1 with bound l- aspartate (see paper)
28% identity, 41% coverage: 123:322/489 of query aligns to 132:340/463 of 3r6vG
3r6qA A triclinic-lattice structure of aspartase from bacillus sp. Ym55-1 (see paper)
28% identity, 41% coverage: 123:322/489 of query aligns to 131:339/462 of 3r6qA
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)
24% identity, 62% coverage: 36:340/489 of query aligns to 1:302/431 of P12047
- H89 (= H124) mutation to Q: Abolishes enzyme activity.
- H141 (= H176) mutation to Q: Abolishes enzyme activity.
- Q212 (≠ N244) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N305) mutation N->D,L: Abolishes enzyme activity.
- R301 (≠ K339) mutation R->K,Q: Abolishes enzyme activity.
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)
29% identity, 31% coverage: 169:322/489 of query aligns to 180:343/474 of P9WN93
- T186 (= T175) binding
- S318 (= S297) active site; mutation S->A,C: Absence of fumarase activity.
- S319 (= S298) binding
- KVN 324:326 (≠ KKN 303:305) binding
Sites not aligning to the query:
- 104:106 binding
- 138:140 binding
4adlA Crystal structures of rv1098c in complex with malate (see paper)
29% identity, 31% coverage: 169:322/489 of query aligns to 172:335/459 of 4adlA
Sites not aligning to the query:
6wngA Crystal structure of an aspartate ammonia-lyase from elizabethkingia anophelis nuhp1
27% identity, 41% coverage: 123:322/489 of query aligns to 135:343/466 of 6wngA
Sites not aligning to the query:
Query Sequence
>Ac3H11_1632 Argininosuccinate lyase (EC 4.3.2.1)
MSKAQATSADSAPSHNQLDTKAQAWSALFSEPMSDLVKRYTSSVFFDKRLWQADIAGSLA
HAEMLAAQGVISAEDHASIQRGMAQITSEIESGAFEWKLDLEDVHLNIEARLTQLVGDAG
KRLHTGRSRNDQVATDVRLWLRGEIDLIGDLLKELQVSLVDVAEQNVEVILPGFTHLQVA
QPVSFGHHMLAYVEMFKRDAERMADVRRRTNVLPLGSAALAGTTYPLDRERVAKTLGMEG
VCQNSLDAVSDRDFAIEFTAAASLCMVHVSRLSEELIIWMSQNFGFIKIADRFTTGSSIM
PQKKNPDVPELARGKTGRVVGHLMGLITLMKGQPLAYNKDNQEDKEPLFDTVDTLKDTLR
IFAEMVGGQLNPATGKKEGGITVNAPAMEQAALKGYATATDLADYLVKKGLPFRDAHETV
AHAVKAATTHACDLSELPLAVLQGFHPAIEKDVYECLSLRGSLNARNTLGGTAPAQVRTQ
LARHRARLG
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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