SitesBLAST
Comparing Synpcc7942_2475 FitnessBrowser__SynE:Synpcc7942_2475 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
53% identity, 92% coverage: 33:468/474 of query aligns to 9:445/450 of 2e9fB
- active site: E71 (= E95), T146 (= T168), H147 (= H169), S268 (= S290), S269 (= S291), K274 (= K296), E281 (= E303)
- binding arginine: R98 (= R122), N99 (= N123), V102 (= V126), Y308 (= Y330), Q313 (= Q335), K316 (= K338)
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
47% identity, 95% coverage: 21:470/474 of query aligns to 1:450/451 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)
42% identity, 98% coverage: 8:471/474 of query aligns to 1:462/468 of P24058
- W11 (= W18) 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 (= S36) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
- D33 (= D40) mutation to N: 99% decrease in catalytic efficiency.
- D89 (= D96) mutation to N: Loss of activity.
- N116 (= N123) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (= D124) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T168) 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 (= H169) mutation to E: Loss of activity.
- R238 (= R245) mutation to Q: Loss of activity.
- T281 (= T288) mutation to V: 80% decrease in catalytic efficiency.
- S283 (= S290) 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 (= N298) binding in chain B; mutation to L: Loss of activity.
- D293 (= D300) mutation to N: 99% decrease in catalytic efficiency.
- E296 (= E303) mutation to D: Loss of activity.
- Y323 (= Y330) binding in chain A
- K325 (= K332) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (= Q335) binding in chain A
- D330 (= D337) mutation to N: Loss of activity.
- K331 (= K338) binding in chain A; mutation to Q: Loss of activity.
1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
43% identity, 94% coverage: 28:471/474 of query aligns to 4:445/450 of 1k7wD
- active site: E71 (= E95), T144 (= T168), H145 (= H169), A266 (≠ S290), S267 (= S291), K272 (= K296), E279 (= E303)
- binding argininosuccinate: R98 (= R122), N99 (= N123), V102 (= V126), T144 (= T168), H145 (= H169), Y306 (= Y330), Q311 (= Q335), K314 (= K338)
P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
44% identity, 96% coverage: 18:472/474 of query aligns to 9:461/464 of P04424
- R12 (= R21) to Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
- D31 (= D40) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
- K51 (≠ E60) mutation to N: 2-fold reduction in activity.
- K69 (≠ Q78) modified: N6-acetyllysine
- E73 (= E82) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
- D87 (= D96) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
- H89 (= H98) mutation to Q: 10-fold reduction in activity.
- R94 (= R103) to C: in ARGINSA; severe; dbSNP:rs374304304
- R95 (= R104) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
- R113 (= R122) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (= D129) to E: in ARGINSA; severe
- V178 (≠ E187) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ E190) to S: in a breast cancer sample; somatic mutation
- R182 (= R191) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (= R195) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (= G209) to V: in a breast cancer sample; somatic mutation
- R236 (= R245) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (= D246) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (= Q295) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (= K297) 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 (= R306) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
- R306 (≠ H315) to W: in ARGINSA; severe; dbSNP:rs868834862
- Q326 (= Q335) to L: in ARGINSA; severe
- V335 (≠ A344) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- M360 (≠ L370) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- M382 (≠ V393) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- R385 (= R396) to L: in ARGINSA; severe
- H388 (≠ Y399) to Q: in ARGINSA; severe
- A398 (≠ C409) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
- R456 (= R467) 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, 94% coverage: 28:471/474 of query aligns to 2:443/447 of 1hy0A
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
39% identity, 95% coverage: 21:471/474 of query aligns to 12:460/466 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, 93% coverage: 29:471/474 of query aligns to 4:446/454 of 6ienB
- binding argininosuccinate: S97 (= S121), R98 (= R122), N99 (= N123), T144 (= T168), H145 (= H169), S266 (= S290), S267 (= S291), M269 (= M293), K272 (= K296), Y306 (= Y330), Q311 (= Q335), K314 (= K338)
6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
42% identity, 93% coverage: 29:471/474 of query aligns to 4:444/452 of 6ienA
- binding argininosuccinate: R98 (= R122), N99 (= N123), V102 (= V126), T144 (= T168), H145 (= H169), Y304 (= Y330), Q309 (= Q335), K312 (= K338)
- binding fumaric acid: S266 (= S290), S267 (= S291), K270 (= K296), N272 (= N298)
6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
46% identity, 79% coverage: 29:402/474 of query aligns to 4:377/418 of 6ienC
- binding arginine: R98 (= R122), N99 (= N123), V102 (= V126), Y306 (= Y330), Q311 (= Q335), K314 (= K338)
- binding argininosuccinate: T144 (= T168), H145 (= H169), S266 (= S290), S267 (= S291), M269 (= M293), K272 (= K296)
- binding fumaric acid: S97 (= S121), R98 (= R122), N99 (= N123)
6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
32% identity, 91% coverage: 35:463/474 of query aligns to 27:454/496 of 6g3iA
Sites not aligning to the query:
6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
32% identity, 91% coverage: 35:463/474 of query aligns to 27:454/497 of 6g3hA
Sites not aligning to the query:
6g3gA Crystal structure of edds lyase in complex with succinate (see paper)
32% identity, 91% coverage: 35:463/474 of query aligns to 27:454/497 of 6g3gA
6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
32% identity, 91% coverage: 35:463/474 of query aligns to 27:454/497 of 6g3fA
3r6qA A triclinic-lattice structure of aspartase from bacillus sp. Ym55-1 (see paper)
24% identity, 80% coverage: 51:429/474 of query aligns to 51:458/462 of 3r6qA
3r6vG Crystal structure of aspartase from bacillus sp. Ym55-1 with bound l- aspartate (see paper)
24% identity, 80% coverage: 51:429/474 of query aligns to 52:459/463 of 3r6vG
4adlA Crystal structures of rv1098c in complex with malate (see paper)
30% identity, 43% coverage: 116:319/474 of query aligns to 125:339/459 of 4adlA
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)
30% identity, 43% coverage: 116:319/474 of query aligns to 133:347/474 of P9WN93
- SSN 138:140 (≠ SRN 121:123) binding
- T186 (= T168) binding
- S318 (= S290) active site; mutation S->A,C: Absence of fumarase activity.
- S319 (= S291) binding
- KVN 324:326 (≠ KKN 296:298) binding
Sites not aligning to the query:
4apbD Crystal structure of mycobacterium tuberculosis fumarase (rv1098c) s318c in complex with fumarate (see paper)
30% identity, 43% coverage: 116:319/474 of query aligns to 125:339/462 of 4apbD
- active site: H179 (= H169), C310 (≠ S290), K316 (= K296), E323 (= E303)
- binding fumaric acid: S130 (= S121), S131 (≠ R122), N132 (= N123), T178 (= T168), H179 (= H169), C310 (≠ S290), S311 (= S291), M313 (= M293), K316 (= K296), N318 (= N298)
Sites not aligning to the query:
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
24% identity, 50% coverage: 100:334/474 of query aligns to 71:302/427 of 2x75A
Sites not aligning to the query:
Query Sequence
>Synpcc7942_2475 FitnessBrowser__SynE:Synpcc7942_2475
LAFRTKILVTQAAAPQPWSDRFETALHPAIVVFNASIGFDLALIEYDLTGSQAHAQMLAE
QDIISREEGEAIVAGLEQIRSEYRTGQFQPGLDAEDVHFAVERRLTELLGDVGKKLHTAR
SRNDQVGTDTRLYLRDRVDHIRQQLRDYQRVLLSQAEQHLETLIPGYTHLQRAQPLSLAH
HLHAYLEMAERDWERLGDLRKRLNTSPLGAGALAGTTFPIDRQRTAALLGFERIYANSLD
AVSDRDSLVEFLAAASLIMVHLSRLAEEVILWASEEFRFVRLSDRCATGSSIMPQKKNPD
VPELVRGKTGRVFGHLQALLVVLKGLPLAYNKDLQEDKEGLFDAVQTVESCLEAMTILFA
EGLSFQPDRLAAAVEADFSNATDVADYLAARGVPFREAYNLVGRVVRTCLEQGKLLKDLS
LAEWQALHPQFEADIYTAIAPQQVVAARNSLGGTGFEQVRSALASVRQRLEATC
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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