SitesBLAST
Comparing WP_013536905.1 NCBI__GCF_000185805.1:WP_013536905.1 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
55% identity, 96% coverage: 15:456/459 of query aligns to 3:446/450 of 2e9fB
- active site: E71 (= E83), T146 (= T156), H147 (= H157), S268 (= S278), S269 (= S279), K274 (= K284), E281 (= E291)
- binding arginine: R98 (= R110), N99 (= N111), V102 (= V114), Y308 (= Y318), Q313 (= Q323), K316 (= K326)
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
49% identity, 96% coverage: 9:450/459 of query aligns to 1:443/451 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)
47% identity, 98% coverage: 4:454/459 of query aligns to 9:458/468 of P24058
- W11 (= W6) 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 (= S24) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
- D33 (= D28) mutation to N: 99% decrease in catalytic efficiency.
- D89 (= D84) mutation to N: Loss of activity.
- N116 (= N111) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (= D112) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T156) 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 (= H157) mutation to E: Loss of activity.
- R238 (= R233) mutation to Q: Loss of activity.
- T281 (= T276) mutation to V: 80% decrease in catalytic efficiency.
- S283 (= S278) 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 (= N286) binding in chain B; mutation to L: Loss of activity.
- D293 (= D288) mutation to N: 99% decrease in catalytic efficiency.
- E296 (= E291) mutation to D: Loss of activity.
- Y323 (= Y318) binding in chain A
- K325 (≠ R320) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (= Q323) binding in chain A
- D330 (= D325) mutation to N: Loss of activity.
- K331 (= K326) 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)
48% identity, 98% coverage: 4:455/459 of query aligns to 7:457/464 of P04424
- R12 (= R9) to Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
- D31 (= D28) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
- K51 (= K48) mutation to N: 2-fold reduction in activity.
- K69 (= K66) modified: N6-acetyllysine
- E73 (= E70) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
- D87 (= D84) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
- H89 (= H86) mutation to Q: 10-fold reduction in activity.
- R94 (≠ K91) to C: in ARGINSA; severe; dbSNP:rs374304304
- R95 (= R92) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
- R113 (= R110) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (= D117) to E: in ARGINSA; severe
- V178 (≠ H175) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ K178) to S: in a breast cancer sample; somatic mutation
- R182 (= R179) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (= R183) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (= G197) to V: in a breast cancer sample; somatic mutation
- R236 (= R233) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (= D234) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (= Q283) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (= K285) 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 (= R294) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
- R306 (≠ D303) to W: in ARGINSA; severe; dbSNP:rs868834862
- Q326 (= Q323) to L: in ARGINSA; severe
- V335 (≠ A332) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- M360 (= M357) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- M382 (= M380) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- R385 (= R383) to L: in ARGINSA; severe
- H388 (= H386) to Q: in ARGINSA; severe
- A398 (≠ C396) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
- R456 (≠ K454) to 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)
46% identity, 96% coverage: 13:454/459 of query aligns to 1:441/450 of 1k7wD
- active site: E71 (= E83), T144 (= T156), H145 (= H157), A266 (≠ S278), S267 (= S279), K272 (= K284), E279 (= E291)
- binding argininosuccinate: R98 (= R110), N99 (= N111), V102 (= V114), T144 (= T156), H145 (= H157), Y306 (= Y318), Q311 (= Q323), K314 (= K326)
1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
45% identity, 96% coverage: 15:454/459 of query aligns to 1:439/447 of 1hy0A
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
45% identity, 98% coverage: 4:454/459 of query aligns to 7:456/466 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)
44% identity, 94% coverage: 21:453/459 of query aligns to 8:441/454 of 6ienB
- binding argininosuccinate: S97 (= S109), R98 (= R110), N99 (= N111), T144 (= T156), H145 (= H157), S266 (= S278), S267 (= S279), M269 (= M281), K272 (= K284), Y306 (= Y318), Q311 (= Q323), K314 (= K326)
6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
44% identity, 94% coverage: 21:453/459 of query aligns to 8:439/452 of 6ienA
- binding argininosuccinate: R98 (= R110), N99 (= N111), V102 (= V114), T144 (= T156), H145 (= H157), Y304 (= Y318), Q309 (= Q323), K312 (= K326)
- binding fumaric acid: S266 (= S278), S267 (= S279), K270 (= K284), N272 (= N286)
6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
43% identity, 94% coverage: 21:453/459 of query aligns to 8:405/418 of 6ienC
- binding arginine: R98 (= R110), N99 (= N111), V102 (= V114), Y306 (= Y318), Q311 (= Q323), K314 (= K326)
- binding argininosuccinate: T144 (= T156), H145 (= H157), S266 (= S278), S267 (= S279), M269 (= M281), K272 (= K284)
- binding fumaric acid: S97 (= S109), R98 (= R110), N99 (= N111)
6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
35% identity, 87% coverage: 9:409/459 of query aligns to 6:405/497 of 6g3hA
6g3gA Crystal structure of edds lyase in complex with succinate (see paper)
35% identity, 87% coverage: 9:409/459 of query aligns to 6:405/497 of 6g3gA
6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
35% identity, 87% coverage: 9:409/459 of query aligns to 6:405/497 of 6g3fA
6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
35% identity, 87% coverage: 9:409/459 of query aligns to 6:405/496 of 6g3iA
Q9LCC6 Aspartate ammonia-lyase; Aspartase; EC 4.3.1.1 from Bacillus sp. (see 3 papers)
26% identity, 71% coverage: 50:376/459 of query aligns to 64:417/468 of Q9LCC6
- T101 (≠ E83) 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 (vs. gap) mutation to A: Retains full activity. Shows a slightly stronger affinity for L-aspartate. Does not affect tertiary structure.
- S140 (= S109) 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 (≠ R110) 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 (= N111) 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 (≠ M152) mutation to A: Loss of activity. Does not affect tertiary structure.
- T187 (= T156) 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 (= H157) 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 (= S278) mutation to A: Loss of activity.
- S319 (= S279) binding L-aspartate; mutation to A: Almost no change in catalytic efficiency.
- I320 (= I280) mutation to A: 50-fold decrease in catalytic efficiency.
- M321 (= M281) mutation to A: 338-fold decrease in catalytic efficiency.
- P322 (= P282) mutation to A: Almost no change in catalytic efficiency.
- K324 (= K284) 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 (= N286) 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.
3r6vG Crystal structure of aspartase from bacillus sp. Ym55-1 with bound l- aspartate (see paper)
26% identity, 71% coverage: 50:376/459 of query aligns to 61:414/463 of 3r6vG
3r6qA A triclinic-lattice structure of aspartase from bacillus sp. Ym55-1 (see paper)
26% identity, 71% coverage: 50:376/459 of query aligns to 60:413/462 of 3r6qA
4adlA Crystal structures of rv1098c in complex with malate (see paper)
25% identity, 73% coverage: 86:418/459 of query aligns to 101:453/459 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)
25% identity, 73% coverage: 86:418/459 of query aligns to 109:461/474 of P9WN93
- SSN 138:140 (≠ SRN 109:111) binding substrate
- T186 (= T156) binding substrate
- S318 (= S278) active site; mutation S->A,C: Absence of fumarase activity.
- S319 (= S279) binding substrate
- KVN 324:326 (≠ KKN 284:286) binding substrate
Sites not aligning to the query:
- 104:106 binding substrate
4apbD Crystal structure of mycobacterium tuberculosis fumarase (rv1098c) s318c in complex with fumarate (see paper)
25% identity, 73% coverage: 86:418/459 of query aligns to 101:453/462 of 4apbD
- active site: H179 (= H157), C310 (≠ S278), K316 (= K284), E323 (= E291)
- binding fumaric acid: S130 (= S109), S131 (≠ R110), N132 (= N111), T178 (= T156), H179 (= H157), C310 (≠ S278), S311 (= S279), M313 (= M281), K316 (= K284), N318 (= N286)
Sites not aligning to the query:
Query Sequence
>WP_013536905.1 NCBI__GCF_000185805.1:WP_013536905.1
MEKKLWGGRFKESTNKLVEQFTESVSYDKRLAPFDIAGSVAHVRMLAKQGILSKEEADRI
VEGLHKVLEEVESGKFEWKTELEDVHMNVEKRLTELVGPVGGKLHTGRSRNDQVATDVRL
YVRHEIEEVLKLLKELRRAFLKQAEEHIDVVMPGYTHLQIAQPVLYSHHMLAYYHMFKRD
EERFRDTLKRVNVSPLGSAALAGTSYPLDREFTAELLGFEGVTRNSMDAVSDRDFVAETI
FNCAMVMMHLSRLSEELIIWSTEEFGFIELPDAFCTGSSIMPQKKNPDVSELTRGKTGRV
YGDLMAILTILKGLPLTYNRDLQEDKEPLFDALDTVKMALKVNALVVAGMKPKAERMREQ
ARKGFSLATDLADYLAKKGMPFREAHRVVGELVAYCLDTGKELDQLTLEEFKRFSDLFGE
DVLSLMSVEGSVNSRNVIGGTAREQVLKEIERIKSEESF
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