SitesBLAST
Comparing WP_057508463.1 NCBI__GCF_001431535.1:WP_057508463.1 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)
A0A0K2JL82 Nitrosuccinate lyase; EC 4.3.99.5 from Streptomyces cremeus (see paper)
45% identity, 96% coverage: 13:446/451 of query aligns to 29:470/476 of A0A0K2JL82
- N93 (= N78) mutation to A: Slight decrease in activity.
- D125 (= D110) mutation D->N,V: Almost loss of activity.
- R137 (≠ Q122) binding
- R140 (≠ G125) binding
- R201 (≠ H186) binding
- H253 (= H229) mutation to A: Loss of activity.
- S302 (= S278) mutation to A: Loss of activity.
- K308 (= K284) binding ; mutation to A: Loss of activity.
- N310 (= N286) binding ; mutation to A: Loss of activity.
- R341 (= R317) mutation to A: Loss of activity.
5xnzA Crystal structure of cred complex with fumarate (see paper)
44% identity, 96% coverage: 13:446/451 of query aligns to 15:439/439 of 5xnzA
P12047 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; Glutamyl--tRNA ligase regulatory factor; EC 4.3.2.2 from Bacillus subtilis (strain 168) (see paper)
29% identity, 96% coverage: 12:443/451 of query aligns to 5:428/431 of P12047
- H89 (= H103) mutation to Q: Abolishes enzyme activity.
- H141 (≠ L155) mutation to Q: Abolishes enzyme activity.
- Q212 (≠ W228) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N286) mutation N->D,L: Abolishes enzyme activity.
- R301 (= R317) mutation R->K,Q: Abolishes enzyme activity.
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
28% identity, 94% coverage: 21:442/451 of query aligns to 13:423/427 of 2x75A
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)
26% identity, 98% coverage: 1:442/451 of query aligns to 1:427/431 of Q9X0I0
- H141 (≠ L155) active site, Proton donor/acceptor
4eeiB Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with amp and succinate
25% identity, 78% coverage: 96:446/451 of query aligns to 82:413/423 of 4eeiB
Sites not aligning to the query:
5hw2A Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with fumaric acid
25% identity, 78% coverage: 96:446/451 of query aligns to 82:409/419 of 5hw2A
Sites not aligning to the query:
1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
25% identity, 77% coverage: 14:361/451 of query aligns to 1:347/447 of 1hy0A
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, 58% coverage: 102:361/451 of query aligns to 109:366/468 of P24058
- N116 (≠ Q109) 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 (≠ L155) mutation to E: Loss of activity.
- R238 (= R232) mutation to Q: Loss of activity.
- T281 (≠ P270) 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 (≠ V288) mutation to N: 99% decrease in catalytic efficiency.
- E296 (≠ V291) mutation to D: Loss of activity.
- Y323 (≠ H315) binding in chain A
- K325 (≠ R317) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (≠ H323) binding in chain A
- D330 (≠ E325) mutation to N: Loss of activity.
- K331 (≠ W326) 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.
- 89 D→N: Loss of activity.
1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
27% identity, 58% coverage: 102:361/451 of query aligns to 92:349/450 of 1k7wD
- active site: T144 (= T154), H145 (≠ L155), A266 (≠ S278), S267 (= S279), K272 (= K284), E279 (≠ V291)
- binding argininosuccinate: R98 (≠ S108), N99 (≠ Q109), V102 (≠ I112), T144 (= T154), H145 (≠ L155), Y306 (≠ A318), Q311 (≠ H323), K314 (≠ W326)
Sites not aligning to the query:
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
27% identity, 68% coverage: 100:407/451 of query aligns to 95:399/451 of 1tj7B
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
24% identity, 80% coverage: 2:361/451 of query aligns to 3:364/466 of P02521
Sites not aligning to the query:
- 2 modified: Blocked amino end (Ala)
P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
28% identity, 58% coverage: 102:361/451 of query aligns to 107:364/464 of P04424
- R113 (≠ S108) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (≠ G115) to E: in ARGINSA; severe
- V178 (≠ D173) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ Q176) 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 (= R232) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (= D233) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (≠ H283) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (≠ R285) 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 (≠ I294) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
- R306 (vs. gap) to W: in ARGINSA; severe; dbSNP:rs868834862
- Q326 (≠ G320) to L: in ARGINSA; severe
- V335 (≠ I332) 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
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.
- 69 modified: N6-acetyllysine
- 73 E → K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
- 87 D → G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
- 89 H→Q: 10-fold reduction in activity.
- 94 R → C: in ARGINSA; severe; dbSNP:rs374304304
- 95 R → C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
- 382 M → R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- 385 R → L: in ARGINSA; severe
- 388 H → Q: in ARGINSA; severe
- 398 A → D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
- 456 R → W: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs759396688
Q05911 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
29% identity, 50% coverage: 98:322/451 of query aligns to 99:323/482 of Q05911
- K196 (≠ G195) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
1fuqA Fumarase with bound 3-trimethylsilylsuccinic acid (see paper)
28% identity, 49% coverage: 84:302/451 of query aligns to 118:339/456 of 1fuqA
- active site: T184 (= T154), H185 (≠ L155), S315 (= S278), K321 (= K284), E328 (≠ V291)
- binding citric acid: S136 (≠ T107), S137 (= S108), N138 (≠ Q109)
- binding 3-trimethylsilylsuccinic acid: R123 (≠ A89), H126 (≠ R92), P127 (≠ A93), N128 (≠ D94), D129 (= D95)
Sites not aligning to the query:
1fuoA FumarasE C with bound citrate (see paper)
28% identity, 49% coverage: 84:302/451 of query aligns to 118:339/456 of 1fuoA
Sites not aligning to the query:
P05042 Fumarate hydratase class II; Fumarase C; Aerobic fumarase; Iron-independent fumarase; EC 4.2.1.2 from Escherichia coli (strain K12) (see 4 papers)
28% identity, 49% coverage: 84:302/451 of query aligns to 121:342/467 of P05042
- R126 (≠ A89) binding ; mutation to A: 10-fold decrease of fumarase activity.
- K127 (≠ R90) mutation to D: No effect.
- H129 (≠ R92) mutation to N: No effect on fumarase activity and essentially same conformation compared to the wild-type, but appears to dramatically reduce binding of ligands at the B-site.
- HPND 129:132 (≠ RADD 92:95) binding in site B
- SSN 139:141 (≠ TSQ 107:109) binding
- H188 (≠ L155) active site, Proton donor/acceptor; mutation to N: 200-fold decrease of fumarase activity.
- E315 (≠ K275) mutation to Q: There is essentially no effect on the affinity values for both S-malate and fumarate. In contrast, the catalytic efficiency values have been lowered by 10-fold in both directions.
1fupA Fumarase with bound pyromellitic acid (see paper)
28% identity, 49% coverage: 84:302/451 of query aligns to 117:338/455 of 1fupA
Sites not aligning to the query:
7c18B Crystal structure of fumarasec from mannheimia succiniciproducens in complex with fumarate
31% identity, 41% coverage: 131:315/451 of query aligns to 164:355/464 of 7c18B
Sites not aligning to the query:
5vkwB Crystal structure of adenylosuccinate lyase ade13 from candida albicans
24% identity, 67% coverage: 98:399/451 of query aligns to 99:402/469 of 5vkwB
Sites not aligning to the query:
Query Sequence
>WP_057508463.1 NCBI__GCF_001431535.1:WP_057508463.1
MSETHSLLGALFGDPLVDAGFTDAARLQAMLDVERALACAQARCGVIPQTALPAIEAACH
AQLYDIAALAQATALAGNPAIPLVKALTARVRADDAEAARWVHWGATSQDIIDTGAVLQL
RQAVGQVQAKLQQLCSALAALAEAERDTGLPGRTLLQQAVPVTFGLKAAGWLDALQRSQQ
RLHALHADTLVLQFGGAAGTLASLQDRGLDVAQALAEELQLPLPALPWHAARDRIAELGS
VFALLVGSLGKIATDIVLLMQSEVAEAFEPAGEGKGGSSAMPHKRNPVGCVAAIAAATRV
PGLLSTLFSAMPQAHERAAGQWHAEWETVPEIVRLCAGSLAQVTVVVRGLQLDRERMQEH
LGSHGGLLYAEAVAVTLAEQIGKAAAHALVEQAAQQALAHARPLREVLQANPEVSRHLDS
AQLDALFAADSWRGMADTWIDRVLARVPHDA
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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