SitesBLAST
Comparing WP_077278530.1 NCBI__GCF_002000365.1:WP_077278530.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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, 95% coverage: 20:462/467 of query aligns to 3:447/450 of 2e9fB
- active site: E71 (= E88), T146 (= T161), H147 (= H162), S268 (= S283), S269 (= S284), K274 (= K289), E281 (= E296)
- binding arginine: R98 (= R115), N99 (= N116), V102 (= V119), Y308 (= Y323), Q313 (= Q328), K316 (= K331)
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
49% identity, 96% coverage: 14:462/467 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)
43% identity, 100% coverage: 1:466/467 of query aligns to 1:465/468 of P24058
- W11 (= W11) 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 (= S29) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
- D33 (= D33) mutation to N: 99% decrease in catalytic efficiency.
- D89 (= D89) mutation to N: Loss of activity.
- N116 (= N116) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (= D117) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T161) 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 (= H162) mutation to E: Loss of activity.
- R238 (= R238) mutation to Q: Loss of activity.
- T281 (= T281) mutation to V: 80% decrease in catalytic efficiency.
- S283 (= S283) 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 (= N291) binding in chain B; mutation to L: Loss of activity.
- D293 (= D293) mutation to N: 99% decrease in catalytic efficiency.
- E296 (= E296) mutation to D: Loss of activity.
- Y323 (= Y323) binding in chain A
- K325 (= K325) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (= Q328) binding in chain A
- D330 (= D330) mutation to N: Loss of activity.
- K331 (= K331) 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)
46% identity, 97% coverage: 9:462/467 of query aligns to 7:459/464 of P04424
- R12 (= R14) to Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
- D31 (= D33) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
- K51 (≠ R53) mutation to N: 2-fold reduction in activity.
- K69 (≠ D71) modified: N6-acetyllysine
- E73 (≠ D75) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
- D87 (= D89) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
- H89 (= H91) mutation to Q: 10-fold reduction in activity.
- R94 (≠ A96) to C: in ARGINSA; severe; dbSNP:rs374304304
- R95 (= R97) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
- R113 (= R115) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (= D122) to E: in ARGINSA; severe
- V178 (≠ E180) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ E183) to S: in a breast cancer sample; somatic mutation
- R182 (= R184) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (= R188) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (= G202) to V: in a breast cancer sample; somatic mutation
- R236 (= R238) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (= D239) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (= Q288) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (= K290) 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 (= R299) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
- R306 (≠ N308) to W: in ARGINSA; severe; dbSNP:rs868834862
- Q326 (= Q328) to L: in ARGINSA; severe
- V335 (≠ T337) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- M360 (= M362) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- M382 (= M385) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- R385 (= R388) to L: in ARGINSA; severe
- H388 (= H391) to Q: in ARGINSA; severe
- A398 (≠ G401) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
- R456 (= R459) 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)
42% identity, 96% coverage: 18:466/467 of query aligns to 1:448/450 of 1k7wD
- active site: E71 (= E88), T144 (= T161), H145 (= H162), A266 (≠ S283), S267 (= S284), K272 (= K289), E279 (= E296)
- binding argininosuccinate: R98 (= R115), N99 (= N116), V102 (= V119), T144 (= T161), H145 (= H162), Y306 (= Y323), Q311 (= Q328), K314 (= K331)
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
42% identity, 99% coverage: 7:466/467 of query aligns to 5:463/466 of P02521
Sites not aligning to the query:
- 2 modified: Blocked amino end (Ala)
1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
41% identity, 96% coverage: 20:466/467 of query aligns to 1:446/447 of 1hy0A
6ienB Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
47% identity, 93% coverage: 25:457/467 of query aligns to 7:440/454 of 6ienB
- binding argininosuccinate: S97 (= S114), R98 (= R115), N99 (= N116), T144 (= T161), H145 (= H162), S266 (= S283), S267 (= S284), M269 (= M286), K272 (= K289), Y306 (= Y323), Q311 (= Q328), K314 (= K331)
6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
46% identity, 93% coverage: 25:457/467 of query aligns to 7:438/452 of 6ienA
- binding argininosuccinate: R98 (= R115), N99 (= N116), V102 (= V119), T144 (= T161), H145 (= H162), Y304 (= Y323), Q309 (= Q328), K312 (= K331)
- binding fumaric acid: S266 (= S283), S267 (= S284), K270 (= K289), N272 (= N291)
6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
44% identity, 93% coverage: 23:457/467 of query aligns to 5:404/418 of 6ienC
- binding arginine: R98 (= R115), N99 (= N116), V102 (= V119), Y306 (= Y323), Q311 (= Q328), K314 (= K331)
- binding argininosuccinate: T144 (= T161), H145 (= H162), S266 (= S283), S267 (= S284), M269 (= M286), K272 (= K289)
- binding fumaric acid: S97 (= S114), R98 (= R115), N99 (= N116)
6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
34% identity, 97% coverage: 14:467/467 of query aligns to 6:466/497 of 6g3hA
6g3gA Crystal structure of edds lyase in complex with succinate (see paper)
34% identity, 97% coverage: 14:467/467 of query aligns to 6:466/497 of 6g3gA
6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
34% identity, 97% coverage: 14:467/467 of query aligns to 6:466/497 of 6g3fA
6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
34% identity, 97% coverage: 14:467/467 of query aligns to 6:466/496 of 6g3iA
P12047 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; Glutamyl--tRNA ligase regulatory factor; EC 4.3.2.2 from Bacillus subtilis (strain 168) (see paper)
25% identity, 63% coverage: 100:394/467 of query aligns to 79:375/431 of P12047
- H89 (= H110) mutation to Q: Abolishes enzyme activity.
- H141 (= H162) mutation to Q: Abolishes enzyme activity.
- Q212 (≠ N230) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N291) mutation N->D,L: Abolishes enzyme activity.
- R301 (≠ K325) mutation R->K,Q: Abolishes enzyme activity.
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
25% identity, 67% coverage: 100:411/467 of query aligns to 78:391/427 of 2x75A
Sites not aligning to the query:
3r6vG Crystal structure of aspartase from bacillus sp. Ym55-1 with bound l- aspartate (see paper)
25% identity, 65% coverage: 109:411/467 of query aligns to 132:450/463 of 3r6vG
3r6qA A triclinic-lattice structure of aspartase from bacillus sp. Ym55-1 (see paper)
25% identity, 65% coverage: 109:411/467 of query aligns to 131:449/462 of 3r6qA
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)
26% identity, 65% coverage: 8:312/467 of query aligns to 19:347/467 of P05042
- R126 (≠ K107) binding ; mutation to A: 10-fold decrease of fumarase activity.
- K127 (= K108) mutation to D: No effect.
- H129 (= H110) 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 (≠ HTG- 110:112) binding in site B
- SSN 139:141 (≠ SRN 114:116) binding
- H188 (= H162) active site, Proton donor/acceptor; mutation to N: 200-fold decrease of fumarase activity.
- E315 (≠ F279) 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)
26% identity, 65% coverage: 8:312/467 of query aligns to 15:343/455 of 1fupA
Query Sequence
>WP_077278530.1 NCBI__GCF_002000365.1:WP_077278530.1
MSSTGNGDKLWGGRFAEATDAFVEAFTASVDFDQRLYRHDIEGSRAHARMLARVGVLTDD
ECRRIQEGLDDILADIERGDFAWLTELEDVHMNIEARLIERIGDTGKKLHTGRSRNDQVA
TDIRLYLREAIDALILEIRRLQAGLLDLAEREADTIMPGFTHLQTAQPVTFGHHMMAWFE
MLERDHARLQDCRRRVNVLPLGAAALAGTSYPLDRRYTAQLLGFDDVTDNSLDSVSDRDF
AIEFCAAGALIMTHLSRFSEELILWASAQFGFVDLPDRFCTGSSIMPQKKNPDVPELVRG
KTGRVNGNLVALLTLMKGQPLAYNKDNQEDKEPLFDTVDTLAGSLRAFADMVPHIQVRAE
TMREAASRGFATATDLADYLVRRGMPFRDAHEVVGKAVRHGVETGRDLGEMRLEELQGFS
KMIEADVFDVLTLEGSVAARNVHGGTAPEQVLARIRAARAELDKGKG
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