SitesBLAST
Comparing WP_011426996.1 NCBI__GCF_000092045.1:WP_011426996.1 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
49% identity, 94% coverage: 22:460/467 of query aligns to 1:440/450 of 2e9fB
- active site: E71 (= E92), T146 (= T165), H147 (= H166), S268 (= S287), S269 (= S288), K274 (= K293), E281 (= E300)
- binding arginine: R98 (= R119), N99 (= N120), V102 (= V123), Y308 (= Y327), Q313 (= Q332), K316 (= K335)
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
45% identity, 96% coverage: 18:466/467 of query aligns to 1:449/451 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, 97% coverage: 12:464/467 of query aligns to 8:458/468 of P24058
- W11 (= W15) 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 (= S33) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
- D33 (= D37) mutation to N: 99% decrease in catalytic efficiency.
- D89 (= D93) mutation to N: Loss of activity.
- N116 (= N120) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (= D121) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T165) 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 (= H166) mutation to E: Loss of activity.
- R238 (= R242) mutation to Q: Loss of activity.
- T281 (= T285) mutation to V: 80% decrease in catalytic efficiency.
- S283 (= S287) 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 (= N295) binding in chain B; mutation to L: Loss of activity.
- D293 (= D297) mutation to N: 99% decrease in catalytic efficiency.
- E296 (= E300) mutation to D: Loss of activity.
- Y323 (= Y327) binding in chain A
- K325 (= K329) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (= Q332) binding in chain A
- D330 (= D334) mutation to N: Loss of activity.
- K331 (= K335) 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)
42% identity, 96% coverage: 11:460/467 of query aligns to 5:452/464 of P04424
- R12 (= R18) to Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
- D31 (= D37) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
- K51 (≠ H57) mutation to N: 2-fold reduction in activity.
- K69 (≠ T75) modified: N6-acetyllysine
- E73 (= E79) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
- D87 (= D93) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
- H89 (= H95) mutation to Q: 10-fold reduction in activity.
- R94 (≠ A100) to C: in ARGINSA; severe; dbSNP:rs374304304
- R95 (= R101) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
- R113 (= R119) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (= D126) to E: in ARGINSA; severe
- V178 (≠ E184) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ G187) to S: in a breast cancer sample; somatic mutation
- R182 (= R188) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (= R192) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (= G206) to V: in a breast cancer sample; somatic mutation
- R236 (= R242) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (= D243) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (= Q292) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (= K294) 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 (= R303) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
- R306 (≠ S312) to W: in ARGINSA; severe; dbSNP:rs868834862
- Q326 (= Q332) to L: in ARGINSA; severe
- V335 (≠ A341) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- M360 (= M366) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- M382 (≠ L390) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- R385 (= R393) to L: in ARGINSA; severe
- H388 (= H396) to Q: in ARGINSA; severe
- A398 (= A406) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
Sites not aligning to the query:
- 456 R → 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)
43% identity, 94% coverage: 24:464/467 of query aligns to 3:441/450 of 1k7wD
- active site: E71 (= E92), T144 (= T165), H145 (= H166), A266 (≠ S287), S267 (= S288), K272 (= K293), E279 (= E300)
- binding argininosuccinate: R98 (= R119), N99 (= N120), V102 (= V123), T144 (= T165), H145 (= H166), Y306 (= Y327), Q311 (= Q332), K314 (= K335)
1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
41% identity, 94% coverage: 24:464/467 of query aligns to 1:439/447 of 1hy0A
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
40% identity, 97% coverage: 12:464/467 of query aligns to 6:456/466 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)
42% identity, 94% coverage: 23:460/467 of query aligns to 1:438/454 of 6ienB
- binding argininosuccinate: S97 (= S118), R98 (= R119), N99 (= N120), T144 (= T165), H145 (= H166), S266 (= S287), S267 (= S288), M269 (= M290), K272 (= K293), Y306 (= Y327), Q311 (= Q332), K314 (= K335)
6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
42% identity, 94% coverage: 23:460/467 of query aligns to 1:436/452 of 6ienA
- binding argininosuccinate: R98 (= R119), N99 (= N120), V102 (= V123), T144 (= T165), H145 (= H166), Y304 (= Y327), Q309 (= Q332), K312 (= K335)
- binding fumaric acid: S266 (= S287), S267 (= S288), K270 (= K293), N272 (= N295)
6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
39% identity, 94% coverage: 23:460/467 of query aligns to 1:402/418 of 6ienC
- binding arginine: R98 (= R119), N99 (= N120), V102 (= V123), Y306 (= Y327), Q311 (= Q332), K314 (= K335)
- binding argininosuccinate: T144 (= T165), H145 (= H166), S266 (= S287), S267 (= S288), M269 (= M290), K272 (= K293)
- binding fumaric acid: S97 (= S118), R98 (= R119), N99 (= N120)
6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
34% identity, 92% coverage: 32:460/467 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)
34% identity, 92% coverage: 32:460/467 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)
34% identity, 92% coverage: 32:460/467 of query aligns to 27:454/497 of 6g3gA
6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
34% identity, 92% coverage: 32:460/467 of query aligns to 27:454/497 of 6g3fA
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)
28% identity, 51% coverage: 163:401/467 of query aligns to 138:377/431 of Q9X0I0
- H141 (= H166) active site, Proton donor/acceptor
Q9LCC6 Aspartate ammonia-lyase; Aspartase; EC 4.3.1.1 from Bacillus sp. (see 3 papers)
26% identity, 43% coverage: 113:312/467 of query aligns to 135:343/468 of Q9LCC6
- S140 (= S118) 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 (≠ R119) 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 (= N120) 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 (≠ M161) mutation to A: Loss of activity. Does not affect tertiary structure.
- T187 (= T165) 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 (= H166) 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 (= S287) mutation to A: Loss of activity.
- S319 (= S288) binding L-aspartate; mutation to A: Almost no change in catalytic efficiency.
- I320 (= I289) mutation to A: 50-fold decrease in catalytic efficiency.
- M321 (= M290) mutation to A: 338-fold decrease in catalytic efficiency.
- P322 (= P291) mutation to A: Almost no change in catalytic efficiency.
- K324 (= K293) 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 (= N295) 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.
Sites not aligning to the query:
- 101 binding L-aspartate; T→A: 7100-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; T→S: 80-fold decrease in catalytic efficiency.
- 134 H→A: Retains full activity. Shows a slightly stronger affinity for L-aspartate. Does not affect tertiary structure.
3r6vG Crystal structure of aspartase from bacillus sp. Ym55-1 with bound l- aspartate (see paper)
26% identity, 43% coverage: 113:312/467 of query aligns to 132:340/463 of 3r6vG
3r6qA A triclinic-lattice structure of aspartase from bacillus sp. Ym55-1 (see paper)
26% identity, 43% coverage: 113:312/467 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)
26% identity, 50% coverage: 135:367/467 of query aligns to 106:342/431 of P12047
- H141 (= H166) mutation to Q: Abolishes enzyme activity.
- Q212 (≠ V239) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N295) mutation N->D,L: Abolishes enzyme activity.
- R301 (≠ K329) mutation R->K,Q: Abolishes enzyme activity.
Sites not aligning to the query:
- 89 H→Q: Abolishes enzyme activity.
3oceA Crystal structure of fumarate lyase:delta crystallin from brucella melitensis bound to cobalt
27% identity, 57% coverage: 113:380/467 of query aligns to 134:411/461 of 3oceA
Query Sequence
>WP_011426996.1 NCBI__GCF_000092045.1:WP_011426996.1
MAENNTDTKSSNQMWGGRFASGPDAIMEEINASIGFDKKLFAQDIRGSIAHATMLAHQGI
ISSDDKDKIVHGLNTILSEIESGNFEFSRQLEDIHMNVEARLATLIGPAAGRLHTARSRN
DQVALDFRLWVKEELQKTEQMLTGLIAAFLDRAEEHAESVMPGFTHLQTAQPVTFGHHCM
AYVEMFGRDRSRVRHAIEHLDESPIGAAALAGTGYPIDRHMTAKALGFREPTRNSIDTVS
DRDFAIEFLAIAAIAGMHLSRLAEEIVIWSTPQFGFVRLSDAFSTGSSIMPQKKNPDAAE
LVRAKTGRINGSLIALLTIMKGLPLAYSKDMQEDKEQVFDAAESLELAIAAMTGMVRDMT
VNTARMKAAAGSGFSTATDLADWLVREAGLPFRDAHHVTGRAVALAESKGCDLAELPLSD
LQAIHSAITDKVYDVLTVEASVASRKSFGGTAPSEVRKQIAFWRARN
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