SitesBLAST
Comparing WP_012505623.1 NCBI__GCF_000020625.1:WP_012505623.1 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
44% identity, 95% coverage: 24:460/460 of query aligns to 9:447/450 of 2e9fB
- active site: E71 (= E86), T146 (= T159), H147 (= H160), S268 (= S281), S269 (= S282), K274 (= K287), E281 (= E294)
- binding arginine: R98 (= R113), N99 (= N114), V102 (= V117), Y308 (= Y321), Q313 (= Q326), K316 (= K329)
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
41% identity, 98% coverage: 12:460/460 of query aligns to 1:450/451 of 1tj7B
P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
41% identity, 99% coverage: 1:457/460 of query aligns to 1:456/464 of P04424
- R12 (= R12) to Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
- D31 (= D31) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
- K51 (≠ E51) mutation to N: 2-fold reduction in activity.
- K69 (≠ E69) modified: N6-acetyllysine
- E73 (= E73) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
- D87 (= D87) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
- H89 (= H89) mutation to Q: 10-fold reduction in activity.
- R94 (≠ N94) to C: in ARGINSA; severe; dbSNP:rs374304304
- R95 (= R95) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
- R113 (= R113) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (= D120) to E: in ARGINSA; severe
- V178 (≠ N178) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ D181) to S: in a breast cancer sample; somatic mutation
- R182 (= R182) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (= R186) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (= G200) to V: in a breast cancer sample; somatic mutation
- R236 (= R236) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (= D237) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (= Q286) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (= K288) 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 (= R297) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
- R306 (≠ D306) to W: in ARGINSA; severe; dbSNP:rs868834862
- Q326 (= Q326) to L: in ARGINSA; severe
- V335 (≠ A335) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- M360 (≠ L360) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- M382 (= M383) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- R385 (= R386) to L: in ARGINSA; severe
- H388 (= H389) to Q: in ARGINSA; severe
- A398 (≠ V399) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
- R456 (= R457) to W: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs759396688
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: 8:457/460 of query aligns to 10:458/468 of P24058
- W11 (= W9) 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 (= S27) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
- D33 (= D31) mutation to N: 99% decrease in catalytic efficiency.
- D89 (= D87) mutation to N: Loss of activity.
- N116 (= N114) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (= D115) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T159) 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 (= H160) mutation to E: Loss of activity.
- R238 (= R236) mutation to Q: Loss of activity.
- T281 (= T279) mutation to V: 80% decrease in catalytic efficiency.
- S283 (= S281) 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 (= N289) binding in chain B; mutation to L: Loss of activity.
- D293 (= D291) mutation to N: 99% decrease in catalytic efficiency.
- E296 (= E294) mutation to D: Loss of activity.
- Y323 (= Y321) binding in chain A
- K325 (≠ R323) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (= Q326) binding in chain A
- D330 (= D328) mutation to N: Loss of activity.
- K331 (= K329) binding in chain A; mutation to Q: Loss of activity.
1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
42% identity, 95% coverage: 23:457/460 of query aligns to 6:439/447 of 1hy0A
1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
43% identity, 94% coverage: 24:457/460 of query aligns to 9:441/450 of 1k7wD
- active site: E71 (= E86), T144 (= T159), H145 (= H160), A266 (≠ S281), S267 (= S282), K272 (= K287), E279 (= E294)
- binding argininosuccinate: R98 (= R113), N99 (= N114), V102 (= V117), T144 (= T159), H145 (= H160), Y306 (= Y321), Q311 (= Q326), K314 (= K329)
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
40% identity, 98% coverage: 1:453/460 of query aligns to 1:452/466 of P02521
- A2 (≠ S2) modified: Blocked amino end (Ala)
6ienB Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
37% identity, 93% coverage: 24:453/460 of query aligns to 8:438/454 of 6ienB
- binding argininosuccinate: S97 (= S112), R98 (= R113), N99 (= N114), T144 (= T159), H145 (= H160), S266 (= S281), S267 (= S282), M269 (= M284), K272 (= K287), Y306 (= Y321), Q311 (= Q326), K314 (= K329)
6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
36% identity, 93% coverage: 24:453/460 of query aligns to 8:436/452 of 6ienA
- binding argininosuccinate: R98 (= R113), N99 (= N114), V102 (= V117), T144 (= T159), H145 (= H160), Y304 (= Y321), Q309 (= Q326), K312 (= K329)
- binding fumaric acid: S266 (= S281), S267 (= S282), K270 (= K287), N272 (= N289)
6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
38% identity, 85% coverage: 16:405/460 of query aligns to 1:394/418 of 6ienC
- binding arginine: R98 (= R113), N99 (= N114), V102 (= V117), Y306 (= Y321), Q311 (= Q326), K314 (= K329)
- binding argininosuccinate: T144 (= T159), H145 (= H160), S266 (= S281), S267 (= S282), M269 (= M284), K272 (= K287)
- binding fumaric acid: S97 (= S112), R98 (= R113), N99 (= N114)
6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
31% identity, 95% coverage: 17:453/460 of query aligns to 24:454/496 of 6g3iA
Sites not aligning to the query:
6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
31% identity, 95% coverage: 17:453/460 of query aligns to 24:454/497 of 6g3hA
Sites not aligning to the query:
6g3gA Crystal structure of edds lyase in complex with succinate (see paper)
31% identity, 95% coverage: 17:453/460 of query aligns to 24:454/497 of 6g3gA
6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
31% identity, 95% coverage: 17:453/460 of query aligns to 24:454/497 of 6g3fA
3r6qA A triclinic-lattice structure of aspartase from bacillus sp. Ym55-1 (see paper)
25% identity, 74% coverage: 91:431/460 of query aligns to 106:452/462 of 3r6qA
3r6vG Crystal structure of aspartase from bacillus sp. Ym55-1 with bound l- aspartate (see paper)
25% identity, 74% coverage: 91:431/460 of query aligns to 107:453/463 of 3r6vG
Q9LCC6 Aspartate ammonia-lyase; Aspartase; EC 4.3.1.1 from Bacillus sp. (see 3 papers)
25% identity, 74% coverage: 91:431/460 of query aligns to 110:456/468 of Q9LCC6
- H134 (vs. gap) mutation to A: Retains full activity. Shows a slightly stronger affinity for L-aspartate. Does not affect tertiary structure.
- S140 (= S112) 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 (≠ R113) 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 (= N114) 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 (≠ I155) mutation to A: Loss of activity. Does not affect tertiary structure.
- T187 (= T159) 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 (= H160) 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 (= S281) mutation to A: Loss of activity.
- S319 (= S282) binding L-aspartate; mutation to A: Almost no change in catalytic efficiency.
- I320 (= I283) mutation to A: 50-fold decrease in catalytic efficiency.
- M321 (= M284) mutation to A: 338-fold decrease in catalytic efficiency.
- P322 (= P285) mutation to A: Almost no change in catalytic efficiency.
- K324 (= K287) 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 (= N289) 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.
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
22% identity, 82% coverage: 15:389/460 of query aligns to 2:371/427 of 2x75A
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)
24% identity, 65% coverage: 98:394/460 of query aligns to 75:377/431 of Q9X0I0
- H141 (= H160) active site, Proton donor/acceptor
3oceA Crystal structure of fumarate lyase:delta crystallin from brucella melitensis bound to cobalt
29% identity, 48% coverage: 87:306/460 of query aligns to 105:342/461 of 3oceA
Query Sequence
>WP_012505623.1 NCBI__GCF_000020625.1:WP_012505623.1
MSKKKELLWQSRFSEPFDREALLFSSSVDVDKELYQEDITGSIAHVTMLSEEAIIPAEEA
RLIIEGLQEIEEEISTGSLVPHWEDEDIHTVIENRLKEKIGPIAGKIHSGRSRNDQVATD
TRLYLKRSIEEIRQALKELKTVLVDKAEAYRRTIIFGYTHLQRAQPISAGHYYLAYFNMF
DRDNQRLQDLYKRVDISPLGAAAFAGSTLALNAERSRDLLEFEGLFHNSIDAVSDRDIII
EFVSACSIIMMHLSRFAEDLILWSSYEFNYLEISDAFATGSSIMPQKKNADIAELVRGKT
GRVYGDLMAMLTIMKGLPLSYNRDMQEDKPPLFDASKTTRSSVRIFTKMLENTSIKENRL
SSLVAKDLSLATEIAEYLVQKNMPFRDAHRVTGKIVSHVIESGTTLPDMTLETYRTFSDL
FDEDLYDALKPEASVNAKKTHGSTSFASVEEQIVSARTRI
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