SitesBLAST
Comparing WP_010875908.1 NCBI__GCF_000008645.1:WP_010875908.1 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
42% identity, 95% coverage: 16:461/468 of query aligns to 6:445/450 of 2e9fB
- active site: E71 (= E80), T146 (= T153), H147 (= H154), S268 (= S275), S269 (= S276), K274 (= K281), E281 (= E288)
- binding arginine: R98 (= R107), N99 (= N108), V102 (= V111), Y308 (= Y315), Q313 (= Q320), K316 (≠ T323)
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
40% identity, 84% coverage: 7:398/468 of query aligns to 1:393/451 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)
35% identity, 100% coverage: 2:468/468 of query aligns to 9:466/468 of P24058
- W11 (≠ R4) 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 (= S22) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
- D33 (= D26) mutation to N: 99% decrease in catalytic efficiency.
- D89 (= D81) mutation to N: Loss of activity.
- N116 (= N108) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (= D109) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T153) 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 (= H154) mutation to E: Loss of activity.
- R238 (= R230) mutation to Q: Loss of activity.
- T281 (≠ S273) mutation to V: 80% decrease in catalytic efficiency.
- S283 (= S275) 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 (= N283) binding in chain B; mutation to L: Loss of activity.
- D293 (= D285) mutation to N: 99% decrease in catalytic efficiency.
- E296 (= E288) mutation to D: Loss of activity.
- Y323 (= Y315) binding in chain A
- K325 (≠ R317) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (= Q320) binding in chain A
- D330 (≠ V322) mutation to N: Loss of activity.
- K331 (≠ T323) binding in chain A; mutation to Q: Loss of activity.
1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
35% identity, 96% coverage: 18:468/468 of query aligns to 8:449/450 of 1k7wD
- active site: E71 (= E80), T144 (= T153), H145 (= H154), A266 (≠ S275), S267 (= S276), K272 (= K281), E279 (= E288)
- binding argininosuccinate: R98 (= R107), N99 (= N108), V102 (= V111), T144 (= T153), H145 (= H154), Y306 (= Y315), Q311 (= Q320), K314 (≠ T323)
P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
34% identity, 100% coverage: 2:467/468 of query aligns to 7:463/464 of P04424
- R12 (= R7) to Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
- D31 (= D26) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
- K51 (≠ H46) mutation to N: 2-fold reduction in activity.
- K69 (≠ S64) modified: N6-acetyllysine
- E73 (= E68) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
- D87 (= D81) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
- H89 (= H83) mutation to Q: 10-fold reduction in activity.
- R94 (≠ N88) to C: in ARGINSA; severe; dbSNP:rs374304304
- R95 (≠ Y89) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
- R113 (= R107) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (= D114) to E: in ARGINSA; severe
- V178 (≠ S172) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ R175) to S: in a breast cancer sample; somatic mutation
- R182 (= R176) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (= R180) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (= G194) to V: in a breast cancer sample; somatic mutation
- R236 (= R230) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (= D231) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (= Q280) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (= K282) 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 (= R291) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
- R306 (≠ E300) to W: in ARGINSA; severe; dbSNP:rs868834862
- Q326 (= Q320) to L: in ARGINSA; severe
- V335 (≠ A329) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- M360 (≠ A354) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- M382 (≠ I378) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- R385 (= R381) to L: in ARGINSA; severe
- H388 (= H384) to Q: in ARGINSA; severe
- A398 (= A394) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
- R456 (≠ K460) to W: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs759396688
6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
34% identity, 99% coverage: 4:467/468 of query aligns to 6:465/497 of 6g3hA
6g3gA Crystal structure of edds lyase in complex with succinate (see paper)
34% identity, 99% coverage: 4:467/468 of query aligns to 6:465/497 of 6g3gA
6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
34% identity, 99% coverage: 4:467/468 of query aligns to 6:465/497 of 6g3fA
6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
34% identity, 99% coverage: 4:467/468 of query aligns to 6:465/496 of 6g3iA
1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
35% identity, 96% coverage: 19:468/468 of query aligns to 7:447/447 of 1hy0A
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
34% identity, 96% coverage: 19:468/468 of query aligns to 24:464/466 of P02521
Sites not aligning to the query:
- 2 modified: Blocked amino end (Ala)
6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
40% identity, 84% coverage: 14:404/468 of query aligns to 3:398/418 of 6ienC
- binding arginine: R98 (= R107), N99 (= N108), V102 (= V111), Y306 (= Y315), Q311 (= Q320), K314 (≠ T323)
- binding argininosuccinate: T144 (= T153), H145 (= H154), S266 (= S275), S267 (= S276), M269 (= M278), K272 (= K281)
- binding fumaric acid: S97 (= S106), R98 (= R107), N99 (= N108)
6ienB Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
40% identity, 79% coverage: 14:384/468 of query aligns to 3:374/454 of 6ienB
- binding argininosuccinate: S97 (= S106), R98 (= R107), N99 (= N108), T144 (= T153), H145 (= H154), S266 (= S275), S267 (= S276), M269 (= M278), K272 (= K281), Y306 (= Y315), Q311 (= Q320), K314 (≠ T323)
6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
40% identity, 79% coverage: 14:384/468 of query aligns to 3:372/452 of 6ienA
- binding argininosuccinate: R98 (= R107), N99 (= N108), V102 (= V111), T144 (= T153), H145 (= H154), Y304 (= Y315), Q309 (= Q320), K312 (≠ T323)
- binding fumaric acid: S266 (= S275), S267 (= S276), K270 (= K281), N272 (= N283)
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, 64% coverage: 21:319/468 of query aligns to 11:303/431 of P12047
- H89 (= H102) mutation to Q: Abolishes enzyme activity.
- H141 (= H154) mutation to Q: Abolishes enzyme activity.
- Q212 (≠ M224) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N283) mutation N->D,L: Abolishes enzyme activity.
- R301 (= R317) mutation R->K,Q: Abolishes enzyme activity.
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
24% identity, 66% coverage: 12:319/468 of query aligns to 1:302/427 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)
26% identity, 54% coverage: 34:288/468 of query aligns to 24:275/431 of Q9X0I0
- H141 (= H154) active site, Proton donor/acceptor
4adlA Crystal structures of rv1098c in complex with malate (see paper)
30% identity, 43% coverage: 88:288/468 of query aligns to 105:323/459 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)
30% identity, 43% coverage: 88:288/468 of query aligns to 113:331/474 of P9WN93
- SSN 138:140 (≠ SRN 106:108) binding substrate
- T186 (= T153) binding substrate
- S318 (= S275) active site; mutation S->A,C: Absence of fumarase activity.
- S319 (= S276) binding substrate
- KVN 324:326 (≠ KKN 281:283) binding substrate
Sites not aligning to the query:
- 104:106 binding substrate
Q9ZCQ4 Fumarate hydratase class II; Fumarase C; Aerobic fumarase; Iron-independent fumarase; EC 4.2.1.2 from Rickettsia prowazekii (strain Madrid E) (see paper)
27% identity, 44% coverage: 101:304/468 of query aligns to 134:347/461 of Q9ZCQ4
Sites not aligning to the query:
Query Sequence
>WP_010875908.1 NCBI__GCF_000008645.1:WP_010875908.1
MNLRAGRLNSGMEDEAAEFTSSLTFDHHIFEADIECNMAHTRMLAHEGIIPEEVAAKIID
ALESLREEGIEALDMDPSVEDIHMAVENYVTARIGEEAGFMHTGKSRNDQVATDLRLALR
ERIRTISRELLDFIDSISDLALDHTETVMVGYTHLQHAQPTTLGHHLMAYASSLRRDYER
LQDTLKRVDQNPLGSAAMTTTSFPINRELTTRLLGFSDYMKNSMDAVSARDFIAETVFDL
SMLAVNLSRISEEMILWSTHEFGIVEIPDEFSSTSSIMPQKKNPDVAEIARAKTSTVQGE
LVTILGIMKALPYTYNRDLQEVTPHLWRAVDTVLSMIRVVRGMLLGIRVNRNRALELAGA
NFATATDLADIIVRERGIPFRVAHRIVGRLVTRAIEDGLAPGDVDSVYLDEVSLEVTGRK
LELDPELVEKALDPLENVRMRRIPGGPAPEMVRVAVEEMKSFIESERK
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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