SitesBLAST
Comparing WP_005456097.1 NCBI__GCF_000244975.1:WP_005456097.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 19 hits to proteins with known functional sites (download)
6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
32% identity, 85% coverage: 29:443/487 of query aligns to 41:451/497 of 6g3hA
Sites not aligning to the query:
6g3gA Crystal structure of edds lyase in complex with succinate (see paper)
32% identity, 85% coverage: 29:443/487 of query aligns to 41:451/497 of 6g3gA
6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
32% identity, 85% coverage: 29:443/487 of query aligns to 41:451/497 of 6g3fA
6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
32% identity, 85% coverage: 29:443/487 of query aligns to 41:451/496 of 6g3iA
Sites not aligning to the query:
2e9fB Crystal structure of t.Th.Hb8 argininosuccinate lyase complexed with l-arginine
34% identity, 75% coverage: 23:387/487 of query aligns to 19:385/450 of 2e9fB
- active site: E71 (= E74), T146 (= T149), H147 (= H150), S268 (= S269), S269 (= S270), K274 (= K275), E281 (= E282)
- binding arginine: R98 (= R103), N99 (= N104), V102 (≠ D107), Y308 (≠ W306), Q313 (≠ N311), K316 (≠ T314)
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
30% identity, 67% coverage: 68:392/487 of query aligns to 70:397/451 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)
27% identity, 74% coverage: 28:388/487 of query aligns to 41:400/468 of P24058
- D89 (= D75) mutation to N: Loss of activity.
- N116 (= N104) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (= D105) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T149) 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 (= H150) mutation to E: Loss of activity.
- R238 (≠ A226) mutation to Q: Loss of activity.
- T281 (≠ Q267) mutation to V: 80% decrease in catalytic efficiency.
- S283 (= S269) 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 (= N277) binding in chain B; mutation to L: Loss of activity.
- D293 (≠ V279) mutation to N: 99% decrease in catalytic efficiency.
- E296 (= E282) mutation to D: Loss of activity.
- Y323 (≠ S310) binding in chain A
- K325 (≠ N312) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (≠ T315) binding in chain A
- D330 (≠ V317) mutation to N: Loss of activity.
- K331 (≠ Q318) 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.
6ienB Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
33% identity, 72% coverage: 28:378/487 of query aligns to 23:374/454 of 6ienB
- binding argininosuccinate: S97 (= S102), R98 (= R103), N99 (= N104), T144 (= T149), H145 (= H150), S266 (= S269), S267 (= S270), M269 (= M272), K272 (= K275), Y306 (≠ D309), Q311 (≠ T314), K314 (≠ Q318)
6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
33% identity, 73% coverage: 28:381/487 of query aligns to 23:377/418 of 6ienC
- binding arginine: R98 (= R103), N99 (= N104), V102 (≠ D107), Y306 (≠ D309), Q311 (≠ T314), K314 (≠ Q318)
- binding argininosuccinate: T144 (= T149), H145 (= H150), S266 (= S269), S267 (= S270), M269 (= M272), K272 (= K275)
- binding fumaric acid: S97 (= S102), R98 (= R103), N99 (= N104)
1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
27% identity, 74% coverage: 28:388/487 of query aligns to 24:383/450 of 1k7wD
- active site: E71 (= E74), T144 (= T149), H145 (= H150), A266 (≠ S269), S267 (= S270), K272 (= K275), E279 (= E282)
- binding argininosuccinate: R98 (= R103), N99 (= N104), V102 (≠ D107), T144 (= T149), H145 (= H150), Y306 (≠ S310), Q311 (≠ T315), K314 (≠ Q318)
P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
27% identity, 75% coverage: 22:388/487 of query aligns to 33:398/464 of P04424
- K51 (≠ E40) mutation to N: 2-fold reduction in activity.
- K69 (≠ E58) modified: N6-acetyllysine
- E73 (≠ A62) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
- D87 (= D75) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
- H89 (≠ Y77) mutation to Q: 10-fold reduction in activity.
- R94 (≠ Q82) to C: in ARGINSA; severe; dbSNP:rs374304304
- R95 (= R83) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
- R113 (= R103) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (≠ V110) to E: in ARGINSA; severe
- V178 (≠ E168) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ L171) to S: in a breast cancer sample; somatic mutation
- R182 (≠ S172) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (≠ E176) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (= G190) to V: in a breast cancer sample; somatic mutation
- R236 (≠ A226) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (≠ E227) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (= Q274) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (= K276) 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 (≠ C285) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
- R306 (≠ A291) to W: in ARGINSA; severe; dbSNP:rs868834862
- Q326 (≠ T315) to L: in ARGINSA; severe
- V335 (≠ A324) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- M360 (≠ P350) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- M382 (≠ V372) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- R385 (= R375) to L: in ARGINSA; severe
- H388 (= H378) to Q: in ARGINSA; severe
- A398 (= A388) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
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
- 456 R → W: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs759396688
1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
27% identity, 74% coverage: 28:388/487 of query aligns to 22:381/447 of 1hy0A
6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
33% identity, 72% coverage: 28:378/487 of query aligns to 23:372/452 of 6ienA
- binding argininosuccinate: R98 (= R103), N99 (= N104), V102 (≠ D107), T144 (= T149), H145 (= H150), Y304 (≠ D309), Q309 (≠ T314), K312 (≠ Q318)
- binding fumaric acid: S266 (= S269), S267 (= S270), K270 (= K275), N272 (= N277)
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
29% identity, 56% coverage: 28:299/487 of query aligns to 39:311/466 of P02521
Sites not aligning to the query:
- 2 modified: Blocked amino end (Ala)
Q05911 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
24% identity, 36% coverage: 134:308/487 of query aligns to 140:325/482 of Q05911
- K196 (≠ G190) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
5nxaB Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
24% identity, 52% coverage: 137:388/487 of query aligns to 77:341/415 of 5nxaB
- active site: T89 (= T149), H90 (= H150), S221 (= S270), K226 (= K275), E233 (= E282)
- binding aminoimidazole 4-carboxamide ribonucleotide: M230 (≠ V279), R234 (≠ H283)
- binding fumaric acid: S220 (= S269), S221 (= S270), M223 (= M272), K226 (= K275), N228 (= N277)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: T89 (= T149), H90 (= H150), Q172 (≠ A226), L262 (vs. gap), S265 (= S310), A266 (≠ N311), R269 (≠ T314)
Sites not aligning to the query:
5nx9D Crystal structure of neanderthal adenylosuccinate lyase (adsl) in complex with its products amp and fumarate (see paper)
24% identity, 52% coverage: 137:388/487 of query aligns to 139:403/477 of 5nx9D
- active site: T151 (= T149), H152 (= H150), S283 (= S270), K288 (= K275), E295 (= E282)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: T151 (= T149), H152 (= H150)
- binding adenosine monophosphate: Q234 (≠ A226), R296 (≠ H283), L324 (vs. gap), S327 (= S310), A328 (≠ N311), R331 (≠ T314)
- binding fumaric acid: Q234 (≠ A226), S282 (= S269), S283 (= S270), K288 (= K275)
Sites not aligning to the query:
7c18B Crystal structure of fumarasec from mannheimia succiniciproducens in complex with fumarate
26% identity, 42% coverage: 83:288/487 of query aligns to 121:337/464 of 7c18B
Sites not aligning to the query:
P30566 Adenylosuccinate lyase; ADSL; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Homo sapiens (Human) (see 13 papers)
24% identity, 52% coverage: 137:388/487 of query aligns to 146:410/484 of P30566
- H159 (= H150) active site, Proton donor/acceptor
- R190 (≠ Y181) to Q: in ADSLD; moderate; dbSNP:rs28941471
- R194 (≠ N185) to C: in ADSLD; severe; reduces protein stability; dbSNP:rs1465152683
- K246 (≠ R231) to E: in ADSLD; moderate; strongly reduced catalytic activity; dbSNP:rs119450944
- D268 (= D252) to N: in ADSLD; severe; total loss of activity; dbSNP:rs746501563
- S289 (= S269) active site, Proton donor/acceptor
- R303 (≠ H283) to C: in ADSLD; mild; strongly reduced activity with SAMP, but only slightly reduced activity with SAICAR; abolishes cooperativity; dbSNP:rs373458753
- L311 (≠ A291) to V: in ADSLD; severe; slightly reduced enzyme activity; dbSNP:rs2044791112
- P318 (≠ T298) to L: in ADSLD; severe; dbSNP:rs202064195
- V364 (≠ T340) to M: in ADSLD; severe; dbSNP:rs370851726
- R374 (≠ P350) to W: in ADSLD; severe; dbSNP:rs376533026
- S395 (≠ P373) to R: in ADSLD; severe
- R396 (≠ W374) to C: in ADSLD; severe; abolishes cooperativity and reduces enzyme activity; dbSNP:rs755492501; to H: in ADSLD; severe; abolishes cooperativity and reduces enzyme activity; dbSNP:rs763542069
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine; A → V: in ADSLD; severe; dbSNP:rs143083947
- 3 A → V: in ADSLD; severe
- 26 M → L: in ADSLD; severe; dbSNP:rs1311171245
- 72 I → V: in ADSLD; severe
- 100 P → A: in ADSLD; moderate; dbSNP:rs119450942
- 114 Y → H: in ADSLD; severe; total loss of activity; dbSNP:rs374259530
- 141 R → W: in ADSLD; severe; dbSNP:rs756210458
- 422 D → Y: in ADSLD; moderate; dbSNP:rs119450943
- 423 L → V: in ADSLD; moderate
- 426 R → H: in ADSLD; severe; most frequent mutation; dbSNP:rs119450941
- 430 D → N: in ADSLD; mild; dbSNP:rs554254383
- 438 S → P: in ADSLD; severe; dbSNP:rs119450940
- 447 S → P: in ADSLD; severe; dbSNP:rs777821034
- 450 T → S: in ADSLD; moderate; dbSNP:rs372895468
- 452 R → P: in ADSLD; severe; dbSNP:rs775671027
Query Sequence
>WP_005456097.1 NCBI__GCF_000244975.1:WP_005456097.1
MPKLSTYWQNHLRVAFEESAPQLYRPMLQASLAHVVMLAEQGLLPGERARALLGGLRELL
SAPDDRLVFDGSVEDVYYLVEQRLAEAAGVQRSELDVQLARSRNDLDAGVFRMVLRENVL
EQARLACAAAEVAAAQADRHADVLIVGYTHRRPAQPTTLGHVLAGYAEALLSQAGELLSV
YDELNVSPLGSCAFAGTDLPIAPDRLTELLGFRETFTSSYEAVAGAEHLVRTAAVQARIL
ASGARMARTMLDWMTFRWIVTPDSYCQGSSIMPQKKNPVVLEHMCSMAGAAAADLAATVN
NVGAAWYEDSNNATTDVQQHLWRAGDRAVRFLTLMHGLLTEITPLEPPAPEEVVATGATT
TAVAEALAAAGVPWRGAHSVVGALVRQAPPAEWTTELVAKAITEAGLGEADDAVVEAALA
AGLRPQQVLDRPQPGGPGTEAVRRTAQRVTERAGTLTTEFDSRRTELRRAEDALTSAVDA
VLAGDRR
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