SitesBLAST
Comparing 199474 FitnessBrowser__MR1:199474 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)
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
66% identity, 98% coverage: 7:454/455 of query aligns to 1:448/451 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)
45% identity, 98% coverage: 3:449/455 of query aligns to 10:454/468 of P24058
- W11 (= W4) 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 (= D83) mutation to N: Loss of activity.
- N116 (= N110) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (= D111) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T155) 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 (= H156) mutation to E: Loss of activity.
- R238 (= R232) mutation to Q: Loss of activity.
- T281 (≠ S275) mutation to V: 80% decrease in catalytic efficiency.
- S283 (= S277) 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 (= N285) binding in chain B; mutation to L: Loss of activity.
- D293 (= D287) mutation to N: 99% decrease in catalytic efficiency.
- E296 (= E290) mutation to D: Loss of activity.
- Y323 (= Y317) binding in chain A
- K325 (= K319) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (= Q322) binding in chain A
- D330 (= D324) mutation to N: Loss of activity.
- K331 (= K325) 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)
44% identity, 99% coverage: 3:454/455 of query aligns to 8:457/464 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 (≠ S46) mutation to N: 2-fold reduction in activity.
- K69 (≠ E64) modified: N6-acetyllysine
- E73 (≠ V69) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
- D87 (= D83) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
- H89 (= H85) mutation to Q: 10-fold reduction in activity.
- R94 (≠ S90) to C: in ARGINSA; severe; dbSNP:rs374304304
- R95 (≠ A91) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
- R113 (= R109) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (= D116) to E: in ARGINSA; severe
- V178 (≠ E174) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ E177) to S: in a breast cancer sample; somatic mutation
- R182 (= R178) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (= R182) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (= G196) to V: in a breast cancer sample; somatic mutation
- R236 (= R232) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (= D233) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (= Q282) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (= K284) 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 (= R293) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
- R306 (≠ S302) to W: in ARGINSA; severe; dbSNP:rs868834862
- Q326 (= Q322) to L: in ARGINSA; severe
- V335 (= V331) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- M360 (≠ A356) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- M382 (= M379) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- R385 (= R382) to L: in ARGINSA; severe
- H388 (= H385) to Q: in ARGINSA; severe
- A398 (= A395) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
- R456 (≠ K453) to W: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs759396688
2e9fB Crystal structure of t.Th.Hb8 argininosuccinate lyase complexed with l-arginine
46% identity, 97% coverage: 14:453/455 of query aligns to 4:444/450 of 2e9fB
- active site: E71 (= E82), T146 (= T155), H147 (= H156), S268 (= S277), S269 (= S278), K274 (= K283), E281 (= E290)
- binding arginine: R98 (= R109), N99 (= N110), V102 (= V113), Y308 (= Y317), Q313 (= Q322), K316 (= K325)
1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
44% identity, 95% coverage: 15:447/455 of query aligns to 3:437/447 of 1hy0A
1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
44% identity, 96% coverage: 12:449/455 of query aligns to 2:437/450 of 1k7wD
- active site: E71 (= E82), T144 (= T155), H145 (= H156), A266 (≠ S277), S267 (= S278), K272 (= K283), E279 (= E290)
- binding argininosuccinate: R98 (= R109), N99 (= N110), V102 (= V113), T144 (= T155), H145 (= H156), Y306 (= Y317), Q311 (= Q322), K314 (= K325)
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
42% identity, 98% coverage: 3:449/455 of query aligns to 8:452/466 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)
40% identity, 94% coverage: 26:451/455 of query aligns to 15:440/454 of 6ienB
- binding argininosuccinate: S97 (= S108), R98 (= R109), N99 (= N110), T144 (= T155), H145 (= H156), S266 (= S277), S267 (= S278), M269 (= M280), K272 (= K283), Y306 (= Y317), Q311 (= Q322), K314 (= K325)
6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
39% identity, 94% coverage: 26:451/455 of query aligns to 15:438/452 of 6ienA
- binding argininosuccinate: R98 (= R109), N99 (= N110), V102 (= V113), T144 (= T155), H145 (= H156), Y304 (= Y317), Q309 (= Q322), K312 (= K325)
- binding fumaric acid: S266 (= S277), S267 (= S278), K270 (= K283), N272 (= N285)
6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
38% identity, 94% coverage: 26:451/455 of query aligns to 15:404/418 of 6ienC
- binding arginine: R98 (= R109), N99 (= N110), V102 (= V113), Y306 (= Y317), Q311 (= Q322), K314 (= K325)
- binding argininosuccinate: T144 (= T155), H145 (= H156), S266 (= S277), S267 (= S278), M269 (= M280), K272 (= K283)
- binding fumaric acid: S97 (= S108), R98 (= R109), N99 (= N110)
6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
32% identity, 69% coverage: 89:400/455 of query aligns to 88:397/496 of 6g3iA
Sites not aligning to the query:
6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
32% identity, 69% coverage: 89:400/455 of query aligns to 88:397/497 of 6g3hA
Sites not aligning to the query:
6g3gA Crystal structure of edds lyase in complex with succinate (see paper)
32% identity, 69% coverage: 89:400/455 of query aligns to 88:397/497 of 6g3gA
6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
32% identity, 69% coverage: 89:400/455 of query aligns to 88:397/497 of 6g3fA
3r6qA A triclinic-lattice structure of aspartase from bacillus sp. Ym55-1 (see paper)
28% identity, 46% coverage: 103:312/455 of query aligns to 131:349/462 of 3r6qA
Sites not aligning to the query:
3r6vG Crystal structure of aspartase from bacillus sp. Ym55-1 with bound l- aspartate (see paper)
28% identity, 46% coverage: 103:312/455 of query aligns to 132:350/463 of 3r6vG
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)
25% identity, 62% coverage: 103:384/455 of query aligns to 134:438/461 of Q9ZCQ4
Sites not aligning to the query:
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)
25% identity, 67% coverage: 3:306/455 of query aligns to 21:347/467 of P05042
- R126 (≠ K101) binding ; mutation to A: 10-fold decrease of fumarase activity.
- K127 (= K102) mutation to D: No effect.
- H129 (= H104) 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 (≠ HTGR 104:107) binding in site B
- SSN 139:141 (≠ ATD 114:116) binding
- H188 (= H156) active site, Proton donor/acceptor; mutation to N: 200-fold decrease of fumarase activity.
- E315 (≠ T274) 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.
P08417 Fumarate hydratase, mitochondrial; Fumarase; EC 4.2.1.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
27% identity, 44% coverage: 107:306/455 of query aligns to 163:372/488 of P08417
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
- 24 M→S: Does not affect processing by the mitochondrial processing peptidase. Localizes both in the mitochondrion and cytosol. Exhibits high fumarate hydratase activity.; mutation M->V,I: Abolishes processing by the mitochondrial processing peptidase. Mainly localizes in the cytosol, with a small fraction in the mitochondrion. Reduced fumarate hydratase activity.
- 24:25 MN→SF: Does not affect processing by the mitochondrial processing peptidase. Localizes both in the mitochondrion and cytosol. Exhibits high fumarate hydratase activity.
- 29:44 mutation Missing: Does not affect subcellular location.
- 154 H→R: Abolished fumarate hydratase activity and ability to participate in DNA repair.
1fuqA Fumarase with bound 3-trimethylsilylsuccinic acid (see paper)
25% identity, 67% coverage: 3:306/455 of query aligns to 18:344/456 of 1fuqA
- active site: N104 (≠ E82), T184 (= T155), H185 (= H156), S315 (= S277), K321 (= K283), E328 (= E290)
- binding citric acid: T97 (vs. gap), S136 (≠ A114), S137 (≠ T115), N138 (≠ D116)
- binding 3-trimethylsilylsuccinic acid: R123 (≠ K101), H126 (= H104), P127 (≠ T105), N128 (≠ G106), D129 (≠ R107)
Query Sequence
>199474 FitnessBrowser__MR1:199474
MALWGGRFQGETSALFKLFNDSLPVDYRLFEQDVVGSIAWADAIASVGIITATECSDLKK
ALNELLVEVKGDPAIILASGAEDIHSFVESALIAKVGDLGKKLHTGRSRNDQVATDLKLW
CQSEGAALVARLQTLRSELIALAEREFDAVMPGYTHLQRAQPVTFGHWCLAYVEMIERDF
SRLTDALKRANTCPLGSGALAGTAYQMDRHALALALNFASPTLNSLDSVSDRDHVVELCS
TASISMMHLSRMAEDLIFFNTGEAGFISLSDEVTSGSSLMPQKKNPDALELIRGKTGRVY
GSLVGILTTMKALPLAYNKDMQEDKEGLFDVVDSWAICLDMAALVLSGLVVNRPNALLAA
QQGYANATELADYLVSKGMPFREAHHVVGVAVVAAIAKKIPLEGFTLAEFKTFADIIEDD
VYPNLTIEACLAKRDVLGGTALTQVKQAIAAKKAG
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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