SitesBLAST
Comparing GFF3577 FitnessBrowser__Phaeo:GFF3577 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 10 hits to proteins with known functional sites (download)
P25080 Urocanate hydratase; Urocanase; Imidazolonepropionate hydrolase; EC 4.2.1.49 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 4 papers)
75% identity, 98% coverage: 10:558/559 of query aligns to 11:555/557 of P25080
- GG 53:54 (= GG 52:53) binding
- C64 (≠ D63) mutation to A: No loss of activity.
- Q131 (= Q130) binding
- GMG 177:179 (= GMG 176:178) binding
- C192 (≠ S191) mutation to A: No loss of activity.
- ECQQSR 197:202 (≠ ECNPDS 196:201) binding
- C198 (= C197) mutation to A: No loss of activity.
- NA 243:244 (= NA 242:243) binding
- QTSAH 264:268 (= QTSAH 267:271) binding
- YL 274:275 (= YL 277:278) binding
- YG 323:324 (= YG 326:327) binding
- C355 (= C358) mutation to A: Minor loss in activity.
- C411 (= C414) mutation to A: Loss of activity.
- RE 455:456 (= RE 458:459) binding
- G493 (= G496) binding
- C544 (= C547) mutation to A: No loss of activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1uwkA The high resolution structure of urocanate hydratase from pseudomonas putida in complex with urocanate (see paper)
75% identity, 98% coverage: 10:558/559 of query aligns to 8:552/554 of 1uwkA
- binding nicotinamide-adenine-dinucleotide: Y49 (= Y51), G50 (= G52), G51 (= G53), I142 (= I144), G173 (= G175), G174 (= G176), M175 (= M177), G176 (= G178), E194 (= E196), S195 (≠ C197), Q196 (≠ N198), N240 (= N242), A241 (= A243), Q261 (= Q267), T262 (= T268), S263 (= S269), H265 (= H271), Y271 (= Y277), L272 (= L278), W278 (≠ M284), Y320 (= Y326), G321 (= G327), N322 (= N328), F342 (= F348), G490 (= G496)
- binding (2e)-3-(1h-imidazol-4-yl)acrylic acid: Y49 (= Y51), M129 (= M131), T130 (= T132), G141 (= G143), M175 (= M177), R359 (= R365), D440 (= D446)
7jfzA Structure of urocanate hydratase from legionella pneumophila bound to NAD
69% identity, 98% coverage: 9:556/559 of query aligns to 1:544/547 of 7jfzA
- binding nicotinamide-adenine-dinucleotide: G167 (= G175), G168 (= G176), M169 (= M177), E188 (= E196), C189 (= C197), R193 (≠ S201), N234 (= N242), A235 (= A243), Q255 (= Q267), T256 (= T268), S257 (= S269), H259 (= H271), Y265 (= Y277), L266 (= L278), Y314 (= Y326), G315 (= G327), N316 (= N328), F336 (= F348), R446 (= R458)
P25503 Urocanate hydratase; Urocanase; Imidazolonepropionate hydrolase; EC 4.2.1.49 from Bacillus subtilis (strain 168)
62% identity, 99% coverage: 1:556/559 of query aligns to 1:549/552 of P25503
2fknB Crystal structure of urocanase from bacillus subtilis
63% identity, 97% coverage: 16:556/559 of query aligns to 7:543/546 of 2fknB
- binding nicotinamide-adenine-dinucleotide: Y42 (= Y51), G43 (= G52), G44 (= G53), I135 (= I144), G166 (= G175), G167 (= G176), M168 (= M177), E187 (= E196), V188 (≠ C197), R192 (≠ S201), N233 (= N242), A234 (= A243), Q254 (= Q267), T255 (= T268), S256 (= S269), H258 (= H271), Y264 (= Y277), V265 (≠ L278), N315 (= N328), F335 (= F348), R445 (= R458), G483 (= G496)
Q5L084 Urocanate hydratase; Urocanase; Imidazolonepropionate hydrolase; EC 4.2.1.49 from Geobacillus kaustophilus (strain HTA426)
62% identity, 98% coverage: 9:556/559 of query aligns to 5:548/551 of Q5L084
1x87A 2.4a x-ray structure of urocanase protein complexed with NAD
55% identity, 98% coverage: 11:556/559 of query aligns to 1:492/495 of 1x87A
- binding nicotinamide-adenine-dinucleotide: G134 (= G175), G135 (= G176), M136 (= M177), E155 (= E196), V156 (≠ C197), R160 (≠ S201), N201 (= N242), A202 (= A243), Q222 (= Q267), T223 (= T268), H226 (= H271), Y232 (= Y277), I233 (≠ L278), Y281 (= Y326), G282 (= G327), N283 (= N328), F303 (= F348)
7nedA Thiourocanate hydratase from paenibacillus sp. Soil724d2 in complex with cofactor NAD+ and urocanate (see paper)
50% identity, 96% coverage: 11:546/559 of query aligns to 3:532/545 of 7nedA
- binding nicotinamide-adenine-dinucleotide: Y41 (= Y51), A42 (≠ G52), A43 (≠ G53), G165 (= G175), G166 (= G176), M167 (= M177), E186 (= E196), V187 (≠ C197), R191 (≠ S201), N232 (= N242), A233 (= A243), Q253 (= Q267), T254 (= T268), H257 (= H271), Y263 (= Y277), V264 (≠ L278), G313 (= G327), N314 (= N328), I444 (≠ R458), Y484 (≠ G498)
- binding (2e)-3-(1h-imidazol-4-yl)acrylic acid: Y41 (= Y51), L121 (≠ M131), T122 (= T132), M167 (= M177), R351 (= R365), D432 (= D446)
6uekA Structure of urocanate hydratase from trypanosoma cruzi in complex with NAD+ (see paper)
38% identity, 96% coverage: 4:540/559 of query aligns to 83:629/660 of 6uekA
- binding nicotinamide-adenine-dinucleotide: G251 (= G173), G253 (= G175), G254 (= G176), M255 (= M177), S256 (≠ G178), A273 (≠ V195), E274 (= E196), N320 (= N242), V321 (≠ A243), Q342 (= Q267), T343 (= T268), S344 (= S269), H346 (= H271), Y354 (≠ L278), Y402 (= Y326), N404 (= N328)
6uekD Structure of urocanate hydratase from trypanosoma cruzi in complex with NAD+ (see paper)
37% identity, 96% coverage: 4:540/559 of query aligns to 68:559/585 of 6uekD
- binding nicotinamide-adenine-dinucleotide: G236 (= G173), G239 (= G176), M240 (= M177), S241 (≠ G178), A258 (≠ V195), N300 (= N242), V301 (≠ A243), Q312 (= Q267), T313 (= T268), S314 (= S269), H316 (= H271), G322 (= G276), Y324 (≠ L278), N368 (= N328)
Query Sequence
>GFF3577 FitnessBrowser__Phaeo:GFF3577
MSDPRKNTRDIFPPTGPEITAKSWMTEAPMRMMMNNLHPDVAENPHELVVYGGIGRAART
WQDFDLIVETLKNLEEDQTLMVQSGKPVGVFQTHKDAPRVLIANSNLVPHWANWDHFNEL
DKKGLMMYGQMTAGSWIYIGTQGIVQGTYETFAEAGRQHFGGSLKGKWILTGGLGGMGGA
QPLAAVFAGASCLAVECNPDSIDFRLRTKYLDEKAETLDEALQMIERWTAAGEAKSVGLL
GNAAEIFPELVKRAETGGIRPDIVTDQTSAHDPVNGYLPLGWTMGEWKERRESDKKAVEK
AARASMKVQVKAMCDFHAMGVPTVDYGNNIRQMALEEGLENAFDFPGFVPAYIRPLFCRG
IGPFRWAALSGDPEDIRKTDAKMKELFPENAGLHRWLDMAQERIAFQGLPARICWIGLGD
RHKAGLAFNEMVRTGELSAPVVIGRDHLDSGSVASPNRETESMLDGSDAVSDWPLLNALL
NTASGATWVSLHHGGGVGMGFSQHSGVVICCDGSEDADRRVGRVLWNDPATGVMRHADAG
YDIAKDCAQEHGLNLPGIL
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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