SitesBLAST
Comparing AO353_12250 FitnessBrowser__pseudo3_N2E3:AO353_12250 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)
92% identity, 97% coverage: 15:566/567 of query aligns to 6:557/557 of P25080
- GG 53:54 (= GG 62:63) binding
- C64 (= C73) mutation to A: No loss of activity.
- Q131 (= Q140) binding
- GMG 177:179 (= GMG 186:188) binding
- C192 (= C201) mutation to A: No loss of activity.
- ECQQSR 197:202 (≠ ECQQVS 206:211) binding
- C198 (= C207) mutation to A: No loss of activity.
- NA 243:244 (= NA 252:253) binding
- QTSAH 264:268 (= QTSAH 273:277) binding
- YL 274:275 (= YL 283:284) binding
- YG 323:324 (= YG 332:333) binding
- C355 (= C364) mutation to A: Minor loss in activity.
- C411 (= C420) mutation to A: Loss of activity.
- RE 455:456 (= RE 464:465) binding
- G493 (= G502) binding
- C544 (= C553) 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)
92% identity, 97% coverage: 15:566/567 of query aligns to 3:554/554 of 1uwkA
- binding nicotinamide-adenine-dinucleotide: Y49 (= Y61), G50 (= G62), G51 (= G63), I142 (= I154), G173 (= G185), G174 (= G186), M175 (= M187), G176 (= G188), E194 (= E206), S195 (≠ C207), Q196 (= Q208), N240 (= N252), A241 (= A253), Q261 (= Q273), T262 (= T274), S263 (= S275), H265 (= H277), Y271 (= Y283), L272 (= L284), W278 (= W290), Y320 (= Y332), G321 (= G333), N322 (= N334), F342 (= F354), G490 (= G502)
- binding (2e)-3-(1h-imidazol-4-yl)acrylic acid: Y49 (= Y61), M129 (= M141), T130 (= T142), G141 (= G153), M175 (= M187), R359 (= R371), D440 (= D452)
7jfzA Structure of urocanate hydratase from legionella pneumophila bound to NAD
72% identity, 96% coverage: 21:563/567 of query aligns to 3:545/547 of 7jfzA
- binding nicotinamide-adenine-dinucleotide: G167 (= G185), G168 (= G186), M169 (= M187), E188 (= E206), C189 (= C207), R193 (≠ S211), N234 (= N252), A235 (= A253), Q255 (= Q273), T256 (= T274), S257 (= S275), H259 (= H277), Y265 (= Y283), L266 (= L284), Y314 (= Y332), G315 (= G333), N316 (= N334), F336 (= F354), R446 (= R464)
2fknB Crystal structure of urocanase from bacillus subtilis
63% identity, 96% coverage: 21:563/567 of query aligns to 2:544/546 of 2fknB
- binding nicotinamide-adenine-dinucleotide: Y42 (= Y61), G43 (= G62), G44 (= G63), I135 (= I154), G166 (= G185), G167 (= G186), M168 (= M187), E187 (= E206), V188 (≠ C207), R192 (≠ S211), N233 (= N252), A234 (= A253), Q254 (= Q273), T255 (= T274), S256 (= S275), H258 (= H277), Y264 (= Y283), V265 (≠ L284), N315 (= N334), F335 (= F354), R445 (= R464), G483 (= G502)
P25503 Urocanate hydratase; Urocanase; Imidazolonepropionate hydrolase; EC 4.2.1.49 from Bacillus subtilis (strain 168)
63% identity, 96% coverage: 21:563/567 of query aligns to 8:550/552 of P25503
Q5L084 Urocanate hydratase; Urocanase; Imidazolonepropionate hydrolase; EC 4.2.1.49 from Geobacillus kaustophilus (strain HTA426)
65% identity, 96% coverage: 21:564/567 of query aligns to 7:550/551 of Q5L084
1x87A 2.4a x-ray structure of urocanase protein complexed with NAD
57% identity, 96% coverage: 21:564/567 of query aligns to 1:494/495 of 1x87A
- binding nicotinamide-adenine-dinucleotide: G134 (= G185), G135 (= G186), M136 (= M187), E155 (= E206), V156 (≠ C207), R160 (≠ S211), N201 (= N252), A202 (= A253), Q222 (= Q273), T223 (= T274), H226 (= H277), Y232 (= Y283), I233 (≠ L284), Y281 (= Y332), G282 (= G333), N283 (= N334), F303 (= F354)
7nedA Thiourocanate hydratase from paenibacillus sp. Soil724d2 in complex with cofactor NAD+ and urocanate (see paper)
51% identity, 94% coverage: 21:552/567 of query aligns to 3:532/545 of 7nedA
- binding nicotinamide-adenine-dinucleotide: Y41 (= Y61), A42 (≠ G62), A43 (≠ G63), G165 (= G185), G166 (= G186), M167 (= M187), E186 (= E206), V187 (≠ C207), R191 (≠ S211), N232 (= N252), A233 (= A253), Q253 (= Q273), T254 (= T274), H257 (= H277), Y263 (= Y283), V264 (≠ L284), G313 (= G333), N314 (= N334), I444 (≠ R464), Y484 (≠ G504)
- binding (2e)-3-(1h-imidazol-4-yl)acrylic acid: Y41 (= Y61), L121 (≠ M141), T122 (= T142), M167 (= M187), R351 (= R371), D432 (= D452)
6uekA Structure of urocanate hydratase from trypanosoma cruzi in complex with NAD+ (see paper)
36% identity, 93% coverage: 20:546/567 of query aligns to 87:629/660 of 6uekA
- binding nicotinamide-adenine-dinucleotide: G251 (= G183), G253 (= G185), G254 (= G186), M255 (= M187), S256 (≠ G188), A273 (≠ I205), E274 (= E206), N320 (= N252), V321 (≠ A253), Q342 (= Q273), T343 (= T274), S344 (= S275), H346 (= H277), Y354 (≠ L284), Y402 (= Y332), N404 (= N334)
6uekD Structure of urocanate hydratase from trypanosoma cruzi in complex with NAD+ (see paper)
36% identity, 93% coverage: 20:546/567 of query aligns to 72:559/585 of 6uekD
- binding nicotinamide-adenine-dinucleotide: G236 (= G183), G239 (= G186), M240 (= M187), S241 (≠ G188), A258 (≠ I205), N300 (= N252), V301 (≠ A253), Q312 (= Q273), T313 (= T274), S314 (= S275), H316 (= H277), G322 (= G282), Y324 (≠ L284), N368 (= N334)
Query Sequence
>AO353_12250 FitnessBrowser__pseudo3_N2E3:AO353_12250
VTDNTQKPTPVTFTKHRDVEIRAPRGNKLTAKSWLTEAPLRMLMNNLDPEVAENPKELVV
YGGIGRAARNWECYDKIVESLTNLNDDETLLVQSGKPVGVFKTHSNAPRVLIANSNLVPH
WASWEHFNELDAKGLAMYGQMTAGSWIYIGSQGIVQGTYETFVEAGRQHYNDNLTGRWVL
TAGLGGMGGAQPLAATLAGACSLNIECQQVSIDFRLKSRYVDEQAKDLDDALARIAKYTK
EGKAISIALLGNAAEILPELVRRGVRPDMVTDQTSAHDPLNGYLPAGWTWEEYRARAKTE
PAAVIKAAKQSMAVHVKAMLDFQKQGIPTFDYGNNIRQMAQEEGVENAFDFPGFVPAYIR
PLFCRGIGPFRWAALSGNAEDIYKTDAKVKELIPDDAHLHNWLDMARERISFQGLPARIC
WVGLGLRAKLGLAFNEMVRSGELSAPIVIGRDHLDSGSVASPNRETESMQDGSDAVSDWP
LLNALLNTASGATWVSLHHGGGVGMGFSQHSGMVIVCDGTDEAAERIARVLHNDPATGVM
RHADAGYQIAIDCAKEQGLNLPMITGK
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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