SitesBLAST
Comparing Pf1N1B4_1587 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_1587 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, 100% coverage: 1:559/560 of query aligns to 1:557/557 of P25080
- M1 (≠ V1) modified: Initiator methionine, Removed
- GG 53:54 (= GG 55:56) binding
- C64 (= C66) mutation to A: No loss of activity.
- Q131 (= Q133) binding
- GMG 177:179 (= GMG 179:181) binding
- C192 (= C194) mutation to A: No loss of activity.
- ECQQSR 197:202 (≠ ECQQVS 199:204) binding
- C198 (= C200) mutation to A: No loss of activity.
- NA 243:244 (= NA 245:246) binding
- QTSAH 264:268 (= QTSAH 266:270) binding
- YL 274:275 (= YL 276:277) binding
- YG 323:324 (= YG 325:326) binding
- C355 (= C357) mutation to A: Minor loss in activity.
- C411 (= C413) mutation to A: Loss of activity.
- RE 455:456 (= RE 457:458) binding
- G493 (= G495) binding
- C544 (= C546) mutation to A: No loss of activity.
1uwkA The high resolution structure of urocanate hydratase from pseudomonas putida in complex with urocanate (see paper)
93% identity, 99% coverage: 8:559/560 of query aligns to 3:554/554 of 1uwkA
- binding nicotinamide-adenine-dinucleotide: Y49 (= Y54), G50 (= G55), G51 (= G56), I142 (= I147), G173 (= G178), G174 (= G179), M175 (= M180), G176 (= G181), E194 (= E199), S195 (≠ C200), Q196 (= Q201), N240 (= N245), A241 (= A246), Q261 (= Q266), T262 (= T267), S263 (= S268), H265 (= H270), Y271 (= Y276), L272 (= L277), W278 (= W283), Y320 (= Y325), G321 (= G326), N322 (= N327), F342 (= F347), G490 (= G495)
- binding (2e)-3-(1h-imidazol-4-yl)acrylic acid: Y49 (= Y54), M129 (= M134), T130 (= T135), G141 (= G146), M175 (= M180), R359 (= R364), D440 (= D445)
7jfzA Structure of urocanate hydratase from legionella pneumophila bound to NAD
73% identity, 97% coverage: 14:556/560 of query aligns to 3:545/547 of 7jfzA
- binding nicotinamide-adenine-dinucleotide: G167 (= G178), G168 (= G179), M169 (= M180), E188 (= E199), C189 (= C200), R193 (≠ S204), N234 (= N245), A235 (= A246), Q255 (= Q266), T256 (= T267), S257 (= S268), H259 (= H270), Y265 (= Y276), L266 (= L277), Y314 (= Y325), G315 (= G326), N316 (= N327), F336 (= F347), R446 (= R457)
2fknB Crystal structure of urocanase from bacillus subtilis
64% identity, 97% coverage: 14:556/560 of query aligns to 2:544/546 of 2fknB
- binding nicotinamide-adenine-dinucleotide: Y42 (= Y54), G43 (= G55), G44 (= G56), I135 (= I147), G166 (= G178), G167 (= G179), M168 (= M180), E187 (= E199), V188 (≠ C200), R192 (≠ S204), N233 (= N245), A234 (= A246), Q254 (= Q266), T255 (= T267), S256 (= S268), H258 (= H270), Y264 (= Y276), V265 (≠ L277), N315 (= N327), F335 (= F347), R445 (= R457), G483 (= G495)
P25503 Urocanate hydratase; Urocanase; Imidazolonepropionate hydrolase; EC 4.2.1.49 from Bacillus subtilis (strain 168)
64% identity, 97% coverage: 14:556/560 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: 19:557/560 of query aligns to 12:550/551 of Q5L084
1x87A 2.4a x-ray structure of urocanase protein complexed with NAD
57% identity, 97% coverage: 14:557/560 of query aligns to 1:494/495 of 1x87A
- binding nicotinamide-adenine-dinucleotide: G134 (= G178), G135 (= G179), M136 (= M180), E155 (= E199), V156 (≠ C200), R160 (≠ S204), N201 (= N245), A202 (= A246), Q222 (= Q266), T223 (= T267), H226 (= H270), Y232 (= Y276), I233 (≠ L277), Y281 (= Y325), G282 (= G326), N283 (= N327), F303 (= F347)
7nedA Thiourocanate hydratase from paenibacillus sp. Soil724d2 in complex with cofactor NAD+ and urocanate (see paper)
51% identity, 95% coverage: 14:545/560 of query aligns to 3:532/545 of 7nedA
- binding nicotinamide-adenine-dinucleotide: Y41 (= Y54), A42 (≠ G55), A43 (≠ G56), G165 (= G178), G166 (= G179), M167 (= M180), E186 (= E199), V187 (≠ C200), R191 (≠ S204), N232 (= N245), A233 (= A246), Q253 (= Q266), T254 (= T267), H257 (= H270), Y263 (= Y276), V264 (≠ L277), G313 (= G326), N314 (= N327), I444 (≠ R457), Y484 (≠ G497)
- binding (2e)-3-(1h-imidazol-4-yl)acrylic acid: Y41 (= Y54), L121 (≠ M134), T122 (= T135), M167 (= M180), R351 (= R364), D432 (= D445)
6uekA Structure of urocanate hydratase from trypanosoma cruzi in complex with NAD+ (see paper)
37% identity, 96% coverage: 5:539/560 of query aligns to 82:629/660 of 6uekA
- binding nicotinamide-adenine-dinucleotide: G251 (= G176), G253 (= G178), G254 (= G179), M255 (= M180), S256 (≠ G181), A273 (≠ I198), E274 (= E199), N320 (= N245), V321 (≠ A246), Q342 (= Q266), T343 (= T267), S344 (= S268), H346 (= H270), Y354 (≠ L277), Y402 (= Y325), N404 (= N327)
6uekD Structure of urocanate hydratase from trypanosoma cruzi in complex with NAD+ (see paper)
36% identity, 96% coverage: 5:539/560 of query aligns to 67:559/585 of 6uekD
- binding nicotinamide-adenine-dinucleotide: G236 (= G176), G239 (= G179), M240 (= M180), S241 (≠ G181), A258 (≠ I198), N300 (= N245), V301 (≠ A246), Q312 (= Q266), T313 (= T267), S314 (= S268), H316 (= H270), G322 (= G275), Y324 (≠ L277), N368 (= N327)
Query Sequence
>Pf1N1B4_1587 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_1587
VTDNKPTKYRNVEIRAARGNKLTAKSWLTEAPLRMLMNNLDPEVAENPKELVVYGGIGRA
ARNWECYDKIVESLTNLNDDETLLVQSGKPVGVFKTHSNAPRVLIANSNLVPHWANWEHF
NELDAKGLAMYGQMTAGSWIYIGSQGIVQGTYETFVEAGRQHYNDDLKGRWVLTAGLGGM
GGAQPLAATLAGACSLNIECQQVSIDFRLNSRYVDEQATDLDDALARIAKYTKEGKAISI
ALLGNAAEILPELVKRGVRPDMVTDQTSAHDPLNGYLPAGWTWEEYRARAKTEPAAVVKA
AKQSMAVHVKAMLDFQKMGIPTFDYGNNIRQMAQEEGVENAFDFPGFVPAYIRPLFCRGI
GPFRWAALSGDPQDIYKTDAKVKELIPDDAHLHNWLDMARERISFQGLPARICWVGLGLR
AKLGLAFNEMVRSGELSAPIVIGRDHLDSGSVSSPNRETESMQDGSDAVSDWPLLNALLN
TASGATWVSLHHGGGVGMGFSQHSGMVIVCDGTDEAAERIARVLHNDPATGVMRHADAGY
QIAIDCAKEQGLNLPMITGK
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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