SitesBLAST
Comparing RR42_RS14645 FitnessBrowser__Cup4G11:RR42_RS14645 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)
91% identity, 99% coverage: 1:556/561 of query aligns to 1:556/557 of P25080
- M1 (= M1) modified: Initiator methionine, Removed
- GG 53:54 (= GG 53:54) binding
- C64 (= C64) mutation to A: No loss of activity.
- Q131 (= Q131) binding
- GMG 177:179 (= GMG 177:179) binding
- C192 (= C192) mutation to A: No loss of activity.
- ECQQSR 197:202 (≠ ECQQAS 197:202) binding
- C198 (= C198) mutation to A: No loss of activity.
- NA 243:244 (= NA 243:244) binding
- QTSAH 264:268 (= QTSAH 264:268) binding
- YL 274:275 (= YL 274:275) binding
- YG 323:324 (= YG 323:324) binding
- C355 (= C355) mutation to A: Minor loss in activity.
- C411 (= C411) mutation to A: Loss of activity.
- RE 455:456 (= RE 455:456) binding
- G493 (= G493) binding
- C544 (= C544) mutation to A: No loss of activity.
1uwkA The high resolution structure of urocanate hydratase from pseudomonas putida in complex with urocanate (see paper)
91% identity, 98% coverage: 5:556/561 of query aligns to 2:553/554 of 1uwkA
- binding nicotinamide-adenine-dinucleotide: Y49 (= Y52), G50 (= G53), G51 (= G54), I142 (= I145), G173 (= G176), G174 (= G177), M175 (= M178), G176 (= G179), E194 (= E197), S195 (≠ C198), Q196 (= Q199), N240 (= N243), A241 (= A244), Q261 (= Q264), T262 (= T265), S263 (= S266), H265 (= H268), Y271 (= Y274), L272 (= L275), W278 (= W281), Y320 (= Y323), G321 (= G324), N322 (= N325), F342 (= F345), G490 (= G493)
- binding (2e)-3-(1h-imidazol-4-yl)acrylic acid: Y49 (= Y52), M129 (= M132), T130 (= T133), G141 (= G144), M175 (= M178), R359 (= R362), D440 (= D443)
7jfzA Structure of urocanate hydratase from legionella pneumophila bound to NAD
71% identity, 97% coverage: 12:554/561 of query aligns to 3:545/547 of 7jfzA
- binding nicotinamide-adenine-dinucleotide: G167 (= G176), G168 (= G177), M169 (= M178), E188 (= E197), C189 (= C198), R193 (≠ S202), N234 (= N243), A235 (= A244), Q255 (= Q264), T256 (= T265), S257 (= S266), H259 (= H268), Y265 (= Y274), L266 (= L275), Y314 (= Y323), G315 (= G324), N316 (= N325), F336 (= F345), R446 (= R455)
P25503 Urocanate hydratase; Urocanase; Imidazolonepropionate hydrolase; EC 4.2.1.49 from Bacillus subtilis (strain 168)
64% identity, 97% coverage: 12:554/561 of query aligns to 8:550/552 of P25503
2fknB Crystal structure of urocanase from bacillus subtilis
64% identity, 97% coverage: 12:554/561 of query aligns to 2:544/546 of 2fknB
- binding nicotinamide-adenine-dinucleotide: Y42 (= Y52), G43 (= G53), G44 (= G54), I135 (= I145), G166 (= G176), G167 (= G177), M168 (= M178), E187 (= E197), V188 (≠ C198), R192 (≠ S202), N233 (= N243), A234 (= A244), Q254 (= Q264), T255 (= T265), S256 (= S266), H258 (= H268), Y264 (= Y274), V265 (≠ L275), N315 (= N325), F335 (= F345), R445 (= R455), G483 (= G493)
Q5L084 Urocanate hydratase; Urocanase; Imidazolonepropionate hydrolase; EC 4.2.1.49 from Geobacillus kaustophilus (strain HTA426)
65% identity, 97% coverage: 12:556/561 of query aligns to 7:551/551 of Q5L084
1x87A 2.4a x-ray structure of urocanase protein complexed with NAD
57% identity, 97% coverage: 12:556/561 of query aligns to 1:495/495 of 1x87A
- binding nicotinamide-adenine-dinucleotide: G134 (= G176), G135 (= G177), M136 (= M178), E155 (= E197), V156 (≠ C198), R160 (≠ S202), N201 (= N243), A202 (= A244), Q222 (= Q264), T223 (= T265), H226 (= H268), Y232 (= Y274), I233 (≠ L275), Y281 (= Y323), G282 (= G324), N283 (= N325), F303 (= F345)
7nedA Thiourocanate hydratase from paenibacillus sp. Soil724d2 in complex with cofactor NAD+ and urocanate (see paper)
51% identity, 95% coverage: 12:546/561 of query aligns to 3:535/545 of 7nedA
- binding nicotinamide-adenine-dinucleotide: Y41 (= Y52), A42 (≠ G53), A43 (≠ G54), G165 (= G176), G166 (= G177), M167 (= M178), E186 (= E197), V187 (≠ C198), R191 (≠ S202), N232 (= N243), A233 (= A244), Q253 (= Q264), T254 (= T265), H257 (= H268), Y263 (= Y274), V264 (≠ L275), G313 (= G324), N314 (= N325), I444 (≠ R455), Y484 (≠ G495)
- binding (2e)-3-(1h-imidazol-4-yl)acrylic acid: Y41 (= Y52), L121 (≠ M132), T122 (= T133), M167 (= M178), R351 (= R362), D432 (= D443)
6uekA Structure of urocanate hydratase from trypanosoma cruzi in complex with NAD+ (see paper)
37% identity, 94% coverage: 11:537/561 of query aligns to 87:629/660 of 6uekA
- binding nicotinamide-adenine-dinucleotide: G251 (= G174), G253 (= G176), G254 (= G177), M255 (= M178), S256 (≠ G179), A273 (≠ I196), E274 (= E197), N320 (= N243), V321 (≠ A244), Q342 (= Q264), T343 (= T265), S344 (= S266), H346 (= H268), Y354 (≠ L275), Y402 (= Y323), N404 (= N325)
6uekD Structure of urocanate hydratase from trypanosoma cruzi in complex with NAD+ (see paper)
36% identity, 94% coverage: 11:537/561 of query aligns to 72:559/585 of 6uekD
- binding nicotinamide-adenine-dinucleotide: G236 (= G174), G239 (= G177), M240 (= M178), S241 (≠ G179), A258 (≠ I196), N300 (= N243), V301 (≠ A244), Q312 (= Q264), T313 (= T265), S314 (= S266), H316 (= H268), G322 (= G273), Y324 (≠ L275), N368 (= N325)
Query Sequence
>RR42_RS14645 FitnessBrowser__Cup4G11:RR42_RS14645
MSNTDRFRDVEIRAPRGNQLNAKSWQTEAPLRMLMNNLDPEVAENPKELVVYGGIGRAAR
NWACYDKIVETLKTLNDDETLLVQSGKPVGVFKTHGNAPRVLIANSNLVPHWATWEHFNE
LDAKGLAMYGQMTAGSWIYIGSQGIVQGTYETFVEAGRQHYNGNLKGRWVLTAGLGGMGG
AQPLAATLAGACSLNIECQQASIDFRLRTRYVDEQATDLDDALARIARYTAEGRAVSIAL
CANAAEVLPELVRRGVRPDMVTDQTSAHDPLNGYLPVGWTWGQYRDRAQTEPARVVKAAK
QSMALHVQAMLDFQKLGVPTFDYGNNIRQMAKEEGVANAFDFPGFVPAYIRPLFCRGVGP
FRWAALSGDPQDIYKTDAKVKELIPDDAHLHRWLDMARERISFQGLPARICWVGLGLRAK
LGLAFNEMVRSGELSAPVVIGRDHLDSGSVASPNRETESMQDGSDAVSDWPLLNALLNTA
SGATWVSLHHGGGVGMGFSQHSGVVIVCDGTDEAAARIARVLHNDPATGVMRHADAGYDI
AIDCAREQGLNLPMLNSKKEA
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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