SitesBLAST
Comparing RR42_RS16915 FitnessBrowser__Cup4G11:RR42_RS16915 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)
76% identity, 98% coverage: 6:554/560 of query aligns to 11:555/557 of P25080
- GG 53:54 (= GG 48:49) binding
- C64 (= C59) mutation to A: No loss of activity.
- Q131 (= Q126) binding
- GMG 177:179 (= GMG 172:174) binding
- C192 (= C187) mutation to A: No loss of activity.
- ECQQSR 197:202 (≠ ECQESR 192:197) binding
- C198 (= C193) mutation to A: No loss of activity.
- NA 243:244 (= NA 238:239) binding
- QTSAH 264:268 (= QTSAH 263:267) binding
- YL 274:275 (= YL 273:274) binding
- YG 323:324 (= YG 322:323) binding
- C355 (= C354) mutation to A: Minor loss in activity.
- C411 (= C410) mutation to A: Loss of activity.
- RE 455:456 (= RE 454:455) binding
- G493 (= G492) binding
- C544 (= C543) 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)
76% identity, 98% coverage: 6:554/560 of query aligns to 8:552/554 of 1uwkA
- binding nicotinamide-adenine-dinucleotide: Y49 (= Y47), G50 (= G48), G51 (= G49), I142 (= I140), G173 (= G171), G174 (= G172), M175 (= M173), G176 (= G174), E194 (= E192), S195 (≠ C193), Q196 (= Q194), N240 (= N238), A241 (= A239), Q261 (= Q263), T262 (= T264), S263 (= S265), H265 (= H267), Y271 (= Y273), L272 (= L274), W278 (≠ V280), Y320 (= Y322), G321 (= G323), N322 (= N324), F342 (= F344), G490 (= G492)
- binding (2e)-3-(1h-imidazol-4-yl)acrylic acid: Y49 (= Y47), M129 (= M127), T130 (= T128), G141 (= G139), M175 (= M173), R359 (= R361), D440 (= D442)
7jfzA Structure of urocanate hydratase from legionella pneumophila bound to NAD
69% identity, 98% coverage: 5:553/560 of query aligns to 1:545/547 of 7jfzA
- binding nicotinamide-adenine-dinucleotide: G167 (= G171), G168 (= G172), M169 (= M173), E188 (= E192), C189 (= C193), R193 (= R197), N234 (= N238), A235 (= A239), Q255 (= Q263), T256 (= T264), S257 (= S265), H259 (= H267), Y265 (= Y273), L266 (= L274), Y314 (= Y322), G315 (= G323), N316 (= N324), F336 (= F344), R446 (= R454)
P25503 Urocanate hydratase; Urocanase; Imidazolonepropionate hydrolase; EC 4.2.1.49 from Bacillus subtilis (strain 168)
63% identity, 98% coverage: 4:553/560 of query aligns to 5:550/552 of P25503
Q5L084 Urocanate hydratase; Urocanase; Imidazolonepropionate hydrolase; EC 4.2.1.49 from Geobacillus kaustophilus (strain HTA426)
65% identity, 99% coverage: 1:554/560 of query aligns to 1:550/551 of Q5L084
2fknB Crystal structure of urocanase from bacillus subtilis
64% identity, 98% coverage: 7:553/560 of query aligns to 2:544/546 of 2fknB
- binding nicotinamide-adenine-dinucleotide: Y42 (= Y47), G43 (= G48), G44 (= G49), I135 (= I140), G166 (= G171), G167 (= G172), M168 (= M173), E187 (= E192), V188 (≠ C193), R192 (= R197), N233 (= N238), A234 (= A239), Q254 (= Q263), T255 (= T264), S256 (= S265), H258 (= H267), Y264 (= Y273), V265 (≠ L274), N315 (= N324), F335 (= F344), R445 (= R454), G483 (= G492)
1x87A 2.4a x-ray structure of urocanase protein complexed with NAD
58% identity, 98% coverage: 7:554/560 of query aligns to 1:494/495 of 1x87A
- binding nicotinamide-adenine-dinucleotide: G134 (= G171), G135 (= G172), M136 (= M173), E155 (= E192), V156 (≠ C193), R160 (= R197), N201 (= N238), A202 (= A239), Q222 (= Q263), T223 (= T264), H226 (= H267), Y232 (= Y273), I233 (≠ L274), Y281 (= Y322), G282 (= G323), N283 (= N324), F303 (= F344)
7nedA Thiourocanate hydratase from paenibacillus sp. Soil724d2 in complex with cofactor NAD+ and urocanate (see paper)
50% identity, 96% coverage: 7:542/560 of query aligns to 3:532/545 of 7nedA
- binding nicotinamide-adenine-dinucleotide: Y41 (= Y47), A42 (≠ G48), A43 (≠ G49), G165 (= G171), G166 (= G172), M167 (= M173), E186 (= E192), V187 (≠ C193), R191 (= R197), N232 (= N238), A233 (= A239), Q253 (= Q263), T254 (= T264), H257 (= H267), Y263 (= Y273), V264 (≠ L274), G313 (= G323), N314 (= N324), I444 (≠ R454), Y484 (≠ G494)
- binding (2e)-3-(1h-imidazol-4-yl)acrylic acid: Y41 (= Y47), L121 (≠ M127), T122 (= T128), M167 (= M173), R351 (= R361), D432 (= D442)
6uekA Structure of urocanate hydratase from trypanosoma cruzi in complex with NAD+ (see paper)
36% identity, 98% coverage: 4:549/560 of query aligns to 85:638/660 of 6uekA
- binding nicotinamide-adenine-dinucleotide: G251 (= G169), G253 (= G171), G254 (= G172), M255 (= M173), S256 (≠ G174), A273 (≠ I191), E274 (= E192), N320 (= N238), V321 (≠ A239), Q342 (= Q263), T343 (= T264), S344 (= S265), H346 (= H267), Y354 (≠ L274), Y402 (= Y322), N404 (= N324)
6uekD Structure of urocanate hydratase from trypanosoma cruzi in complex with NAD+ (see paper)
35% identity, 98% coverage: 4:549/560 of query aligns to 70:568/585 of 6uekD
- binding nicotinamide-adenine-dinucleotide: G236 (= G169), G239 (= G172), M240 (= M173), S241 (≠ G174), A258 (≠ I191), N300 (= N238), V301 (≠ A239), Q312 (= Q263), T313 (= T264), S314 (= S265), H316 (= H267), G322 (= G272), Y324 (≠ L274), N368 (= N324)
Query Sequence
>RR42_RS16915 FitnessBrowser__Cup4G11:RR42_RS16915
MRGQREIRAPRGTELHCKNWLIEAAYRMLQNNLDPDVAERPQDLVVYGGIGKAARNWECF
DAILDSLRNLGEEESLLVQSGKPVGVFRTHADAPRVLIANSNLVPHWATWDKFNELDRAG
LMMYGQMTAGSWIYIGTQGIVQGTFETFVEAGRQHYNNDLTGKWILTAGLGGMGGAQTLA
GVLAGACVLAIECQESRIDFRLRTRYVDKKATSIDEALAMIEEATRNKQAISVGLLGNAA
EIMPELVKRAQAGGMRPDIVTDQTSAHDLVNGYLPAGWTVGQWEAARTADPKSVEAAAKT
SIVKHVQAMLAFQQMGVPTLDYGNNIRQVAFDEGVANAFDFPGFVPAYIRPLFCRGKGPF
RWVALSGDPEDIYKTDAKMKELFPEDAHLHRWLDMARDRIAFQGLPARICWVGLDERHRA
GLAFNEMVKNGELKAPIVIGRDHLDCGSVASPNRETEAMRDGSDAVSDWPLLNALLNTAG
GATWVSLHHGGGVGMGFSQHSGVVIVCDGTDAAAKRIERVLWNDPATGVMRHADAGYESA
IDCAHEKGLNLPMVPKAAGV
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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