SitesBLAST
Comparing CCNA_01008 FitnessBrowser__Caulo:CCNA_01008 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)
78% identity, 98% coverage: 10:553/554 of query aligns to 12:555/557 of P25080
- GG 53:54 (= GG 51:52) binding
- C64 (≠ S62) mutation to A: No loss of activity.
- Q131 (= Q129) binding
- GMG 177:179 (= GMG 175:177) binding
- C192 (≠ A190) mutation to A: No loss of activity.
- ECQQSR 197:202 (≠ ECQPSS 195:200) binding
- C198 (= C196) mutation to A: No loss of activity.
- NA 243:244 (= NA 241:242) binding
- QTSAH 264:268 (= QTSAH 262:266) binding
- YL 274:275 (= YL 272:273) binding
- YG 323:324 (= YG 321:322) binding
- C355 (= C353) mutation to A: Minor loss in activity.
- C411 (= C409) mutation to A: Loss of activity.
- RE 455:456 (= RE 453:454) binding
- G493 (= G491) binding
- C544 (= C542) 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)
78% identity, 98% coverage: 10:553/554 of query aligns to 9:552/554 of 1uwkA
- binding nicotinamide-adenine-dinucleotide: Y49 (= Y50), G50 (= G51), G51 (= G52), I142 (= I143), G173 (= G174), G174 (= G175), M175 (= M176), G176 (= G177), E194 (= E195), S195 (≠ C196), Q196 (= Q197), N240 (= N241), A241 (= A242), Q261 (= Q262), T262 (= T263), S263 (= S264), H265 (= H266), Y271 (= Y272), L272 (= L273), W278 (≠ L279), Y320 (= Y321), G321 (= G322), N322 (= N323), F342 (= F343), G490 (= G491)
- binding (2e)-3-(1h-imidazol-4-yl)acrylic acid: Y49 (= Y50), M129 (= M130), T130 (= T131), G141 (= G142), M175 (= M176), R359 (= R360), D440 (= D441)
7jfzA Structure of urocanate hydratase from legionella pneumophila bound to NAD
73% identity, 98% coverage: 8:551/554 of query aligns to 1:544/547 of 7jfzA
- binding nicotinamide-adenine-dinucleotide: G167 (= G174), G168 (= G175), M169 (= M176), E188 (= E195), C189 (= C196), R193 (≠ S200), N234 (= N241), A235 (= A242), Q255 (= Q262), T256 (= T263), S257 (= S264), H259 (= H266), Y265 (= Y272), L266 (= L273), Y314 (= Y321), G315 (= G322), N316 (= N323), F336 (= F343), R446 (= R453)
Q5L084 Urocanate hydratase; Urocanase; Imidazolonepropionate hydrolase; EC 4.2.1.49 from Geobacillus kaustophilus (strain HTA426)
67% identity, 98% coverage: 8:551/554 of query aligns to 5:548/551 of Q5L084
P25503 Urocanate hydratase; Urocanase; Imidazolonepropionate hydrolase; EC 4.2.1.49 from Bacillus subtilis (strain 168)
63% identity, 99% coverage: 5:551/554 of query aligns to 3:549/552 of P25503
2fknB Crystal structure of urocanase from bacillus subtilis
64% identity, 98% coverage: 10:551/554 of query aligns to 2:543/546 of 2fknB
- binding nicotinamide-adenine-dinucleotide: Y42 (= Y50), G43 (= G51), G44 (= G52), I135 (= I143), G166 (= G174), G167 (= G175), M168 (= M176), E187 (= E195), V188 (≠ C196), R192 (≠ S200), N233 (= N241), A234 (= A242), Q254 (= Q262), T255 (= T263), S256 (= S264), H258 (= H266), Y264 (= Y272), V265 (≠ L273), N315 (= N323), F335 (= F343), R445 (= R453), G483 (= G491)
1x87A 2.4a x-ray structure of urocanase protein complexed with NAD
59% identity, 98% coverage: 10:551/554 of query aligns to 1:492/495 of 1x87A
- binding nicotinamide-adenine-dinucleotide: G134 (= G174), G135 (= G175), M136 (= M176), E155 (= E195), V156 (≠ C196), R160 (≠ S200), N201 (= N241), A202 (= A242), Q222 (= Q262), T223 (= T263), H226 (= H266), Y232 (= Y272), I233 (≠ L273), Y281 (= Y321), G282 (= G322), N283 (= N323), F303 (= F343)
7nedA Thiourocanate hydratase from paenibacillus sp. Soil724d2 in complex with cofactor NAD+ and urocanate (see paper)
51% identity, 95% coverage: 10:537/554 of query aligns to 3:528/545 of 7nedA
- binding nicotinamide-adenine-dinucleotide: Y41 (= Y50), A42 (≠ G51), A43 (≠ G52), G165 (= G174), G166 (= G175), M167 (= M176), E186 (= E195), V187 (≠ C196), R191 (≠ S200), N232 (= N241), A233 (= A242), Q253 (= Q262), T254 (= T263), H257 (= H266), Y263 (= Y272), V264 (≠ L273), G313 (= G322), N314 (= N323), I444 (≠ R453), Y484 (≠ G493)
- binding (2e)-3-(1h-imidazol-4-yl)acrylic acid: Y41 (= Y50), L121 (≠ M130), T122 (= T131), M167 (= M176), R351 (= R360), D432 (= D441)
6uekA Structure of urocanate hydratase from trypanosoma cruzi in complex with NAD+ (see paper)
37% identity, 93% coverage: 34:548/554 of query aligns to 112:638/660 of 6uekA
- binding nicotinamide-adenine-dinucleotide: G251 (= G172), G253 (= G174), G254 (= G175), M255 (= M176), S256 (≠ G177), A273 (≠ I194), E274 (= E195), N320 (= N241), V321 (≠ A242), Q342 (= Q262), T343 (= T263), S344 (= S264), H346 (= H266), Y354 (≠ L273), Y402 (= Y321), N404 (= N323)
6uekD Structure of urocanate hydratase from trypanosoma cruzi in complex with NAD+ (see paper)
37% identity, 93% coverage: 34:548/554 of query aligns to 97:568/585 of 6uekD
- binding nicotinamide-adenine-dinucleotide: G236 (= G172), G239 (= G175), M240 (= M176), S241 (≠ G177), A258 (≠ I194), N300 (= N241), V301 (≠ A242), Q312 (= Q262), T313 (= T263), S314 (= S264), H316 (= H266), G322 (= G271), Y324 (≠ L273), N368 (= N323)
Query Sequence
>CCNA_01008 FitnessBrowser__Caulo:CCNA_01008
MTRRDTTRVIRPATGPERTCKSWLTEAALRMLMNNLHPDVAERPEELVVYGGIGRAARDW
ESYDKIVETLRRLEDDETLLVQSGKPVGVFRTHADAPRVLIANSNLVPRWASWEHFNELD
RKGLAMYGQMTAGSWIYIGAQGIVQGTYETFVEMGRQHYGGDLSGRWLLTAGLGGMGGAQ
PLAAVMAGAACLAIECQPSSIEMRLRTGYLDRSTDKVEEALAWIEESCAAKTPISVGLLG
NAAELLPELFKRGVRPDLLTDQTSAHDPVNGYLPAGWSLERWHAMRDQDPPQVAEAAKAS
MAAHVKAMLDFQAAGVPTVDYGNNIRQMALEEGVTNAFDFPGFVPAYIRPLFCRGVGPFR
WAALSGDPEDIAKTDAKVKELIPDNPHLHNWLDMAGQKIRFQGLPARICWVGLGDRHRLG
LAFNEMVAKGELKAPIVIGRDHLDSGSVASPNRETEAMRDGSDAVSDWPLLNALLNTASG
ATWVSLHHGGGVGMGFSQHAGMVIVCDGTEAAAKRVARVLWNDPATGVMRHADAGYDIAL
ACAREKGLDLPGIL
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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