SitesBLAST
Comparing N515DRAFT_0165 FitnessBrowser__Dyella79:N515DRAFT_0165 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)
1uwkA The high resolution structure of urocanate hydratase from pseudomonas putida in complex with urocanate (see paper)
84% identity, 98% coverage: 13:555/556 of query aligns to 9:551/554 of 1uwkA
- binding nicotinamide-adenine-dinucleotide: Y49 (= Y53), G50 (= G54), G51 (= G55), I142 (= I146), G173 (= G177), G174 (= G178), M175 (= M179), G176 (= G180), E194 (= E198), S195 (≠ C199), Q196 (= Q200), N240 (= N244), A241 (= A245), Q261 (= Q265), T262 (= T266), S263 (= S267), H265 (= H269), Y271 (= Y275), L272 (= L276), W278 (≠ V282), Y320 (= Y324), G321 (= G325), N322 (= N326), F342 (= F346), G490 (= G494)
- binding (2e)-3-(1h-imidazol-4-yl)acrylic acid: Y49 (= Y53), M129 (= M133), T130 (= T134), G141 (= G145), M175 (= M179), R359 (= R363), D440 (= D444)
P25080 Urocanate hydratase; Urocanase; Imidazolonepropionate hydrolase; EC 4.2.1.49 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 4 papers)
83% identity, 98% coverage: 13:555/556 of query aligns to 12:554/557 of P25080
- GG 53:54 (= GG 54:55) binding
- C64 (= C65) mutation to A: No loss of activity.
- Q131 (= Q132) binding
- GMG 177:179 (= GMG 178:180) binding
- C192 (= C193) mutation to A: No loss of activity.
- ECQQSR 197:202 (= ECQQSR 198:203) binding
- C198 (= C199) mutation to A: No loss of activity.
- NA 243:244 (= NA 244:245) binding
- QTSAH 264:268 (= QTSAH 265:269) binding
- YL 274:275 (= YL 275:276) binding
- YG 323:324 (= YG 324:325) binding
- C355 (= C356) mutation to A: Minor loss in activity.
- C411 (= C412) mutation to A: Loss of activity.
- RE 455:456 (= RE 456:457) binding
- G493 (= G494) binding
- C544 (= C545) mutation to A: No loss of activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
7jfzA Structure of urocanate hydratase from legionella pneumophila bound to NAD
70% identity, 98% coverage: 11:555/556 of query aligns to 1:545/547 of 7jfzA
- binding nicotinamide-adenine-dinucleotide: G167 (= G177), G168 (= G178), M169 (= M179), E188 (= E198), C189 (= C199), R193 (= R203), N234 (= N244), A235 (= A245), Q255 (= Q265), T256 (= T266), S257 (= S267), H259 (= H269), Y265 (= Y275), L266 (= L276), Y314 (= Y324), G315 (= G325), N316 (= N326), F336 (= F346), R446 (= R456)
P25503 Urocanate hydratase; Urocanase; Imidazolonepropionate hydrolase; EC 4.2.1.49 from Bacillus subtilis (strain 168)
66% identity, 99% coverage: 8:556/556 of query aligns to 3:551/552 of P25503
2fknB Crystal structure of urocanase from bacillus subtilis
66% identity, 98% coverage: 12:556/556 of query aligns to 1:545/546 of 2fknB
- binding nicotinamide-adenine-dinucleotide: Y42 (= Y53), G43 (= G54), G44 (= G55), I135 (= I146), G166 (= G177), G167 (= G178), M168 (= M179), E187 (= E198), V188 (≠ C199), R192 (= R203), N233 (= N244), A234 (= A245), Q254 (= Q265), T255 (= T266), S256 (= S267), H258 (= H269), Y264 (= Y275), V265 (≠ L276), N315 (= N326), F335 (= F346), R445 (= R456), G483 (= G494)
Q5L084 Urocanate hydratase; Urocanase; Imidazolonepropionate hydrolase; EC 4.2.1.49 from Geobacillus kaustophilus (strain HTA426)
65% identity, 98% coverage: 11:555/556 of query aligns to 5:549/551 of Q5L084
1x87A 2.4a x-ray structure of urocanase protein complexed with NAD
57% identity, 98% coverage: 13:555/556 of query aligns to 1:493/495 of 1x87A
- binding nicotinamide-adenine-dinucleotide: G134 (= G177), G135 (= G178), M136 (= M179), E155 (= E198), V156 (≠ C199), R160 (= R203), N201 (= N244), A202 (= A245), Q222 (= Q265), T223 (= T266), H226 (= H269), Y232 (= Y275), I233 (≠ L276), Y281 (= Y324), G282 (= G325), N283 (= N326), F303 (= F346)
7nedA Thiourocanate hydratase from paenibacillus sp. Soil724d2 in complex with cofactor NAD+ and urocanate (see paper)
52% identity, 97% coverage: 13:552/556 of query aligns to 3:537/545 of 7nedA
- binding nicotinamide-adenine-dinucleotide: Y41 (= Y53), A42 (≠ G54), A43 (≠ G55), G165 (= G177), G166 (= G178), M167 (= M179), E186 (= E198), V187 (≠ C199), R191 (= R203), N232 (= N244), A233 (= A245), Q253 (= Q265), T254 (= T266), H257 (= H269), Y263 (= Y275), V264 (≠ L276), G313 (= G325), N314 (= N326), I444 (≠ R456), Y484 (≠ G496)
- binding (2e)-3-(1h-imidazol-4-yl)acrylic acid: Y41 (= Y53), L121 (≠ M133), T122 (= T134), M167 (= M179), R351 (= R363), D432 (= D444)
6uekA Structure of urocanate hydratase from trypanosoma cruzi in complex with NAD+ (see paper)
38% identity, 90% coverage: 37:538/556 of query aligns to 112:629/660 of 6uekA
- binding nicotinamide-adenine-dinucleotide: G251 (= G175), G253 (= G177), G254 (= G178), M255 (= M179), S256 (≠ G180), A273 (≠ I197), E274 (= E198), N320 (= N244), V321 (≠ A245), Q342 (= Q265), T343 (= T266), S344 (= S267), H346 (= H269), Y354 (≠ L276), Y402 (= Y324), N404 (= N326)
6uekD Structure of urocanate hydratase from trypanosoma cruzi in complex with NAD+ (see paper)
38% identity, 90% coverage: 37:538/556 of query aligns to 97:559/585 of 6uekD
- binding nicotinamide-adenine-dinucleotide: G236 (= G175), G239 (= G178), M240 (= M179), S241 (≠ G180), A258 (≠ I197), N300 (= N244), V301 (≠ A245), Q312 (= Q265), T313 (= T266), S314 (= S267), H316 (= H269), G322 (= G274), Y324 (≠ L276), N368 (= N326)
Query Sequence
>N515DRAFT_0165 FitnessBrowser__Dyella79:N515DRAFT_0165
MNAPTRIDTTRTIRAPRGGELSCKSWLTEAPFRMLQNNLDPEVAENPAELVVYGGIGRAA
RNWECFDAILRALRELNDDETLLIQSGKPVGVFPTHADAPRVLLANSNLVPAWANWEHFN
ELDKKGLMMYGQMTAGSWIYIGSQGIVQGTYETFVEMGRQHYAGSLKGKWILTAGLGGMG
GAQPLAASLAGACSLNIECQQSRIDFRLKTRYVDEQATDLDDALARIARYTAAGEAKSIA
LLGNAADVLPELVRRGVKPDAVTDQTSAHDPVNGYLPGGWSVEEWFERRKSDPAGTAKAA
KQSMRTHVEAMLAFQRQGIPTFDYGNNIRQMAKDEGCADAFEFPGFVPAYVRPLFCRGVG
PFRWVALSGDPEDIYKTDAKVKELIPDDPHLHRWLDMARERISFQGLPARICWVGLGLRH
KLGLAFNEMVRKGELKAPVVIGRDHLDSGSVASPNRETEAMQDGSDAVSDWPLLNAMLNV
AGGATWVSLHHGGGVGMGYSQHSGVVIVCDGSEAADQRIARVLWNDPGTGVMRHADAGYD
IAVQCAKEQGLKLPMR
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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