SitesBLAST
Comparing Ac3H11_2557 FitnessBrowser__acidovorax_3H11:Ac3H11_2557 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)
75% identity, 96% coverage: 24:573/574 of query aligns to 12:555/557 of P25080
- GG 53:54 (= GG 65:66) binding
- C64 (= C76) mutation to A: No loss of activity.
- Q131 (= Q143) binding
- GMG 177:179 (= GMG 189:191) binding
- C192 (≠ V204) mutation to A: No loss of activity.
- ECQQSR 197:202 (≠ ECQQSS 209:214) binding
- C198 (= C210) mutation to A: No loss of activity.
- NA 243:244 (= NA 255:256) binding
- QTSAH 264:268 (= QTSAH 280:284) binding
- YL 274:275 (= YL 290:291) binding
- YG 323:324 (= YG 341:342) binding
- C355 (= C373) mutation to A: Minor loss in activity.
- C411 (= C429) mutation to A: Loss of activity.
- RE 455:456 (= RE 473:474) binding
- G493 (= G511) binding
- C544 (≠ T562) 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)
75% identity, 96% coverage: 24:573/574 of query aligns to 9:552/554 of 1uwkA
- binding nicotinamide-adenine-dinucleotide: Y49 (= Y64), G50 (= G65), G51 (= G66), I142 (= I157), G173 (= G188), G174 (= G189), M175 (= M190), G176 (= G191), E194 (= E209), S195 (≠ C210), Q196 (= Q211), N240 (= N255), A241 (= A256), Q261 (= Q280), T262 (= T281), S263 (= S282), H265 (= H284), Y271 (= Y290), L272 (= L291), W278 (≠ V297), Y320 (= Y341), G321 (= G342), N322 (= N343), F342 (= F363), G490 (= G511)
- binding (2e)-3-(1h-imidazol-4-yl)acrylic acid: Y49 (= Y64), M129 (= M144), T130 (= T145), G141 (= G156), M175 (= M190), R359 (= R380), D440 (= D461)
7jfzA Structure of urocanate hydratase from legionella pneumophila bound to NAD
68% identity, 96% coverage: 22:572/574 of query aligns to 1:545/547 of 7jfzA
- binding nicotinamide-adenine-dinucleotide: G167 (= G188), G168 (= G189), M169 (= M190), E188 (= E209), C189 (= C210), R193 (≠ S214), N234 (= N255), A235 (= A256), Q255 (= Q280), T256 (= T281), S257 (= S282), H259 (= H284), Y265 (= Y290), L266 (= L291), Y314 (= Y341), G315 (= G342), N316 (= N343), F336 (= F363), R446 (= R473)
P25503 Urocanate hydratase; Urocanase; Imidazolonepropionate hydrolase; EC 4.2.1.49 from Bacillus subtilis (strain 168)
63% identity, 97% coverage: 19:574/574 of query aligns to 3:552/552 of P25503
2fknB Crystal structure of urocanase from bacillus subtilis
64% identity, 96% coverage: 24:574/574 of query aligns to 2:546/546 of 2fknB
- binding nicotinamide-adenine-dinucleotide: Y42 (= Y64), G43 (= G65), G44 (= G66), I135 (= I157), G166 (= G188), G167 (= G189), M168 (= M190), E187 (= E209), V188 (≠ C210), R192 (≠ S214), N233 (= N255), A234 (= A256), Q254 (= Q280), T255 (= T281), S256 (= S282), H258 (= H284), Y264 (= Y290), V265 (≠ L291), N315 (= N343), F335 (= F363), R445 (= R473), G483 (= G511)
Q5L084 Urocanate hydratase; Urocanase; Imidazolonepropionate hydrolase; EC 4.2.1.49 from Geobacillus kaustophilus (strain HTA426)
64% identity, 96% coverage: 22:574/574 of query aligns to 5:551/551 of Q5L084
1x87A 2.4a x-ray structure of urocanase protein complexed with NAD
57% identity, 96% coverage: 24:574/574 of query aligns to 1:495/495 of 1x87A
- binding nicotinamide-adenine-dinucleotide: G134 (= G188), G135 (= G189), M136 (= M190), E155 (= E209), V156 (≠ C210), R160 (≠ S214), N201 (= N255), A202 (= A256), Q222 (= Q280), T223 (= T281), H226 (= H284), Y232 (= Y290), I233 (≠ L291), Y281 (= Y341), G282 (= G342), N283 (= N343), F303 (= F363)
7nedA Thiourocanate hydratase from paenibacillus sp. Soil724d2 in complex with cofactor NAD+ and urocanate (see paper)
49% identity, 95% coverage: 24:569/574 of query aligns to 3:540/545 of 7nedA
- binding nicotinamide-adenine-dinucleotide: Y41 (= Y64), A42 (≠ G65), A43 (≠ G66), G165 (= G188), G166 (= G189), M167 (= M190), E186 (= E209), V187 (≠ C210), R191 (≠ S214), N232 (= N255), A233 (= A256), Q253 (= Q280), T254 (= T281), H257 (= H284), Y263 (= Y290), V264 (≠ L291), G313 (= G342), N314 (= N343), I444 (≠ R473), Y484 (≠ G513)
- binding (2e)-3-(1h-imidazol-4-yl)acrylic acid: Y41 (= Y64), L121 (≠ M144), T122 (= T145), M167 (= M190), R351 (= R380), D432 (= D461)
6uekA Structure of urocanate hydratase from trypanosoma cruzi in complex with NAD+ (see paper)
36% identity, 89% coverage: 48:555/574 of query aligns to 112:629/660 of 6uekA
- binding nicotinamide-adenine-dinucleotide: G251 (= G186), G253 (= G188), G254 (= G189), M255 (= M190), S256 (≠ G191), A273 (≠ I208), E274 (= E209), N320 (= N255), V321 (≠ A256), Q342 (= Q280), T343 (= T281), S344 (= S282), H346 (= H284), Y354 (≠ L291), Y402 (= Y341), N404 (= N343)
6uekD Structure of urocanate hydratase from trypanosoma cruzi in complex with NAD+ (see paper)
35% identity, 89% coverage: 48:555/574 of query aligns to 97:559/585 of 6uekD
- binding nicotinamide-adenine-dinucleotide: G236 (= G186), G239 (= G189), M240 (= M190), S241 (≠ G191), A258 (≠ I208), N300 (= N255), V301 (≠ A256), Q312 (= Q280), T313 (= T281), S314 (= S282), H316 (= H284), G322 (= G289), Y324 (≠ L291), N368 (= N343)
Query Sequence
>Ac3H11_2557 FitnessBrowser__acidovorax_3H11:Ac3H11_2557
MNANDAIIAAASNTDPRHDASRVIRAPRGSQLTCKSWLTEAAYRMIQNNLDAEVAERPQD
LVVYGGIGRAARNWECYDQILASLKDLNDDETLLIQSGKPVGVFKTHANAPRVLLANSNL
VPKWANWEHFSELDQKGLFMYGQMTAGSWIYIGTQGIVQGTYETFAEAGRKHYGGSLEGK
WILTAGLGGMGGAQPLAATFAGAVSLNIECQQSSIDFRLRTRYVDKQARDIDHAFELIQQ
HTAAKEAVSIALLGNAAEILPELVRRAKAGGLKPDLVTDQTSAHDLVNGYLPAGWTVAQW
RAAQQDVTQHEVLKKAAAKSCAVHVQAMLDFQHMGIPVVDYGNNIRQVAFDEGVKNAFDF
PGFVPAYIRPLFCEGKGPFRWVALSGDPEDIRKTDAKIKELFPENKHVHRWLDMAGERIA
FQGLPARICWLGLGERHIAGLAFNEMVKNGELKAPIVIGRDHLDTGSVASPNRETEGMKD
GTDAVSDWPLLNALLNTSGGATWVSLHHGGGVGMGYSQHSGMVIVADGTDAAAQRLANVL
VNDCGSGVMRHADAGYELAVETAKKQGLKLPMVK
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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