SitesBLAST
Comparing BPHYT_RS07565 FitnessBrowser__BFirm:BPHYT_RS07565 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)
72% identity, 97% coverage: 17:560/562 of query aligns to 12:555/557 of P25080
- GG 53:54 (= GG 58:59) binding
- C64 (= C69) mutation to A: No loss of activity.
- Q131 (= Q136) binding
- GMG 177:179 (= GMG 182:184) binding
- C192 (≠ S197) mutation to A: No loss of activity.
- ECQQSR 197:202 (≠ ECDETR 202:207) binding
- C198 (= C203) mutation to A: No loss of activity.
- NA 243:244 (= NA 248:249) binding
- QTSAH 264:268 (= QTSAH 269:273) binding
- YL 274:275 (= YL 279:280) binding
- YG 323:324 (= YG 328:329) binding
- C355 (= C360) mutation to A: Minor loss in activity.
- C411 (= C416) mutation to A: Loss of activity.
- RE 455:456 (= RE 460:461) binding
- G493 (= G498) binding
- C544 (≠ T549) 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)
71% identity, 97% coverage: 17:560/562 of query aligns to 9:552/554 of 1uwkA
- binding nicotinamide-adenine-dinucleotide: Y49 (= Y57), G50 (= G58), G51 (= G59), I142 (= I150), G173 (= G181), G174 (= G182), M175 (= M183), G176 (= G184), E194 (= E202), S195 (≠ C203), Q196 (≠ D204), N240 (= N248), A241 (= A249), Q261 (= Q269), T262 (= T270), S263 (= S271), H265 (= H273), Y271 (= Y279), L272 (= L280), W278 (≠ V286), Y320 (= Y328), G321 (= G329), N322 (= N330), F342 (= F350), G490 (= G498)
- binding (2e)-3-(1h-imidazol-4-yl)acrylic acid: Y49 (= Y57), M129 (= M137), T130 (= T138), G141 (= G149), M175 (= M183), R359 (= R367), D440 (= D448)
7jfzA Structure of urocanate hydratase from legionella pneumophila bound to NAD
71% identity, 97% coverage: 15:559/562 of query aligns to 1:545/547 of 7jfzA
- binding nicotinamide-adenine-dinucleotide: G167 (= G181), G168 (= G182), M169 (= M183), E188 (= E202), C189 (= C203), R193 (= R207), N234 (= N248), A235 (= A249), Q255 (= Q269), T256 (= T270), S257 (= S271), H259 (= H273), Y265 (= Y279), L266 (= L280), Y314 (= Y328), G315 (= G329), N316 (= N330), F336 (= F350), R446 (= R460)
P25503 Urocanate hydratase; Urocanase; Imidazolonepropionate hydrolase; EC 4.2.1.49 from Bacillus subtilis (strain 168)
66% identity, 98% coverage: 12:559/562 of query aligns to 3:550/552 of P25503
2fknB Crystal structure of urocanase from bacillus subtilis
66% identity, 97% coverage: 16:559/562 of query aligns to 1:544/546 of 2fknB
- binding nicotinamide-adenine-dinucleotide: Y42 (= Y57), G43 (= G58), G44 (= G59), I135 (= I150), G166 (= G181), G167 (= G182), M168 (= M183), E187 (= E202), V188 (≠ C203), R192 (= R207), N233 (= N248), A234 (= A249), Q254 (= Q269), T255 (= T270), S256 (= S271), H258 (= H273), Y264 (= Y279), V265 (≠ L280), N315 (= N330), F335 (= F350), R445 (= R460), G483 (= G498)
Q5L084 Urocanate hydratase; Urocanase; Imidazolonepropionate hydrolase; EC 4.2.1.49 from Geobacillus kaustophilus (strain HTA426)
65% identity, 97% coverage: 15:560/562 of query aligns to 5:550/551 of Q5L084
1x87A 2.4a x-ray structure of urocanase protein complexed with NAD
57% identity, 97% coverage: 17:560/562 of query aligns to 1:494/495 of 1x87A
- binding nicotinamide-adenine-dinucleotide: G134 (= G181), G135 (= G182), M136 (= M183), E155 (= E202), V156 (≠ C203), R160 (= R207), N201 (= N248), A202 (= A249), Q222 (= Q269), T223 (= T270), H226 (= H273), Y232 (= Y279), I233 (≠ L280), Y281 (= Y328), G282 (= G329), N283 (= N330), F303 (= F350)
7nedA Thiourocanate hydratase from paenibacillus sp. Soil724d2 in complex with cofactor NAD+ and urocanate (see paper)
52% identity, 95% coverage: 17:551/562 of query aligns to 3:535/545 of 7nedA
- binding nicotinamide-adenine-dinucleotide: Y41 (= Y57), A42 (≠ G58), A43 (≠ G59), G165 (= G181), G166 (= G182), M167 (= M183), E186 (= E202), V187 (≠ C203), R191 (= R207), N232 (= N248), A233 (= A249), Q253 (= Q269), T254 (= T270), H257 (= H273), Y263 (= Y279), V264 (≠ L280), G313 (= G329), N314 (= N330), I444 (≠ R460), Y484 (≠ G500)
- binding (2e)-3-(1h-imidazol-4-yl)acrylic acid: Y41 (= Y57), L121 (≠ M137), T122 (= T138), M167 (= M183), R351 (= R367), D432 (= D448)
6uekA Structure of urocanate hydratase from trypanosoma cruzi in complex with NAD+ (see paper)
35% identity, 97% coverage: 10:553/562 of query aligns to 80:640/660 of 6uekA
- binding nicotinamide-adenine-dinucleotide: G251 (= G179), G253 (= G181), G254 (= G182), M255 (= M183), S256 (≠ G184), A273 (≠ V201), E274 (= E202), N320 (= N248), V321 (≠ A249), Q342 (= Q269), T343 (= T270), S344 (= S271), H346 (= H273), Y354 (≠ L280), Y402 (= Y328), N404 (= N330)
6uekD Structure of urocanate hydratase from trypanosoma cruzi in complex with NAD+ (see paper)
35% identity, 97% coverage: 10:553/562 of query aligns to 65:570/585 of 6uekD
- binding nicotinamide-adenine-dinucleotide: G236 (= G179), G239 (= G182), M240 (= M183), S241 (≠ G184), A258 (≠ V201), N300 (= N248), V301 (≠ A249), Q312 (= Q269), T313 (= T270), S314 (= S271), H316 (= H273), G322 (= G278), Y324 (≠ L280), N368 (= N330)
Query Sequence
>BPHYT_RS07565 FitnessBrowser__BFirm:BPHYT_RS07565
MNNPKHIDPRLDPTRTIRAPRGAEKTCKTWIAEAAYRMIQNNLDPEVAEHPHALVVYGGI
GRAARNWDCFDQILKSLKDLEENETLLIQSGKPVGVFRTHADAPRVLLANSNLVPHWATW
EHFHELDRKGLMMYGQMTAGSWIYIGSQGIVQGTYETFFSVANQHFNGDPSGRWILTGGL
GGMGGAQPLAATMAGFSMIAVECDETRIDFRLKTRYVDKKAATLDEALAMLEEAKKAGKP
VSIGLLGNAADVFAECVTRGITPDCVTDQTSAHDPIHGYLPQGWNVEDWRERQKTVPDSI
VLPAKQSMAKQVQAMLTLQERGAATLDYGNNIRQMALEMGVENAFDFPGFVPAYIRPLFC
EGKGPFRWVALSGDPEDIYKTDAKVKELIPDDPHLHNWLDMARERIAFQGLPARICWVGV
KDRYRLGQAFNEMVKNGELKAPIVIGRDHLDTGSVASPNRETESMKDGSDAVSDWPLLNA
LLNTAGGASWVSLHHGGGVGMGFSQHSGVVIVADGTDAAKERLGRVLFNDPATGVMRHAD
AGYELAQETAREAGLNLPMLGR
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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