SitesBLAST
Comparing AZOBR_RS21740 FitnessBrowser__azobra:AZOBR_RS21740 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: 13:561/562 of query aligns to 12:555/557 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 (≠ S193) mutation to A: No loss of activity.
- ECQQSR 197:202 (≠ ECSARS 198:203) binding
- C198 (= C199) mutation to A: No loss of activity.
- NA 243:244 (= NA 244:245) binding
- QTSAH 264:268 (= QTSAH 270:274) binding
- YL 274:275 (= YL 280:281) binding
- YG 323:324 (= YG 329:330) binding
- C355 (= C361) mutation to A: Minor loss in activity.
- C411 (= C417) mutation to A: Loss of activity.
- RE 455:456 (= RE 461:462) binding
- G493 (= G499) binding
- C544 (= C550) 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: 13:561/562 of query aligns to 9:552/554 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 (≠ S200), N240 (= N244), A241 (= A245), Q261 (= Q270), T262 (= T271), S263 (= S272), H265 (= H274), Y271 (= Y280), L272 (= L281), W278 (≠ M287), Y320 (= Y329), G321 (= G330), N322 (= N331), F342 (= F351), G490 (= G499)
- binding (2e)-3-(1h-imidazol-4-yl)acrylic acid: Y49 (= Y53), M129 (= M133), T130 (= T134), G141 (= G145), M175 (= M179), R359 (= R368), D440 (= D449)
7jfzA Structure of urocanate hydratase from legionella pneumophila bound to NAD
74% identity, 98% coverage: 11:560/562 of query aligns to 1:545/547 of 7jfzA
- binding nicotinamide-adenine-dinucleotide: G167 (= G177), G168 (= G178), M169 (= M179), E188 (= E198), C189 (= C199), R193 (≠ S203), N234 (= N244), A235 (= A245), Q255 (= Q270), T256 (= T271), S257 (= S272), H259 (= H274), Y265 (= Y280), L266 (= L281), Y314 (= Y329), G315 (= G330), N316 (= N331), F336 (= F351), R446 (= R461)
Q5L084 Urocanate hydratase; Urocanase; Imidazolonepropionate hydrolase; EC 4.2.1.49 from Geobacillus kaustophilus (strain HTA426)
68% identity, 99% coverage: 8:561/562 of query aligns to 2:550/551 of Q5L084
P25503 Urocanate hydratase; Urocanase; Imidazolonepropionate hydrolase; EC 4.2.1.49 from Bacillus subtilis (strain 168)
65% identity, 98% coverage: 10:560/562 of query aligns to 5:550/552 of P25503
2fknB Crystal structure of urocanase from bacillus subtilis
66% identity, 98% coverage: 13:560/562 of query aligns to 2:544/546 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 (≠ S203), N233 (= N244), A234 (= A245), Q254 (= Q270), T255 (= T271), S256 (= S272), H258 (= H274), Y264 (= Y280), V265 (≠ L281), N315 (= N331), F335 (= F351), R445 (= R461), G483 (= G499)
1x87A 2.4a x-ray structure of urocanase protein complexed with NAD
60% identity, 98% coverage: 13:561/562 of query aligns to 1:494/495 of 1x87A
- binding nicotinamide-adenine-dinucleotide: G134 (= G177), G135 (= G178), M136 (= M179), E155 (= E198), V156 (≠ C199), R160 (≠ S203), N201 (= N244), A202 (= A245), Q222 (= Q270), T223 (= T271), H226 (= H274), Y232 (= Y280), I233 (≠ L281), Y281 (= Y329), G282 (= G330), N283 (= N331), F303 (= F351)
7nedA Thiourocanate hydratase from paenibacillus sp. Soil724d2 in complex with cofactor NAD+ and urocanate (see paper)
52% identity, 96% coverage: 13:549/562 of query aligns to 3:532/545 of 7nedA
- binding nicotinamide-adenine-dinucleotide: Y41 (= Y53), A42 (≠ G54), A43 (≠ G55), G165 (= G177), G166 (= G178), M167 (= M179), E186 (= E198), V187 (≠ C199), R191 (≠ S203), N232 (= N244), A233 (= A245), Q253 (= Q270), T254 (= T271), H257 (= H274), Y263 (= Y280), V264 (≠ L281), G313 (= G330), N314 (= N331), I444 (≠ R461), Y484 (≠ G501)
- binding (2e)-3-(1h-imidazol-4-yl)acrylic acid: Y41 (= Y53), L121 (≠ M133), T122 (= T134), M167 (= M179), R351 (= R368), D432 (= D449)
6uekA Structure of urocanate hydratase from trypanosoma cruzi in complex with NAD+ (see paper)
37% identity, 94% coverage: 13:543/562 of query aligns to 88:629/660 of 6uekA
- binding nicotinamide-adenine-dinucleotide: G251 (= G175), G253 (= G177), G254 (= G178), M255 (= M179), S256 (≠ G180), A273 (≠ V197), E274 (= E198), N320 (= N244), V321 (≠ A245), Q342 (= Q270), T343 (= T271), S344 (= S272), H346 (= H274), Y354 (≠ L281), Y402 (= Y329), N404 (= N331)
6uekD Structure of urocanate hydratase from trypanosoma cruzi in complex with NAD+ (see paper)
37% identity, 94% coverage: 13:543/562 of query aligns to 73:559/585 of 6uekD
- binding nicotinamide-adenine-dinucleotide: G236 (= G175), G239 (= G178), M240 (= M179), S241 (≠ G180), A258 (≠ V197), N300 (= N244), V301 (≠ A245), Q312 (= Q270), T313 (= T271), S314 (= S272), H316 (= H274), G322 (= G279), Y324 (≠ L281), N368 (= N331)
Query Sequence
>AZOBR_RS21740 FitnessBrowser__azobra:AZOBR_RS21740
MSDTKPPANRRVIRAPHGTDLSAKSWLTEAPLRMLMNNLDPDVAENPDELVVYGGIGRAA
RNWDCFDAIVASLKTLNEDETLLVQSGKPVGVFRTHADAPRVLIANSNLVPHWATWDHFR
ELDAKGLMMYGQMTAGSWIYIGSQGIVQGTYETFVEVGRRHYGGDLKGRWILTGGLGGMG
GAQPLAATMAGASMLAVECSARSIERRLETKYLDRSATSLDEAMAILWEAQAAGTAVSVG
LLGNAAEVFPELVRRAKTDPRFRPDAVTDQTSAHDPLNGYLPAGWTMEEAETKRRSDPAA
VVAAAKASMATHVRAMLDFHAMGVPTLDYGNNIRQVAKDEGVADAFAFPGFVPAYIRPLF
CRGIGPFRWAALSGDPEDIYRTDAKVKELIPDNPHLHNWLDMARERIRFQGLPARICWVG
LGDRARLGLAFNEMVAKGELKAPIVIGRDHLDSGSVASPNRETEGMIDGSDAVSDWPLLN
ALLNCASGATWVSLHHGGGVGMGFSQHSGMVIVADGTDAAAKRLERVLTNDPGTGVMRHA
DAGYDIAKDCAKEQGLTLPMIG
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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