SitesBLAST
Comparing WP_011650166.1 NCBI__GCF_000009265.1:WP_011650166.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 11 hits to proteins with known functional sites (download)
7nedA Thiourocanate hydratase from paenibacillus sp. Soil724d2 in complex with cofactor NAD+ and urocanate (see paper)
67% identity, 97% coverage: 16:551/553 of query aligns to 8:543/545 of 7nedA
- binding nicotinamide-adenine-dinucleotide: Y41 (= Y49), A42 (= A50), A43 (= A51), G165 (= G173), G166 (= G174), M167 (= M175), E186 (≠ D194), V187 (≠ I195), R191 (= R199), N232 (= N240), A233 (= A241), Q253 (= Q261), T254 (= T262), H257 (= H265), Y263 (= Y271), V264 (= V272), G313 (= G321), N314 (= N322), I444 (= I452), Y484 (= Y492)
- binding (2e)-3-(1h-imidazol-4-yl)acrylic acid: Y41 (= Y49), L121 (= L129), T122 (= T130), M167 (= M175), R351 (= R359), D432 (= D440)
Q5L084 Urocanate hydratase; Urocanase; Imidazolonepropionate hydrolase; EC 4.2.1.49 from Geobacillus kaustophilus (strain HTA426)
52% identity, 97% coverage: 14:551/553 of query aligns to 10:551/551 of Q5L084
7jfzA Structure of urocanate hydratase from legionella pneumophila bound to NAD
50% identity, 97% coverage: 14:550/553 of query aligns to 6:543/547 of 7jfzA
- binding nicotinamide-adenine-dinucleotide: G167 (= G173), G168 (= G174), M169 (= M175), E188 (≠ D194), C189 (≠ I195), R193 (= R199), N234 (= N240), A235 (= A241), Q255 (= Q261), T256 (= T262), S257 (= S263), H259 (= H265), Y265 (= Y271), L266 (≠ V272), Y314 (≠ N320), G315 (= G321), N316 (= N322), F336 (= F342), R446 (≠ I452)
1uwkA The high resolution structure of urocanate hydratase from pseudomonas putida in complex with urocanate (see paper)
50% identity, 97% coverage: 14:550/553 of query aligns to 12:552/554 of 1uwkA
- binding nicotinamide-adenine-dinucleotide: Y49 (= Y49), G50 (≠ A50), G51 (≠ A51), I142 (≠ V142), G173 (= G173), G174 (= G174), M175 (= M175), G176 (= G176), E194 (≠ D194), S195 (≠ I195), Q196 (≠ D196), N240 (= N240), A241 (= A241), Q261 (= Q261), T262 (= T262), S263 (= S263), H265 (= H265), Y271 (= Y271), L272 (≠ V272), W278 (≠ L278), Y320 (≠ N320), G321 (= G321), N322 (= N322), F342 (= F342), G490 (= G490)
- binding (2e)-3-(1h-imidazol-4-yl)acrylic acid: Y49 (= Y49), M129 (≠ L129), T130 (= T130), G141 (= G141), M175 (= M175), R359 (= R359), D440 (= D440)
P25080 Urocanate hydratase; Urocanase; Imidazolonepropionate hydrolase; EC 4.2.1.49 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 4 papers)
49% identity, 97% coverage: 14:550/553 of query aligns to 15:555/557 of P25080
- GG 53:54 (≠ AA 50:51) binding NAD(+)
- C64 (≠ A61) mutation to A: No loss of activity.
- Q131 (≠ G128) binding NAD(+)
- GMG 177:179 (= GMG 174:176) binding NAD(+)
- C192 (≠ A189) mutation to A: No loss of activity.
- ECQQSR 197:202 (≠ DIDPER 194:199) binding NAD(+)
- C198 (≠ I195) mutation to A: No loss of activity.
- NA 243:244 (= NA 240:241) binding NAD(+)
- QTSAH 264:268 (= QTSAH 261:265) binding NAD(+)
- YL 274:275 (≠ YV 271:272) binding NAD(+)
- YG 323:324 (≠ NG 320:321) binding NAD(+)
- C355 (≠ A352) mutation to A: Minor loss in activity.
- C411 (≠ A408) mutation to A: Loss of activity.
- RE 455:456 (≠ IM 452:453) binding NAD(+)
- G493 (= G490) binding NAD(+)
- C544 (≠ E541) mutation to A: No loss of activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
P25503 Urocanate hydratase; Urocanase; Imidazolonepropionate hydrolase; EC 4.2.1.49 from Bacillus subtilis (strain 168)
50% identity, 96% coverage: 16:547/553 of query aligns to 13:546/552 of P25503
2fknB Crystal structure of urocanase from bacillus subtilis
50% identity, 96% coverage: 16:547/553 of query aligns to 7:540/546 of 2fknB
- binding nicotinamide-adenine-dinucleotide: Y42 (= Y49), G43 (≠ A50), G44 (≠ A51), I135 (≠ V142), G166 (= G173), G167 (= G174), M168 (= M175), E187 (≠ D194), V188 (≠ I195), R192 (= R199), N233 (= N240), A234 (= A241), Q254 (= Q261), T255 (= T262), S256 (= S263), H258 (= H265), Y264 (= Y271), V265 (= V272), N315 (= N322), F335 (= F342), R445 (≠ I452), G483 (= G490)
8q9vA S-methylthiourocanate hydratase from variovorax sp. Ra8 in complex with NAD+ and imidazolone propionate (see paper)
50% identity, 95% coverage: 16:538/553 of query aligns to 10:527/543 of 8q9vA
- binding nicotinamide-adenine-dinucleotide: Y43 (= Y49), M44 (≠ A50), N45 (≠ A51), I136 (≠ V142), G167 (= G173), G168 (= G174), M169 (= M175), D188 (= D194), V189 (≠ I195), S193 (≠ R199), N234 (= N240), A235 (= A241), Q255 (= Q261), C256 (≠ T262), M257 (≠ S263), Y264 (= Y271), V265 (= V272), Y313 (≠ N320), N315 (= N322)
- binding 3-[(4~{R})-5-oxidanylidene-1,4-dihydroimidazol-4-yl]propanoic acid: Y43 (= Y49), M44 (≠ A50), M123 (≠ L129), D433 (= D440), R445 (≠ I452)
1x87A 2.4a x-ray structure of urocanase protein complexed with NAD
47% identity, 97% coverage: 16:551/553 of query aligns to 6:495/495 of 1x87A
- binding nicotinamide-adenine-dinucleotide: G134 (= G173), G135 (= G174), M136 (= M175), E155 (≠ D194), V156 (≠ I195), R160 (= R199), N201 (= N240), A202 (= A241), Q222 (= Q261), T223 (= T262), H226 (= H265), Y232 (= Y271), I233 (≠ V272), Y281 (≠ N320), G282 (= G321), N283 (= N322), F303 (= F342)
6uekA Structure of urocanate hydratase from trypanosoma cruzi in complex with NAD+ (see paper)
33% identity, 89% coverage: 43:534/553 of query aligns to 122:629/660 of 6uekA
- binding nicotinamide-adenine-dinucleotide: G251 (= G171), G253 (= G173), G254 (= G174), M255 (= M175), S256 (≠ G176), A273 (≠ V193), E274 (≠ D194), N320 (= N240), V321 (≠ A241), Q342 (= Q261), T343 (= T262), S344 (= S263), H346 (= H265), Y354 (≠ V272), Y402 (≠ N320), N404 (= N322)
6uekD Structure of urocanate hydratase from trypanosoma cruzi in complex with NAD+ (see paper)
32% identity, 91% coverage: 43:544/553 of query aligns to 107:573/585 of 6uekD
- binding nicotinamide-adenine-dinucleotide: G236 (= G171), G239 (= G174), M240 (= M175), S241 (≠ G176), A258 (≠ V193), N300 (= N240), V301 (≠ A241), Q312 (= Q261), T313 (= T262), S314 (= S263), H316 (= H265), G322 (= G270), Y324 (≠ V272), N368 (= N322)
Query Sequence
>WP_011650166.1 NCBI__GCF_000009265.1:WP_011650166.1
MPKANPRHPKFPIPGGPELRAKGWRQEALLRLLENVLSVGEDPDNLIVYAALGKAARNWA
AHRGIVKALTEMEEDQTLLIQSGKPIGLVRTHAKAPLVIMANCNIVGQWAKAEVFYELQR
KGLICWGGLTAGAWQYIGSQGVIQGTYEIFMRIAERRFGGDLLGRFVLTAGLGGMGGAQP
LAGRMAGAAILCVDIDPERARKRQQIGYLQEIAPDLDSALQMIDAAVKDKRALSVGLVGN
AAEVYPEIARRGIVPDIVTDQTSAHDLVYGYVPKGMNLDQVKGLRDDGQGQLMAASRASI
VEHVTAMLEFQKKGSEVFDNGNLIRTQAKEGGVANAFDIPIFTEAYLRPLFARAIGPFRW
MALSGEESDIARIDDLLLEMFPDNKIITNWIRLAREHVPFEGLPARIAWLGHGERTALAR
RVNALVASGELKGPVAFSRDHLDAGAMAHPNIMTEGMKDGSDAIADWPLIDAMMLCSSMA
DLVVIHSGGGGYAGYMTSCGVTVVADGTDDADERLDHALTNDTALGVMRYADAGYEEALD
EVAKKDVPYIRLG
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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