SitesBLAST
Comparing Echvi_0695 FitnessBrowser__Cola:Echvi_0695 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 13 hits to proteins with known functional sites (download)
P09148 Galactose-1-phosphate uridylyltransferase; Gal-1-P uridylyltransferase; UDP-glucose--hexose-1-phosphate uridylyltransferase; EC 2.7.7.12 from Escherichia coli (strain K12) (see 4 papers)
51% identity, 100% coverage: 1:346/347 of query aligns to 1:344/348 of P09148
- RAKR 28:31 (≠ RGKR 28:31) binding
- C52 (= C52) binding ; mutation to S: Decreases enzyme activity 3000-fold.
- C55 (= C55) binding ; mutation to S: Decreases enzyme activity 600-fold.
- V61 (≠ I61) binding in other chain
- ND 77:78 (= ND 77:78) binding in other chain
- H115 (= H115) binding ; mutation to N: Decreases enzyme activity by 98%.
- N153 (= N155) binding in other chain
- GCS 159:161 (= GCS 161:163) binding in other chain
- C160 (= C162) mutation C->S,A: Slight inhibition of enzymatic activity.
- S161 (= S163) mutation to A: 7000-fold reduction in specific activity.
- H164 (= H166) binding ; mutation to N: Decreases enzyme activity 10000-fold.
- H166 (= H168) active site, Tele-UMP-histidine intermediate; mutation to G: Abolishes enzymatic activity.
- Q168 (= Q170) binding in other chain
- E182 (≠ K184) binding ; mutation to A: Decreases enzyme activity by about 50%. Abolishes iron binding, but has no effect on zinc binding.
- H281 (= H283) binding
- H296 (= H298) binding
- H298 (≠ V300) binding
- KF 311:312 (= KF 313:314) binding
- YE 316:317 (= YE 318:319) binding
- Q323 (= Q325) binding in other chain
1guqA Structure of nucleotidyltransferase complexed with udp-glucose (see paper)
51% identity, 99% coverage: 2:346/347 of query aligns to 1:343/347 of 1guqA
- active site: C51 (= C52), C54 (= C55), H114 (= H115), N152 (= N155), S160 (= S163), H163 (= H166), G165 (≠ H168), Q167 (= Q170)
- binding fe (iii) ion: E181 (≠ K184), H280 (= H283), H295 (= H298), H297 (≠ V300)
- binding potassium ion: E151 (= E154), N152 (= N155), K153 (= K156), G165 (≠ H168)
- binding uridine-5'-diphosphate-glucose: R27 (= R28), R30 (= R31), W32 (= W33), F52 (≠ Y53), V60 (≠ I61), N76 (= N77), D77 (= D78), F150 (= F153), N152 (= N155), G158 (= G161), C159 (= C162), S160 (= S163), Q167 (= Q170), K310 (= K313), F311 (= F314), Y315 (= Y318), E316 (= E319)
- binding zinc ion: C51 (= C52), C54 (= C55), H114 (= H115), H163 (= H166)
1gupA Structure of nucleotidyltransferase complexed with udp-galactose (see paper)
51% identity, 99% coverage: 2:346/347 of query aligns to 1:343/347 of 1gupA
- active site: C51 (= C52), C54 (= C55), H114 (= H115), N152 (= N155), S160 (= S163), H163 (= H166), G165 (≠ H168), Q167 (= Q170)
- binding fe (iii) ion: E181 (≠ K184), H280 (= H283), H295 (= H298), H297 (≠ V300)
- binding galactose-uridine-5'-diphosphate: R27 (= R28), R30 (= R31), F52 (≠ Y53), R59 (= R60), V60 (≠ I61), N76 (= N77), D77 (= D78), F78 (= F79), F150 (= F153), N152 (= N155), G158 (= G161), C159 (= C162), S160 (= S163), Q167 (= Q170), W169 (= W172), K310 (= K313), F311 (= F314), V313 (= V316), G314 (= G317), E316 (= E319)
- binding potassium ion: N152 (= N155), K153 (= K156), G165 (≠ H168)
- binding zinc ion: C51 (= C52), C54 (= C55), H114 (= H115), H163 (= H166)
1hxpA Nucleotide transferase (see paper)
51% identity, 99% coverage: 2:346/347 of query aligns to 1:336/340 of 1hxpA
- active site: C44 (= C52), C47 (= C55), H107 (= H115), N145 (= N155), S153 (= S163), H156 (= H166), H158 (= H168), Q160 (= Q170)
- binding beta-mercaptoethanol: N145 (= N155), C152 (= C162), Q160 (= Q170), C264 (≠ V274), S265 (= S275), L295 (= L305), A299 (= A309)
- binding fe (iii) ion: E174 (≠ K184), H273 (= H283), H288 (= H298), H290 (≠ V300)
- binding uridine-5'-monophosphate: F45 (≠ Y53), V53 (≠ I61), N69 (= N77), D70 (= D78)
- binding zinc ion: C44 (= C52), C47 (= C55), H107 (= H115), H156 (= H166)
1hxpB Nucleotide transferase (see paper)
49% identity, 99% coverage: 2:346/347 of query aligns to 1:327/329 of 1hxpB
- active site: C35 (= C52), C38 (= C55), H98 (= H115), N136 (= N155), S144 (= S163), H147 (= H166), H149 (= H168), Q151 (= Q170)
- binding beta-mercaptoethanol: F3 (= F4), P5 (≠ F6), H10 (= H11), N136 (= N155), C143 (= C162), Q151 (= Q170), Y208 (≠ F227)
- binding fe (iii) ion: E165 (≠ K184), H264 (= H283), H279 (= H298), H281 (≠ V300)
- binding uridine-5'-diphosphate: R43 (= R60), V44 (≠ I61), F58 (= F75), N60 (= N77), D61 (= D78), S144 (= S163), N145 (= N164)
- binding zinc ion: C35 (= C52), C38 (= C55), H98 (= H115), H147 (= H166)
P07902 Galactose-1-phosphate uridylyltransferase; Gal-1-P uridylyltransferase; UDP-glucose--hexose-1-phosphate uridylyltransferase; EC 2.7.7.12 from Homo sapiens (Human) (see 22 papers)
46% identity, 99% coverage: 4:347/347 of query aligns to 24:368/379 of P07902
- I32 (≠ R12) to N: in GALAC1; mild; dbSNP:rs111033644
- Y34 (= Y14) to N: in GALAC1; affects protein stability; dbSNP:rs111033836
- V44 (= V24) to M: in GALAC1; reduced enzyme activity; dbSNP:rs111033647
- L62 (≠ E42) to M: in dbSNP:rs1800461
- L74 (= L54) to P: in GALAC1; reduced enzyme activity; dbSNP:rs111033663
- H132 (≠ S112) to Q: in GALAC1; affects protein stability; dbSNP:rs367543256
- S135 (≠ H115) to L: in GALAC1; about 5% of normal galactose uridylyltransferase activity; dbSNP:rs111033690
- T138 (= T118) to M: in GALAC1; mild; dbSNP:rs111033686
- M142 (≠ L122) to K: in GALAC1; 4% of normal activity; dbSNP:rs111033695
- R148 (≠ T128) to W: in GALAC1; unstable protein; dbSNP:rs111033693
- V151 (= V131) to A: in GALAC1; approximately 3% of normal activity; dbSNP:rs111033701
- V168 (= V150) to L: in GALAC1; loss of activity; dbSNP:rs367543258
- I170 (= I152) to T: in GALAC1; loss of activity; dbSNP:rs111033839
- F171 (= F153) to S: in GALAC1; reduced enzyme activity; dbSNP:rs111033715
- G175 (= G157) to D: in GALAC1; strongly reduces galactose uridylyltransferase activity; dbSNP:rs111033718
- P185 (= P167) to H: in GALAC1; loss of activity; dbSNP:rs111033722
- H186 (= H168) active site, Tele-UMP-histidine intermediate
- Q188 (= Q170) to R: in GALAC1; most common mutation; 10% of normal galactose uridylyltransferase activity; impairs protein folding; dbSNP:rs75391579
- L195 (≠ I177) to P: in GALAC1; no enzymatic activity; dbSNP:rs111033728
- R201 (≠ K183) to C: in GALAC1; 2-fold decrease in activity; dbSNP:rs111033739
- E202 (≠ K184) binding
- E220 (≠ D202) to K: in GALAC1; 3-fold decrease in activity; dbSNP:rs111033747
- R223 (≠ Y205) to S: in GALAC1; 3-fold decrease in activity; dbSNP:rs111033750
- L227 (≠ K209) to P: in GALAC1; results in no detectable protein in the soluble fraction; dbSNP:rs111033846
- R231 (= R213) to H: in GALAC1; 15% of normal activity; dbSNP:rs111033754
- R259 (≠ T241) to Q: in GALAC1; loss of activity; dbSNP:rs886042070; to W: in GALAC1; mild; dbSNP:rs786204763
- I278 (≠ A260) to N: in GALAC1; 18-fold decrease in activity; dbSNP:rs111033778
- K285 (≠ M267) to N: in GALAC1; severe; impairs protein folding; nearly abolishes enzyme activity; dbSNP:rs111033773
- L289 (≠ V271) to F: in GALAC1; 3-fold decrease in activity; dbSNP:rs111033774
- E291 (≠ K273) to V: in GALAC1; 2-fold decrease in activity; dbSNP:rs111033841
- H301 (= H283) binding
- N314 (≠ P293) to D: in GALAC1; allele Duarte; exists as allelic variants Duarte-1 and Duarte-2; Duarte-1 has normal or increased activity; Duarte-2 has activity reduced to about 35-45% of normal; dbSNP:rs2070074
- H319 (= H298) binding
- H321 (≠ V300) binding
- L327 (= L306) to P: in GALAC1; results in no detectable protein in the soluble fraction; dbSNP:rs111033832
- A330 (= A309) to V: in GALAC1; mild; dbSNP:rs111033804
- R333 (≠ K312) to W: in GALAC1; no enzymatic activity; dbSNP:rs111033800
- T350 (= T329) to A: in GALAC1; mild; dbSNP:rs111033817
6gqdA Structure of human galactose-1-phosphate uridylyltransferase (galt), with crystallization epitope mutations a21y:a22t:t23p:r25l
46% identity, 100% coverage: 2:347/347 of query aligns to 2:344/344 of 6gqdA
- active site: N48 (≠ C52), C51 (= C55), S111 (≠ H115), N149 (= N155), S157 (= S163), H160 (= H166), H162 (= H168), Q164 (= Q170)
- binding 5,6-dihydrouridine-5'-monophosphate: P49 (≠ Y53), A57 (≠ I61), N73 (= N77), D74 (= D78), H162 (= H168), Q164 (= Q170)
- binding zinc ion: E178 (≠ K184), H277 (= H283), H295 (= H298), H297 (≠ V300)
5in3A Crystal structure of glucose-1-phosphate bound nucleotidylated human galactose-1-phosphate uridylyltransferase (see paper)
44% identity, 97% coverage: 8:345/347 of query aligns to 1:324/324 of 5in3A
- active site: N30 (≠ C52), C33 (= C55), S93 (≠ H115), N131 (= N155), S139 (= S163), H142 (= H166), H144 (= H168), Q146 (= Q170)
- binding 1-O-phosphono-alpha-D-glucopyranose: F129 (= F153), N131 (= N155), Q146 (= Q170), V295 (= V316), G296 (= G317), E298 (= E319)
- binding 5,6-dihydrouridine-5'-monophosphate: P31 (≠ Y53), A39 (≠ I61), F53 (= F75), N55 (= N77), D56 (= D78), V86 (= V108), H144 (= H168), Q146 (= Q170)
- binding zinc ion: E160 (≠ K184), H259 (= H283), H277 (= H298), H279 (≠ V300)
6k5zB Structure of uridylyltransferase (see paper)
30% identity, 79% coverage: 13:286/347 of query aligns to 4:255/314 of 6k5zB
- active site: C30 (= C52), C33 (= C55), H86 (= H115), N127 (= N155), S135 (= S163), H138 (= H166), H140 (= H168), Q142 (= Q170)
- binding fe (iii) ion: E156 (≠ K187), H252 (= H283)
- binding phosphate ion: V134 (≠ C162), S135 (= S163), L136 (≠ N164), H140 (= H168)
- binding zinc ion: C30 (= C52), C33 (= C55), H86 (= H115), H138 (= H166), C170 (≠ S198), C173 (≠ L201), H211 (= H242)
Sites not aligning to the query:
Q9FK51 ADP-glucose phosphorylase; ADP-glucose:phosphate adenylyltransferase; EC 2.7.7.- from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
26% identity, 94% coverage: 13:338/347 of query aligns to 26:346/351 of Q9FK51
- RAKR 41:44 (≠ RGKR 28:31) binding
- C63 (= C52) binding
- C66 (= C55) binding
- ECA 72:74 (≠ ING 61:63) binding
- N94 (= N77) binding
- H133 (= H115) binding
- N173 (= N155) binding
- GASM 179:182 (≠ GCSN 161:164) binding
- H184 (= H166) binding
- H186 (= H168) active site, Tele-AMP-histidine intermediate
- Q188 (= Q170) binding
- C216 (≠ S198) binding
- C219 (≠ L201) binding
- H255 (= H242) binding
- H310 (≠ E294) binding
- G321 (≠ T310) binding
- FE 325:326 (≠ FM 314:315) binding
6k9zA Structure of uridylyltransferase mutant (see paper)
28% identity, 79% coverage: 13:286/347 of query aligns to 4:248/309 of 6k9zA
- active site: C23 (= C52), C26 (= C55), H79 (= H115), N120 (= N155), S128 (= S163), H131 (= H166), F133 (≠ H168), Q135 (= Q170)
- binding fe (iii) ion: E149 (≠ K187), H245 (= H283)
- binding uridine-5'-diphosphate: P24 (≠ Y53), N43 (= N77), R44 (≠ D78), Y45 (≠ F79), L129 (≠ N164), Q135 (= Q170), Y137 (≠ W172)
- binding zinc ion: C23 (= C52), C26 (= C55), H79 (= H115), H131 (= H166), C163 (≠ S198), C166 (≠ L201), H204 (= H242)
Sites not aligning to the query:
2h39B Crystal structure of an adp-glucose phosphorylase from arabidopsis thaliana with bound adp-glucose
25% identity, 94% coverage: 13:338/347 of query aligns to 6:308/313 of 2h39B
- active site: C32 (= C52), C35 (= C55), H95 (= H115), N135 (= N155), S143 (= S163), H146 (= H166), G148 (≠ H168), Q150 (= Q170)
- binding adenosine-5'-diphosphate-glucose: R21 (= R28), R24 (= R31), F34 (≠ L54), C42 (≠ N62), N63 (= N77), L64 (≠ D78), Y65 (≠ F79), F133 (= F153), N135 (= N155), G141 (= G161), A142 (≠ C162), S143 (= S163), M144 (≠ N164), Q150 (= Q170), G285 (≠ K312), F287 (= F314), E288 (≠ M315)
- binding zinc ion: C32 (= C52), H95 (= H115), H146 (= H166), C178 (≠ S198), C181 (≠ L201), H217 (= H242), H272 (≠ E294)
1z84A X-ray structure of galt-like protein from arabidopsis thaliana at5g18200 (see paper)
24% identity, 94% coverage: 13:338/347 of query aligns to 5:306/311 of 1z84A
- active site: C31 (= C52), C34 (= C55), H93 (= H115), N133 (= N155), S141 (= S163), H144 (= H166), H146 (= H168), Q148 (= Q170)
- binding adenosine monophosphate: F33 (≠ L54), N62 (= N77), L63 (≠ D78), Y64 (≠ F79), N133 (= N155), A140 (≠ C162), S141 (= S163), M142 (≠ N164), H146 (= H168), Q148 (= Q170)
- binding zinc ion: C31 (= C52), C34 (= C55), H93 (= H115), H144 (= H166), C176 (≠ S198), C179 (≠ L201), H215 (= H242), H270 (≠ E294)
Query Sequence
>Echvi_0695 FitnessBrowser__Cola:Echvi_0695
MTDFNFEDHSHRRYNPFTGDWLQVSPHRGKRPWQGQEEDTAEAQKPAYDEKCYLCPGNTR
INGEKNPDYTGAYVFQNDFGALTSDIPQGEMSEGEFFRAKSERGICKVICFSPRHDLTIP
ELDVQAITKVVELWKKEYQELGGKDFINHVQIFENKGSVMGCSNPHPHGQIWAQESIPVE
PAKKQVKFGEYYQKYGRSMVLDYVYEELKKGERILFENDYFVGLVPFWAVWPFEAMIAPK
THIASLSEMDAAQMEALADAYRQLAIMYDNVFKVSFPYSAGIHQAPTDGQNHPEWDLHMV
FYPPLLRSATVKKFMVGYEMLANPQRDITAESAVKILKSQPKEHYKV
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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