SitesBLAST
Comparing 5209835 FitnessBrowser__PV4:5209835 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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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)
58% identity, 95% coverage: 9:352/363 of query aligns to 2:346/348 of P09148
- RAKR 28:31 (≠ RSKR 35:38) binding
- C52 (= C59) binding ; mutation to S: Decreases enzyme activity 3000-fold.
- C55 (= C62) binding ; mutation to S: Decreases enzyme activity 600-fold.
- V61 (≠ I68) binding in other chain
- ND 77:78 (= ND 84:85) binding in other chain
- H115 (= H121) binding ; mutation to N: Decreases enzyme activity by 98%.
- N153 (= N159) binding in other chain
- GCS 159:161 (= GCS 165:167) binding in other chain
- C160 (= C166) mutation C->S,A: Slight inhibition of enzymatic activity.
- S161 (= S167) mutation to A: 7000-fold reduction in specific activity.
- H164 (= H170) binding ; mutation to N: Decreases enzyme activity 10000-fold.
- H166 (= H172) active site, Tele-UMP-histidine intermediate; mutation to G: Abolishes enzymatic activity.
- Q168 (= Q174) binding in other chain
- E182 (≠ K188) binding ; mutation to A: Decreases enzyme activity by about 50%. Abolishes iron binding, but has no effect on zinc binding.
- H281 (= H287) binding
- H296 (= H302) binding
- H298 (= H304) binding
- KF 311:312 (= KF 317:318) binding
- YE 316:317 (= YE 322:323) binding
- Q323 (= Q329) binding in other chain
1guqA Structure of nucleotidyltransferase complexed with udp-glucose (see paper)
58% identity, 95% coverage: 9:352/363 of query aligns to 1:345/347 of 1guqA
- active site: C51 (= C59), C54 (= C62), H114 (= H121), N152 (= N159), S160 (= S167), H163 (= H170), G165 (≠ H172), Q167 (= Q174)
- binding fe (iii) ion: E181 (≠ K188), H280 (= H287), H295 (= H302), H297 (= H304)
- binding potassium ion: E151 (= E158), N152 (= N159), K153 (= K160), G165 (≠ H172)
- binding uridine-5'-diphosphate-glucose: R27 (= R35), R30 (= R38), W32 (= W40), F52 (= F60), V60 (≠ I68), N76 (= N84), D77 (= D85), F150 (= F157), N152 (= N159), G158 (= G165), C159 (= C166), S160 (= S167), Q167 (= Q174), K310 (= K317), F311 (= F318), Y315 (= Y322), E316 (= E323)
- binding zinc ion: C51 (= C59), C54 (= C62), H114 (= H121), H163 (= H170)
1gupA Structure of nucleotidyltransferase complexed with udp-galactose (see paper)
58% identity, 95% coverage: 9:352/363 of query aligns to 1:345/347 of 1gupA
- active site: C51 (= C59), C54 (= C62), H114 (= H121), N152 (= N159), S160 (= S167), H163 (= H170), G165 (≠ H172), Q167 (= Q174)
- binding fe (iii) ion: E181 (≠ K188), H280 (= H287), H295 (= H302), H297 (= H304)
- binding galactose-uridine-5'-diphosphate: R27 (= R35), R30 (= R38), F52 (= F60), R59 (= R67), V60 (≠ I68), N76 (= N84), D77 (= D85), F78 (= F86), F150 (= F157), N152 (= N159), G158 (= G165), C159 (= C166), S160 (= S167), Q167 (= Q174), W169 (= W176), K310 (= K317), F311 (= F318), V313 (= V320), G314 (= G321), E316 (= E323)
- binding potassium ion: N152 (= N159), K153 (= K160), G165 (≠ H172)
- binding zinc ion: C51 (= C59), C54 (= C62), H114 (= H121), H163 (= H170)
1hxpA Nucleotide transferase (see paper)
57% identity, 95% coverage: 9:352/363 of query aligns to 1:338/340 of 1hxpA
- active site: C44 (= C59), C47 (= C62), H107 (= H121), N145 (= N159), S153 (= S167), H156 (= H170), H158 (= H172), Q160 (= Q174)
- binding beta-mercaptoethanol: N145 (= N159), C152 (= C166), Q160 (= Q174), C264 (= C278), S265 (≠ A279), L295 (= L309), A299 (= A313)
- binding fe (iii) ion: E174 (≠ K188), H273 (= H287), H288 (= H302), H290 (= H304)
- binding uridine-5'-monophosphate: F45 (= F60), V53 (≠ I68), N69 (= N84), D70 (= D85)
- binding zinc ion: C44 (= C59), C47 (= C62), H107 (= H121), H156 (= H170)
1hxpB Nucleotide transferase (see paper)
56% identity, 95% coverage: 9:352/363 of query aligns to 1:329/329 of 1hxpB
- active site: C35 (= C59), C38 (= C62), H98 (= H121), N136 (= N159), S144 (= S167), H147 (= H170), H149 (= H172), Q151 (= Q174)
- binding beta-mercaptoethanol: F3 (= F11), P5 (≠ T13), H10 (= H18), N136 (= N159), C143 (= C166), Q151 (= Q174), Y208 (= Y231)
- binding fe (iii) ion: E165 (≠ K188), H264 (= H287), H279 (= H302), H281 (= H304)
- binding uridine-5'-diphosphate: R43 (= R67), V44 (≠ I68), F58 (= F82), N60 (= N84), D61 (= D85), S144 (= S167), N145 (= N168)
- binding zinc ion: C35 (= C59), C38 (= C62), H98 (= H121), H147 (= H170)
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)
52% identity, 93% coverage: 11:349/363 of query aligns to 24:366/379 of P07902
- I32 (≠ R19) to N: in GALAC1; mild; dbSNP:rs111033644
- Y34 (≠ F21) to N: in GALAC1; affects protein stability; dbSNP:rs111033836
- V44 (≠ L31) to M: in GALAC1; reduced enzyme activity; dbSNP:rs111033647
- L62 (= L49) to M: in dbSNP:rs1800461
- L74 (= L61) to P: in GALAC1; reduced enzyme activity; dbSNP:rs111033663
- H132 (≠ S118) to Q: in GALAC1; affects protein stability; dbSNP:rs367543256
- S135 (≠ H121) to L: in GALAC1; about 5% of normal galactose uridylyltransferase activity; dbSNP:rs111033690
- T138 (= T124) to M: in GALAC1; mild; dbSNP:rs111033686
- M142 (≠ L128) to K: in GALAC1; 4% of normal activity; dbSNP:rs111033695
- R148 (≠ Q134) to W: in GALAC1; unstable protein; dbSNP:rs111033693
- V151 (≠ I137) to A: in GALAC1; approximately 3% of normal activity; dbSNP:rs111033701
- V168 (= V154) to L: in GALAC1; loss of activity; dbSNP:rs367543258
- I170 (≠ V156) to T: in GALAC1; loss of activity; dbSNP:rs111033839
- F171 (= F157) to S: in GALAC1; reduced enzyme activity; dbSNP:rs111033715
- G175 (= G161) to D: in GALAC1; strongly reduces galactose uridylyltransferase activity; dbSNP:rs111033718
- P185 (= P171) to H: in GALAC1; loss of activity; dbSNP:rs111033722
- H186 (= H172) active site, Tele-UMP-histidine intermediate
- Q188 (= Q174) to R: in GALAC1; most common mutation; 10% of normal galactose uridylyltransferase activity; impairs protein folding; dbSNP:rs75391579
- L195 (= L181) to P: in GALAC1; no enzymatic activity; dbSNP:rs111033728
- R201 (≠ T187) to C: in GALAC1; 2-fold decrease in activity; dbSNP:rs111033739
- E202 (≠ K188) binding
- E220 (≠ D206) to K: in GALAC1; 3-fold decrease in activity; dbSNP:rs111033747
- R223 (≠ E209) to S: in GALAC1; 3-fold decrease in activity; dbSNP:rs111033750
- L227 (≠ Q213) to P: in GALAC1; results in no detectable protein in the soluble fraction; dbSNP:rs111033846
- R231 (= R217) to H: in GALAC1; 15% of normal activity; dbSNP:rs111033754
- R259 (≠ F245) to Q: in GALAC1; loss of activity; dbSNP:rs886042070; to W: in GALAC1; mild; dbSNP:rs786204763
- I278 (= I264) to N: in GALAC1; 18-fold decrease in activity; dbSNP:rs111033778
- K285 (≠ R271) to N: in GALAC1; severe; impairs protein folding; nearly abolishes enzyme activity; dbSNP:rs111033773
- L289 (= L275) to F: in GALAC1; 3-fold decrease in activity; dbSNP:rs111033774
- E291 (≠ Q277) to V: in GALAC1; 2-fold decrease in activity; dbSNP:rs111033841
- H301 (= H287) binding
- N314 (≠ P297) 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 (= H302) binding
- H321 (= H304) binding
- L327 (= L310) to P: in GALAC1; results in no detectable protein in the soluble fraction; dbSNP:rs111033832
- A330 (= A313) to V: in GALAC1; mild; dbSNP:rs111033804
- R333 (≠ K316) to W: in GALAC1; no enzymatic activity; dbSNP:rs111033800
- T350 (= T333) to A: in GALAC1; mild; dbSNP:rs111033817
6gqdA Structure of human galactose-1-phosphate uridylyltransferase (galt), with crystallization epitope mutations a21y:a22t:t23p:r25l
51% identity, 93% coverage: 11:349/363 of query aligns to 4:342/344 of 6gqdA
- active site: N48 (≠ C59), C51 (= C62), S111 (≠ H121), N149 (= N159), S157 (= S167), H160 (= H170), H162 (= H172), Q164 (= Q174)
- binding 5,6-dihydrouridine-5'-monophosphate: P49 (≠ F60), A57 (≠ I68), N73 (= N84), D74 (= D85), H162 (= H172), Q164 (= Q174)
- binding zinc ion: E178 (≠ K188), H277 (= H287), H295 (= H302), H297 (= H304)
5in3A Crystal structure of glucose-1-phosphate bound nucleotidylated human galactose-1-phosphate uridylyltransferase (see paper)
49% identity, 92% coverage: 15:349/363 of query aligns to 1:324/324 of 5in3A
- active site: N30 (≠ C59), C33 (= C62), S93 (≠ H121), N131 (= N159), S139 (= S167), H142 (= H170), H144 (= H172), Q146 (= Q174)
- binding 1-O-phosphono-alpha-D-glucopyranose: F129 (= F157), N131 (= N159), Q146 (= Q174), V295 (= V320), G296 (= G321), E298 (= E323)
- binding 5,6-dihydrouridine-5'-monophosphate: P31 (≠ F60), A39 (≠ I68), F53 (= F82), N55 (= N84), D56 (= D85), V86 (= V114), H144 (= H172), Q146 (= Q174)
- binding zinc ion: E160 (≠ K188), H259 (= H287), H277 (= H302), H279 (= H304)
6k5zB Structure of uridylyltransferase (see paper)
31% identity, 89% coverage: 20:342/363 of query aligns to 4:306/314 of 6k5zB
- active site: C30 (= C59), C33 (= C62), H86 (= H121), N127 (= N159), S135 (= S167), H138 (= H170), H140 (= H172), Q142 (= Q174)
- binding fe (iii) ion: E156 (≠ K188), H252 (= H287), H266 (= H304), E268 (vs. gap)
- binding phosphate ion: V134 (≠ C166), S135 (= S167), L136 (≠ N168), H140 (= H172)
- binding zinc ion: C30 (= C59), C33 (= C62), H86 (= H121), H138 (= H170), C170 (≠ N202), C173 (≠ G205), H211 (≠ D246), H264 (= H302)
6k9zA Structure of uridylyltransferase mutant (see paper)
28% identity, 89% coverage: 20:342/363 of query aligns to 4:299/309 of 6k9zA
- active site: C23 (= C59), C26 (= C62), H79 (= H121), N120 (= N159), S128 (= S167), H131 (= H170), F133 (≠ H172), Q135 (= Q174)
- binding fe (iii) ion: E149 (≠ K188), H245 (= H287), H259 (= H304), E261 (vs. gap)
- binding uridine-5'-diphosphate: P24 (≠ F60), N43 (= N84), R44 (≠ D85), Y45 (≠ F86), L129 (≠ N168), Q135 (= Q174), Y137 (≠ W176)
- binding zinc ion: C23 (= C59), C26 (= C62), H79 (= H121), H131 (= H170), C163 (≠ N202), C166 (≠ G205), H204 (≠ D246), H257 (= H302)
Q9FK51 ADP-glucose phosphorylase; ADP-glucose:phosphate adenylyltransferase; EC 2.7.7.- from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
25% identity, 64% coverage: 14:244/363 of query aligns to 20:253/351 of Q9FK51
- RAKR 41:44 (≠ RSKR 35:38) binding
- C63 (= C59) binding
- C66 (= C62) binding
- ECA 72:74 (≠ ING 68:70) binding
- N94 (= N84) binding
- H133 (= H121) binding
- N173 (= N159) binding
- GASM 179:182 (≠ GCSN 165:168) binding
- H184 (= H170) binding
- H186 (= H172) active site, Tele-AMP-histidine intermediate
- Q188 (= Q174) binding
- C216 (≠ Y207) binding
- C219 (≠ R210) binding
Sites not aligning to the query:
- 255 binding
- 310 binding
- 321 binding
- 325:326 binding
2h39B Crystal structure of an adp-glucose phosphorylase from arabidopsis thaliana with bound adp-glucose
25% identity, 63% coverage: 15:244/363 of query aligns to 1:215/313 of 2h39B
- active site: C32 (= C59), C35 (= C62), H95 (= H121), N135 (= N159), S143 (= S167), H146 (= H170), G148 (≠ H172), Q150 (= Q174)
- binding adenosine-5'-diphosphate-glucose: R21 (= R35), R24 (= R38), F34 (≠ L61), C42 (≠ N69), N63 (= N84), L64 (≠ D85), Y65 (≠ F86), F133 (= F157), N135 (= N159), G141 (= G165), A142 (≠ C166), S143 (= S167), M144 (≠ N168), Q150 (= Q174)
- binding zinc ion: C32 (= C59), H95 (= H121), H146 (= H170), C178 (≠ Y207), C181 (≠ R210)
Sites not aligning to the query:
1z84A X-ray structure of galt-like protein from arabidopsis thaliana at5g18200 (see paper)
24% identity, 63% coverage: 17:244/363 of query aligns to 2:213/311 of 1z84A
- active site: C31 (= C59), C34 (= C62), H93 (= H121), N133 (= N159), S141 (= S167), H144 (= H170), H146 (= H172), Q148 (= Q174)
- binding adenosine monophosphate: F33 (≠ L61), N62 (= N84), L63 (≠ D85), Y64 (≠ F86), N133 (= N159), A140 (≠ C166), S141 (= S167), M142 (≠ N168), H146 (= H172), Q148 (= Q174)
- binding zinc ion: C31 (= C59), C34 (= C62), H93 (= H121), H144 (= H170), C176 (≠ Y207), C179 (≠ R210)
Sites not aligning to the query:
Query Sequence
>5209835 FitnessBrowser__PV4:5209835
MFQKTQAKSQFSTDEHPHRRFNPLTGEWVLLSPHRSKRPWQGQTEALDLTTAPSYDSECF
LCPGNKRINGEQNPKYDTTFVFQNDFAALNSDGPKAQGEDPLFRFETVEGESRVLCFSPD
HSLTLAQLDPEAMQAVIAAWQSQSELLGKKYLWVQVFENKGAAMGCSNPHPHGQIWAHNH
LPTLVATKQQRLADYYQQHHSNLLGDYVERELQQEVRIVVSNHDWVALVPYWASWPFETL
VLPRFDIRRMTELTAETRESLGEIIGALTVRYDNLFQCAFPYSMGWHGAPFDGQDHPEWC
LHAHFYPPLLRSASVKKFMVGYELLAEIQRDITPEQAAARLREQSPIHYKSSHYKNSHNK
QSQ
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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