SitesBLAST
Comparing CA265_RS06120 FitnessBrowser__Pedo557:CA265_RS06120 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, 97% coverage: 10:351/351 of query aligns to 9:348/348 of P09148
- RAKR 28:31 (≠ RTKR 29:32) binding
- C52 (= C53) binding ; mutation to S: Decreases enzyme activity 3000-fold.
- C55 (= C56) binding ; mutation to S: Decreases enzyme activity 600-fold.
- V61 (≠ A62) binding in other chain
- ND 77:78 (= ND 78:79) binding in other chain
- H115 (= H116) binding ; mutation to N: Decreases enzyme activity by 98%.
- N153 (= N156) binding in other chain
- GCS 159:161 (= GCS 162:164) binding in other chain
- C160 (= C163) mutation C->S,A: Slight inhibition of enzymatic activity.
- S161 (= S164) mutation to A: 7000-fold reduction in specific activity.
- H164 (= H167) binding ; mutation to N: Decreases enzyme activity 10000-fold.
- H166 (= H169) active site, Tele-UMP-histidine intermediate; mutation to G: Abolishes enzymatic activity.
- Q168 (= Q171) binding in other chain
- E182 (= E185) binding ; mutation to A: Decreases enzyme activity by about 50%. Abolishes iron binding, but has no effect on zinc binding.
- H281 (= H284) binding
- H296 (= H299) binding
- H298 (= H301) binding
- KF 311:312 (= KF 314:315) binding
- YE 316:317 (= YE 319:320) binding
- Q323 (= Q326) binding in other chain
1guqA Structure of nucleotidyltransferase complexed with udp-glucose (see paper)
50% identity, 97% coverage: 10:351/351 of query aligns to 8:347/347 of 1guqA
- active site: C51 (= C53), C54 (= C56), H114 (= H116), N152 (= N156), S160 (= S164), H163 (= H167), G165 (≠ H169), Q167 (= Q171)
- binding fe (iii) ion: E181 (= E185), H280 (= H284), H295 (= H299), H297 (= H301)
- binding potassium ion: E151 (= E155), N152 (= N156), K153 (= K157), G165 (≠ H169)
- binding uridine-5'-diphosphate-glucose: R27 (= R29), R30 (= R32), W32 (= W34), F52 (≠ Y54), V60 (≠ A62), N76 (= N78), D77 (= D79), F150 (= F154), N152 (= N156), G158 (= G162), C159 (= C163), S160 (= S164), Q167 (= Q171), K310 (= K314), F311 (= F315), Y315 (= Y319), E316 (= E320)
- binding zinc ion: C51 (= C53), C54 (= C56), H114 (= H116), H163 (= H167)
1gupA Structure of nucleotidyltransferase complexed with udp-galactose (see paper)
50% identity, 97% coverage: 10:351/351 of query aligns to 8:347/347 of 1gupA
- active site: C51 (= C53), C54 (= C56), H114 (= H116), N152 (= N156), S160 (= S164), H163 (= H167), G165 (≠ H169), Q167 (= Q171)
- binding fe (iii) ion: E181 (= E185), H280 (= H284), H295 (= H299), H297 (= H301)
- binding galactose-uridine-5'-diphosphate: R27 (= R29), R30 (= R32), F52 (≠ Y54), R59 (= R61), V60 (≠ A62), N76 (= N78), D77 (= D79), F78 (= F80), F150 (= F154), N152 (= N156), G158 (= G162), C159 (= C163), S160 (= S164), Q167 (= Q171), W169 (= W173), K310 (= K314), F311 (= F315), V313 (= V317), G314 (= G318), E316 (= E320)
- binding potassium ion: N152 (= N156), K153 (= K157), G165 (≠ H169)
- binding zinc ion: C51 (= C53), C54 (= C56), H114 (= H116), H163 (= H167)
1hxpA Nucleotide transferase (see paper)
50% identity, 97% coverage: 10:351/351 of query aligns to 8:340/340 of 1hxpA
- active site: C44 (= C53), C47 (= C56), H107 (= H116), N145 (= N156), S153 (= S164), H156 (= H167), H158 (= H169), Q160 (= Q171)
- binding beta-mercaptoethanol: N145 (= N156), C152 (= C163), Q160 (= Q171), C264 (≠ T275), S265 (= S276), L295 (= L306), A299 (= A310)
- binding fe (iii) ion: E174 (= E185), H273 (= H284), H288 (= H299), H290 (= H301)
- binding uridine-5'-monophosphate: F45 (≠ Y54), V53 (≠ A62), N69 (= N78), D70 (= D79)
- binding zinc ion: C44 (= C53), C47 (= C56), H107 (= H116), H156 (= H167)
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)
50% identity, 99% coverage: 4:350/351 of query aligns to 23:370/379 of P07902
- I32 (≠ T13) to N: in GALAC1; mild; dbSNP:rs111033644
- Y34 (≠ L15) to N: in GALAC1; affects protein stability; dbSNP:rs111033836
- V44 (= V25) to M: in GALAC1; reduced enzyme activity; dbSNP:rs111033647
- L62 (≠ P43) to M: in dbSNP:rs1800461
- L74 (= L55) to P: in GALAC1; reduced enzyme activity; dbSNP:rs111033663
- H132 (≠ S113) to Q: in GALAC1; affects protein stability; dbSNP:rs367543256
- S135 (≠ H116) to L: in GALAC1; about 5% of normal galactose uridylyltransferase activity; dbSNP:rs111033690
- T138 (= T119) to M: in GALAC1; mild; dbSNP:rs111033686
- M142 (= M123) to K: in GALAC1; 4% of normal activity; dbSNP:rs111033695
- R148 (≠ T129) to W: in GALAC1; unstable protein; dbSNP:rs111033693
- V151 (= V132) to A: in GALAC1; approximately 3% of normal activity; dbSNP:rs111033701
- V168 (≠ I151) to L: in GALAC1; loss of activity; dbSNP:rs367543258
- I170 (= I153) to T: in GALAC1; loss of activity; dbSNP:rs111033839
- F171 (= F154) to S: in GALAC1; reduced enzyme activity; dbSNP:rs111033715
- G175 (= G158) to D: in GALAC1; strongly reduces galactose uridylyltransferase activity; dbSNP:rs111033718
- P185 (= P168) to H: in GALAC1; loss of activity; dbSNP:rs111033722
- H186 (= H169) active site, Tele-UMP-histidine intermediate
- Q188 (= Q171) to R: in GALAC1; most common mutation; 10% of normal galactose uridylyltransferase activity; impairs protein folding; dbSNP:rs75391579
- L195 (≠ I178) to P: in GALAC1; no enzymatic activity; dbSNP:rs111033728
- R201 (≠ E185) to C: in GALAC1; 2-fold decrease in activity; dbSNP:rs111033739
- E202 (≠ T186) binding
- E220 (≠ D203) to K: in GALAC1; 3-fold decrease in activity; dbSNP:rs111033747
- R223 (≠ K206) to S: in GALAC1; 3-fold decrease in activity; dbSNP:rs111033750
- L227 (≠ K210) to P: in GALAC1; results in no detectable protein in the soluble fraction; dbSNP:rs111033846
- R231 (= R214) to H: in GALAC1; 15% of normal activity; dbSNP:rs111033754
- R259 (= R242) to Q: in GALAC1; loss of activity; dbSNP:rs886042070; to W: in GALAC1; mild; dbSNP:rs786204763
- I278 (≠ A261) to N: in GALAC1; 18-fold decrease in activity; dbSNP:rs111033778
- K285 (= K268) to N: in GALAC1; severe; impairs protein folding; nearly abolishes enzyme activity; dbSNP:rs111033773
- L289 (= L272) to F: in GALAC1; 3-fold decrease in activity; dbSNP:rs111033774
- E291 (= E274) to V: in GALAC1; 2-fold decrease in activity; dbSNP:rs111033841
- H301 (= H284) binding
- N314 (vs. gap) 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 (= H299) binding
- H321 (= H301) binding
- L327 (= L307) to P: in GALAC1; results in no detectable protein in the soluble fraction; dbSNP:rs111033832
- A330 (= A310) to V: in GALAC1; mild; dbSNP:rs111033804
- R333 (≠ K313) to W: in GALAC1; no enzymatic activity; dbSNP:rs111033800
- T350 (= T330) to A: in GALAC1; mild; dbSNP:rs111033817
1hxpB Nucleotide transferase (see paper)
49% identity, 97% coverage: 10:349/351 of query aligns to 8:329/329 of 1hxpB
- active site: C35 (= C53), C38 (= C56), H98 (= H116), N136 (= N156), S144 (= S164), H147 (= H167), H149 (= H169), Q151 (= Q171)
- binding beta-mercaptoethanol: H10 (= H12), N136 (= N156), C143 (= C163), Q151 (= Q171), Y208 (≠ F228)
- binding fe (iii) ion: E165 (= E185), H264 (= H284), H279 (= H299), H281 (= H301)
- binding uridine-5'-diphosphate: R43 (= R61), V44 (≠ A62), F58 (= F76), N60 (= N78), D61 (= D79), S144 (= S164), N145 (= N165)
- binding zinc ion: C35 (= C53), C38 (= C56), H98 (= H116), H147 (= H167)
Sites not aligning to the query:
6gqdA Structure of human galactose-1-phosphate uridylyltransferase (galt), with crystallization epitope mutations a21y:a22t:t23p:r25l
49% identity, 98% coverage: 5:348/351 of query aligns to 4:344/344 of 6gqdA
- active site: N48 (≠ C53), C51 (= C56), S111 (≠ H116), N149 (= N156), S157 (= S164), H160 (= H167), H162 (= H169), Q164 (= Q171)
- binding 5,6-dihydrouridine-5'-monophosphate: P49 (≠ Y54), A57 (= A62), N73 (= N78), D74 (= D79), H162 (= H169), Q164 (= Q171)
- binding zinc ion: E178 (≠ T186), H277 (= H284), H295 (= H299), H297 (= H301)
5in3A Crystal structure of glucose-1-phosphate bound nucleotidylated human galactose-1-phosphate uridylyltransferase (see paper)
49% identity, 95% coverage: 12:346/351 of query aligns to 4:324/324 of 5in3A
- active site: N30 (≠ C53), C33 (= C56), S93 (≠ H116), N131 (= N156), S139 (= S164), H142 (= H167), H144 (= H169), Q146 (= Q171)
- binding 1-O-phosphono-alpha-D-glucopyranose: F129 (= F154), N131 (= N156), Q146 (= Q171), V295 (= V317), G296 (= G318), E298 (= E320)
- binding 5,6-dihydrouridine-5'-monophosphate: P31 (≠ Y54), A39 (= A62), F53 (= F76), N55 (= N78), D56 (= D79), V86 (= V109), H144 (= H169), Q146 (= Q171)
- binding zinc ion: E160 (≠ T186), H259 (= H284), H277 (= H299), H279 (= H301)
6k5zB Structure of uridylyltransferase (see paper)
30% identity, 93% coverage: 14:339/351 of query aligns to 4:306/314 of 6k5zB
- active site: C30 (= C53), C33 (= C56), H86 (= H116), N127 (= N156), S135 (= S164), H138 (= H167), H140 (= H169), Q142 (= Q171)
- binding fe (iii) ion: E156 (= E185), H252 (= H284), H266 (= H301), E268 (vs. gap)
- binding phosphate ion: V134 (≠ C163), S135 (= S164), L136 (≠ N165), H140 (= H169)
- binding zinc ion: C30 (= C53), C33 (= C56), H86 (= H116), H138 (= H167), C170 (≠ S199), C173 (≠ L205), H211 (= H243), H264 (= H299)
Q9FK51 ADP-glucose phosphorylase; ADP-glucose:phosphate adenylyltransferase; EC 2.7.7.- from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
26% identity, 96% coverage: 8:344/351 of query aligns to 20:351/351 of Q9FK51
- RAKR 41:44 (≠ RTKR 29:32) binding
- C63 (= C53) binding
- C66 (= C56) binding
- ECA 72:74 (≠ ADG 62:64) binding
- N94 (= N78) binding
- H133 (= H116) binding
- N173 (= N156) binding
- GASM 179:182 (≠ GCSN 162:165) binding
- H184 (= H167) binding
- H186 (= H169) active site, Tele-AMP-histidine intermediate
- Q188 (= Q171) binding
- C216 (≠ S199) binding
- C219 (≠ L207) binding
- H255 (= H243) binding
- H310 (= H297) binding
- G321 (≠ S311) binding
- FE 325:326 (≠ FM 315:316) binding
6k9zA Structure of uridylyltransferase mutant (see paper)
28% identity, 93% coverage: 14:339/351 of query aligns to 4:299/309 of 6k9zA
- active site: C23 (= C53), C26 (= C56), H79 (= H116), N120 (= N156), S128 (= S164), H131 (= H167), F133 (≠ H169), Q135 (= Q171)
- binding fe (iii) ion: E149 (= E185), H245 (= H284), H259 (= H301), E261 (vs. gap)
- binding uridine-5'-diphosphate: P24 (≠ Y54), N43 (= N78), R44 (≠ D79), Y45 (≠ F80), L129 (≠ N165), Q135 (= Q171), Y137 (≠ W173)
- binding zinc ion: C23 (= C53), C26 (= C56), H79 (= H116), H131 (= H167), C163 (≠ S199), C166 (≠ L205), H204 (= H243), H257 (= H299)
2h39B Crystal structure of an adp-glucose phosphorylase from arabidopsis thaliana with bound adp-glucose
25% identity, 95% coverage: 10:344/351 of query aligns to 2:313/313 of 2h39B
- active site: C32 (= C53), C35 (= C56), H95 (= H116), N135 (= N156), S143 (= S164), H146 (= H167), G148 (≠ H169), Q150 (= Q171)
- binding adenosine-5'-diphosphate-glucose: R21 (= R29), R24 (= R32), F34 (≠ L55), C42 (≠ D63), N63 (= N78), L64 (≠ D79), Y65 (≠ F80), F133 (= F154), N135 (= N156), G141 (= G162), A142 (≠ C163), S143 (= S164), M144 (≠ N165), Q150 (= Q171), G285 (≠ K313), F287 (= F315), E288 (≠ M316)
- binding zinc ion: C32 (= C53), H95 (= H116), H146 (= H167), C178 (≠ S199), C181 (≠ S202), H217 (= H243), H272 (= H297)
1z84A X-ray structure of galt-like protein from arabidopsis thaliana at5g18200 (see paper)
24% identity, 95% coverage: 10:344/351 of query aligns to 1:311/311 of 1z84A
- active site: C31 (= C53), C34 (= C56), H93 (= H116), N133 (= N156), S141 (= S164), H144 (= H167), H146 (= H169), Q148 (= Q171)
- binding adenosine monophosphate: F33 (≠ L55), N62 (= N78), L63 (≠ D79), Y64 (≠ F80), N133 (= N156), A140 (≠ C163), S141 (= S164), M142 (≠ N165), H146 (= H169), Q148 (= Q171)
- binding zinc ion: C31 (= C53), C34 (= C56), H93 (= H116), H144 (= H167), C176 (≠ S199), C179 (≠ S202), H215 (= H243), H270 (= H297)
Query Sequence
>CA265_RS06120 FitnessBrowser__Pedo557:CA265_RS06120
MNQTFELDSNPHTRLNILTGEWVLVSPHRTKRPWQGKVEDVTPDNRPEYDPKCYLCPGNS
RADGDSNPEYTESFVFNNDFAALLEDTPAGNMNEHDLLVASNQRGLCKVISFSPKHHLTL
PEMSVKAITAVVNVWQNEFNSLAENNWIKYIQIFENKGEIMGCSNPHPHGQIWSQGDIPL
EIAKETERQKSYYAIHKRSLLSDYLKLEQKKKERIIFENDHFAVLVPFWAVWPYETMIIS
KRHVNSIRLFTEAEKESLAEAIKVLTTKYDNLFETSFPYSAGMHQAPVNNGYYPEWHWHM
HFYPPLLRSASVKKFMVGYEMLANPQRDITPEFAANRLKEMSATHYKISKV
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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