SitesBLAST
Comparing BWI76_RS08620 FitnessBrowser__Koxy:BWI76_RS08620 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)
92% identity, 100% coverage: 1:348/348 of query aligns to 1:348/348 of P09148
- RAKR 28:31 (= RAKR 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 (= V61) 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 (= N153) binding in other chain
- GCS 159:161 (= GCS 159:161) binding in other chain
- C160 (= C160) mutation C->S,A: Slight inhibition of enzymatic activity.
- S161 (= S161) mutation to A: 7000-fold reduction in specific activity.
- H164 (= H164) binding ; mutation to N: Decreases enzyme activity 10000-fold.
- H166 (= H166) active site, Tele-UMP-histidine intermediate; mutation to G: Abolishes enzymatic activity.
- Q168 (= Q168) binding in other chain
- E182 (= E182) binding ; mutation to A: Decreases enzyme activity by about 50%. Abolishes iron binding, but has no effect on zinc binding.
- H281 (= H281) binding
- H296 (= H296) binding
- H298 (= H298) binding
- KF 311:312 (= KF 311:312) binding
- YE 316:317 (= YE 316:317) binding
- Q323 (= Q323) binding in other chain
1guqA Structure of nucleotidyltransferase complexed with udp-glucose (see paper)
92% identity, 99% coverage: 4:348/348 of query aligns to 3:347/347 of 1guqA
- active site: C51 (= C52), C54 (= C55), H114 (= H115), N152 (= N153), S160 (= S161), H163 (= H164), G165 (≠ H166), Q167 (= Q168)
- binding fe (iii) ion: E181 (= E182), H280 (= H281), H295 (= H296), H297 (= H298)
- binding potassium ion: E151 (= E152), N152 (= N153), K153 (= K154), G165 (≠ H166)
- binding uridine-5'-diphosphate-glucose: R27 (= R28), R30 (= R31), W32 (= W33), F52 (= F53), V60 (= V61), N76 (= N77), D77 (= D78), F150 (= F151), N152 (= N153), G158 (= G159), C159 (= C160), S160 (= S161), Q167 (= Q168), K310 (= K311), F311 (= F312), Y315 (= Y316), E316 (= E317)
- binding zinc ion: C51 (= C52), C54 (= C55), H114 (= H115), H163 (= H164)
1gupA Structure of nucleotidyltransferase complexed with udp-galactose (see paper)
92% identity, 99% coverage: 4:348/348 of query aligns to 3:347/347 of 1gupA
- active site: C51 (= C52), C54 (= C55), H114 (= H115), N152 (= N153), S160 (= S161), H163 (= H164), G165 (≠ H166), Q167 (= Q168)
- binding fe (iii) ion: E181 (= E182), H280 (= H281), H295 (= H296), H297 (= H298)
- binding galactose-uridine-5'-diphosphate: R27 (= R28), R30 (= R31), F52 (= F53), R59 (= R60), V60 (= V61), N76 (= N77), D77 (= D78), F78 (= F79), F150 (= F151), N152 (= N153), G158 (= G159), C159 (= C160), S160 (= S161), Q167 (= Q168), W169 (= W170), K310 (= K311), F311 (= F312), V313 (= V314), G314 (= G315), E316 (= E317)
- binding potassium ion: N152 (= N153), K153 (= K154), G165 (≠ H166)
- binding zinc ion: C51 (= C52), C54 (= C55), H114 (= H115), H163 (= H164)
1hxpA Nucleotide transferase (see paper)
90% identity, 99% coverage: 4:348/348 of query aligns to 3:340/340 of 1hxpA
- active site: C44 (= C52), C47 (= C55), H107 (= H115), N145 (= N153), S153 (= S161), H156 (= H164), H158 (= H166), Q160 (= Q168)
- binding beta-mercaptoethanol: N145 (= N153), C152 (= C160), Q160 (= Q168), C264 (= C272), S265 (= S273), L295 (= L303), A299 (= A307)
- binding fe (iii) ion: E174 (= E182), H273 (= H281), H288 (= H296), H290 (= H298)
- binding uridine-5'-monophosphate: F45 (= F53), V53 (= V61), N69 (= N77), D70 (= D78)
- binding zinc ion: C44 (= C52), C47 (= C55), H107 (= H115), H156 (= H164)
1hxpB Nucleotide transferase (see paper)
88% identity, 99% coverage: 4:346/348 of query aligns to 3:329/329 of 1hxpB
- active site: C35 (= C52), C38 (= C55), H98 (= H115), N136 (= N153), S144 (= S161), H147 (= H164), H149 (= H166), Q151 (= Q168)
- binding beta-mercaptoethanol: F3 (= F4), P5 (= P6), H10 (= H11), N136 (= N153), C143 (= C160), Q151 (= Q168), Y208 (= Y225)
- binding fe (iii) ion: E165 (= E182), H264 (= H281), H279 (= H296), H281 (= H298)
- binding uridine-5'-diphosphate: R43 (= R60), V44 (= V61), F58 (= F75), N60 (= N77), D61 (= D78), S144 (= S161), N145 (= N162)
- binding zinc ion: C35 (= C52), C38 (= C55), H98 (= H115), H147 (= H164)
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)
59% identity, 98% coverage: 3:343/348 of query aligns to 23:366/379 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 (≠ K42) 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 (≠ E128) to W: in GALAC1; unstable protein; dbSNP:rs111033693
- V151 (= V131) to A: in GALAC1; approximately 3% of normal activity; dbSNP:rs111033701
- V168 (= V148) to L: in GALAC1; loss of activity; dbSNP:rs367543258
- I170 (≠ V150) to T: in GALAC1; loss of activity; dbSNP:rs111033839
- F171 (= F151) to S: in GALAC1; reduced enzyme activity; dbSNP:rs111033715
- G175 (= G155) to D: in GALAC1; strongly reduces galactose uridylyltransferase activity; dbSNP:rs111033718
- P185 (= P165) to H: in GALAC1; loss of activity; dbSNP:rs111033722
- H186 (= H166) active site, Tele-UMP-histidine intermediate
- Q188 (= Q168) to R: in GALAC1; most common mutation; 10% of normal galactose uridylyltransferase activity; impairs protein folding; dbSNP:rs75391579
- L195 (= L175) to P: in GALAC1; no enzymatic activity; dbSNP:rs111033728
- R201 (= R181) to C: in GALAC1; 2-fold decrease in activity; dbSNP:rs111033739
- E202 (= E182) binding
- E220 (≠ D200) to K: in GALAC1; 3-fold decrease in activity; dbSNP:rs111033747
- R223 (≠ Q203) to S: in GALAC1; 3-fold decrease in activity; dbSNP:rs111033750
- L227 (≠ A207) to P: in GALAC1; results in no detectable protein in the soluble fraction; dbSNP:rs111033846
- R231 (= R211) to H: in GALAC1; 15% of normal activity; dbSNP:rs111033754
- R259 (≠ A239) to Q: in GALAC1; loss of activity; dbSNP:rs886042070; to W: in GALAC1; mild; dbSNP:rs786204763
- I278 (≠ A258) to N: in GALAC1; 18-fold decrease in activity; dbSNP:rs111033778
- K285 (≠ R265) to N: in GALAC1; severe; impairs protein folding; nearly abolishes enzyme activity; dbSNP:rs111033773
- L289 (= L269) to F: in GALAC1; 3-fold decrease in activity; dbSNP:rs111033774
- E291 (≠ Q271) to V: in GALAC1; 2-fold decrease in activity; dbSNP:rs111033841
- H301 (= H281) binding
- N314 (= N291) 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 (= H296) binding
- H321 (= H298) binding
- L327 (= L304) to P: in GALAC1; results in no detectable protein in the soluble fraction; dbSNP:rs111033832
- A330 (= A307) to V: in GALAC1; mild; dbSNP:rs111033804
- R333 (= R310) to W: in GALAC1; no enzymatic activity; dbSNP:rs111033800
- T350 (= T327) to A: in GALAC1; mild; dbSNP:rs111033817
6gqdA Structure of human galactose-1-phosphate uridylyltransferase (galt), with crystallization epitope mutations a21y:a22t:t23p:r25l
59% identity, 97% coverage: 8:343/348 of query aligns to 8:342/344 of 6gqdA
- active site: N48 (≠ C52), C51 (= C55), S111 (≠ H115), N149 (= N153), S157 (= S161), H160 (= H164), H162 (= H166), Q164 (= Q168)
- binding 5,6-dihydrouridine-5'-monophosphate: P49 (≠ F53), A57 (≠ V61), N73 (= N77), D74 (= D78), H162 (= H166), Q164 (= Q168)
- binding zinc ion: E178 (= E182), H277 (= H281), H295 (= H296), H297 (= H298)
5in3A Crystal structure of glucose-1-phosphate bound nucleotidylated human galactose-1-phosphate uridylyltransferase (see paper)
58% identity, 97% coverage: 8:343/348 of query aligns to 1:324/324 of 5in3A
- active site: N30 (≠ C52), C33 (= C55), S93 (≠ H115), N131 (= N153), S139 (= S161), H142 (= H164), H144 (= H166), Q146 (= Q168)
- binding 1-O-phosphono-alpha-D-glucopyranose: F129 (= F151), N131 (= N153), Q146 (= Q168), V295 (= V314), G296 (= G315), E298 (= E317)
- binding 5,6-dihydrouridine-5'-monophosphate: P31 (≠ F53), A39 (≠ V61), F53 (= F75), N55 (= N77), D56 (= D78), V86 (= V108), H144 (= H166), Q146 (= Q168)
- binding zinc ion: E160 (= E182), H259 (= H281), H277 (= H296), H279 (= H298)
6k5zB Structure of uridylyltransferase (see paper)
29% identity, 93% coverage: 13:337/348 of query aligns to 4:307/314 of 6k5zB
- active site: C30 (= C52), C33 (= C55), H86 (= H115), N127 (= N153), S135 (= S161), H138 (= H164), H140 (= H166), Q142 (= Q168)
- binding fe (iii) ion: E156 (= E182), H252 (= H281), H266 (= H296), E268 (≠ H298)
- binding phosphate ion: V134 (≠ C160), S135 (= S161), L136 (≠ N162), H140 (= H166)
- binding zinc ion: C30 (= C52), C33 (= C55), H86 (= H115), H138 (= H164), C170 (≠ P196), C173 (≠ V199), H211 (= H240), H264 (≠ Q294)
6k9zA Structure of uridylyltransferase mutant (see paper)
28% identity, 93% coverage: 13:337/348 of query aligns to 4:300/309 of 6k9zA
- active site: C23 (= C52), C26 (= C55), H79 (= H115), N120 (= N153), S128 (= S161), H131 (= H164), F133 (≠ H166), Q135 (= Q168)
- binding fe (iii) ion: E149 (= E182), H245 (= H281), H259 (= H296), E261 (≠ H298)
- binding uridine-5'-diphosphate: P24 (≠ F53), N43 (= N77), R44 (≠ D78), Y45 (≠ F79), L129 (≠ N162), Q135 (= Q168), Y137 (≠ W170)
- binding zinc ion: C23 (= C52), C26 (= C55), H79 (= H115), H131 (= H164), C163 (≠ P196), C166 (≠ V199), H204 (= H240), H257 (≠ Q294)
Q9FK51 ADP-glucose phosphorylase; ADP-glucose:phosphate adenylyltransferase; EC 2.7.7.- from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
26% identity, 82% coverage: 10:295/348 of query aligns to 23:313/351 of Q9FK51
- RAKR 41:44 (= RAKR 28:31) binding
- C63 (≠ D49) binding
- C66 (= C52) binding
- ECA 72:74 (≠ LCP 54:56) binding
- N94 (= N77) binding
- H133 (= H115) binding
- N173 (= N153) binding
- GASM 179:182 (≠ GCSN 159:162) binding
- H184 (= H164) binding
- H186 (= H166) active site, Tele-AMP-histidine intermediate
- Q188 (= Q168) binding
- C216 (≠ P196) binding
- C219 (≠ V199) binding
- H255 (= H240) binding
- H310 (= H292) binding
Sites not aligning to the query:
- 321 binding
- 325:326 binding
2h39B Crystal structure of an adp-glucose phosphorylase from arabidopsis thaliana with bound adp-glucose
25% identity, 82% coverage: 10:295/348 of query aligns to 3:275/313 of 2h39B
- active site: C32 (≠ D49), C35 (= C52), H95 (= H115), N135 (= N153), S143 (= S161), H146 (= H164), G148 (≠ H166), Q150 (= Q168)
- binding adenosine-5'-diphosphate-glucose: R21 (= R28), R24 (= R31), F34 (≠ D51), C42 (= C55), N63 (= N77), L64 (≠ D78), Y65 (≠ F79), F133 (= F151), N135 (= N153), G141 (= G159), A142 (≠ C160), S143 (= S161), M144 (≠ N162), Q150 (= Q168)
- binding zinc ion: C32 (≠ D49), H95 (= H115), H146 (= H164), C178 (≠ P196), C181 (≠ V199), H217 (= H240), H272 (= H292)
Sites not aligning to the query:
1z84A X-ray structure of galt-like protein from arabidopsis thaliana at5g18200 (see paper)
24% identity, 82% coverage: 10:295/348 of query aligns to 2:273/311 of 1z84A
- active site: C31 (= C52), C34 (= C55), H93 (= H115), N133 (= N153), S141 (= S161), H144 (= H164), H146 (= H166), Q148 (= Q168)
- binding adenosine monophosphate: F33 (≠ L54), N62 (= N77), L63 (≠ D78), Y64 (≠ F79), N133 (= N153), A140 (≠ C160), S141 (= S161), M142 (≠ N162), H146 (= H166), Q148 (= Q168)
- binding zinc ion: C31 (= C52), C34 (= C55), H93 (= H115), H144 (= H164), C176 (≠ P196), C179 (≠ V199), H215 (= H240), H270 (= H292)
Query Sequence
>BWI76_RS08620 FitnessBrowser__Koxy:BWI76_RS08620
MSVFNPVDHPHRRYNPLTGQWILVSPHRAKRPWQGAQETPAKQSLPAHDPDCFLCPGNTR
VTGDKNPNYTGTFVFTNDFAALMTDTPDAPESDDPLMRCQSARGTSRVICFSPDHSKTLP
ELSVEALEGVVKTWQEQTADLGKTYPWVQVFENKGAAMGCSNPHPHGQVWANSFLPNEAE
REDRLQKAYFTEHGAPMLVDYAQRELADGSRTVVETEHWLAVVPYWAAWPFETLLLPKAH
VQRLTDLTDDQRSDLALALKKLTSRYDNLFQCSFPYSMGWHGAPFNDEENNHWQLHAHFY
PPLLRSATVRKFMVGYEMLAETQRDLTAEQAAERLRAVSDVHFRESGV
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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