SitesBLAST
Comparing WP_052665606.1 NCBI__GCF_000969705.1:WP_052665606.1 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)
6k5zB Structure of uridylyltransferase (see paper)
33% identity, 82% coverage: 42:373/406 of query aligns to 1:307/314 of 6k5zB
- active site: C30 (= C91), C33 (= C94), H86 (= H146), N127 (= N186), S135 (≠ T194), H138 (= H197), H140 (= H199), Q142 (= Q201)
- binding fe (iii) ion: E156 (≠ R215), H252 (≠ Q315), H266 (≠ S332), E268 (= E334)
- binding phosphate ion: V134 (≠ A193), S135 (≠ T194), L136 (= L195), H140 (= H199)
- binding zinc ion: C30 (= C91), C33 (= C94), H86 (= H146), H138 (= H197), C170 (= C229), C173 (= C232), H211 (= H273), H264 (= H330)
6k9zA Structure of uridylyltransferase mutant (see paper)
35% identity, 71% coverage: 87:373/406 of query aligns to 19:300/309 of 6k9zA
- active site: C23 (= C91), C26 (= C94), H79 (= H146), N120 (= N186), S128 (≠ T194), H131 (= H197), F133 (≠ H199), Q135 (= Q201)
- binding fe (iii) ion: E149 (≠ R215), H245 (≠ Q315), H259 (≠ S332), E261 (= E334)
- binding uridine-5'-diphosphate: P24 (= P92), N43 (= N111), R44 (= R112), Y45 (≠ W113), L129 (= L195), Q135 (= Q201), Y137 (= Y203)
- binding zinc ion: C23 (= C91), C26 (= C94), H79 (= H146), H131 (= H197), C163 (= C229), C166 (= C232), H204 (= H273), H257 (= H330)
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)
33% identity, 73% coverage: 43:338/406 of query aligns to 11:302/348 of P09148
- RAKR 28:31 (≠ RNTR 60:63) binding UDP-alpha-D-glucose
- C52 (= C91) binding Zn(2+); mutation to S: Decreases enzyme activity 3000-fold.
- C55 (= C94) binding Zn(2+); mutation to S: Decreases enzyme activity 600-fold.
- V61 (vs. gap) binding in other chain
- ND 77:78 (≠ NR 111:112) binding in other chain
- H115 (= H146) binding Zn(2+); mutation to N: Decreases enzyme activity by 98%.
- N153 (= N186) binding in other chain
- GCS 159:161 (≠ GAT 192:194) binding in other chain
- C160 (≠ A193) mutation C->S,A: Slight inhibition of enzymatic activity.
- S161 (≠ T194) mutation to A: 7000-fold reduction in specific activity.
- H164 (= H197) binding Zn(2+); mutation to N: Decreases enzyme activity 10000-fold.
- H166 (= H199) active site, Tele-UMP-histidine intermediate; mutation to G: Abolishes enzymatic activity.
- Q168 (= Q201) binding in other chain
- E182 (≠ R215) binding Fe cation; mutation to A: Decreases enzyme activity by about 50%. Abolishes iron binding, but has no effect on zinc binding.
- H281 (≠ Q315) binding Fe cation
- H296 (≠ S332) binding Fe cation
- H298 (≠ E334) binding Fe cation
Sites not aligning to the query:
- 311:312 binding UDP-alpha-D-glucose
- 316:317 binding UDP-alpha-D-glucose
- 323 binding in other chain
1guqA Structure of nucleotidyltransferase complexed with udp-glucose (see paper)
33% identity, 73% coverage: 43:338/406 of query aligns to 10:301/347 of 1guqA
- active site: C51 (= C91), C54 (= C94), H114 (= H146), N152 (= N186), S160 (≠ T194), H163 (= H197), G165 (≠ H199), Q167 (= Q201)
- binding fe (iii) ion: E181 (≠ R215), H280 (≠ Q315), H295 (≠ S332), H297 (≠ E334)
- binding potassium ion: E151 (= E185), N152 (= N186), K153 (≠ R187), G165 (≠ H199)
- binding uridine-5'-diphosphate-glucose: R27 (= R60), R30 (= R63), W32 (≠ V72), F52 (≠ P92), V60 (vs. gap), N76 (= N111), D77 (≠ R112), F150 (= F184), N152 (= N186), G158 (= G192), C159 (≠ A193), S160 (≠ T194), Q167 (= Q201)
- binding zinc ion: C51 (= C91), C54 (= C94), H114 (= H146), H163 (= H197)
Sites not aligning to the query:
1gupA Structure of nucleotidyltransferase complexed with udp-galactose (see paper)
33% identity, 73% coverage: 43:338/406 of query aligns to 10:301/347 of 1gupA
- active site: C51 (= C91), C54 (= C94), H114 (= H146), N152 (= N186), S160 (≠ T194), H163 (= H197), G165 (≠ H199), Q167 (= Q201)
- binding fe (iii) ion: E181 (≠ R215), H280 (≠ Q315), H295 (≠ S332), H297 (≠ E334)
- binding galactose-uridine-5'-diphosphate: R27 (= R60), R30 (= R63), F52 (≠ P92), R59 (vs. gap), V60 (vs. gap), N76 (= N111), D77 (≠ R112), F78 (≠ W113), F150 (= F184), N152 (= N186), G158 (= G192), C159 (≠ A193), S160 (≠ T194), Q167 (= Q201), W169 (≠ Y203)
- binding potassium ion: N152 (= N186), K153 (≠ R187), G165 (≠ H199)
- binding zinc ion: C51 (= C91), C54 (= C94), H114 (= H146), H163 (= H197)
Sites not aligning to the query:
1hxpA Nucleotide transferase (see paper)
33% identity, 73% coverage: 43:338/406 of query aligns to 10:294/340 of 1hxpA
- active site: C44 (= C91), C47 (= C94), H107 (= H146), N145 (= N186), S153 (≠ T194), H156 (= H197), H158 (= H199), Q160 (= Q201)
- binding beta-mercaptoethanol: N145 (= N186), C152 (≠ A193), Q160 (= Q201), C264 (≠ E306), S265 (≠ P307)
- binding fe (iii) ion: E174 (≠ R215), H273 (≠ Q315), H288 (≠ S332), H290 (≠ E334)
- binding uridine-5'-monophosphate: F45 (≠ P92), V53 (vs. gap), N69 (= N111), D70 (≠ R112)
- binding zinc ion: C44 (= C91), C47 (= C94), H107 (= H146), H156 (= H197)
Sites not aligning to the query:
1hxpB Nucleotide transferase (see paper)
32% identity, 73% coverage: 43:338/406 of query aligns to 10:285/329 of 1hxpB
- active site: C35 (= C91), C38 (= C94), H98 (= H146), N136 (= N186), S144 (≠ T194), H147 (= H197), H149 (= H199), Q151 (= Q201)
- binding beta-mercaptoethanol: H10 (= H43), N136 (= N186), C143 (≠ A193), Q151 (= Q201), Y208 (≠ F258)
- binding fe (iii) ion: E165 (≠ R215), H264 (≠ Q315), H279 (≠ S332), H281 (≠ E334)
- binding uridine-5'-diphosphate: R43 (vs. gap), V44 (vs. gap), F58 (= F109), N60 (= N111), D61 (≠ R112), S144 (≠ T194), N145 (≠ L195)
- binding zinc ion: C35 (= C91), C38 (= C94), H98 (= H146), H147 (= H197)
Sites not aligning to the query:
6gqdA Structure of human galactose-1-phosphate uridylyltransferase (galt), with crystallization epitope mutations a21y:a22t:t23p:r25l
31% identity, 84% coverage: 43:382/406 of query aligns to 11:341/344 of 6gqdA
- active site: N48 (≠ A89), C51 (= C94), S111 (≠ H146), N149 (= N186), S157 (≠ T194), H160 (= H197), H162 (= H199), Q164 (= Q201)
- binding 5,6-dihydrouridine-5'-monophosphate: P49 (= P92), A57 (vs. gap), N73 (= N111), D74 (≠ R112), H162 (= H199), Q164 (= Q201)
- binding zinc ion: E178 (≠ R215), H277 (≠ Q315), H295 (≠ S332), H297 (≠ E334)
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)
31% identity, 84% coverage: 43:382/406 of query aligns to 31:365/379 of P07902
- I32 (≠ L44) to N: in GALAC1; mild; dbSNP:rs111033644
- Y34 (≠ H46) to N: in GALAC1; affects protein stability; dbSNP:rs111033836
- V44 (≠ I56) to M: in GALAC1; reduced enzyme activity; dbSNP:rs111033647
- L62 (≠ E82) to M: in dbSNP:rs1800461
- L74 (= L93) to P: in GALAC1; reduced enzyme activity; dbSNP:rs111033663
- H132 (≠ T143) to Q: in GALAC1; affects protein stability; dbSNP:rs367543256
- S135 (≠ H146) to L: in GALAC1; about 5% of normal galactose uridylyltransferase activity; dbSNP:rs111033690
- T138 (≠ S149) to M: in GALAC1; mild; dbSNP:rs111033686
- M142 (≠ L153) to K: in GALAC1; 4% of normal activity; dbSNP:rs111033695
- R148 (≠ A159) to W: in GALAC1; unstable protein; dbSNP:rs111033693
- V151 (= V162) to A: in GALAC1; approximately 3% of normal activity; dbSNP:rs111033701
- V168 (= V181) to L: in GALAC1; loss of activity; dbSNP:rs367543258
- I170 (≠ P183) to T: in GALAC1; loss of activity; dbSNP:rs111033839
- F171 (= F184) to S: in GALAC1; reduced enzyme activity; dbSNP:rs111033715
- G175 (= G188) to D: in GALAC1; strongly reduces galactose uridylyltransferase activity; dbSNP:rs111033718
- P185 (= P198) to H: in GALAC1; loss of activity; dbSNP:rs111033722
- H186 (= H199) active site, Tele-UMP-histidine intermediate
- Q188 (= Q201) to R: in GALAC1; most common mutation; 10% of normal galactose uridylyltransferase activity; impairs protein folding; dbSNP:rs75391579
- L195 (= L208) to P: in GALAC1; no enzymatic activity; dbSNP:rs111033728
- R201 (≠ Q214) to C: in GALAC1; 2-fold decrease in activity; dbSNP:rs111033739
- E202 (≠ R215) binding Zn(2+)
- E220 (= E233) to K: in GALAC1; 3-fold decrease in activity; dbSNP:rs111033747
- R223 (≠ A236) to S: in GALAC1; 3-fold decrease in activity; dbSNP:rs111033750
- L227 (≠ A240) to P: in GALAC1; results in no detectable protein in the soluble fraction; dbSNP:rs111033846
- R231 (= R244) to H: in GALAC1; 15% of normal activity; dbSNP:rs111033754
- R259 (= R272) to Q: in GALAC1; loss of activity; dbSNP:rs886042070; to W: in GALAC1; mild; dbSNP:rs786204763
- I278 (≠ A292) to N: in GALAC1; 18-fold decrease in activity; dbSNP:rs111033778
- K285 (≠ R299) to N: in GALAC1; severe; impairs protein folding; nearly abolishes enzyme activity; dbSNP:rs111033773
- L289 (= L303) to F: in GALAC1; 3-fold decrease in activity; dbSNP:rs111033774
- E291 (≠ D305) to V: in GALAC1; 2-fold decrease in activity; dbSNP:rs111033841
- H301 (≠ Q315) binding Zn(2+)
- N314 (≠ A327) 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 (≠ S332) binding Zn(2+)
- H321 (≠ E334) binding Zn(2+)
- L327 (≠ H339) to P: in GALAC1; results in no detectable protein in the soluble fraction; dbSNP:rs111033832
- A330 (≠ P342) to V: in GALAC1; mild; dbSNP:rs111033804
- R333 (≠ L345) to W: in GALAC1; no enzymatic activity; dbSNP:rs111033800
- T350 (≠ V363) to A: in GALAC1; mild; dbSNP:rs111033817
5in3A Crystal structure of glucose-1-phosphate bound nucleotidylated human galactose-1-phosphate uridylyltransferase (see paper)
31% identity, 84% coverage: 43:382/406 of query aligns to 4:323/324 of 5in3A
- active site: N30 (≠ A89), C33 (= C94), S93 (≠ H146), N131 (= N186), S139 (≠ T194), H142 (= H197), H144 (= H199), Q146 (= Q201)
- binding 1-O-phosphono-alpha-D-glucopyranose: F129 (= F184), N131 (= N186), Q146 (= Q201), V295 (≠ A349), G296 (≠ S350), E298 (= E352)
- binding 5,6-dihydrouridine-5'-monophosphate: P31 (= P92), A39 (vs. gap), F53 (= F109), N55 (= N111), D56 (≠ R112), V86 (= V139), H144 (= H199), Q146 (= Q201)
- binding zinc ion: E160 (≠ R215), H259 (≠ Q315), H277 (≠ S332), H279 (≠ E334)
Q9FK51 ADP-glucose phosphorylase; ADP-glucose:phosphate adenylyltransferase; EC 2.7.7.- from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
24% identity, 86% coverage: 24:374/406 of query aligns to 5:348/351 of Q9FK51
- RAKR 41:44 (≠ RNTR 60:63) binding ADP-alpha-D-glucose
- C63 (= C91) binding Zn(2+)
- C66 (= C94) binding Zn(2+)
- ECA 72:74 (≠ VPF 100:102) binding ADP-alpha-D-glucose
- N94 (= N111) binding ADP-alpha-D-glucose
- H133 (= H146) binding Zn(2+)
- N173 (= N186) binding ADP-alpha-D-glucose
- GASM 179:182 (≠ GATL 192:195) binding ADP-alpha-D-glucose
- H184 (= H197) binding Zn(2+)
- H186 (= H199) active site, Tele-AMP-histidine intermediate
- Q188 (= Q201) binding ADP-alpha-D-glucose
- C216 (= C229) binding Zn(2+)
- C219 (= C232) binding Zn(2+)
- H255 (= H273) binding Zn(2+)
- H310 (= H330) binding Zn(2+)
- G321 (≠ V347) binding ADP-alpha-D-glucose
- FE 325:326 (≠ VE 351:352) binding ADP-alpha-D-glucose
2h39B Crystal structure of an adp-glucose phosphorylase from arabidopsis thaliana with bound adp-glucose
23% identity, 81% coverage: 44:371/406 of query aligns to 5:307/313 of 2h39B
- active site: C32 (= C91), C35 (= C94), H95 (= H146), N135 (= N186), S143 (≠ T194), H146 (= H197), G148 (≠ H199), Q150 (= Q201)
- binding adenosine-5'-diphosphate-glucose: R21 (= R60), R24 (= R63), F34 (≠ L93), C42 (≠ P101), N63 (= N111), L64 (≠ R112), Y65 (≠ W113), F133 (= F184), N135 (= N186), G141 (= G192), A142 (= A193), S143 (≠ T194), M144 (≠ L195), Q150 (= Q201), G285 (≠ A349), F287 (≠ V351), E288 (= E352)
- binding zinc ion: C32 (= C91), H95 (= H146), H146 (= H197), C178 (= C229), C181 (= C232), H217 (= H273), H272 (= H330)
1z84A X-ray structure of galt-like protein from arabidopsis thaliana at5g18200 (see paper)
23% identity, 82% coverage: 44:375/406 of query aligns to 4:309/311 of 1z84A
- active site: C31 (= C91), C34 (= C94), H93 (= H146), N133 (= N186), S141 (≠ T194), H144 (= H197), H146 (= H199), Q148 (= Q201)
- binding adenosine monophosphate: F33 (≠ L93), N62 (= N111), L63 (≠ R112), Y64 (≠ W113), N133 (= N186), A140 (= A193), S141 (≠ T194), M142 (≠ L195), H146 (= H199), Q148 (= Q201)
- binding zinc ion: C31 (= C91), C34 (= C94), H93 (= H146), H144 (= H197), C176 (= C229), C179 (= C232), H215 (= H273), H270 (= H330)
Query Sequence
>WP_052665606.1 NCBI__GCF_000969705.1:WP_052665606.1
METEALPRTDLRHADGRRLSLYGAHAGHQLPSDGAPPAPAAIHLRHDALTDRWVAISPAR
NTRPDADDAPPVVAAGDAPAVEATAPPVAGCPLCPGGPEVPFPYDAAVFENRWPTLVADP
PAAPELEGPTAPARGRCEVVLYTSTHEGSLATLSGRELARVVAIWTDRTRELWADPSLRY
VLPFENRGNEVGATLPHPHGQIYALDHLPPGAGQRVTALREHRDRAGACLHCEVVARDAA
ATQRTVASNDSFTVTVPFAPDWPFELHVRARRHGARRLTDLTTAERHDLAIALRDVVHRY
DRLYDEPMAYLMVAQEAPRDVDGDPAADWHLSFEFLPPHRAPNKLKVRASVETAAGLFIN
DTVPEASAAALVAVGGPDPTVHDPIPDVQVVTHHTVGTDTEDVRPP
Or try a new SitesBLAST search
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